---
_id: '15001'
abstract:
- lang: eng
text: "Self-replication of amyloid fibrils via secondary nucleation is an intriguing
physicochemical phenomenon in which existing fibrils catalyze the formation of
their own copies. The molecular events behind this fibril surface-mediated process
remain largely inaccessible to current structural and imaging techniques. Using
statistical mechanics, computer modeling, and chemical kinetics, we show that
the catalytic structure of the fibril surface can be inferred from the aggregation
behavior in the presence and absence of a fibril-binding inhibitor. We apply our
approach to the case of Alzheimer’s A\r\n amyloid fibrils formed in the presence
of proSP-C Brichos inhibitors. We find that self-replication of A\r\n fibrils
occurs on small catalytic sites on the fibril surface, which are far apart from
each other, and each of which can be covered by a single Brichos inhibitor."
acknowledgement: We acknowledge support from the Erasmus programme and the University
College London Institute for the Physics of Living Systems (S.C., T.C.T.M., A.Š.),
the Biotechnology and Biological Sciences Research Council (T.P.J.K.), the Engineering
and Physical Sciences Research Council (D.F.), the European Research Council (T.P.J.K.,
S.L., D.F., and A.Š.), the Frances and Augustus Newman Foundation (T.P.J.K.), the
Academy of Medical Sciences and Wellcome Trust (A.Š.), and the Royal Society (S.C.
and A.Š.).
article_number: e2220075121
article_processing_charge: Yes
article_type: original
author:
- first_name: Samo
full_name: Curk, Samo
id: 031eff0d-d481-11ee-8508-cd12a7a86e5b
last_name: Curk
orcid: 0000-0001-6160-9766
- first_name: Johannes
full_name: Krausser, Johannes
last_name: Krausser
- first_name: Georg
full_name: Meisl, Georg
last_name: Meisl
- first_name: Daan
full_name: Frenkel, Daan
last_name: Frenkel
- first_name: Sara
full_name: Linse, Sara
last_name: Linse
- first_name: Thomas C.T.
full_name: Michaels, Thomas C.T.
last_name: Michaels
- first_name: Tuomas P.J.
full_name: Knowles, Tuomas P.J.
last_name: Knowles
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
citation:
ama: Curk S, Krausser J, Meisl G, et al. Self-replication of Aβ42 aggregates occurs
on small and isolated fibril sites. Proceedings of the National Academy of
Sciences of the United States of America. 2024;121(7). doi:10.1073/pnas.2220075121
apa: Curk, S., Krausser, J., Meisl, G., Frenkel, D., Linse, S., Michaels, T. C.
T., … Šarić, A. (2024). Self-replication of Aβ42 aggregates occurs on small and
isolated fibril sites. Proceedings of the National Academy of Sciences of the
United States of America. Proceedings of the National Academy of Sciences.
https://doi.org/10.1073/pnas.2220075121
chicago: Curk, Samo, Johannes Krausser, Georg Meisl, Daan Frenkel, Sara Linse, Thomas
C.T. Michaels, Tuomas P.J. Knowles, and Anđela Šarić. “Self-Replication of Aβ42
Aggregates Occurs on Small and Isolated Fibril Sites.” Proceedings of the National
Academy of Sciences of the United States of America. Proceedings of the National
Academy of Sciences, 2024. https://doi.org/10.1073/pnas.2220075121.
ieee: S. Curk et al., “Self-replication of Aβ42 aggregates occurs on small
and isolated fibril sites,” Proceedings of the National Academy of Sciences
of the United States of America, vol. 121, no. 7. Proceedings of the National
Academy of Sciences, 2024.
ista: Curk S, Krausser J, Meisl G, Frenkel D, Linse S, Michaels TCT, Knowles TPJ,
Šarić A. 2024. Self-replication of Aβ42 aggregates occurs on small and isolated
fibril sites. Proceedings of the National Academy of Sciences of the United States
of America. 121(7), e2220075121.
mla: Curk, Samo, et al. “Self-Replication of Aβ42 Aggregates Occurs on Small and
Isolated Fibril Sites.” Proceedings of the National Academy of Sciences of
the United States of America, vol. 121, no. 7, e2220075121, Proceedings of
the National Academy of Sciences, 2024, doi:10.1073/pnas.2220075121.
short: S. Curk, J. Krausser, G. Meisl, D. Frenkel, S. Linse, T.C.T. Michaels, T.P.J.
Knowles, A. Šarić, Proceedings of the National Academy of Sciences of the United
States of America 121 (2024).
date_created: 2024-02-18T23:01:00Z
date_published: 2024-02-13T00:00:00Z
date_updated: 2024-02-26T08:45:56Z
day: '13'
ddc:
- '570'
department:
- _id: AnSa
doi: 10.1073/pnas.2220075121
ec_funded: 1
external_id:
pmid:
- '38335256'
file:
- access_level: open_access
checksum: 5aeb65bcc0dd829b1f9ab307c5031d4b
content_type: application/pdf
creator: dernst
date_created: 2024-02-26T08:20:00Z
date_updated: 2024-02-26T08:20:00Z
file_id: '15026'
file_name: 2024_PNAS_Curk.pdf
file_size: 7699487
relation: main_file
success: 1
file_date_updated: 2024-02-26T08:20:00Z
has_accepted_license: '1'
intvolume: ' 121'
issue: '7'
language:
- iso: eng
month: '02'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: eba2549b-77a9-11ec-83b8-a81e493eae4e
call_identifier: H2020
grant_number: '802960'
name: 'Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines'
publication: Proceedings of the National Academy of Sciences of the United States
of America
publication_identifier:
eissn:
- 1091-6490
publication_status: published
publisher: Proceedings of the National Academy of Sciences
quality_controlled: '1'
related_material:
record:
- id: '15027'
relation: research_data
status: public
scopus_import: '1'
status: public
title: Self-replication of Aβ42 aggregates occurs on small and isolated fibril sites
tmp:
image: /images/cc_by_nc_nd.png
legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode
name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
(CC BY-NC-ND 4.0)
short: CC BY-NC-ND (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 121
year: '2024'
...
---
_id: '15116'
abstract:
- lang: eng
text: Water is known to play an important role in collagen self-assembly, but it
is still largely unclear how water–collagen interactions influence the assembly
process and determine the fibril network properties. Here, we use the H2O/D2O
isotope effect on the hydrogen-bond strength in water to investigate the role
of hydration in collagen self-assembly. We dissolve collagen in H2O and D2O and
compare the growth kinetics and the structure of the collagen assemblies formed
in these water isotopomers. Surprisingly, collagen assembly occurs ten times faster
in D2O than in H2O, and collagen in D2O self-assembles into much thinner fibrils,
that form a more inhomogeneous and softer network, with a fourfold reduction in
elastic modulus when compared to H2O. Combining spectroscopic measurements with
atomistic simulations, we show that collagen in D2O is less hydrated than in H2O.
This partial dehydration lowers the enthalpic penalty for water removal and reorganization
at the collagen–water interface, increasing the self-assembly rate and the number
of nucleation centers, leading to thinner fibrils and a softer network. Coarse-grained
simulations show that the acceleration in the initial nucleation rate can be reproduced
by the enhancement of electrostatic interactions. These results show that water
acts as a mediator between collagen monomers, by modulating their interactions
so as to optimize the assembly process and, thus, the final network properties.
We believe that isotopically modulating the hydration of proteins can be a valuable
method to investigate the role of water in protein structural dynamics and protein
self-assembly.
acknowledgement: We thank Dr. Steven Roeters (Aarhus University), Dr. Federica Burla,
and Prof. Dr. Mischa Bonn (Institute for Polymer Research, Mainz, Germany) for the
useful discussions. We thank Dr. Wim Roeterdink and Michiel Hilberts for technical
support. G.H.K. acknowledges financial support by the “BaSyC Building a Synthetic
Cell” Gravitation grant (024.003.019) of The Netherlands Ministry of Education,
Culture and Science (OCW) and The Netherlands Organization for Scientific Research
and from NWO grant OCENW.GROOT.2019.022. This work has received support from the
National Research Foundation of Korea (NRF), funded by the Ministry of Science and
ICT, under Grant No. 2022K1A3A1A04062969. This publication is part of the project
(with Project Number VI.Veni.212.240) of the research programme NWO Talent Programme
Veni 2021, which is financed by the Dutch Research Council (NWO). I.M.I. acknowledges
support from the Sectorplan Bèta & Techniek of the Dutch Government and the Dementia
Research - Synapsis Foundation Switzerland. A.Š. and K.K. acknowledge support from
Royal Society and European Research Council Starting Grant. G. Giubertoni kindly
thanks to the Care4Bones community and the Collagen Café community for reminding
that we do not own the knowledge we create, but it is, rather, a collective resource
intended for the advancement of human progress.
article_number: e2313162121
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Giulia
full_name: Giubertoni, Giulia
last_name: Giubertoni
- first_name: Liru
full_name: Feng, Liru
last_name: Feng
- first_name: Kevin
full_name: Klein, Kevin
last_name: Klein
- first_name: Guido
full_name: Giannetti, Guido
last_name: Giannetti
- first_name: Luco
full_name: Rutten, Luco
last_name: Rutten
- first_name: Yeji
full_name: Choi, Yeji
last_name: Choi
- first_name: Anouk
full_name: Van Der Net, Anouk
last_name: Van Der Net
- first_name: Gerard
full_name: Castro-Linares, Gerard
last_name: Castro-Linares
- first_name: Federico
full_name: Caporaletti, Federico
last_name: Caporaletti
- first_name: Dimitra
full_name: Micha, Dimitra
last_name: Micha
- first_name: Johannes
full_name: Hunger, Johannes
last_name: Hunger
- first_name: Antoine
full_name: Deblais, Antoine
last_name: Deblais
- first_name: Daniel
full_name: Bonn, Daniel
last_name: Bonn
- first_name: Nico
full_name: Sommerdijk, Nico
last_name: Sommerdijk
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Ioana M.
full_name: Ilie, Ioana M.
last_name: Ilie
- first_name: Gijsje H.
full_name: Koenderink, Gijsje H.
last_name: Koenderink
- first_name: Sander
full_name: Woutersen, Sander
last_name: Woutersen
citation:
ama: Giubertoni G, Feng L, Klein K, et al. Elucidating the role of water in collagen
self-assembly by isotopically modulating collagen hydration. Proceedings of
the National Academy of Sciences of the United States of America. 2024;121(11).
doi:10.1073/pnas.2313162121
apa: Giubertoni, G., Feng, L., Klein, K., Giannetti, G., Rutten, L., Choi, Y., …
Woutersen, S. (2024). Elucidating the role of water in collagen self-assembly
by isotopically modulating collagen hydration. Proceedings of the National
Academy of Sciences of the United States of America. Proceedings of the National
Academy of Sciences. https://doi.org/10.1073/pnas.2313162121
chicago: Giubertoni, Giulia, Liru Feng, Kevin Klein, Guido Giannetti, Luco Rutten,
Yeji Choi, Anouk Van Der Net, et al. “Elucidating the Role of Water in Collagen
Self-Assembly by Isotopically Modulating Collagen Hydration.” Proceedings of
the National Academy of Sciences of the United States of America. Proceedings
of the National Academy of Sciences, 2024. https://doi.org/10.1073/pnas.2313162121.
ieee: G. Giubertoni et al., “Elucidating the role of water in collagen self-assembly
by isotopically modulating collagen hydration,” Proceedings of the National
Academy of Sciences of the United States of America, vol. 121, no. 11. Proceedings
of the National Academy of Sciences, 2024.
ista: Giubertoni G, Feng L, Klein K, Giannetti G, Rutten L, Choi Y, Van Der Net
A, Castro-Linares G, Caporaletti F, Micha D, Hunger J, Deblais A, Bonn D, Sommerdijk
N, Šarić A, Ilie IM, Koenderink GH, Woutersen S. 2024. Elucidating the role of
water in collagen self-assembly by isotopically modulating collagen hydration.
Proceedings of the National Academy of Sciences of the United States of America.
121(11), e2313162121.
mla: Giubertoni, Giulia, et al. “Elucidating the Role of Water in Collagen Self-Assembly
by Isotopically Modulating Collagen Hydration.” Proceedings of the National
Academy of Sciences of the United States of America, vol. 121, no. 11, e2313162121,
Proceedings of the National Academy of Sciences, 2024, doi:10.1073/pnas.2313162121.
short: G. Giubertoni, L. Feng, K. Klein, G. Giannetti, L. Rutten, Y. Choi, A. Van
Der Net, G. Castro-Linares, F. Caporaletti, D. Micha, J. Hunger, A. Deblais, D.
Bonn, N. Sommerdijk, A. Šarić, I.M. Ilie, G.H. Koenderink, S. Woutersen, Proceedings
of the National Academy of Sciences of the United States of America 121 (2024).
date_created: 2024-03-17T23:00:57Z
date_published: 2024-03-12T00:00:00Z
date_updated: 2024-03-19T11:41:32Z
day: '12'
ddc:
- '550'
department:
- _id: AnSa
doi: 10.1073/pnas.2313162121
external_id:
pmid:
- '38451946'
file:
- access_level: open_access
checksum: a3f7fdc29dd9f0a38952ab4e322b3a05
content_type: application/pdf
creator: dernst
date_created: 2024-03-19T10:22:42Z
date_updated: 2024-03-19T10:22:42Z
file_id: '15125'
file_name: 2024_PNAS_Giubertoni.pdf
file_size: 12952586
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success: 1
file_date_updated: 2024-03-19T10:22:42Z
has_accepted_license: '1'
intvolume: ' 121'
issue: '11'
language:
- iso: eng
month: '03'
oa: 1
oa_version: Published Version
pmid: 1
publication: Proceedings of the National Academy of Sciences of the United States
of America
publication_identifier:
eissn:
- 1091-6490
issn:
- 0027-8424
publication_status: published
publisher: Proceedings of the National Academy of Sciences
quality_controlled: '1'
related_material:
record:
- id: '15126'
relation: research_data
status: public
scopus_import: '1'
status: public
title: Elucidating the role of water in collagen self-assembly by isotopically modulating
collagen hydration
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 121
year: '2024'
...
---
_id: '12708'
abstract:
- lang: eng
text: Self-organisation is the spontaneous emergence of spatio-temporal structures
and patterns from the interaction of smaller individual units. Examples are found
across many scales in very different systems and scientific disciplines, from
physics, materials science and robotics to biology, geophysics and astronomy.
Recent research has highlighted how self-organisation can be both mediated and
controlled by confinement. Confinement is an action over a system that limits
its units’ translational and rotational degrees of freedom, thus also influencing
the system's phase space probability density; it can function as either a catalyst
or inhibitor of self-organisation. Confinement can then become a means to actively
steer the emergence or suppression of collective phenomena in space and time.
Here, to provide a common framework and perspective for future research, we examine
the role of confinement in the self-organisation of soft-matter systems and identify
overarching scientific challenges that need to be addressed to harness its full
scientific and technological potential in soft matter and related fields. By drawing
analogies with other disciplines, this framework will accelerate a common deeper
understanding of self-organisation and trigger the development of innovative strategies
to steer it using confinement, with impact on, e.g., the design of smarter materials,
tissue engineering for biomedicine and in guiding active matter.
acknowledgement: 'All authors are grateful to the Lorentz Center for providing a venue
for stimulating scientific discussions and to sponsor a workshop on the topic of
“Self-organisation under confinement” along with the 4TU Federation, the J. M. Burgers
Center for Fluid Dynamics and the MESA+ Institute for Nanotechnology at the University
of Twente. The authors are also grateful to Paolo Malgaretti, Federico Toschi, Twan
Wilting and Jaap den Toonder for valuable feedback. N. A. acknowledges financial
support from the Portuguese Foundation for Science and Technology (FCT) under Contracts
no. PTDC/FIS-MAC/28146/2017 (LISBOA-01-0145-FEDER-028146), UIDB/00618/2020, and
UIDP/00618/2020. L. M. C. J. acknowledges financial support from the Netherlands
Organisation for Scientific Research (NWO) through a START-UP, Physics Projectruimte,
and Vidi grant. I. C. was supported in part by a grant from by the Army Research
Office (ARO W911NF-18-1-0032) and the Cornell Center for Materials Research (DMR-1719875).
O. D. acknowledges funding by the Agence Nationale pour la Recherche under Grant
No ANR-18-CE33-0006 MSR. M. D. acknowledges financial support from the European
Research Council (Grant No. ERC-2019-ADV-H2020 884902 SoftML). W. M. D. acknowledges
funding from a BBSRC New Investigator Grant (BB/R018383/1). S. G. was supported
by DARPA Young Faculty Award # D19AP00046, and NSF IIS grant # 1955210. H. G. acknowledges
financial support from the Netherlands Organisation for Scientific Research (NWO)
through Veni Grant No. 680-47-451. R. G. acknowledges support from the Max Planck
School Matter to Life and the MaxSynBio Consortium, which are jointly funded by
the Federal Ministry of Education and Research (BMBF) of Germany, and the Max Planck
Society. L. I. acknowledges funding from the Horizon Europe ERC Consolidator Grant
ACTIVE_ ADAPTIVE (Grant No. 101001514). G. H. K. gratefully acknowledges the NWO
Talent Programme which is financed by the Dutch Research Council (project number
VI.C.182.004). H. L. and N. V. acknowledge funding from the Deutsche Forschungsgemeinschaft
(DFG) under grant numbers VO 1824/8-1 and LO 418/22-1. R. M. acknowledges funding
from the Deutsche Forschungsgemeinschaft (DFG) under grant number ME 1535/13-1 and
ME 1535/16-1. M. P. acknowledges funding from the Ramón y Cajal Program, grant no.
RYC-2018-02534, and the Leverhulme Trust, grant no. RPG-2018-345. A. Š. acknowledges
financial support from the European Research Council (Grant No. ERC-2018-STG-H2020
802960 NEPA). A. S. acknowledges funding from an ATTRACT Investigator Grant (No.
A17/MS/11572821/MBRACE) from the Luxembourg National Research Fund. C. S. acknowledges
funding from the French Agence Nationale pour la Recherche (ANR), grant ANR-14-CE090006
and ANR-12-BSV5001401, by the Fondation pour la Recherche Médicale (FRM), grant
DEQ20120323737, and from the PIC3I of Institut Curie, France. I. T. acknowledges
funding from grant IED2019-00058I/AEI/10.13039/501100011033. M. P. and I. T. also
acknowledge funding from grant PID2019-104232B-I00/AEI/10.13039/501100011033 and
from the H2020 MSCA ITN PHYMOT (Grant agreement No 95591). I. Z. acknowledges funding
from Project PID2020-114839GB-I00 MINECO/AEI/FEDER, UE. A. M. acknowledges funding
from the European Research Council, Starting Grant No. 678573 NanoPacks. G. V. acknowledges
sponsorship for this work by the US Office of Naval Research Global (Award No. N62909-18-1-2170).'
article_processing_charge: No
article_type: original
author:
- first_name: Nuno A.M.
full_name: Araújo, Nuno A.M.
last_name: Araújo
- first_name: Liesbeth M.C.
full_name: Janssen, Liesbeth M.C.
last_name: Janssen
- first_name: Thomas
full_name: Barois, Thomas
last_name: Barois
- first_name: Guido
full_name: Boffetta, Guido
last_name: Boffetta
- first_name: Itai
full_name: Cohen, Itai
last_name: Cohen
- first_name: Alessandro
full_name: Corbetta, Alessandro
last_name: Corbetta
- first_name: Olivier
full_name: Dauchot, Olivier
last_name: Dauchot
- first_name: Marjolein
full_name: Dijkstra, Marjolein
last_name: Dijkstra
- first_name: William M.
full_name: Durham, William M.
last_name: Durham
- first_name: Audrey
full_name: Dussutour, Audrey
last_name: Dussutour
- first_name: Simon
full_name: Garnier, Simon
last_name: Garnier
- first_name: Hanneke
full_name: Gelderblom, Hanneke
last_name: Gelderblom
- first_name: Ramin
full_name: Golestanian, Ramin
last_name: Golestanian
- first_name: Lucio
full_name: Isa, Lucio
last_name: Isa
- first_name: Gijsje H.
full_name: Koenderink, Gijsje H.
last_name: Koenderink
- first_name: Hartmut
full_name: Löwen, Hartmut
last_name: Löwen
- first_name: Ralf
full_name: Metzler, Ralf
last_name: Metzler
- first_name: Marco
full_name: Polin, Marco
last_name: Polin
- first_name: C. Patrick
full_name: Royall, C. Patrick
last_name: Royall
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Anupam
full_name: Sengupta, Anupam
last_name: Sengupta
- first_name: Cécile
full_name: Sykes, Cécile
last_name: Sykes
- first_name: Vito
full_name: Trianni, Vito
last_name: Trianni
- first_name: Idan
full_name: Tuval, Idan
last_name: Tuval
- first_name: Nicolas
full_name: Vogel, Nicolas
last_name: Vogel
- first_name: Julia M.
full_name: Yeomans, Julia M.
last_name: Yeomans
- first_name: Iker
full_name: Zuriguel, Iker
last_name: Zuriguel
- first_name: Alvaro
full_name: Marin, Alvaro
last_name: Marin
- first_name: Giorgio
full_name: Volpe, Giorgio
last_name: Volpe
citation:
ama: Araújo NAM, Janssen LMC, Barois T, et al. Steering self-organisation through
confinement. Soft Matter. 2023;19:1695-1704. doi:10.1039/d2sm01562e
apa: Araújo, N. A. M., Janssen, L. M. C., Barois, T., Boffetta, G., Cohen, I., Corbetta,
A., … Volpe, G. (2023). Steering self-organisation through confinement. Soft
Matter. Royal Society of Chemistry. https://doi.org/10.1039/d2sm01562e
chicago: Araújo, Nuno A.M., Liesbeth M.C. Janssen, Thomas Barois, Guido Boffetta,
Itai Cohen, Alessandro Corbetta, Olivier Dauchot, et al. “Steering Self-Organisation
through Confinement.” Soft Matter. Royal Society of Chemistry, 2023. https://doi.org/10.1039/d2sm01562e.
ieee: N. A. M. Araújo et al., “Steering self-organisation through confinement,”
Soft Matter, vol. 19. Royal Society of Chemistry, pp. 1695–1704, 2023.
ista: Araújo NAM, Janssen LMC, Barois T, Boffetta G, Cohen I, Corbetta A, Dauchot
O, Dijkstra M, Durham WM, Dussutour A, Garnier S, Gelderblom H, Golestanian R,
Isa L, Koenderink GH, Löwen H, Metzler R, Polin M, Royall CP, Šarić A, Sengupta
A, Sykes C, Trianni V, Tuval I, Vogel N, Yeomans JM, Zuriguel I, Marin A, Volpe
G. 2023. Steering self-organisation through confinement. Soft Matter. 19, 1695–1704.
mla: Araújo, Nuno A. M., et al. “Steering Self-Organisation through Confinement.”
Soft Matter, vol. 19, Royal Society of Chemistry, 2023, pp. 1695–704, doi:10.1039/d2sm01562e.
short: N.A.M. Araújo, L.M.C. Janssen, T. Barois, G. Boffetta, I. Cohen, A. Corbetta,
O. Dauchot, M. Dijkstra, W.M. Durham, A. Dussutour, S. Garnier, H. Gelderblom,
R. Golestanian, L. Isa, G.H. Koenderink, H. Löwen, R. Metzler, M. Polin, C.P.
Royall, A. Šarić, A. Sengupta, C. Sykes, V. Trianni, I. Tuval, N. Vogel, J.M.
Yeomans, I. Zuriguel, A. Marin, G. Volpe, Soft Matter 19 (2023) 1695–1704.
date_created: 2023-03-05T23:01:06Z
date_published: 2023-02-06T00:00:00Z
date_updated: 2023-08-01T13:28:39Z
day: '06'
ddc:
- '540'
department:
- _id: AnSa
doi: 10.1039/d2sm01562e
ec_funded: 1
external_id:
arxiv:
- '2204.10059'
isi:
- '000940388100001'
file:
- access_level: open_access
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content_type: application/pdf
creator: cchlebak
date_created: 2023-03-07T09:19:41Z
date_updated: 2023-03-07T09:19:41Z
file_id: '12711'
file_name: 2023_SoftMatter_Araujo.pdf
file_size: 3581939
relation: main_file
success: 1
file_date_updated: 2023-03-07T09:19:41Z
has_accepted_license: '1'
intvolume: ' 19'
isi: 1
language:
- iso: eng
month: '02'
oa: 1
oa_version: Published Version
page: 1695-1704
project:
- _id: eba2549b-77a9-11ec-83b8-a81e493eae4e
call_identifier: H2020
grant_number: '802960'
name: 'Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines'
publication: Soft Matter
publication_identifier:
eissn:
- 1744-6848
issn:
- 1744-683X
publication_status: published
publisher: Royal Society of Chemistry
quality_controlled: '1'
scopus_import: '1'
status: public
title: Steering self-organisation through confinement
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 19
year: '2023'
...
---
_id: '12756'
abstract:
- lang: eng
text: ESCRT-III family proteins form composite polymers that deform and cut membrane
tubes in the context of a wide range of cell biological processes across the tree
of life. In reconstituted systems, sequential changes in the composition of ESCRT-III
polymers induced by the AAA–adenosine triphosphatase Vps4 have been shown to remodel
membranes. However, it is not known how composite ESCRT-III polymers are organized
and remodeled in space and time in a cellular context. Taking advantage of the
relative simplicity of the ESCRT-III–dependent division system in Sulfolobus acidocaldarius,
one of the closest experimentally tractable prokaryotic relatives of eukaryotes,
we use super-resolution microscopy, electron microscopy, and computational modeling
to show how CdvB/CdvB1/CdvB2 proteins form a precisely patterned composite ESCRT-III
division ring, which undergoes stepwise Vps4-dependent disassembly and contracts
to cut cells into two. These observations lead us to suggest sequential changes
in a patterned composite polymer as a general mechanism of ESCRT-III–dependent
membrane remodeling.
acknowledgement: "We thank Y. Liu and V. Hale for help with electron cryotomography;
the Medical Research Council (MRC) LMB Electron Microscopy Facility for access,
training, and support; and T. Darling and J. Grimmett at the MRC LMB for help with
computing infrastructure. We also thank the Flow Cytometry Facility and the MRC
LMB for training and support.\r\n F.H. and G.T.-R. were supported by a grant from
the Wellcome Trust (203276/Z/16/Z). A.C. was supported by an EMBO long-term fellowship:
ALTF_1041-2021. J.T. was supported by a grant from the VW Foundation (94933). A.A.P.
was supported by the Wellcome Trust (203276/Z/16/Z) and the HFSP (LT001027/2019).
B.B. received support from the MRC LMB, the Wellcome Trust (203276/Z/16/Z), the
VW Foundation (94933), the Life Sciences–Moore-Simons Foundation (735929LPI), and
a Gordon and Betty Moore Foundation’s Symbiosis in Aquatic Systems Initiative (9346).
A.Š. and X.J. acknowledge funding from the European Research Council (ERC) under
the European Union’s Horizon 2020 research and innovation programme (grant no. 802960).
L.H.-K. acknowledges support from Biotechnology and Biological Sciences Research
Council LIDo Programme. T.N. and J.L. were supported by the MRC (U105184326) and
the Wellcome Trust (203276/Z/16/Z)."
article_number: eade5224
article_processing_charge: No
article_type: original
author:
- first_name: Fredrik
full_name: Hurtig, Fredrik
last_name: Hurtig
- first_name: Thomas C.Q.
full_name: Burgers, Thomas C.Q.
last_name: Burgers
- first_name: Alice
full_name: Cezanne, Alice
last_name: Cezanne
- first_name: Xiuyun
full_name: Jiang, Xiuyun
last_name: Jiang
- first_name: Frank N.
full_name: Mol, Frank N.
last_name: Mol
- first_name: Jovan
full_name: Traparić, Jovan
last_name: Traparić
- first_name: Andre Arashiro
full_name: Pulschen, Andre Arashiro
last_name: Pulschen
- first_name: Tim
full_name: Nierhaus, Tim
last_name: Nierhaus
- first_name: Gabriel
full_name: Tarrason-Risa, Gabriel
last_name: Tarrason-Risa
- first_name: Lena
full_name: Harker-Kirschneck, Lena
last_name: Harker-Kirschneck
- first_name: Jan
full_name: Löwe, Jan
last_name: Löwe
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Rifka
full_name: Vlijm, Rifka
last_name: Vlijm
- first_name: Buzz
full_name: Baum, Buzz
last_name: Baum
citation:
ama: Hurtig F, Burgers TCQ, Cezanne A, et al. The patterned assembly and stepwise
Vps4-mediated disassembly of composite ESCRT-III polymers drives archaeal cell
division. Science Advances. 2023;9(11). doi:10.1126/sciadv.ade5224
apa: Hurtig, F., Burgers, T. C. Q., Cezanne, A., Jiang, X., Mol, F. N., Traparić,
J., … Baum, B. (2023). The patterned assembly and stepwise Vps4-mediated disassembly
of composite ESCRT-III polymers drives archaeal cell division. Science Advances.
American Association for the Advancement of Science. https://doi.org/10.1126/sciadv.ade5224
chicago: Hurtig, Fredrik, Thomas C.Q. Burgers, Alice Cezanne, Xiuyun Jiang, Frank
N. Mol, Jovan Traparić, Andre Arashiro Pulschen, et al. “The Patterned Assembly
and Stepwise Vps4-Mediated Disassembly of Composite ESCRT-III Polymers Drives
Archaeal Cell Division.” Science Advances. American Association for the
Advancement of Science, 2023. https://doi.org/10.1126/sciadv.ade5224.
ieee: F. Hurtig et al., “The patterned assembly and stepwise Vps4-mediated
disassembly of composite ESCRT-III polymers drives archaeal cell division,” Science
Advances, vol. 9, no. 11. American Association for the Advancement of Science,
2023.
ista: Hurtig F, Burgers TCQ, Cezanne A, Jiang X, Mol FN, Traparić J, Pulschen AA,
Nierhaus T, Tarrason-Risa G, Harker-Kirschneck L, Löwe J, Šarić A, Vlijm R, Baum
B. 2023. The patterned assembly and stepwise Vps4-mediated disassembly of composite
ESCRT-III polymers drives archaeal cell division. Science Advances. 9(11), eade5224.
mla: Hurtig, Fredrik, et al. “The Patterned Assembly and Stepwise Vps4-Mediated
Disassembly of Composite ESCRT-III Polymers Drives Archaeal Cell Division.” Science
Advances, vol. 9, no. 11, eade5224, American Association for the Advancement
of Science, 2023, doi:10.1126/sciadv.ade5224.
short: F. Hurtig, T.C.Q. Burgers, A. Cezanne, X. Jiang, F.N. Mol, J. Traparić, A.A.
Pulschen, T. Nierhaus, G. Tarrason-Risa, L. Harker-Kirschneck, J. Löwe, A. Šarić,
R. Vlijm, B. Baum, Science Advances 9 (2023).
date_created: 2023-03-26T22:01:06Z
date_published: 2023-03-17T00:00:00Z
date_updated: 2023-08-01T13:45:54Z
day: '17'
ddc:
- '570'
department:
- _id: AnSa
doi: 10.1126/sciadv.ade5224
ec_funded: 1
external_id:
isi:
- '000968083500010'
file:
- access_level: open_access
checksum: 6d7dbe9ed86a116c8a002d62971202c5
content_type: application/pdf
creator: dernst
date_created: 2023-03-27T06:24:49Z
date_updated: 2023-03-27T06:24:49Z
file_id: '12768'
file_name: 2023_ScienceAdvances_Hurtig.pdf
file_size: 1826471
relation: main_file
success: 1
file_date_updated: 2023-03-27T06:24:49Z
has_accepted_license: '1'
intvolume: ' 9'
isi: 1
issue: '11'
language:
- iso: eng
month: '03'
oa: 1
oa_version: Published Version
project:
- _id: eba2549b-77a9-11ec-83b8-a81e493eae4e
call_identifier: H2020
grant_number: '802960'
name: 'Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines'
publication: Science Advances
publication_identifier:
eissn:
- 2375-2548
publication_status: published
publisher: American Association for the Advancement of Science
quality_controlled: '1'
scopus_import: '1'
status: public
title: The patterned assembly and stepwise Vps4-mediated disassembly of composite
ESCRT-III polymers drives archaeal cell division
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 9
year: '2023'
...
---
_id: '13094'
abstract:
- lang: eng
text: 'Endocytosis is a key cellular process involved in the uptake of nutrients,
pathogens, or the therapy of diseases. Most studies have focused on spherical
objects, whereas biologically relevant shapes can be highly anisotropic. In this
letter, we use an experimental model system based on Giant Unilamellar Vesicles
(GUVs) and dumbbell-shaped colloidal particles to mimic and investigate the first
stage of the passive endocytic process: engulfment of an anisotropic object by
the membrane. Our model has specific ligand–receptor interactions realized by
mobile receptors on the vesicles and immobile ligands on the particles. Through
a series of experiments, theory, and molecular dynamics simulations, we quantify
the wrapping process of anisotropic dumbbells by GUVs and identify distinct stages
of the wrapping pathway. We find that the strong curvature variation in the neck
of the dumbbell as well as membrane tension are crucial in determining both the
speed of wrapping and the final states.'
acknowledgement: We sincerely thank Casper van der Wel for providing open-source packages
for tracking, as well as Yogesh Shelke for his assistance with PAA coverslip preparation
and Rachel Doherty for her assistance with particle functionalization. We are grateful
to Felix Frey for useful discussions on the theory of membrane wrapping. B.M. and
A.Š. acknowledge funding by the European Union’s Horizon 2020 research and innovation
programme (ERC Starting Grant No. 802960).
article_processing_charge: No
article_type: letter_note
author:
- first_name: Ali
full_name: Azadbakht, Ali
last_name: Azadbakht
- first_name: Billie
full_name: Meadowcroft, Billie
id: a4725fd6-932b-11ed-81e2-c098c7f37ae1
last_name: Meadowcroft
- first_name: Thijs
full_name: Varkevisser, Thijs
last_name: Varkevisser
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Daniela J.
full_name: Kraft, Daniela J.
last_name: Kraft
citation:
ama: Azadbakht A, Meadowcroft B, Varkevisser T, Šarić A, Kraft DJ. Wrapping pathways
of anisotropic dumbbell particles by Giant Unilamellar Vesicles. Nano Letters.
2023;23(10):4267–4273. doi:10.1021/acs.nanolett.3c00375
apa: Azadbakht, A., Meadowcroft, B., Varkevisser, T., Šarić, A., & Kraft, D.
J. (2023). Wrapping pathways of anisotropic dumbbell particles by Giant Unilamellar
Vesicles. Nano Letters. American Chemical Society. https://doi.org/10.1021/acs.nanolett.3c00375
chicago: Azadbakht, Ali, Billie Meadowcroft, Thijs Varkevisser, Anđela Šarić, and
Daniela J. Kraft. “Wrapping Pathways of Anisotropic Dumbbell Particles by Giant
Unilamellar Vesicles.” Nano Letters. American Chemical Society, 2023. https://doi.org/10.1021/acs.nanolett.3c00375.
ieee: A. Azadbakht, B. Meadowcroft, T. Varkevisser, A. Šarić, and D. J. Kraft, “Wrapping
pathways of anisotropic dumbbell particles by Giant Unilamellar Vesicles,” Nano
Letters, vol. 23, no. 10. American Chemical Society, pp. 4267–4273, 2023.
ista: Azadbakht A, Meadowcroft B, Varkevisser T, Šarić A, Kraft DJ. 2023. Wrapping
pathways of anisotropic dumbbell particles by Giant Unilamellar Vesicles. Nano
Letters. 23(10), 4267–4273.
mla: Azadbakht, Ali, et al. “Wrapping Pathways of Anisotropic Dumbbell Particles
by Giant Unilamellar Vesicles.” Nano Letters, vol. 23, no. 10, American
Chemical Society, 2023, pp. 4267–4273, doi:10.1021/acs.nanolett.3c00375.
short: A. Azadbakht, B. Meadowcroft, T. Varkevisser, A. Šarić, D.J. Kraft, Nano
Letters 23 (2023) 4267–4273.
date_created: 2023-05-28T22:01:03Z
date_published: 2023-05-04T00:00:00Z
date_updated: 2023-08-01T14:51:25Z
day: '04'
ddc:
- '540'
department:
- _id: AnSa
doi: 10.1021/acs.nanolett.3c00375
ec_funded: 1
external_id:
isi:
- '000985481400001'
pmid:
- '37141427'
file:
- access_level: open_access
checksum: 9734d4c617bab3578ef62916b764547a
content_type: application/pdf
creator: dernst
date_created: 2023-05-30T07:55:31Z
date_updated: 2023-05-30T07:55:31Z
file_id: '13100'
file_name: 2023_NanoLetters_Azadbakht.pdf
file_size: 3654910
relation: main_file
success: 1
file_date_updated: 2023-05-30T07:55:31Z
has_accepted_license: '1'
intvolume: ' 23'
isi: 1
issue: '10'
language:
- iso: eng
month: '05'
oa: 1
oa_version: Published Version
page: 4267–4273
pmid: 1
project:
- _id: eba2549b-77a9-11ec-83b8-a81e493eae4e
call_identifier: H2020
grant_number: '802960'
name: 'Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines'
publication: Nano Letters
publication_identifier:
eissn:
- 1530-6992
issn:
- 1530-6984
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Wrapping pathways of anisotropic dumbbell particles by Giant Unilamellar Vesicles
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 23
year: '2023'
...
---
_id: '13237'
abstract:
- lang: eng
text: The formation of amyloid fibrils is a general class of protein self-assembly
behaviour, which is associated with both functional biology and the development
of a number of disorders, such as Alzheimer and Parkinson diseases. In this Review,
we discuss how general physical concepts from the study of phase transitions can
be used to illuminate the fundamental mechanisms of amyloid self-assembly. We
summarize progress in the efforts to describe the essential biophysical features
of amyloid self-assembly as a nucleation-and-growth process and discuss how master
equation approaches can reveal the key molecular pathways underlying this process,
including the role of secondary nucleation. Additionally, we outline how non-classical
aspects of aggregate formation involving oligomers or biomolecular condensates
have emerged, inspiring developments in understanding, modelling and modulating
complex protein assembly pathways. Finally, we consider how these concepts can
be applied to kinetics-based drug discovery and therapeutic design to develop
treatments for protein aggregation diseases.
acknowledgement: The authors acknowledge support from the Institute for the Physics
of Living Systems, University College London (T.C.T.M.), the Swedish Research Council
(2015-00143) (S.L.), the European Research Council under the European Union’s Seventh
Framework Programme (FP7/2007-2013) through the ERC grant PhysProt (agreement no.
337969) (T.P.J.K.), the BBSRC (T.P.J.K.), the Newman Foundation (T.P.J.K.) and the
Wellcome Trust Collaborative Award 203249/Z/16/Z (T.P.J.K.). The authors thank C.
Flandoli for help with illustrations.
article_processing_charge: No
article_type: original
author:
- first_name: Thomas C.T.
full_name: Michaels, Thomas C.T.
last_name: Michaels
- first_name: Daoyuan
full_name: Qian, Daoyuan
last_name: Qian
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Michele
full_name: Vendruscolo, Michele
last_name: Vendruscolo
- first_name: Sara
full_name: Linse, Sara
last_name: Linse
- first_name: Tuomas P.J.
full_name: Knowles, Tuomas P.J.
last_name: Knowles
citation:
ama: Michaels TCT, Qian D, Šarić A, Vendruscolo M, Linse S, Knowles TPJ. Amyloid
formation as a protein phase transition. Nature Reviews Physics. 2023;5:379–397.
doi:10.1038/s42254-023-00598-9
apa: Michaels, T. C. T., Qian, D., Šarić, A., Vendruscolo, M., Linse, S., &
Knowles, T. P. J. (2023). Amyloid formation as a protein phase transition. Nature
Reviews Physics. Springer Nature. https://doi.org/10.1038/s42254-023-00598-9
chicago: Michaels, Thomas C.T., Daoyuan Qian, Anđela Šarić, Michele Vendruscolo,
Sara Linse, and Tuomas P.J. Knowles. “Amyloid Formation as a Protein Phase Transition.”
Nature Reviews Physics. Springer Nature, 2023. https://doi.org/10.1038/s42254-023-00598-9.
ieee: T. C. T. Michaels, D. Qian, A. Šarić, M. Vendruscolo, S. Linse, and T. P.
J. Knowles, “Amyloid formation as a protein phase transition,” Nature Reviews
Physics, vol. 5. Springer Nature, pp. 379–397, 2023.
ista: Michaels TCT, Qian D, Šarić A, Vendruscolo M, Linse S, Knowles TPJ. 2023.
Amyloid formation as a protein phase transition. Nature Reviews Physics. 5, 379–397.
mla: Michaels, Thomas C. T., et al. “Amyloid Formation as a Protein Phase Transition.”
Nature Reviews Physics, vol. 5, Springer Nature, 2023, pp. 379–397, doi:10.1038/s42254-023-00598-9.
short: T.C.T. Michaels, D. Qian, A. Šarić, M. Vendruscolo, S. Linse, T.P.J. Knowles,
Nature Reviews Physics 5 (2023) 379–397.
date_created: 2023-07-16T22:01:12Z
date_published: 2023-07-01T00:00:00Z
date_updated: 2023-08-02T06:28:38Z
day: '01'
department:
- _id: AnSa
doi: 10.1038/s42254-023-00598-9
external_id:
isi:
- '001017539800001'
intvolume: ' 5'
isi: 1
language:
- iso: eng
month: '07'
oa_version: None
page: 379–397
publication: Nature Reviews Physics
publication_identifier:
eissn:
- 2522-5820
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Amyloid formation as a protein phase transition
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 5
year: '2023'
...
---
_id: '14610'
abstract:
- lang: eng
text: AbstractEndomembrane damage represents a
form of stress that is detrimental for eukaryotic cells1,2.
To cope with this threat, cells possess mechanisms that repair the damage and
restore cellular homeostasis3–7. Endomembrane damage also
results in organelle instability and the mechanisms by which cells stabilize damaged
endomembranes to enable membrane repair remains unknown. Here, by combining in
vitro and in cellulo studies with computational modelling we uncover a biological
function for stress granules whereby these biomolecular condensates form rapidly
at endomembrane damage sites and act as a plug that stabilizes the ruptured membrane.
Functionally, we demonstrate that stress granule formation and membrane stabilization
enable efficient repair of damaged endolysosomes, through both ESCRT (endosomal
sorting complex required for transport)-dependent and independent mechanisms.
We also show that blocking stress granule formation in human macrophages creates
a permissive environment for Mycobacterium tuberculosis,
a human pathogen that exploits endomembrane damage to survive within the host.
acknowledgement: "We thank the Human Embryonic Stem Cell Unit, Advanced Light Microscopy
and High-throughput Screening facilities at the Crick for their support in various
aspects of the work. We thank the laboratory of P. Anderson for providing the G3BP-DKO
U2OS cells. The authors thank N. Chen for providing the purified glycinin protein;
Z. Zhao for providing the microfluidic chip wafers; and M. Amaral and F. Frey for
helpful discussions and valuable input regarding analysis methods. This work was
supported by the Francis Crick Institute (to M.G.G.), which receives its core funding
from Cancer Research UK (FC001092), the UK Medical Research Council (FC001092) and
the Wellcome Trust (FC001092). This project has received funding from the European
Research Council (ERC) under the European Union’s Horizon 2020 research and innovation
programme (grant agreement no. 772022 to M.G.G.). C.B. has received funding from
the European Respiratory Society and the European Union’s H2020 research and innovation
programme under the Marie Sklodowska-Curie grant agreement no. 713406. A.M. acknowledges
support from Alexander von Humboldt Foundation and C.V.-C. acknowledges funding
by the Royal Society and the European Research Council under the European Union’s
Horizon 2020 Research and Innovation Programme (grant no. 802960 to A.S.). All simulations
were carried out on the high-performance computing cluster at the Institute of Science
and Technology Austria. For the purpose of Open Access, the author has applied a
CC BY public copyright licence to any Author Accepted Manuscript version arising
from this submission.\r\nOpen Access funding provided by The Francis Crick Institute."
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Claudio
full_name: Bussi, Claudio
last_name: Bussi
- first_name: Agustín
full_name: Mangiarotti, Agustín
last_name: Mangiarotti
- first_name: Christian Eduardo
full_name: Vanhille-Campos, Christian Eduardo
id: 3adeca52-9313-11ed-b1ac-c170b2505714
last_name: Vanhille-Campos
- first_name: Beren
full_name: Aylan, Beren
last_name: Aylan
- first_name: Enrica
full_name: Pellegrino, Enrica
last_name: Pellegrino
- first_name: Natalia
full_name: Athanasiadi, Natalia
last_name: Athanasiadi
- first_name: Antony
full_name: Fearns, Antony
last_name: Fearns
- first_name: Angela
full_name: Rodgers, Angela
last_name: Rodgers
- first_name: Titus M.
full_name: Franzmann, Titus M.
last_name: Franzmann
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Rumiana
full_name: Dimova, Rumiana
last_name: Dimova
- first_name: Maximiliano G.
full_name: Gutierrez, Maximiliano G.
last_name: Gutierrez
citation:
ama: Bussi C, Mangiarotti A, Vanhille-Campos CE, et al. Stress granules plug and
stabilize damaged endolysosomal membranes. Nature. 2023. doi:10.1038/s41586-023-06726-w
apa: Bussi, C., Mangiarotti, A., Vanhille-Campos, C. E., Aylan, B., Pellegrino,
E., Athanasiadi, N., … Gutierrez, M. G. (2023). Stress granules plug and stabilize
damaged endolysosomal membranes. Nature. Springer Nature. https://doi.org/10.1038/s41586-023-06726-w
chicago: Bussi, Claudio, Agustín Mangiarotti, Christian Eduardo Vanhille-Campos,
Beren Aylan, Enrica Pellegrino, Natalia Athanasiadi, Antony Fearns, et al. “Stress
Granules Plug and Stabilize Damaged Endolysosomal Membranes.” Nature. Springer
Nature, 2023. https://doi.org/10.1038/s41586-023-06726-w.
ieee: C. Bussi et al., “Stress granules plug and stabilize damaged endolysosomal
membranes,” Nature. Springer Nature, 2023.
ista: Bussi C, Mangiarotti A, Vanhille-Campos CE, Aylan B, Pellegrino E, Athanasiadi
N, Fearns A, Rodgers A, Franzmann TM, Šarić A, Dimova R, Gutierrez MG. 2023. Stress
granules plug and stabilize damaged endolysosomal membranes. Nature.
mla: Bussi, Claudio, et al. “Stress Granules Plug and Stabilize Damaged Endolysosomal
Membranes.” Nature, Springer Nature, 2023, doi:10.1038/s41586-023-06726-w.
short: C. Bussi, A. Mangiarotti, C.E. Vanhille-Campos, B. Aylan, E. Pellegrino,
N. Athanasiadi, A. Fearns, A. Rodgers, T.M. Franzmann, A. Šarić, R. Dimova, M.G.
Gutierrez, Nature (2023).
date_created: 2023-11-27T07:56:37Z
date_published: 2023-11-15T00:00:00Z
date_updated: 2023-11-27T09:05:08Z
day: '15'
department:
- _id: AnSa
doi: 10.1038/s41586-023-06726-w
external_id:
pmid:
- '37968398'
keyword:
- Multidisciplinary
language:
- iso: eng
main_file_link:
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url: https://doi.org/10.1038/s41586-023-06726-w
month: '11'
oa: 1
oa_version: Published Version
pmid: 1
publication: Nature
publication_identifier:
eissn:
- 1476-4687
issn:
- 0028-0836
publication_status: epub_ahead
publisher: Springer Nature
quality_controlled: '1'
related_material:
link:
- relation: erratum
url: https://doi.org/10.1038/s41586-023-06882-z
record:
- id: '14472'
relation: research_data
status: public
status: public
title: Stress granules plug and stabilize damaged endolysosomal membranes
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2023'
...
---
_id: '14472'
abstract:
- lang: eng
text: "Data related to the following paper:\r\n\"Stress granules plug and stabilize
damaged endolysosomal membranes\" (https://doi.org/10.1038/s41586-023-06726-w)\r\n\r\nAbstract:
\r\nEndomembrane damage represents a form of stress that is detrimental for eukaryotic
cells. To cope with this threat, cells possess mechanisms that repair the damage
and restore cellular homeostasis. Endomembrane damage also results in organelle
instability and the mechanisms by which cells stabilize damaged endomembranes
to enable membrane repair remains unknown. In this work we use a minimal coarse-grained
molecular dynamics system to explore how lipid vesicles undergoing poration in
a protein-rich medium can be plugged and stabilised by condensate formation. The
solution of proteins in and out of the vesicle is described by beads dispersed
in implicit solvent. The membrane is described as a one-bead-thick fluid elastic
layer of mechanical properties that mimic biological membranes. We tune the interactions
between solution beads in the different compartments to capture the differences
between the cytoplasmic and endosomal protein solutions and explore how the system
responds to different degrees of membrane poration. We find that, in the right
interaction regime, condensates form rapidly at the damage site upon solution
mixing and act as a plug that prevents futher mixing and destabilisation of the
vesicle. Further, when the condensate can interact with the membrane (wetting
interactions) we find that it mediates pore sealing and membrane repair. This
research is part of the work published in \"Stress granules plug and stabilize
damaged endolysosomal membranes\", Bussi et al, Nature, 2023 - 10.1038/s41586-023-06726-w."
article_processing_charge: No
author:
- first_name: Christian Eduardo
full_name: Vanhille-Campos, Christian Eduardo
id: 3adeca52-9313-11ed-b1ac-c170b2505714
last_name: Vanhille-Campos
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
citation:
ama: Vanhille-Campos CE, Šarić A. Stress granules plug and stabilize damaged endolysosomal
membranes. 2023. doi:10.15479/AT:ISTA:14472
apa: Vanhille-Campos, C. E., & Šarić, A. (2023). Stress granules plug and stabilize
damaged endolysosomal membranes. Institute of Science and Technology Austria.
https://doi.org/10.15479/AT:ISTA:14472
chicago: Vanhille-Campos, Christian Eduardo, and Anđela Šarić. “Stress Granules
Plug and Stabilize Damaged Endolysosomal Membranes.” Institute of Science and
Technology Austria, 2023. https://doi.org/10.15479/AT:ISTA:14472.
ieee: C. E. Vanhille-Campos and A. Šarić, “Stress granules plug and stabilize damaged
endolysosomal membranes.” Institute of Science and Technology Austria, 2023.
ista: Vanhille-Campos CE, Šarić A. 2023. Stress granules plug and stabilize damaged
endolysosomal membranes, Institute of Science and Technology Austria, 10.15479/AT:ISTA:14472.
mla: Vanhille-Campos, Christian Eduardo, and Anđela Šarić. Stress Granules Plug
and Stabilize Damaged Endolysosomal Membranes. Institute of Science and Technology
Austria, 2023, doi:10.15479/AT:ISTA:14472.
short: C.E. Vanhille-Campos, A. Šarić, (2023).
date_created: 2023-10-30T16:38:32Z
date_published: 2023-10-31T00:00:00Z
date_updated: 2023-11-27T09:05:07Z
day: '31'
ddc:
- '570'
department:
- _id: AnSa
doi: 10.15479/AT:ISTA:14472
file:
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checksum: a18706e952e8660c51ede52a167270b7
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creator: ipalaia
date_created: 2023-10-30T16:31:08Z
date_updated: 2023-10-30T16:31:08Z
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file_size: 62821432
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content_type: text/plain
creator: dernst
date_created: 2023-10-31T08:57:50Z
date_updated: 2023-10-31T08:57:50Z
file_id: '14474'
file_name: README.txt
file_size: 1697
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success: 1
file_date_updated: 2023-10-31T08:57:50Z
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month: '10'
oa: 1
oa_version: Published Version
publisher: Institute of Science and Technology Austria
related_material:
record:
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relation: used_in_publication
status: public
status: public
title: Stress granules plug and stabilize damaged endolysosomal membranes
tmp:
image: /images/cc_0.png
legal_code_url: https://creativecommons.org/publicdomain/zero/1.0/legalcode
name: Creative Commons Public Domain Dedication (CC0 1.0)
short: CC0 (1.0)
type: research_data
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2023'
...
---
_id: '14844'
abstract:
- lang: eng
text: 'Many cell functions require a concerted effort from multiple membrane proteins,
for example, for signaling, cell division, and endocytosis. One contribution to
their successful self-organization stems from the membrane deformations that these
proteins induce. While the pairwise interaction potential of two membrane-deforming
spheres has recently been measured, membrane-deformation-induced interactions
have been predicted to be nonadditive, and hence their collective behavior cannot
be deduced from this measurement. We here employ a colloidal model system consisting
of adhesive spheres and giant unilamellar vesicles to test these predictions by
measuring the interaction potential of the simplest case of three membrane-deforming,
spherical particles. We quantify their interactions and arrangements and, for
the first time, experimentally confirm and quantify the nonadditive nature of
membrane-deformation-induced interactions. We furthermore conclude that there
exist two favorable configurations on the membrane: (1) a linear and (2) a triangular
arrangement of the three spheres. Using Monte Carlo simulations, we corroborate
the experimentally observed energy minima and identify a lowering of the membrane
deformation as the cause for the observed configurations. The high symmetry of
the preferred arrangements for three particles suggests that arrangements of many
membrane-deforming objects might follow simple rules.'
acknowledgement: We gratefully acknowledge useful discussions with Casper van der
Wel, help by Yogesh Shelke with PAA coverslip preparation, and support by Rachel
Doherty with particle functionalization. A.A. and D.J.K. would like to thank Timon
Idema and George Dadunashvili for initial attempts to simulate the experimental
system. D.J.K. would like to thank the physics department at Leiden University for
funding the PhD position of A.A. B.M. and A.Š. acknowledge funding by the European
Union’s Horizon 2020 research and innovation programme (ERC starting grant no. 802960).
article_processing_charge: No
article_type: original
author:
- first_name: Ali
full_name: Azadbakht, Ali
last_name: Azadbakht
- first_name: Billie
full_name: Meadowcroft, Billie
id: a4725fd6-932b-11ed-81e2-c098c7f37ae1
last_name: Meadowcroft
orcid: 0000-0003-3441-1337
- first_name: Juraj
full_name: Majek, Juraj
id: 3e6d9473-f38e-11ec-8ae0-c4e05a8aa9e1
last_name: Majek
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Daniela J.
full_name: Kraft, Daniela J.
last_name: Kraft
citation:
ama: Azadbakht A, Meadowcroft B, Majek J, Šarić A, Kraft DJ. Nonadditivity in interactions
between three membrane-wrapped colloidal spheres. Biophysical Journal.
doi:10.1016/j.bpj.2023.12.020
apa: Azadbakht, A., Meadowcroft, B., Majek, J., Šarić, A., & Kraft, D. J. (n.d.).
Nonadditivity in interactions between three membrane-wrapped colloidal spheres.
Biophysical Journal. Elsevier. https://doi.org/10.1016/j.bpj.2023.12.020
chicago: Azadbakht, Ali, Billie Meadowcroft, Juraj Majek, Anđela Šarić, and Daniela
J. Kraft. “Nonadditivity in Interactions between Three Membrane-Wrapped Colloidal
Spheres.” Biophysical Journal. Elsevier, n.d. https://doi.org/10.1016/j.bpj.2023.12.020.
ieee: A. Azadbakht, B. Meadowcroft, J. Majek, A. Šarić, and D. J. Kraft, “Nonadditivity
in interactions between three membrane-wrapped colloidal spheres,” Biophysical
Journal. Elsevier.
ista: Azadbakht A, Meadowcroft B, Majek J, Šarić A, Kraft DJ. Nonadditivity in interactions
between three membrane-wrapped colloidal spheres. Biophysical Journal.
mla: Azadbakht, Ali, et al. “Nonadditivity in Interactions between Three Membrane-Wrapped
Colloidal Spheres.” Biophysical Journal, Elsevier, doi:10.1016/j.bpj.2023.12.020.
short: A. Azadbakht, B. Meadowcroft, J. Majek, A. Šarić, D.J. Kraft, Biophysical
Journal (n.d.).
date_created: 2024-01-21T23:00:56Z
date_published: 2023-12-29T00:00:00Z
date_updated: 2024-01-23T09:26:35Z
day: '29'
ddc:
- '570'
department:
- _id: AnSa
doi: 10.1016/j.bpj.2023.12.020
ec_funded: 1
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.bpj.2023.12.020
month: '12'
oa: 1
oa_version: Published Version
project:
- _id: eba2549b-77a9-11ec-83b8-a81e493eae4e
call_identifier: H2020
grant_number: '802960'
name: 'Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines'
publication: Biophysical Journal
publication_identifier:
eissn:
- 1542-0086
issn:
- 0006-3495
publication_status: inpress
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Nonadditivity in interactions between three membrane-wrapped colloidal spheres
tmp:
image: /images/cc_by_nc_nd.png
legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode
name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
(CC BY-NC-ND 4.0)
short: CC BY-NC-ND (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2023'
...
---
_id: '13971'
abstract:
- lang: eng
text: When in equilibrium, thermal forces agitate molecules, which then diffuse,
collide and bind to form materials. However, the space of accessible structures
in which micron-scale particles can be organized by thermal forces is limited,
owing to the slow dynamics and metastable states. Active agents in a passive fluid
generate forces and flows, forming a bath with active fluctuations. Two unanswered
questions are whether those active agents can drive the assembly of passive components
into unconventional states and which material properties they will exhibit. Here
we show that passive, sticky beads immersed in a bath of swimming Escherichia
coli bacteria aggregate into unconventional clusters and gels that are controlled
by the activity of the bath. We observe a slow but persistent rotation of the
aggregates that originates in the chirality of the E. coli flagella and directs
aggregation into structures that are not accessible thermally. We elucidate the
aggregation mechanism with a numerical model of spinning, sticky beads and reproduce
quantitatively the experimental results. We show that internal activity controls
the phase diagram and the structure of the aggregates. Overall, our results highlight
the promising role of active baths in designing the structural and mechanical
properties of materials with unconventional phases.
acknowledgement: D.G. and J.P. thank E. Krasnopeeva, C. Guet, G. Guessous and T. Hwa
for providing the E. coli strains. This material is based upon work supported by
the US Department of Energy under award DE-SC0019769. I.P. acknowledges funding
by the European Union’s Horizon 2020 research and innovation programme under Marie
Skłodowska-Curie Grant Agreement No. 101034413. A.Š. acknowledges funding from the
European Research Council under the European Union’s Horizon 2020 research and innovation
programme (Grant No. 802960). M.C.U. acknowledges funding from the European Union’s
Horizon 2020 research and innovation programme under Marie Skłodowska-Curie Grant
Agreement No. 754411.
article_processing_charge: Yes
article_type: original
author:
- first_name: Daniel
full_name: Grober, Daniel
id: abdfc56f-34fb-11ee-bd33-fd766fce5a99
last_name: Grober
- first_name: Ivan
full_name: Palaia, Ivan
id: 9c805cd2-4b75-11ec-a374-db6dd0ed57fa
last_name: Palaia
orcid: ' 0000-0002-8843-9485 '
- first_name: Mehmet C
full_name: Ucar, Mehmet C
id: 50B2A802-6007-11E9-A42B-EB23E6697425
last_name: Ucar
orcid: 0000-0003-0506-4217
- first_name: Edouard B
full_name: Hannezo, Edouard B
id: 3A9DB764-F248-11E8-B48F-1D18A9856A87
last_name: Hannezo
orcid: 0000-0001-6005-1561
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Jérémie A
full_name: Palacci, Jérémie A
id: 8fb92548-2b22-11eb-b7c1-a3f0d08d7c7d
last_name: Palacci
orcid: 0000-0002-7253-9465
citation:
ama: Grober D, Palaia I, Ucar MC, Hannezo EB, Šarić A, Palacci JA. Unconventional
colloidal aggregation in chiral bacterial baths. Nature Physics. 2023;19:1680-1688.
doi:10.1038/s41567-023-02136-x
apa: Grober, D., Palaia, I., Ucar, M. C., Hannezo, E. B., Šarić, A., & Palacci,
J. A. (2023). Unconventional colloidal aggregation in chiral bacterial baths.
Nature Physics. Springer Nature. https://doi.org/10.1038/s41567-023-02136-x
chicago: Grober, Daniel, Ivan Palaia, Mehmet C Ucar, Edouard B Hannezo, Anđela Šarić,
and Jérémie A Palacci. “Unconventional Colloidal Aggregation in Chiral Bacterial
Baths.” Nature Physics. Springer Nature, 2023. https://doi.org/10.1038/s41567-023-02136-x.
ieee: D. Grober, I. Palaia, M. C. Ucar, E. B. Hannezo, A. Šarić, and J. A. Palacci,
“Unconventional colloidal aggregation in chiral bacterial baths,” Nature Physics,
vol. 19. Springer Nature, pp. 1680–1688, 2023.
ista: Grober D, Palaia I, Ucar MC, Hannezo EB, Šarić A, Palacci JA. 2023. Unconventional
colloidal aggregation in chiral bacterial baths. Nature Physics. 19, 1680–1688.
mla: Grober, Daniel, et al. “Unconventional Colloidal Aggregation in Chiral Bacterial
Baths.” Nature Physics, vol. 19, Springer Nature, 2023, pp. 1680–88, doi:10.1038/s41567-023-02136-x.
short: D. Grober, I. Palaia, M.C. Ucar, E.B. Hannezo, A. Šarić, J.A. Palacci, Nature
Physics 19 (2023) 1680–1688.
date_created: 2023-08-06T22:01:11Z
date_published: 2023-11-01T00:00:00Z
date_updated: 2024-01-30T12:26:55Z
day: '01'
ddc:
- '530'
department:
- _id: EdHa
- _id: AnSa
- _id: JePa
doi: 10.1038/s41567-023-02136-x
ec_funded: 1
external_id:
isi:
- '001037346400005'
file:
- access_level: open_access
checksum: 7e282c2ebc0ac82125a04f6b4742d4c1
content_type: application/pdf
creator: dernst
date_created: 2024-01-30T12:26:08Z
date_updated: 2024-01-30T12:26:08Z
file_id: '14906'
file_name: 2023_NaturePhysics_Grober.pdf
file_size: 6365607
relation: main_file
success: 1
file_date_updated: 2024-01-30T12:26:08Z
has_accepted_license: '1'
intvolume: ' 19'
isi: 1
language:
- iso: eng
month: '11'
oa: 1
oa_version: Published Version
page: 1680-1688
project:
- _id: fc2ed2f7-9c52-11eb-aca3-c01059dda49c
call_identifier: H2020
grant_number: '101034413'
name: 'IST-BRIDGE: International postdoctoral program'
- _id: eba2549b-77a9-11ec-83b8-a81e493eae4e
call_identifier: H2020
grant_number: '802960'
name: 'Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines'
- _id: 260C2330-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '754411'
name: ISTplus - Postdoctoral Fellowships
publication: Nature Physics
publication_identifier:
eissn:
- 1745-2481
issn:
- 1745-2473
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Unconventional colloidal aggregation in chiral bacterial baths
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 19
year: '2023'
...
---
_id: '12108'
abstract:
- lang: eng
text: The sequential exchange of filament composition to increase filament curvature
was proposed as a mechanism for how some biological polymers deform and cut membranes.
The relationship between the filament composition and its mechanical effect is
lacking. We develop a kinetic model for the assembly of composite filaments that
includes protein–membrane adhesion, filament mechanics and membrane mechanics.
We identify the physical conditions for such a membrane remodeling and show this
mechanism of sequential polymer assembly lowers the energetic barrier for membrane
deformation.
acknowledgement: "We thank T. C. T. Michaels and J. Palacci for useful discussions.
We thank Claudia Flandoli for the illustrations in Fig. 1(b) and Fig. 2. We acknowledge
funding by the European Union’s Horizon 2020 Research and Innovation Programme under
the Marie Skłodowska-Curie Grant\r\nAgreement No. 101034413 (I. P.), the Royal Society
Grant No. UF160266 (A. Š.), the European Research Council under the European Union’s
Horizon 2020 Research and Innovation Programme (Grant No. 802960; B. M., I. P.,
and A. Š.), and the Volkswagen Foundation\r\nLife Grant (B. B. and A. Š). "
article_number: '268101'
article_processing_charge: No
article_type: original
author:
- first_name: Billie
full_name: Meadowcroft, Billie
id: a4725fd6-932b-11ed-81e2-c098c7f37ae1
last_name: Meadowcroft
- first_name: Ivan
full_name: Palaia, Ivan
id: 9c805cd2-4b75-11ec-a374-db6dd0ed57fa
last_name: Palaia
orcid: ' 0000-0002-8843-9485 '
- first_name: Anna Katharina
full_name: Pfitzner, Anna Katharina
last_name: Pfitzner
- first_name: Aurélien
full_name: Roux, Aurélien
last_name: Roux
- first_name: Buzz
full_name: Baum, Buzz
last_name: Baum
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
citation:
ama: Meadowcroft B, Palaia I, Pfitzner AK, Roux A, Baum B, Šarić A. Mechanochemical
rules for shape-shifting filaments that remodel membranes. Physical Review
Letters. 2022;129(26). doi:10.1103/PhysRevLett.129.268101
apa: Meadowcroft, B., Palaia, I., Pfitzner, A. K., Roux, A., Baum, B., & Šarić,
A. (2022). Mechanochemical rules for shape-shifting filaments that remodel membranes.
Physical Review Letters. American Physical Society. https://doi.org/10.1103/PhysRevLett.129.268101
chicago: Meadowcroft, Billie, Ivan Palaia, Anna Katharina Pfitzner, Aurélien Roux,
Buzz Baum, and Anđela Šarić. “Mechanochemical Rules for Shape-Shifting Filaments
That Remodel Membranes.” Physical Review Letters. American Physical Society,
2022. https://doi.org/10.1103/PhysRevLett.129.268101.
ieee: B. Meadowcroft, I. Palaia, A. K. Pfitzner, A. Roux, B. Baum, and A. Šarić,
“Mechanochemical rules for shape-shifting filaments that remodel membranes,” Physical
Review Letters, vol. 129, no. 26. American Physical Society, 2022.
ista: Meadowcroft B, Palaia I, Pfitzner AK, Roux A, Baum B, Šarić A. 2022. Mechanochemical
rules for shape-shifting filaments that remodel membranes. Physical Review Letters.
129(26), 268101.
mla: Meadowcroft, Billie, et al. “Mechanochemical Rules for Shape-Shifting Filaments
That Remodel Membranes.” Physical Review Letters, vol. 129, no. 26, 268101,
American Physical Society, 2022, doi:10.1103/PhysRevLett.129.268101.
short: B. Meadowcroft, I. Palaia, A.K. Pfitzner, A. Roux, B. Baum, A. Šarić, Physical
Review Letters 129 (2022).
date_created: 2023-01-08T23:00:53Z
date_published: 2022-12-23T00:00:00Z
date_updated: 2023-08-03T14:10:59Z
day: '23'
department:
- _id: AnSa
doi: 10.1103/PhysRevLett.129.268101
ec_funded: 1
external_id:
isi:
- '000906721500001'
pmid:
- '36608212'
intvolume: ' 129'
isi: 1
issue: '26'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: 'https://doi.org/10.1101/2022.05.10.490642 '
month: '12'
oa: 1
oa_version: Preprint
pmid: 1
project:
- _id: fc2ed2f7-9c52-11eb-aca3-c01059dda49c
call_identifier: H2020
grant_number: '101034413'
name: 'IST-BRIDGE: International postdoctoral program'
- _id: eba2549b-77a9-11ec-83b8-a81e493eae4e
call_identifier: H2020
grant_number: '802960'
name: 'Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines'
- _id: eba0f67c-77a9-11ec-83b8-cc8501b3e222
grant_number: '96752'
name: 'The evolution of trafficking: from archaea to eukaryotes'
publication: Physical Review Letters
publication_identifier:
eissn:
- 1079-7114
issn:
- 0031-9007
publication_status: published
publisher: American Physical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Mechanochemical rules for shape-shifting filaments that remodel membranes
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 129
year: '2022'
...
---
_id: '12152'
abstract:
- lang: eng
text: ESCRT-III filaments are composite cytoskeletal polymers that can constrict
and cut cell membranes from the inside of the membrane neck. Membrane-bound ESCRT-III
filaments undergo a series of dramatic composition and geometry changes in the
presence of an ATP-consuming Vps4 enzyme, which causes stepwise changes in the
membrane morphology. We set out to understand the physical mechanisms involved
in translating the changes in ESCRT-III polymer composition into membrane deformation.
We have built a coarse-grained model in which ESCRT-III polymers of different
geometries and mechanical properties are allowed to copolymerise and bind to a
deformable membrane. By modelling ATP-driven stepwise depolymerisation of specific
polymers, we identify mechanical regimes in which changes in filament composition
trigger the associated membrane transition from a flat to a buckled state, and
then to a tubule state that eventually undergoes scission to release a small cargo-loaded
vesicle. We then characterise how the location and kinetics of polymer loss affects
the extent of membrane deformation and the efficiency of membrane neck scission.
Our results identify the near-minimal mechanical conditions for the operation
of shape-shifting composite polymers that sever membrane necks.
acknowledgement: "A.S . received an award from European Research Council (https://erc.europa.eu,
“NEPA\"\r\n802960), and an award from the Royal Society (https://royalsociety.org,
UF160266). L. H.-K.\r\nreceived an award from the Biotechnology and Biological Sciences
Research Council (https://\r\nwww.ukri.org/councils/bbsrc/). E. L. received an award
from the University College London (https://www.ucl.ac.uk/biophysics/news/2022/feb/applications-biop-brian-duff-and-ipls-summerundergraduate-studentships-now-open,
Brian Duff Undergraduate Summer Research Studentship). B.B. and A.S. received an
award from Volkswagen Foundation https://www.volkswagenstiftung.de/en/foundation,
Az 96727), and an award from Medical Research Council (https://www.ukri.org/councils/mrc,
MC_CF1226). A. R. received an\r\naward from the Swiss National Fund for Research
(https://www.snf.ch/en, 31003A_130520,\r\n31003A_149975, and 31003A_173087) and
an award from the European Research Council\r\nConsolidator (https://erc.europa.eu,
311536). The funders had no role in study design, data collection and analysis,
decision to publish, or preparation of the manuscript."
article_number: e1010586
article_processing_charge: No
article_type: original
author:
- first_name: Xiuyun
full_name: Jiang, Xiuyun
last_name: Jiang
- first_name: Lena
full_name: Harker-Kirschneck, Lena
last_name: Harker-Kirschneck
- first_name: Christian Eduardo
full_name: Vanhille-Campos, Christian Eduardo
id: 3adeca52-9313-11ed-b1ac-c170b2505714
last_name: Vanhille-Campos
- first_name: Anna-Katharina
full_name: Pfitzner, Anna-Katharina
last_name: Pfitzner
- first_name: Elene
full_name: Lominadze, Elene
last_name: Lominadze
- first_name: Aurélien
full_name: Roux, Aurélien
last_name: Roux
- first_name: Buzz
full_name: Baum, Buzz
last_name: Baum
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
citation:
ama: Jiang X, Harker-Kirschneck L, Vanhille-Campos CE, et al. Modelling membrane
reshaping by staged polymerization of ESCRT-III filaments. PLOS Computational
Biology. 2022;18(10). doi:10.1371/journal.pcbi.1010586
apa: Jiang, X., Harker-Kirschneck, L., Vanhille-Campos, C. E., Pfitzner, A.-K.,
Lominadze, E., Roux, A., … Šarić, A. (2022). Modelling membrane reshaping by staged
polymerization of ESCRT-III filaments. PLOS Computational Biology. Public
Library of Science. https://doi.org/10.1371/journal.pcbi.1010586
chicago: Jiang, Xiuyun, Lena Harker-Kirschneck, Christian Eduardo Vanhille-Campos,
Anna-Katharina Pfitzner, Elene Lominadze, Aurélien Roux, Buzz Baum, and Anđela
Šarić. “Modelling Membrane Reshaping by Staged Polymerization of ESCRT-III Filaments.”
PLOS Computational Biology. Public Library of Science, 2022. https://doi.org/10.1371/journal.pcbi.1010586.
ieee: X. Jiang et al., “Modelling membrane reshaping by staged polymerization
of ESCRT-III filaments,” PLOS Computational Biology, vol. 18, no. 10. Public
Library of Science, 2022.
ista: Jiang X, Harker-Kirschneck L, Vanhille-Campos CE, Pfitzner A-K, Lominadze
E, Roux A, Baum B, Šarić A. 2022. Modelling membrane reshaping by staged polymerization
of ESCRT-III filaments. PLOS Computational Biology. 18(10), e1010586.
mla: Jiang, Xiuyun, et al. “Modelling Membrane Reshaping by Staged Polymerization
of ESCRT-III Filaments.” PLOS Computational Biology, vol. 18, no. 10, e1010586,
Public Library of Science, 2022, doi:10.1371/journal.pcbi.1010586.
short: X. Jiang, L. Harker-Kirschneck, C.E. Vanhille-Campos, A.-K. Pfitzner, E.
Lominadze, A. Roux, B. Baum, A. Šarić, PLOS Computational Biology 18 (2022).
date_created: 2023-01-12T12:08:10Z
date_published: 2022-10-17T00:00:00Z
date_updated: 2023-08-04T09:03:21Z
day: '17'
ddc:
- '570'
department:
- _id: AnSa
doi: 10.1371/journal.pcbi.1010586
ec_funded: 1
external_id:
isi:
- '000924885500005'
file:
- access_level: open_access
checksum: bada6a7865e470cf42bbdfa67dd471d2
content_type: application/pdf
creator: dernst
date_created: 2023-01-24T10:45:01Z
date_updated: 2023-01-24T10:45:01Z
file_id: '12359'
file_name: 2022_PLoSCompBio_Jiang.pdf
file_size: 2641067
relation: main_file
success: 1
file_date_updated: 2023-01-24T10:45:01Z
has_accepted_license: '1'
intvolume: ' 18'
isi: 1
issue: '10'
keyword:
- Computational Theory and Mathematics
- Cellular and Molecular Neuroscience
- Genetics
- Molecular Biology
- Ecology
- Modeling and Simulation
- Ecology
- Evolution
- Behavior and Systematics
language:
- iso: eng
month: '10'
oa: 1
oa_version: Published Version
project:
- _id: eba2549b-77a9-11ec-83b8-a81e493eae4e
call_identifier: H2020
grant_number: '802960'
name: 'Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines'
- _id: eba0f67c-77a9-11ec-83b8-cc8501b3e222
grant_number: '96752'
name: 'The evolution of trafficking: from archaea to eukaryotes'
publication: PLOS Computational Biology
publication_identifier:
issn:
- 1553-7358
publication_status: published
publisher: Public Library of Science
quality_controlled: '1'
related_material:
link:
- relation: software
url: https://github.com/sharonJXY/3-filament-model
scopus_import: '1'
status: public
title: Modelling membrane reshaping by staged polymerization of ESCRT-III filaments
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 18
year: '2022'
...
---
_id: '12251'
abstract:
- lang: eng
text: Amyloid formation is linked to devastating neurodegenerative diseases, motivating
detailed studies of the mechanisms of amyloid formation. For Aβ, the peptide associated
with Alzheimer’s disease, the mechanism and rate of aggregation have been established
for a range of variants and conditions in vitro and
in bodily fluids. A key outstanding question is how the relative stabilities of
monomers, fibrils and intermediates affect each step in the fibril formation process.
By monitoring the kinetics of aggregation of Aβ42, in the presence of urea or
guanidinium hydrochloride (GuHCl), we here determine the rates of the underlying
microscopic steps and establish the importance of changes in relative stability
induced by the presence of denaturant for each individual step. Denaturants shift
the equilibrium towards the unfolded state of each species. We find that a non-ionic
denaturant, urea, reduces the overall aggregation rate, and that the effect on
nucleation is stronger than the effect on elongation. Urea reduces the rate of
secondary nucleation by decreasing the coverage of fibril surfaces and the rate
of nucleus formation. It also reduces the rate of primary nucleation, increasing
its reaction order. The ionic denaturant, GuHCl, accelerates the aggregation at
low denaturant concentrations and decelerates the aggregation at high denaturant
concentrations. Below approximately 0.25 M GuHCl, the screening of repulsive electrostatic
interactions between peptides by the charged denaturant dominates, leading to
an increased aggregation rate. At higher GuHCl concentrations, the electrostatic
repulsion is completely screened, and the denaturing effect dominates. The results
illustrate how the differential effects of denaturants on stability of monomer,
oligomer and fibril translate to differential effects on microscopic steps, with
the rate of nucleation being most strongly reduced.
acknowledgement: This work was supported by grants from the Swedish Research Council
(grant no. 2015-00143) and the European Research Council (grant no. 340890).
article_number: '943355'
article_processing_charge: No
article_type: original
author:
- first_name: Tanja
full_name: Weiffert, Tanja
last_name: Weiffert
- first_name: Georg
full_name: Meisl, Georg
last_name: Meisl
- first_name: Samo
full_name: Curk, Samo
last_name: Curk
- first_name: Risto
full_name: Cukalevski, Risto
last_name: Cukalevski
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Tuomas P. J.
full_name: Knowles, Tuomas P. J.
last_name: Knowles
- first_name: Sara
full_name: Linse, Sara
last_name: Linse
citation:
ama: Weiffert T, Meisl G, Curk S, et al. Influence of denaturants on amyloid β42
aggregation kinetics. Frontiers in Neuroscience. 2022;16. doi:10.3389/fnins.2022.943355
apa: Weiffert, T., Meisl, G., Curk, S., Cukalevski, R., Šarić, A., Knowles, T. P.
J., & Linse, S. (2022). Influence of denaturants on amyloid β42 aggregation
kinetics. Frontiers in Neuroscience. Frontiers Media. https://doi.org/10.3389/fnins.2022.943355
chicago: Weiffert, Tanja, Georg Meisl, Samo Curk, Risto Cukalevski, Anđela Šarić,
Tuomas P. J. Knowles, and Sara Linse. “Influence of Denaturants on Amyloid Β42
Aggregation Kinetics.” Frontiers in Neuroscience. Frontiers Media, 2022.
https://doi.org/10.3389/fnins.2022.943355.
ieee: T. Weiffert et al., “Influence of denaturants on amyloid β42 aggregation
kinetics,” Frontiers in Neuroscience, vol. 16. Frontiers Media, 2022.
ista: Weiffert T, Meisl G, Curk S, Cukalevski R, Šarić A, Knowles TPJ, Linse S.
2022. Influence of denaturants on amyloid β42 aggregation kinetics. Frontiers
in Neuroscience. 16, 943355.
mla: Weiffert, Tanja, et al. “Influence of Denaturants on Amyloid Β42 Aggregation
Kinetics.” Frontiers in Neuroscience, vol. 16, 943355, Frontiers Media,
2022, doi:10.3389/fnins.2022.943355.
short: T. Weiffert, G. Meisl, S. Curk, R. Cukalevski, A. Šarić, T.P.J. Knowles,
S. Linse, Frontiers in Neuroscience 16 (2022).
date_created: 2023-01-16T09:56:43Z
date_published: 2022-09-20T00:00:00Z
date_updated: 2023-08-04T09:48:56Z
day: '20'
ddc:
- '570'
department:
- _id: AnSa
doi: 10.3389/fnins.2022.943355
external_id:
isi:
- '000866287100001'
file:
- access_level: open_access
checksum: e67d16113ffb4fb4fa38a183d169f210
content_type: application/pdf
creator: dernst
date_created: 2023-01-30T09:15:13Z
date_updated: 2023-01-30T09:15:13Z
file_id: '12442'
file_name: 2022_FrontiersNeuroscience_Weiffert2.pdf
file_size: 19798610
relation: main_file
success: 1
file_date_updated: 2023-01-30T09:15:13Z
has_accepted_license: '1'
intvolume: ' 16'
isi: 1
keyword:
- General Neuroscience
language:
- iso: eng
month: '09'
oa: 1
oa_version: Published Version
publication: Frontiers in Neuroscience
publication_identifier:
issn:
- 1662-453X
publication_status: published
publisher: Frontiers Media
quality_controlled: '1'
scopus_import: '1'
status: public
title: Influence of denaturants on amyloid β42 aggregation kinetics
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 16
year: '2022'
...
---
_id: '11400'
abstract:
- lang: eng
text: By varying the concentration of molecules in the cytoplasm or on the membrane,
cells can induce the formation of condensates and liquid droplets, similar to
phase separation. Their thermodynamics, much studied, depends on the mutual interactions
between microscopic constituents. Here, we focus on the kinetics and size control
of 2D clusters, forming on membranes. Using molecular dynamics of patchy colloids,
we model a system of two species of proteins, giving origin to specific heterotypic
bonds. We find that concentrations, together with valence and bond strength, control
both the size and the growth time rate of the clusters. In particular, if one
species is in large excess, it gradually saturates the binding sites of the other
species; the system then becomes kinetically arrested and cluster coarsening slows
down or stops, thus yielding effective size selection. This phenomenology is observed
both in solid and fluid clusters, which feature additional generic homotypic interactions
and are reminiscent of the ones observed on biological membranes.
acknowledgement: "The authors thank Longhui Zeng and Xiaolei Su (Yale University)
for bringing the topic to their attention and for useful comments. This work has
received funding from the European Research Council under the European Union’s Horizon\r\n2020
research and innovation program (ERC Grant No. 802960 and Marie Skłodowska-Curie
Grant No. 101034413). The authors are grateful to the UK Materials and Molecular
Modeling Hub for computational resources, which is partially funded by EPSRC (Grant
Nos. EP/P020194/1 and EP/T022213/1). The authors acknowledge support from ISTA and
from the Royal Society (Grant No. UF160266)."
article_number: '194902'
article_processing_charge: No
article_type: original
author:
- first_name: Ivan
full_name: Palaia, Ivan
id: 9c805cd2-4b75-11ec-a374-db6dd0ed57fa
last_name: Palaia
orcid: ' 0000-0002-8843-9485 '
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
citation:
ama: Palaia I, Šarić A. Controlling cluster size in 2D phase-separating binary mixtures
with specific interactions. The Journal of Chemical Physics. 2022;156(19).
doi:10.1063/5.0087769
apa: Palaia, I., & Šarić, A. (2022). Controlling cluster size in 2D phase-separating
binary mixtures with specific interactions. The Journal of Chemical Physics.
AIP Publishing. https://doi.org/10.1063/5.0087769
chicago: Palaia, Ivan, and Anđela Šarić. “Controlling Cluster Size in 2D Phase-Separating
Binary Mixtures with Specific Interactions.” The Journal of Chemical Physics.
AIP Publishing, 2022. https://doi.org/10.1063/5.0087769.
ieee: I. Palaia and A. Šarić, “Controlling cluster size in 2D phase-separating binary
mixtures with specific interactions,” The Journal of Chemical Physics,
vol. 156, no. 19. AIP Publishing, 2022.
ista: Palaia I, Šarić A. 2022. Controlling cluster size in 2D phase-separating binary
mixtures with specific interactions. The Journal of Chemical Physics. 156(19),
194902.
mla: Palaia, Ivan, and Anđela Šarić. “Controlling Cluster Size in 2D Phase-Separating
Binary Mixtures with Specific Interactions.” The Journal of Chemical Physics,
vol. 156, no. 19, 194902, AIP Publishing, 2022, doi:10.1063/5.0087769.
short: I. Palaia, A. Šarić, The Journal of Chemical Physics 156 (2022).
date_created: 2022-05-22T17:04:48Z
date_published: 2022-05-16T00:00:00Z
date_updated: 2023-09-05T11:59:00Z
day: '16'
ddc:
- '540'
department:
- _id: AnSa
doi: 10.1063/5.0087769
ec_funded: 1
external_id:
isi:
- '000797236000004'
file:
- access_level: open_access
checksum: 7fada58059676a4bb0944b82247af740
content_type: application/pdf
creator: dernst
date_created: 2022-05-23T07:45:33Z
date_updated: 2022-05-23T07:45:33Z
file_id: '11405'
file_name: 2022_JourChemPhysics_Palaia.pdf
file_size: 6387208
relation: main_file
success: 1
file_date_updated: 2022-05-23T07:45:33Z
has_accepted_license: '1'
intvolume: ' 156'
isi: 1
issue: '19'
keyword:
- Physical and Theoretical Chemistry
- General Physics and Astronomy
language:
- iso: eng
month: '05'
oa: 1
oa_version: Published Version
project:
- _id: eba2549b-77a9-11ec-83b8-a81e493eae4e
call_identifier: H2020
grant_number: '802960'
name: 'Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines'
- _id: fc2ed2f7-9c52-11eb-aca3-c01059dda49c
call_identifier: H2020
grant_number: '101034413'
name: 'IST-BRIDGE: International postdoctoral program'
publication: The Journal of Chemical Physics
publication_identifier:
eissn:
- 1089-7690
issn:
- 0021-9606
publication_status: published
publisher: AIP Publishing
quality_controlled: '1'
status: public
title: Controlling cluster size in 2D phase-separating binary mixtures with specific
interactions
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 156
year: '2022'
...
---
_id: '11841'
abstract:
- lang: eng
text: Primary nucleation is the fundamental event that initiates the conversion
of proteins from their normal physiological forms into pathological amyloid aggregates
associated with the onset and development of disorders including systemic amyloidosis,
as well as the neurodegenerative conditions Alzheimer’s and Parkinson’s diseases.
It has become apparent that the presence of surfaces can dramatically modulate
nucleation. However, the underlying physicochemical parameters governing this
process have been challenging to elucidate, with interfaces in some cases having
been found to accelerate aggregation, while in others they can inhibit the kinetics
of this process. Here we show through kinetic analysis that for three different
fibril-forming proteins, interfaces affect the aggregation reaction mainly through
modulating the primary nucleation step. Moreover, we show through direct measurements
of the Gibbs free energy of adsorption, combined with theory and coarse-grained
computer simulations, that overall nucleation rates are suppressed at high and
at low surface interaction strengths but significantly enhanced at intermediate
strengths, and we verify these regimes experimentally. Taken together, these results
provide a quantitative description of the fundamental process which triggers amyloid
formation and shed light on the key factors that control this process.
acknowledgement: "The research leading to these results has received funding from
the European Research Council (ERC) under the European Union’s Seventh Framework
Programme (FP7/2007-2013) through the ERC grant PhysProt\r\n(agreement 337969).
We are grateful for financial support from the Biotechnology and Biological Sciences
Research Council (BBSRC) (T.P.J.K.), the Newman\r\nFoundation (T.P.J.K.), the Wellcome
Trust (T.P.J.K. and M.V.), Peterhouse College\r\nCambridge (T.C.T.M.), the ERC Starting
Grant (StG) Non-Equilibrium Protein Assembly (NEPA) (A.S.), the Royal Society (A.S.),
the Academy of Medical Sciences\r\n(A.S. and J.K.), and the Cambridge Centre for
Misfolding Diseases (CMD)."
article_number: e2109718119
article_processing_charge: No
article_type: original
author:
- first_name: Zenon
full_name: Toprakcioglu, Zenon
last_name: Toprakcioglu
- first_name: Ayaka
full_name: Kamada, Ayaka
last_name: Kamada
- first_name: Thomas C.T.
full_name: Michaels, Thomas C.T.
last_name: Michaels
- first_name: Mengqi
full_name: Xie, Mengqi
last_name: Xie
- first_name: Johannes
full_name: Krausser, Johannes
last_name: Krausser
- first_name: Jiapeng
full_name: Wei, Jiapeng
last_name: Wei
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Michele
full_name: Vendruscolo, Michele
last_name: Vendruscolo
- first_name: Tuomas P.J.
full_name: Knowles, Tuomas P.J.
last_name: Knowles
citation:
ama: Toprakcioglu Z, Kamada A, Michaels TCT, et al. Adsorption free energy predicts
amyloid protein nucleation rates. Proceedings of the National Academy of Sciences
of the United States of America. 2022;119(31). doi:10.1073/pnas.2109718119
apa: Toprakcioglu, Z., Kamada, A., Michaels, T. C. T., Xie, M., Krausser, J., Wei,
J., … Knowles, T. P. J. (2022). Adsorption free energy predicts amyloid protein
nucleation rates. Proceedings of the National Academy of Sciences of the United
States of America. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.2109718119
chicago: Toprakcioglu, Zenon, Ayaka Kamada, Thomas C.T. Michaels, Mengqi Xie, Johannes
Krausser, Jiapeng Wei, Anđela Šarić, Michele Vendruscolo, and Tuomas P.J. Knowles.
“Adsorption Free Energy Predicts Amyloid Protein Nucleation Rates.” Proceedings
of the National Academy of Sciences of the United States of America. Proceedings
of the National Academy of Sciences, 2022. https://doi.org/10.1073/pnas.2109718119.
ieee: Z. Toprakcioglu et al., “Adsorption free energy predicts amyloid protein
nucleation rates,” Proceedings of the National Academy of Sciences of the United
States of America, vol. 119, no. 31. Proceedings of the National Academy of
Sciences, 2022.
ista: Toprakcioglu Z, Kamada A, Michaels TCT, Xie M, Krausser J, Wei J, Šarić A,
Vendruscolo M, Knowles TPJ. 2022. Adsorption free energy predicts amyloid protein
nucleation rates. Proceedings of the National Academy of Sciences of the United
States of America. 119(31), e2109718119.
mla: Toprakcioglu, Zenon, et al. “Adsorption Free Energy Predicts Amyloid Protein
Nucleation Rates.” Proceedings of the National Academy of Sciences of the United
States of America, vol. 119, no. 31, e2109718119, Proceedings of the National
Academy of Sciences, 2022, doi:10.1073/pnas.2109718119.
short: Z. Toprakcioglu, A. Kamada, T.C.T. Michaels, M. Xie, J. Krausser, J. Wei,
A. Šarić, M. Vendruscolo, T.P.J. Knowles, Proceedings of the National Academy
of Sciences of the United States of America 119 (2022).
date_created: 2022-08-14T22:01:45Z
date_published: 2022-07-28T00:00:00Z
date_updated: 2023-10-04T09:06:52Z
day: '28'
ddc:
- '570'
department:
- _id: AnSa
doi: 10.1073/pnas.2109718119
ec_funded: 1
external_id:
isi:
- '000903753500002'
file:
- access_level: open_access
checksum: 0fe3878896cbeb6c44e29222ec2f336a
content_type: application/pdf
creator: dernst
date_created: 2023-10-04T09:05:44Z
date_updated: 2023-10-04T09:05:44Z
file_id: '14386'
file_name: 2022_PNAS_Toprakcioglu.pdf
file_size: 2476021
relation: main_file
success: 1
file_date_updated: 2023-10-04T09:05:44Z
has_accepted_license: '1'
intvolume: ' 119'
isi: 1
issue: '31'
language:
- iso: eng
month: '07'
oa: 1
oa_version: Published Version
project:
- _id: eba2549b-77a9-11ec-83b8-a81e493eae4e
call_identifier: H2020
grant_number: '802960'
name: 'Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines'
publication: Proceedings of the National Academy of Sciences of the United States
of America
publication_identifier:
eissn:
- 1091-6490
issn:
- 0027-8424
publication_status: published
publisher: Proceedings of the National Academy of Sciences
quality_controlled: '1'
scopus_import: '1'
status: public
title: Adsorption free energy predicts amyloid protein nucleation rates
tmp:
image: /images/cc_by_nc_nd.png
legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode
name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
(CC BY-NC-ND 4.0)
short: CC BY-NC-ND (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 119
year: '2022'
...
---
_id: '10124'
abstract:
- lang: eng
text: The transport of macromolecules and nanoscopic particles to a target cellular
site is a crucial aspect in many physiological processes. This directional motion
is generally controlled via active mechanical and chemical processes. Here we
show, by means of molecular dynamics simulations and an analytical theory, that
completely passive nanoparticles can exhibit directional motion when embedded
in non-uniform mechanical environments. Specifically, we study the motion of a
passive nanoparticle adhering to a mechanically non-uniform elastic membrane.
We observe a non-monotonic affinity of the particle to the membrane as a function
of the membrane’s rigidity, which results in the particle transport. This transport
can be both up or down the rigidity gradient, depending on the absolute values
of the rigidities that the gradient spans across. We conclude that rigidity gradients
can be used to direct average motion of passive macromolecules and nanoparticles
on deformable membranes, resulting in the preferential accumulation of the macromolecules
in regions of certain mechanical properties.
acknowledgement: We acknowledge support from the Engineering and Physical Sciences
Research Council (A.P. and A.Š.), the Royal Society (A.Š.) and the European Research
Council (I.P. and A.Š.).
article_processing_charge: No
article_type: original
author:
- first_name: Ivan
full_name: Palaia, Ivan
last_name: Palaia
- first_name: Alexandru
full_name: Paraschiv, Alexandru
last_name: Paraschiv
- first_name: Vincent
full_name: Debets, Vincent
last_name: Debets
- first_name: Cornelis
full_name: Storm, Cornelis
last_name: Storm
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
citation:
ama: Palaia I, Paraschiv A, Debets V, Storm C, Šarić A. Durotaxis of passive nanoparticles
on elastic membranes. ACS Nano. 2021. doi:10.1021/acsnano.1c02777
apa: Palaia, I., Paraschiv, A., Debets, V., Storm, C., & Šarić, A. (2021). Durotaxis
of passive nanoparticles on elastic membranes. ACS Nano. American Chemical
Society. https://doi.org/10.1021/acsnano.1c02777
chicago: Palaia, Ivan, Alexandru Paraschiv, Vincent Debets, Cornelis Storm, and
Anđela Šarić. “Durotaxis of Passive Nanoparticles on Elastic Membranes.” ACS
Nano. American Chemical Society, 2021. https://doi.org/10.1021/acsnano.1c02777 .
ieee: I. Palaia, A. Paraschiv, V. Debets, C. Storm, and A. Šarić, “Durotaxis of
passive nanoparticles on elastic membranes,” ACS Nano. American Chemical
Society, 2021.
ista: Palaia I, Paraschiv A, Debets V, Storm C, Šarić A. 2021. Durotaxis of passive
nanoparticles on elastic membranes. ACS Nano.
mla: Palaia, Ivan, et al. “Durotaxis of Passive Nanoparticles on Elastic Membranes.”
ACS Nano, American Chemical Society, 2021, doi:10.1021/acsnano.1c02777 .
short: I. Palaia, A. Paraschiv, V. Debets, C. Storm, A. Šarić, ACS Nano (2021).
date_created: 2021-10-12T07:31:21Z
date_published: 2021-09-22T00:00:00Z
date_updated: 2021-10-12T09:50:19Z
day: '22'
doi: '10.1021/acsnano.1c02777 '
extern: '1'
external_id:
pmid:
- '34550677 '
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.biorxiv.org/content/10.1101/2021.04.01.438065
month: '09'
oa: 1
oa_version: Preprint
pmid: 1
publication: ACS Nano
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
status: public
title: Durotaxis of passive nanoparticles on elastic membranes
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
year: '2021'
...
---
_id: '10125'
abstract:
- lang: eng
text: Living systems propagate by undergoing rounds of cell growth and division.
Cell division is at heart a physical process that requires mechanical forces,
usually exerted by protein assemblies. Here we developed the first physical model
for the division of archaeal cells, which despite their structural simplicity
share machinery and evolutionary origins with eukaryotes. We show how active geometry
changes of elastic ESCRT-III filaments, coupled to filament disassembly, are sufficient
to efficiently split the cell. We explore how the non-equilibrium processes that
govern the filament behaviour impact the resulting cell division. We show how
a quantitative comparison between our simulations and dynamic data for ESCRTIII-mediated
division in Sulfolobus acidocaldarius, the closest archaeal relative to eukaryotic
cells that can currently be cultured in the lab, and reveal the most likely physical
mechanism behind its division.
acknowledgement: We acknowledge support from the Biotechnology and Biological Sciences
Research Council (L.H.K.), EPSRC (A.E.H), UCL IPLS (T.Y and D. H.), Wellcome Trust
(203276/Z/16/Z, A.P., S.C., R. H., B.B.), Volkswagen Foundation (Az 96727, A.P.,
B.B., A.Š.), MRC (MC CF1226, R.H., B.B., A.Š.), the ERC grant (”NEPA” 802960, A.Š.),
the Royal Society (C.V.-H., A.Š.), the UK Materials and Molecular Modelling Hub
for computational resources (EP/P020194/1).
article_processing_charge: No
author:
- first_name: L.
full_name: Harker-Kirschneck, L.
last_name: Harker-Kirschneck
- first_name: A. E.
full_name: Hafner, A. E.
last_name: Hafner
- first_name: T.
full_name: Yao, T.
last_name: Yao
- first_name: A.
full_name: Pulschen, A.
last_name: Pulschen
- first_name: F.
full_name: Hurtig, F.
last_name: Hurtig
- first_name: C.
full_name: Vanhille-Campos, C.
last_name: Vanhille-Campos
- first_name: D.
full_name: Hryniuk, D.
last_name: Hryniuk
- first_name: S.
full_name: Culley, S.
last_name: Culley
- first_name: R.
full_name: Henriques, R.
last_name: Henriques
- first_name: B.
full_name: Baum, B.
last_name: Baum
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
citation:
ama: Harker-Kirschneck L, Hafner AE, Yao T, et al. Physical mechanisms of ESCRT-III-driven
cell division in archaea. bioRxiv. doi:10.1101/2021.03.23.436559
apa: Harker-Kirschneck, L., Hafner, A. E., Yao, T., Pulschen, A., Hurtig, F., Vanhille-Campos,
C., … Šarić, A. (n.d.). Physical mechanisms of ESCRT-III-driven cell division
in archaea. bioRxiv. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2021.03.23.436559
chicago: Harker-Kirschneck, L., A. E. Hafner, T. Yao, A. Pulschen, F. Hurtig, C.
Vanhille-Campos, D. Hryniuk, et al. “Physical Mechanisms of ESCRT-III-Driven Cell
Division in Archaea.” BioRxiv. Cold Spring Harbor Laboratory, n.d. https://doi.org/10.1101/2021.03.23.436559.
ieee: L. Harker-Kirschneck et al., “Physical mechanisms of ESCRT-III-driven
cell division in archaea,” bioRxiv. Cold Spring Harbor Laboratory.
ista: Harker-Kirschneck L, Hafner AE, Yao T, Pulschen A, Hurtig F, Vanhille-Campos
C, Hryniuk D, Culley S, Henriques R, Baum B, Šarić A. Physical mechanisms of ESCRT-III-driven
cell division in archaea. bioRxiv, 10.1101/2021.03.23.436559.
mla: Harker-Kirschneck, L., et al. “Physical Mechanisms of ESCRT-III-Driven Cell
Division in Archaea.” BioRxiv, Cold Spring Harbor Laboratory, doi:10.1101/2021.03.23.436559.
short: L. Harker-Kirschneck, A.E. Hafner, T. Yao, A. Pulschen, F. Hurtig, C. Vanhille-Campos,
D. Hryniuk, S. Culley, R. Henriques, B. Baum, A. Šarić, BioRxiv (n.d.).
date_created: 2021-10-12T07:45:07Z
date_published: 2021-03-23T00:00:00Z
date_updated: 2021-10-12T09:50:26Z
day: '23'
doi: 10.1101/2021.03.23.436559
extern: '1'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.biorxiv.org/content/10.1101/2021.03.23.436559
month: '03'
oa: 1
oa_version: Preprint
publication: bioRxiv
publication_status: submitted
publisher: Cold Spring Harbor Laboratory
status: public
title: Physical mechanisms of ESCRT-III-driven cell division in archaea
type: preprint
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
year: '2021'
...
---
_id: '10340'
abstract:
- lang: eng
text: 'The cell membrane is an inhomogeneous system composed of phospholipids, sterols,
carbohydrates, and proteins that can be directly attached to underlying cytoskeleton.
The protein linkers between the membrane and the cytoskeleton are believed to
have a profound effect on the mechanical properties of the cell membrane and its
ability to reshape. Here, we investigate the role of membrane-cortex linkers on
the extrusion of membrane tubes using computer simulations and experiments. In
simulations, we find that the force for tube extrusion has a nonlinear dependence
on the density of membrane-cortex attachments: at a range of low and intermediate
linker densities, the force is not significantly influenced by the presence of
the membrane-cortex attachments and resembles that of the bare membrane. For large
concentrations of linkers, however, the force substantially increases compared
with the bare membrane. In both cases, the linkers provided membrane tubes with
increased stability against coalescence. We then pulled tubes from HEK cells using
optical tweezers for varying expression levels of the membrane-cortex attachment
protein Ezrin. In line with simulations, we observed that overexpression of Ezrin
led to an increased extrusion force, while Ezrin depletion had a negligible effect
on the force. Our results shed light on the importance of local protein rearrangements
for membrane reshaping at nanoscopic scales.'
acknowledgement: We thank Ewa Paluch, Alba Diz-Muñoz, Guillaume Salbreux, Guillaume
Charras, and Shiladitya Banerjee for helpful discussions. We acknowledge support
from the Engineering and Physical Sciences Research Council (A.P. and A.Š.), the
UCL Institute for the Physics of Living Systems (A.P., C.V.C., and A.Š.), the Royal
Society (C.V.C. and A.Š.), and the European Research Council (Starting grant EP/R011818/1
to A.Š.; E.C. and P.B. are partners of the advanced grant, project 339847) and from
Institut Curie (E.C. and P.B.) and Centre National de la Recherche Scientifique
(CNRS) (E.C. and P.B.). The P.B. and E.C. groups belong to Labex CelTisPhyBio (ANR-11-LABX0038)
and to Paris Sciences et Lettres (ANR-10-IDEX-0001-02). T.L. received a PhD grant
from Paris Sciences et Lettres Research University and support from the Institut
Curie.
article_processing_charge: No
article_type: original
author:
- first_name: Alexandru
full_name: Paraschiv, Alexandru
last_name: Paraschiv
- first_name: Thibaut J.
full_name: Lagny, Thibaut J.
last_name: Lagny
- first_name: Christian Vanhille
full_name: Campos, Christian Vanhille
last_name: Campos
- first_name: Evelyne
full_name: Coudrier, Evelyne
last_name: Coudrier
- first_name: Patricia
full_name: Bassereau, Patricia
last_name: Bassereau
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
citation:
ama: Paraschiv A, Lagny TJ, Campos CV, Coudrier E, Bassereau P, Šarić A. Influence
of membrane-cortex linkers on the extrusion of membrane tubes. Biophysical
Journal. 2021;120(4):598-606. doi:10.1016/j.bpj.2020.12.028
apa: Paraschiv, A., Lagny, T. J., Campos, C. V., Coudrier, E., Bassereau, P., &
Šarić, A. (2021). Influence of membrane-cortex linkers on the extrusion of membrane
tubes. Biophysical Journal. Cell Press. https://doi.org/10.1016/j.bpj.2020.12.028
chicago: Paraschiv, Alexandru, Thibaut J. Lagny, Christian Vanhille Campos, Evelyne
Coudrier, Patricia Bassereau, and Anđela Šarić. “Influence of Membrane-Cortex
Linkers on the Extrusion of Membrane Tubes.” Biophysical Journal. Cell
Press, 2021. https://doi.org/10.1016/j.bpj.2020.12.028.
ieee: A. Paraschiv, T. J. Lagny, C. V. Campos, E. Coudrier, P. Bassereau, and A.
Šarić, “Influence of membrane-cortex linkers on the extrusion of membrane tubes,”
Biophysical Journal, vol. 120, no. 4. Cell Press, pp. 598–606, 2021.
ista: Paraschiv A, Lagny TJ, Campos CV, Coudrier E, Bassereau P, Šarić A. 2021.
Influence of membrane-cortex linkers on the extrusion of membrane tubes. Biophysical
Journal. 120(4), 598–606.
mla: Paraschiv, Alexandru, et al. “Influence of Membrane-Cortex Linkers on the Extrusion
of Membrane Tubes.” Biophysical Journal, vol. 120, no. 4, Cell Press, 2021,
pp. 598–606, doi:10.1016/j.bpj.2020.12.028.
short: A. Paraschiv, T.J. Lagny, C.V. Campos, E. Coudrier, P. Bassereau, A. Šarić,
Biophysical Journal 120 (2021) 598–606.
date_created: 2021-11-25T16:18:23Z
date_published: 2021-01-16T00:00:00Z
date_updated: 2022-04-01T10:38:01Z
day: '16'
doi: 10.1016/j.bpj.2020.12.028
extern: '1'
external_id:
pmid:
- '33460596'
intvolume: ' 120'
issue: '4'
keyword:
- biophysics
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1101/2020.07.28.224741
month: '01'
oa: 1
oa_version: Preprint
page: 598-606
pmid: 1
publication: Biophysical Journal
publication_identifier:
issn:
- 0006-3495
publication_status: published
publisher: Cell Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: Influence of membrane-cortex linkers on the extrusion of membrane tubes
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 120
year: '2021'
...
---
_id: '10338'
abstract:
- lang: eng
text: In the nuclear pore complex, intrinsically disordered proteins (FG Nups),
along with their interactions with more globular proteins called nuclear transport
receptors (NTRs), are vital to the selectivity of transport into and out of the
cell nucleus. Although such interactions can be modeled at different levels of
coarse graining, in vitro experimental data have been quantitatively described
by minimal models that describe FG Nups as cohesive homogeneous polymers and NTRs
as uniformly cohesive spheres, in which the heterogeneous effects have been smeared
out. By definition, these minimal models do not account for the explicit heterogeneities
in FG Nup sequences, essentially a string of cohesive and noncohesive polymer
units, and at the NTR surface. Here, we develop computational and analytical models
that do take into account such heterogeneity in a minimal fashion and compare
them with experimental data on single-molecule interactions between FG Nups and
NTRs. Overall, we find that the heterogeneous nature of FG Nups and NTRs does
play a role in determining equilibrium binding properties but is of much greater
significance when it comes to unbinding and binding kinetics. Using our models,
we predict how binding equilibria and kinetics depend on the distribution of cohesive
blocks in the FG Nup sequences and of the binding pockets at the NTR surface,
with multivalency playing a key role. Finally, we observe that single-molecule
binding kinetics has a rather minor influence on the diffusion of NTRs in polymer
melts consisting of FG-Nup-like sequences.
article_processing_charge: No
article_type: original
author:
- first_name: Luke K.
full_name: Davis, Luke K.
last_name: Davis
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Bart W.
full_name: Hoogenboom, Bart W.
last_name: Hoogenboom
- first_name: Anton
full_name: Zilman, Anton
last_name: Zilman
citation:
ama: Davis LK, Šarić A, Hoogenboom BW, Zilman A. Physical modeling of multivalent
interactions in the nuclear pore complex. Biophysical Journal. 2021;120(9):1565-1577.
doi:10.1016/j.bpj.2021.01.039
apa: Davis, L. K., Šarić, A., Hoogenboom, B. W., & Zilman, A. (2021). Physical
modeling of multivalent interactions in the nuclear pore complex. Biophysical
Journal. Elsevier. https://doi.org/10.1016/j.bpj.2021.01.039
chicago: Davis, Luke K., Anđela Šarić, Bart W. Hoogenboom, and Anton Zilman. “Physical
Modeling of Multivalent Interactions in the Nuclear Pore Complex.” Biophysical
Journal. Elsevier, 2021. https://doi.org/10.1016/j.bpj.2021.01.039.
ieee: L. K. Davis, A. Šarić, B. W. Hoogenboom, and A. Zilman, “Physical modeling
of multivalent interactions in the nuclear pore complex,” Biophysical Journal,
vol. 120, no. 9. Elsevier, pp. 1565–1577, 2021.
ista: Davis LK, Šarić A, Hoogenboom BW, Zilman A. 2021. Physical modeling of multivalent
interactions in the nuclear pore complex. Biophysical Journal. 120(9), 1565–1577.
mla: Davis, Luke K., et al. “Physical Modeling of Multivalent Interactions in the
Nuclear Pore Complex.” Biophysical Journal, vol. 120, no. 9, Elsevier,
2021, pp. 1565–77, doi:10.1016/j.bpj.2021.01.039.
short: L.K. Davis, A. Šarić, B.W. Hoogenboom, A. Zilman, Biophysical Journal 120
(2021) 1565–1577.
date_created: 2021-11-25T15:36:36Z
date_published: 2021-02-19T00:00:00Z
date_updated: 2022-04-01T10:34:38Z
day: '19'
doi: 10.1016/j.bpj.2021.01.039
extern: '1'
external_id:
pmid:
- '33617830'
intvolume: ' 120'
issue: '9'
keyword:
- biophysics
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1101/2020.10.01.322156
month: '02'
oa: 1
oa_version: Preprint
page: 1565-1577
pmid: 1
publication: Biophysical Journal
publication_identifier:
issn:
- 0006-3495
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Physical modeling of multivalent interactions in the nuclear pore complex
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 120
year: '2021'
...
---
_id: '10337'
abstract:
- lang: eng
text: The T cell receptor (TCR) pathway receives, processes, and amplifies the signal
from pathogenic antigens to the activation of T cells. Although major components
in this pathway have been identified, the knowledge on how individual components
cooperate to effectively transduce signals remains limited. Phase separation emerges
as a biophysical principle in organizing signaling molecules into liquid-like
condensates. Here, we report that phospholipase Cγ1 (PLCγ1) promotes phase separation
of LAT, a key adaptor protein in the TCR pathway. PLCγ1 directly cross-links LAT
through its two SH2 domains. PLCγ1 also protects LAT from dephosphorylation by
the phosphatase CD45 and promotes LAT-dependent ERK activation and SLP76 phosphorylation.
Intriguingly, a nonmonotonic effect of PLCγ1 on LAT clustering was discovered.
Computer simulations, based on patchy particles, revealed how the cluster size
is regulated by protein compositions. Together, these results define a critical
function of PLCγ1 in promoting phase separation of the LAT complex and TCR signal
transduction.
acknowledgement: Charles H. Hood Foundation (NO AWARD) ; Rally Foundation (NO AWARD)
article_number: e202009154
article_processing_charge: No
article_type: original
author:
- first_name: Longhui
full_name: Zeng, Longhui
last_name: Zeng
- first_name: Ivan
full_name: Palaia, Ivan
last_name: Palaia
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Xiaolei
full_name: Su, Xiaolei
last_name: Su
citation:
ama: Zeng L, Palaia I, Šarić A, Su X. PLCγ1 promotes phase separation of T cell
signaling components. Journal of Cell Biology. 2021;220(6). doi:10.1083/jcb.202009154
apa: Zeng, L., Palaia, I., Šarić, A., & Su, X. (2021). PLCγ1 promotes phase
separation of T cell signaling components. Journal of Cell Biology. Rockefeller
University Press. https://doi.org/10.1083/jcb.202009154
chicago: Zeng, Longhui, Ivan Palaia, Anđela Šarić, and Xiaolei Su. “PLCγ1 Promotes
Phase Separation of T Cell Signaling Components.” Journal of Cell Biology.
Rockefeller University Press, 2021. https://doi.org/10.1083/jcb.202009154.
ieee: L. Zeng, I. Palaia, A. Šarić, and X. Su, “PLCγ1 promotes phase separation
of T cell signaling components,” Journal of Cell Biology, vol. 220, no.
6. Rockefeller University Press, 2021.
ista: Zeng L, Palaia I, Šarić A, Su X. 2021. PLCγ1 promotes phase separation of
T cell signaling components. Journal of Cell Biology. 220(6), e202009154.
mla: Zeng, Longhui, et al. “PLCγ1 Promotes Phase Separation of T Cell Signaling
Components.” Journal of Cell Biology, vol. 220, no. 6, e202009154, Rockefeller
University Press, 2021, doi:10.1083/jcb.202009154.
short: L. Zeng, I. Palaia, A. Šarić, X. Su, Journal of Cell Biology 220 (2021).
date_created: 2021-11-25T15:21:30Z
date_published: 2021-04-30T00:00:00Z
date_updated: 2021-11-25T15:33:08Z
day: '30'
doi: 10.1083/jcb.202009154
extern: '1'
external_id:
pmid:
- '33929486'
intvolume: ' 220'
issue: '6'
keyword:
- cell biology
language:
- iso: eng
license: https://creativecommons.org/licenses/by-nc-sa/4.0/
month: '04'
oa_version: None
pmid: 1
publication: Journal of Cell Biology
publication_identifier:
eissn:
- 1540-8140
issn:
- 0021-9525
publication_status: published
publisher: Rockefeller University Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: PLCγ1 promotes phase separation of T cell signaling components
tmp:
image: /images/cc_by_nc_sa.png
legal_code_url: https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode
name: Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC
BY-NC-SA 4.0)
short: CC BY-NC-SA (4.0)
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 220
year: '2021'
...
---
_id: '10339'
abstract:
- lang: eng
text: We study the effects of osmotic shocks on lipid vesicles via coarse-grained
molecular dynamics simulations by explicitly considering the solute in the system.
We find that depending on their nature (hypo- or hypertonic) such shocks can lead
to bursting events or engulfing of external material into inner compartments,
among other morphology transformations. We characterize the dynamics of these
processes and observe a separation of time scales between the osmotic shock absorption
and the shape relaxation. Our work consequently provides an insight into the dynamics
of compartmentalization in vesicular systems as a result of osmotic shocks, which
can be of interest in the context of early proto-cell development and proto-cell
compartmentalisation.
acknowledgement: We acknowledge support from the Royal Society (C. V. C. and A. Sˇ.),
the Medical Research Council (C. V. C. and A. Sˇ.), and the European Research Council
(Starting grant ‘‘NEPA’’ 802960 to A. Sˇ.). We thank Johannes Krausser and Ivan
Palaia for fruitful discussions.
article_processing_charge: No
article_type: original
author:
- first_name: Christian
full_name: Vanhille-Campos, Christian
last_name: Vanhille-Campos
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
citation:
ama: Vanhille-Campos C, Šarić A. Modelling the dynamics of vesicle reshaping and
scission under osmotic shocks. Soft Matter. 2021;17(14):3798-3806. doi:10.1039/d0sm02012e
apa: Vanhille-Campos, C., & Šarić, A. (2021). Modelling the dynamics of vesicle
reshaping and scission under osmotic shocks. Soft Matter. Royal Society
of Chemistry. https://doi.org/10.1039/d0sm02012e
chicago: Vanhille-Campos, Christian, and Anđela Šarić. “Modelling the Dynamics of
Vesicle Reshaping and Scission under Osmotic Shocks.” Soft Matter. Royal
Society of Chemistry, 2021. https://doi.org/10.1039/d0sm02012e.
ieee: C. Vanhille-Campos and A. Šarić, “Modelling the dynamics of vesicle reshaping
and scission under osmotic shocks,” Soft Matter, vol. 17, no. 14. Royal
Society of Chemistry, pp. 3798–3806, 2021.
ista: Vanhille-Campos C, Šarić A. 2021. Modelling the dynamics of vesicle reshaping
and scission under osmotic shocks. Soft Matter. 17(14), 3798–3806.
mla: Vanhille-Campos, Christian, and Anđela Šarić. “Modelling the Dynamics of Vesicle
Reshaping and Scission under Osmotic Shocks.” Soft Matter, vol. 17, no.
14, Royal Society of Chemistry, 2021, pp. 3798–806, doi:10.1039/d0sm02012e.
short: C. Vanhille-Campos, A. Šarić, Soft Matter 17 (2021) 3798–3806.
date_created: 2021-11-25T16:06:42Z
date_published: 2021-02-16T00:00:00Z
date_updated: 2021-11-30T08:20:09Z
day: '16'
doi: 10.1039/d0sm02012e
extern: '1'
external_id:
pmid:
- '33629089'
intvolume: ' 17'
issue: '14'
keyword:
- condensed matter physics
- general chemistry
language:
- iso: eng
license: https://creativecommons.org/licenses/by-nc/3.0/
main_file_link:
- open_access: '1'
url: https://pubs.rsc.org/en/content/articlehtml/2021/sm/d0sm02012e
month: '02'
oa: 1
oa_version: Published Version
page: 3798-3806
pmid: 1
publication: Soft Matter
publication_identifier:
eissn:
- 1744-6848
issn:
- 1744-683X
publication_status: published
publisher: Royal Society of Chemistry
quality_controlled: '1'
related_material:
link:
- relation: earlier_version
url: https://www.biorxiv.org/content/10.1101/2020.11.16.384602v2
scopus_import: '1'
status: public
title: Modelling the dynamics of vesicle reshaping and scission under osmotic shocks
tmp:
image: /images/cc_by_nc.png
legal_code_url: https://creativecommons.org/licenses/by-nc/3.0/legalcode
name: Creative Commons Attribution-NonCommercial 3.0 Unported (CC BY-NC 3.0)
short: CC BY-NC (3.0)
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 17
year: '2021'
...
---
_id: '10336'
abstract:
- lang: eng
text: Biological membranes can dramatically accelerate the aggregation of normally
soluble protein molecules into amyloid fibrils and alter the fibril morphologies,
yet the molecular mechanisms through which this accelerated nucleation takes place
are not yet understood. Here, we develop a coarse-grained model to systematically
explore the effect that the structural properties of the lipid membrane and the
nature of protein–membrane interactions have on the nucleation rates of amyloid
fibrils. We identify two physically distinct nucleation pathways—protein-rich
and lipid-rich—and quantify how the membrane fluidity and protein–membrane affinity
control the relative importance of those molecular pathways. We find that the
membrane’s susceptibility to reshaping and being incorporated into the fibrillar
aggregates is a key determinant of its ability to promote protein aggregation.
We then characterize the rates and the free-energy profile associated with this
heterogeneous nucleation process, in which the surface itself participates in
the aggregate structure. Finally, we compare quantitatively our data to experiments
on membrane-catalyzed amyloid aggregation of α-synuclein, a protein implicated
in Parkinson’s disease that predominately nucleates on membranes. More generally,
our results provide a framework for understanding macromolecular aggregation on
lipid membranes in a broad biological and biotechnological context.
acknowledgement: We thank T. C. T. Michaels for reading the manuscript. This work
was supported by the Academy of Medical Science (J.K. and A.Š.), the Cambridge Center
for Misfolding Diseases (T.P.J.K.), the Biotechnology and Biological Sciences Research
Council (T.P.J.K.), the Frances and Augustus Newman Foundation (T.P.J.K.), the European
Research Council Grant PhysProt Agreement 337969, the Wellcome Trust (A.Š. and T.P.J.K.),
the Royal Society (A.Š.), the Medical Research Council (J.K. and A.Š.), and the
UK Materials and Molecular Modeling Hub for computational resources, which is partially
funded by Engineering and Physical Sciences Research Council Grant EP/P020194/1.
article_processing_charge: No
article_type: original
author:
- first_name: Johannes
full_name: Krausser, Johannes
last_name: Krausser
- first_name: Tuomas P. J.
full_name: Knowles, Tuomas P. J.
last_name: Knowles
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
citation:
ama: Krausser J, Knowles TPJ, Šarić A. Physical mechanisms of amyloid nucleation
on fluid membranes. Proceedings of the National Academy of Sciences. 2020;117(52):33090-33098.
doi:10.1073/pnas.2007694117
apa: Krausser, J., Knowles, T. P. J., & Šarić, A. (2020). Physical mechanisms
of amyloid nucleation on fluid membranes. Proceedings of the National Academy
of Sciences. National Academy of Sciences. https://doi.org/10.1073/pnas.2007694117
chicago: Krausser, Johannes, Tuomas P. J. Knowles, and Anđela Šarić. “Physical Mechanisms
of Amyloid Nucleation on Fluid Membranes.” Proceedings of the National Academy
of Sciences. National Academy of Sciences, 2020. https://doi.org/10.1073/pnas.2007694117.
ieee: J. Krausser, T. P. J. Knowles, and A. Šarić, “Physical mechanisms of amyloid
nucleation on fluid membranes,” Proceedings of the National Academy of Sciences,
vol. 117, no. 52. National Academy of Sciences, pp. 33090–33098, 2020.
ista: Krausser J, Knowles TPJ, Šarić A. 2020. Physical mechanisms of amyloid nucleation
on fluid membranes. Proceedings of the National Academy of Sciences. 117(52),
33090–33098.
mla: Krausser, Johannes, et al. “Physical Mechanisms of Amyloid Nucleation on Fluid
Membranes.” Proceedings of the National Academy of Sciences, vol. 117,
no. 52, National Academy of Sciences, 2020, pp. 33090–98, doi:10.1073/pnas.2007694117.
short: J. Krausser, T.P.J. Knowles, A. Šarić, Proceedings of the National Academy
of Sciences 117 (2020) 33090–33098.
date_created: 2021-11-25T15:07:09Z
date_published: 2020-12-16T00:00:00Z
date_updated: 2021-11-25T15:35:58Z
day: '16'
doi: 10.1073/pnas.2007694117
extern: '1'
external_id:
pmid:
- '33328273'
intvolume: ' 117'
issue: '52'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.biorxiv.org/content/10.1101/2019.12.22.886267v2
month: '12'
oa: 1
oa_version: Published Version
page: 33090-33098
pmid: 1
publication: Proceedings of the National Academy of Sciences
publication_identifier:
eissn:
- 1091-6490
issn:
- 0027-8424
publication_status: published
publisher: National Academy of Sciences
quality_controlled: '1'
scopus_import: '1'
status: public
title: Physical mechanisms of amyloid nucleation on fluid membranes
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 117
year: '2020'
...
---
_id: '10342'
abstract:
- lang: eng
text: The blood-brain barrier is made of polarized brain endothelial cells (BECs)
phenotypically conditioned by the central nervous system (CNS). Although transport
across BECs is of paramount importance for nutrient uptake as well as ridding
the brain of waste products, the intracellular sorting mechanisms that regulate
successful receptor-mediated transcytosis in BECs remain to be elucidated. Here,
we used a synthetic multivalent system with tunable avidity to the low-density
lipoprotein receptor–related protein 1 (LRP1) to investigate the mechanisms of
transport across BECs. We used a combination of conventional and super-resolution
microscopy, both in vivo and in vitro, accompanied with biophysical modeling of
transport kinetics and membrane-bound interactions to elucidate the role of membrane-sculpting
protein syndapin-2 on fast transport via tubule formation. We show that high-avidity
cargo biases the LRP1 toward internalization associated with fast degradation,
while mid-avidity augments the formation of syndapin-2 tubular carriers promoting
a fast shuttling across.
acknowledgement: 'Funding: G.B. thanks the ERC for the starting grant (MEViC 278793)
and consolidator award (CheSSTaG 769798), EPSRC/BTG Healthcare Partnership (EP/I001697/1),
EPSRC Established Career Fellowship (EP/N026322/1), EPSRC/SomaNautix Healthcare
Partnership EP/R024723/1, and Children with Cancer UK for the research project (16-227).
X.T. and G.B. thank that Anhui 100 Talent program for facilitating data sharing
and research visits. A.D.-C. and L.R. acknowledge the Royal Society for a Newton
fellowship and the Marie Skłodowska-Curie Actions for a European Fellowship. Author
contributions: X.T. prepared and characterized POs, performed all the fast imaging
in both conventional and STED microscopy, set up the initial BBB model, encapsulated
the PtA2 in POs, and supervised the PtA2-PO animal work. D.M.L. prepared and characterized
POs; performed all the permeability studies, PLA assays, WB and associated data
analysis, and part of the colocalization assays; and performed experiments with
the shRNA for knockdown of syndapin-2. E.S. prepared and characterized POs and performed
part of colocalization assays and Cy7-labeled PO animal experiments. S.N. prepared
and characterized POs and performed part of the colocalization and inhibition assays.
G.F. designed, performed, and analyzed the agent-based simulations of transcytosis.
J.F. designed the image-based algorithm to analyze the PLA data. D.M. prepared and
characterized POs and helped with Cy7-labeled PO animal experiments. A.A. performed
TEM imaging of the POs. A.P. and A.D.-C. synthesized the dye- and peptide-functionalized
and pristine copolymers. M.V., L.H.-K., and A.Š. designed, performed, and analyzed
the MD simulations. Z.Z. supervised and supported STED imaging. P.X., B.F., and
Y.T. synthesized and characterized the PtA2 compound. L.L. performed some of the
animal work. L.R. supported and helped with the BBB characterization. G.B. analyzed
all fast imaging and supervised and coordinated the overall work. X.T., D.M.L.,
E.S., and G.B. wrote the manuscript. Competing interests: The authors declare that
part of the work is associated with the UCL spin-out company SomaNautix Ltd. Data
and materials availability: All data needed to evaluate the conclusions in the paper
are present in the paper and/or the Supplementary Materials. Additional data related
to this paper may be requested from the authors.'
article_number: 'eabc4397 '
article_processing_charge: No
article_type: original
author:
- first_name: Xiaohe
full_name: Tian, Xiaohe
last_name: Tian
- first_name: Diana M.
full_name: Leite, Diana M.
last_name: Leite
- first_name: Edoardo
full_name: Scarpa, Edoardo
last_name: Scarpa
- first_name: Sophie
full_name: Nyberg, Sophie
last_name: Nyberg
- first_name: Gavin
full_name: Fullstone, Gavin
last_name: Fullstone
- first_name: Joe
full_name: Forth, Joe
last_name: Forth
- first_name: Diana
full_name: Matias, Diana
last_name: Matias
- first_name: Azzurra
full_name: Apriceno, Azzurra
last_name: Apriceno
- first_name: Alessandro
full_name: Poma, Alessandro
last_name: Poma
- first_name: Aroa
full_name: Duro-Castano, Aroa
last_name: Duro-Castano
- first_name: Manish
full_name: Vuyyuru, Manish
last_name: Vuyyuru
- first_name: Lena
full_name: Harker-Kirschneck, Lena
last_name: Harker-Kirschneck
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Zhongping
full_name: Zhang, Zhongping
last_name: Zhang
- first_name: Pan
full_name: Xiang, Pan
last_name: Xiang
- first_name: Bin
full_name: Fang, Bin
last_name: Fang
- first_name: Yupeng
full_name: Tian, Yupeng
last_name: Tian
- first_name: Lei
full_name: Luo, Lei
last_name: Luo
- first_name: Loris
full_name: Rizzello, Loris
last_name: Rizzello
- first_name: Giuseppe
full_name: Battaglia, Giuseppe
last_name: Battaglia
citation:
ama: 'Tian X, Leite DM, Scarpa E, et al. On the shuttling across the blood-brain
barrier via tubule formation: Mechanism and cargo avidity bias. Science Advances.
2020;6(48). doi:10.1126/sciadv.abc4397'
apa: 'Tian, X., Leite, D. M., Scarpa, E., Nyberg, S., Fullstone, G., Forth, J.,
… Battaglia, G. (2020). On the shuttling across the blood-brain barrier via tubule
formation: Mechanism and cargo avidity bias. Science Advances. American
Association for the Advancement of Science. https://doi.org/10.1126/sciadv.abc4397'
chicago: 'Tian, Xiaohe, Diana M. Leite, Edoardo Scarpa, Sophie Nyberg, Gavin Fullstone,
Joe Forth, Diana Matias, et al. “On the Shuttling across the Blood-Brain Barrier
via Tubule Formation: Mechanism and Cargo Avidity Bias.” Science Advances.
American Association for the Advancement of Science, 2020. https://doi.org/10.1126/sciadv.abc4397.'
ieee: 'X. Tian et al., “On the shuttling across the blood-brain barrier via
tubule formation: Mechanism and cargo avidity bias,” Science Advances,
vol. 6, no. 48. American Association for the Advancement of Science, 2020.'
ista: 'Tian X, Leite DM, Scarpa E, Nyberg S, Fullstone G, Forth J, Matias D, Apriceno
A, Poma A, Duro-Castano A, Vuyyuru M, Harker-Kirschneck L, Šarić A, Zhang Z, Xiang
P, Fang B, Tian Y, Luo L, Rizzello L, Battaglia G. 2020. On the shuttling across
the blood-brain barrier via tubule formation: Mechanism and cargo avidity bias.
Science Advances. 6(48), eabc4397.'
mla: 'Tian, Xiaohe, et al. “On the Shuttling across the Blood-Brain Barrier via
Tubule Formation: Mechanism and Cargo Avidity Bias.” Science Advances,
vol. 6, no. 48, eabc4397, American Association for the Advancement of Science,
2020, doi:10.1126/sciadv.abc4397.'
short: X. Tian, D.M. Leite, E. Scarpa, S. Nyberg, G. Fullstone, J. Forth, D. Matias,
A. Apriceno, A. Poma, A. Duro-Castano, M. Vuyyuru, L. Harker-Kirschneck, A. Šarić,
Z. Zhang, P. Xiang, B. Fang, Y. Tian, L. Luo, L. Rizzello, G. Battaglia, Science
Advances 6 (2020).
date_created: 2021-11-26T06:40:28Z
date_published: 2020-11-27T00:00:00Z
date_updated: 2021-11-26T07:00:24Z
day: '27'
ddc:
- '611'
doi: 10.1126/sciadv.abc4397
extern: '1'
external_id:
pmid:
- '33246953'
file:
- access_level: open_access
checksum: 3ba2eca975930cdb0b1ce1ae876885a7
content_type: application/pdf
creator: cchlebak
date_created: 2021-11-26T06:50:09Z
date_updated: 2021-11-26T06:50:09Z
file_id: '10343'
file_name: 2020_SciAdv_Tian.pdf
file_size: 10381298
relation: main_file
success: 1
file_date_updated: 2021-11-26T06:50:09Z
has_accepted_license: '1'
intvolume: ' 6'
issue: '48'
keyword:
- multidisciplinary
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.biorxiv.org/content/10.1101/2020.04.04.025866v1
month: '11'
oa: 1
oa_version: Published Version
pmid: 1
publication: Science Advances
publication_identifier:
issn:
- 2375-2548
publication_status: published
publisher: American Association for the Advancement of Science
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'On the shuttling across the blood-brain barrier via tubule formation: Mechanism
and cargo avidity bias'
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 6
year: '2020'
...
---
_id: '10344'
abstract:
- lang: eng
text: In this study, we investigate the role of the surface patterning of nanostructures
for cell membrane reshaping. To accomplish this, we combine an evolutionary algorithm
with coarse-grained molecular dynamics simulations and explore the solution space
of ligand patterns on a nanoparticle that promote efficient and reliable cell
uptake. Surprisingly, we find that in the regime of low ligand number the best-performing
structures are characterized by ligands arranged into long one-dimensional chains
that pattern the surface of the particle. We show that these chains of ligands
provide particles with high rotational freedom and they lower the free energy
barrier for membrane crossing. Our approach reveals a set of nonintuitive design
rules that can be used to inform artificial nanoparticle construction and the
search for inhibitors of viral entry.
acknowledgement: We acknowledge support from EPSRC (J. C. F.), MRC (B. B. and A. Š.),
the ERC StG 802960 “NEPA” (J. K. and A. Š.), the Royal Society (A. Š.), and the
United Kingdom Materials and Molecular Modelling Hub for computational resources,
which is partially funded by EPSRC (EP/P020194/1).
article_number: '228101'
article_processing_charge: No
article_type: original
author:
- first_name: Joel C.
full_name: Forster, Joel C.
last_name: Forster
- first_name: Johannes
full_name: Krausser, Johannes
last_name: Krausser
- first_name: Manish R.
full_name: Vuyyuru, Manish R.
last_name: Vuyyuru
- first_name: Buzz
full_name: Baum, Buzz
last_name: Baum
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
citation:
ama: Forster JC, Krausser J, Vuyyuru MR, Baum B, Šarić A. Exploring the design rules
for efficient membrane-reshaping nanostructures. Physical Review Letters.
2020;125(22). doi:10.1103/physrevlett.125.228101
apa: Forster, J. C., Krausser, J., Vuyyuru, M. R., Baum, B., & Šarić, A. (2020).
Exploring the design rules for efficient membrane-reshaping nanostructures. Physical
Review Letters. American Physical Society. https://doi.org/10.1103/physrevlett.125.228101
chicago: Forster, Joel C., Johannes Krausser, Manish R. Vuyyuru, Buzz Baum, and
Anđela Šarić. “Exploring the Design Rules for Efficient Membrane-Reshaping Nanostructures.”
Physical Review Letters. American Physical Society, 2020. https://doi.org/10.1103/physrevlett.125.228101.
ieee: J. C. Forster, J. Krausser, M. R. Vuyyuru, B. Baum, and A. Šarić, “Exploring
the design rules for efficient membrane-reshaping nanostructures,” Physical
Review Letters, vol. 125, no. 22. American Physical Society, 2020.
ista: Forster JC, Krausser J, Vuyyuru MR, Baum B, Šarić A. 2020. Exploring the design
rules for efficient membrane-reshaping nanostructures. Physical Review Letters.
125(22), 228101.
mla: Forster, Joel C., et al. “Exploring the Design Rules for Efficient Membrane-Reshaping
Nanostructures.” Physical Review Letters, vol. 125, no. 22, 228101, American
Physical Society, 2020, doi:10.1103/physrevlett.125.228101.
short: J.C. Forster, J. Krausser, M.R. Vuyyuru, B. Baum, A. Šarić, Physical Review
Letters 125 (2020).
date_created: 2021-11-26T07:10:43Z
date_published: 2020-11-23T00:00:00Z
date_updated: 2021-11-30T08:33:14Z
day: '23'
ddc:
- '530'
doi: 10.1103/physrevlett.125.228101
extern: '1'
external_id:
pmid:
- '33315453'
file:
- access_level: open_access
checksum: fbf2e1415e332d6add90222d60401a1d
content_type: application/pdf
creator: cchlebak
date_created: 2021-11-26T07:16:49Z
date_updated: 2021-11-26T07:16:49Z
file_id: '10345'
file_name: 2020_PhysRevLett_Forster.pdf
file_size: 844353
relation: main_file
success: 1
file_date_updated: 2021-11-26T07:16:49Z
has_accepted_license: '1'
intvolume: ' 125'
issue: '22'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.biorxiv.org/content/10.1101/2020.02.27.968149v1
month: '11'
oa: 1
oa_version: Published Version
pmid: 1
publication: Physical Review Letters
publication_identifier:
eissn:
- 1079-7114
issn:
- 0031-9007
publication_status: published
publisher: American Physical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Exploring the design rules for efficient membrane-reshaping nanostructures
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 125
year: '2020'
...
---
_id: '10341'
abstract:
- lang: eng
text: Tracing the motion of macromolecules, viruses, and nanoparticles adsorbed
onto cell membranes is currently the most direct way of probing the complex dynamic
interactions behind vital biological processes, including cell signalling, trafficking,
and viral infection. The resulting trajectories are usually consistent with some
type of anomalous diffusion, but the molecular origins behind the observed anomalous
behaviour are usually not obvious. Here we use coarse-grained molecular dynamics
simulations to help identify the physical mechanisms that can give rise to experimentally
observed trajectories of nanoscopic objects moving on biological membranes. We
find that diffusion on membranes of high fluidities typically results in normal
diffusion of the adsorbed nanoparticle, irrespective of the concentration of receptors,
receptor clustering, or multivalent interactions between the particle and membrane
receptors. Gel-like membranes on the other hand result in anomalous diffusion
of the particle, which becomes more pronounced at higher receptor concentrations.
This anomalous diffusion is characterised by local particle trapping in the regions
of high receptor concentrations and fast hopping between such regions. The normal
diffusion is recovered in the limit where the gel membrane is saturated with receptors.
We conclude that hindered receptor diffusivity can be a common reason behind the
observed anomalous diffusion of viruses, vesicles, and nanoparticles adsorbed
on cell and model membranes. Our results enable direct comparison with experiments
and offer a new route for interpreting motility experiments on cell membranes.
acknowledgement: We thank Jessica McQuade for her input at the start of the project.
We acknowledge support from the ERASMUS Placement Programme (V. E. D.), the UCL
Institute for the Physics of Living Systems (V. E. D. and A. Š.), the UCL Global
Engagement Fund (L. M. C. J.), and the Royal Society (A. Š.).
article_processing_charge: No
article_type: original
author:
- first_name: V. E.
full_name: Debets, V. E.
last_name: Debets
- first_name: L. M. C.
full_name: Janssen, L. M. C.
last_name: Janssen
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
citation:
ama: Debets VE, Janssen LMC, Šarić A. Characterising the diffusion of biological
nanoparticles on fluid and cross-linked membranes. Soft Matter. 2020;16(47):10628-10639.
doi:10.1039/d0sm00712a
apa: Debets, V. E., Janssen, L. M. C., & Šarić, A. (2020). Characterising the
diffusion of biological nanoparticles on fluid and cross-linked membranes. Soft
Matter. Royal Society of Chemistry. https://doi.org/10.1039/d0sm00712a
chicago: Debets, V. E., L. M. C. Janssen, and Anđela Šarić. “Characterising the
Diffusion of Biological Nanoparticles on Fluid and Cross-Linked Membranes.” Soft
Matter. Royal Society of Chemistry, 2020. https://doi.org/10.1039/d0sm00712a.
ieee: V. E. Debets, L. M. C. Janssen, and A. Šarić, “Characterising the diffusion
of biological nanoparticles on fluid and cross-linked membranes,” Soft Matter,
vol. 16, no. 47. Royal Society of Chemistry, pp. 10628–10639, 2020.
ista: Debets VE, Janssen LMC, Šarić A. 2020. Characterising the diffusion of biological
nanoparticles on fluid and cross-linked membranes. Soft Matter. 16(47), 10628–10639.
mla: Debets, V. E., et al. “Characterising the Diffusion of Biological Nanoparticles
on Fluid and Cross-Linked Membranes.” Soft Matter, vol. 16, no. 47, Royal
Society of Chemistry, 2020, pp. 10628–39, doi:10.1039/d0sm00712a.
short: V.E. Debets, L.M.C. Janssen, A. Šarić, Soft Matter 16 (2020) 10628–10639.
date_created: 2021-11-26T06:29:41Z
date_published: 2020-10-06T00:00:00Z
date_updated: 2021-11-26T07:00:33Z
day: '06'
doi: 10.1039/d0sm00712a
extern: '1'
external_id:
pmid:
- '33084724'
intvolume: ' 16'
issue: '47'
keyword:
- condensed matter physics
- general chemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.biorxiv.org/content/10.1101/2020.05.01.071761v1
month: '10'
oa: 1
oa_version: Published Version
page: 10628-10639
pmid: 1
publication: Soft Matter
publication_identifier:
issn:
- 1744-683X
- 1744-6848
publication_status: published
publisher: Royal Society of Chemistry
quality_controlled: '1'
scopus_import: '1'
status: public
title: Characterising the diffusion of biological nanoparticles on fluid and cross-linked
membranes
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 16
year: '2020'
...
---
_id: '10346'
abstract:
- lang: eng
text: One of the most robust examples of self-assembly in living organisms is the
formation of collagen architectures. Collagen type I molecules are a crucial component
of the extracellular matrix, where they self-assemble into fibrils of well-defined
axial striped patterns. This striped fibrillar pattern is preserved across the
animal kingdom and is important for the determination of cell phenotype, cell
adhesion, and tissue regulation and signaling. The understanding of the physical
processes that determine such a robust morphology of self-assembled collagen fibrils
is currently almost completely missing. Here, we develop a minimal coarse-grained
computational model to identify the physical principles of the assembly of collagen-mimetic
molecules. We find that screened electrostatic interactions can drive the formation
of collagen-like filaments of well-defined striped morphologies. The fibril axial
pattern is determined solely by the distribution of charges on the molecule and
is robust to the changes in protein concentration, monomer rigidity, and environmental
conditions. We show that the striped fibrillar pattern cannot be easily predicted
from the interactions between two monomers but is an emergent result of multibody
interactions. Our results can help address collagen remodeling in diseases and
aging and guide the design of collagen scaffolds for biotechnological applications.
acknowledgement: We thank Melinda Duer, Patrick Mesquida, Lucy Colwell, Lucie Liu,
Daan Frenkel, and Ivan Palaia for helpful discussions. We acknowledge support from
the Engineering and Physical Sciences Research Council (A.E.H., L.K.D., and A.Š.),
Biotechnology and Biological Sciences Research Council LIDo programme (N.G.G. and
C.A.B.), the Royal Society (A.Š.), and the UK Materials and Molecular Modelling
Hub for computational resources, which is partially funded by EPSRC ( EP/P020194/1).
article_processing_charge: No
article_type: original
author:
- first_name: Anne E.
full_name: Hafner, Anne E.
last_name: Hafner
- first_name: Noemi G.
full_name: Gyori, Noemi G.
last_name: Gyori
- first_name: Ciaran A.
full_name: Bench, Ciaran A.
last_name: Bench
- first_name: Luke K.
full_name: Davis, Luke K.
last_name: Davis
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
citation:
ama: Hafner AE, Gyori NG, Bench CA, Davis LK, Šarić A. Modeling fibrillogenesis
of collagen-mimetic molecules. Biophysical Journal. 2020;119(9):1791-1799.
doi:10.1016/j.bpj.2020.09.013
apa: Hafner, A. E., Gyori, N. G., Bench, C. A., Davis, L. K., & Šarić, A. (2020).
Modeling fibrillogenesis of collagen-mimetic molecules. Biophysical Journal.
Cell Press. https://doi.org/10.1016/j.bpj.2020.09.013
chicago: Hafner, Anne E., Noemi G. Gyori, Ciaran A. Bench, Luke K. Davis, and Anđela
Šarić. “Modeling Fibrillogenesis of Collagen-Mimetic Molecules.” Biophysical
Journal. Cell Press, 2020. https://doi.org/10.1016/j.bpj.2020.09.013.
ieee: A. E. Hafner, N. G. Gyori, C. A. Bench, L. K. Davis, and A. Šarić, “Modeling
fibrillogenesis of collagen-mimetic molecules,” Biophysical Journal, vol.
119, no. 9. Cell Press, pp. 1791–1799, 2020.
ista: Hafner AE, Gyori NG, Bench CA, Davis LK, Šarić A. 2020. Modeling fibrillogenesis
of collagen-mimetic molecules. Biophysical Journal. 119(9), 1791–1799.
mla: Hafner, Anne E., et al. “Modeling Fibrillogenesis of Collagen-Mimetic Molecules.”
Biophysical Journal, vol. 119, no. 9, Cell Press, 2020, pp. 1791–99, doi:10.1016/j.bpj.2020.09.013.
short: A.E. Hafner, N.G. Gyori, C.A. Bench, L.K. Davis, A. Šarić, Biophysical Journal
119 (2020) 1791–1799.
date_created: 2021-11-26T07:27:24Z
date_published: 2020-09-23T00:00:00Z
date_updated: 2021-11-26T07:45:24Z
day: '23'
doi: 10.1016/j.bpj.2020.09.013
extern: '1'
external_id:
pmid:
- '33049216'
intvolume: ' 119'
issue: '9'
keyword:
- biophysics
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.biorxiv.org/content/10.1101/2020.06.08.140061v1
month: '09'
oa: 1
oa_version: Published Version
page: 1791-1799
pmid: 1
publication: Biophysical Journal
publication_identifier:
issn:
- 0006-3495
publication_status: published
publisher: Cell Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: Modeling fibrillogenesis of collagen-mimetic molecules
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 119
year: '2020'
...
---
_id: '10350'
abstract:
- lang: eng
text: The misfolding and aberrant aggregation of proteins into fibrillar structures
is a key factor in some of the most prevalent human diseases, including diabetes
and dementia. Low molecular weight oligomers are thought to be a central factor
in the pathology of these diseases, as well as critical intermediates in the fibril
formation process, and as such have received much recent attention. Moreover,
on-pathway oligomeric intermediates are potential targets for therapeutic strategies
aimed at interrupting the fibril formation process. However, a consistent framework
for distinguishing on-pathway from off-pathway oligomers has hitherto been lacking
and, in particular, no consensus definition of on- and off-pathway oligomers is
available. In this paper, we argue that a non-binary definition of oligomers'
contribution to fibril-forming pathways may be more informative and we suggest
a quantitative framework, in which each oligomeric species is assigned a value
between 0 and 1 describing its relative contribution to the formation of fibrils.
First, we clarify the distinction between oligomers and fibrils, and then we use
the formalism of reaction networks to develop a general definition for on-pathway
oligomers, that yields meaningful classifications in the context of amyloid formation.
By applying these concepts to Monte Carlo simulations of a minimal aggregating
system, and by revisiting several previous studies of amyloid oligomers in light
of our new framework, we demonstrate how to perform these classifications in practice.
For each oligomeric species we obtain the degree to which it is on-pathway, highlighting
the most effective pharmaceutical targets for the inhibition of amyloid fibril
formation.
acknowledgement: We are grateful to the Schiff Foundation (AJD), Peterhouse, Cambridge
(TCTM), the Swiss National Science foundation (TCTM), Ramon Jenkins Fellowship,
Sidney Sussex, Cambridge (GM), the Royal Society (AŠ), the Academy of Medical Sciences
and Wellcome Trust (AŠ), the Danish Research Council (MK), the Lundbeck Foundation
(MK), the Swedish Research Council (SL), the Wellcome Trust (TPJK), the Cambridge
Centre for Misfolding Diseases (TPJK), the BBSRC (TPJK), the Frances and Augustus
Newman Foundation (TPJK) for financial support. The research leading to these results
has received funding from the European Research Council under the European Union's
Seventh Framework Programme (FP7/2007-2013) through the ERC grants PhysProt (agreement
no. 337969), MAMBA (agreement no. 340890) and NovoNordiskFonden (SL).
article_processing_charge: No
article_type: original
author:
- first_name: Alexander J.
full_name: Dear, Alexander J.
last_name: Dear
- first_name: Georg
full_name: Meisl, Georg
last_name: Meisl
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Thomas C. T.
full_name: Michaels, Thomas C. T.
last_name: Michaels
- first_name: Magnus
full_name: Kjaergaard, Magnus
last_name: Kjaergaard
- first_name: Sara
full_name: Linse, Sara
last_name: Linse
- first_name: Tuomas P. J.
full_name: Knowles, Tuomas P. J.
last_name: Knowles
citation:
ama: Dear AJ, Meisl G, Šarić A, et al. Identification of on- and off-pathway oligomers
in amyloid fibril formation. Chemical Science. 2020;11(24):6236-6247. doi:10.1039/c9sc06501f
apa: Dear, A. J., Meisl, G., Šarić, A., Michaels, T. C. T., Kjaergaard, M., Linse,
S., & Knowles, T. P. J. (2020). Identification of on- and off-pathway oligomers
in amyloid fibril formation. Chemical Science. Royal Society of Chemistry.
https://doi.org/10.1039/c9sc06501f
chicago: Dear, Alexander J., Georg Meisl, Anđela Šarić, Thomas C. T. Michaels, Magnus
Kjaergaard, Sara Linse, and Tuomas P. J. Knowles. “Identification of On- and off-Pathway
Oligomers in Amyloid Fibril Formation.” Chemical Science. Royal Society
of Chemistry, 2020. https://doi.org/10.1039/c9sc06501f.
ieee: A. J. Dear et al., “Identification of on- and off-pathway oligomers
in amyloid fibril formation,” Chemical Science, vol. 11, no. 24. Royal
Society of Chemistry, pp. 6236–6247, 2020.
ista: Dear AJ, Meisl G, Šarić A, Michaels TCT, Kjaergaard M, Linse S, Knowles TPJ.
2020. Identification of on- and off-pathway oligomers in amyloid fibril formation.
Chemical Science. 11(24), 6236–6247.
mla: Dear, Alexander J., et al. “Identification of On- and off-Pathway Oligomers
in Amyloid Fibril Formation.” Chemical Science, vol. 11, no. 24, Royal
Society of Chemistry, 2020, pp. 6236–47, doi:10.1039/c9sc06501f.
short: A.J. Dear, G. Meisl, A. Šarić, T.C.T. Michaels, M. Kjaergaard, S. Linse,
T.P.J. Knowles, Chemical Science 11 (2020) 6236–6247.
date_created: 2021-11-26T09:08:19Z
date_published: 2020-06-08T00:00:00Z
date_updated: 2021-11-26T11:21:20Z
day: '08'
doi: 10.1039/c9sc06501f
extern: '1'
external_id:
pmid:
- '32953019'
intvolume: ' 11'
issue: '24'
keyword:
- general chemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://pubs.rsc.org/en/content/articlehtml/2020/sc/c9sc06501f
month: '06'
oa: 1
oa_version: Published Version
page: 6236-6247
pmid: 1
publication: Chemical Science
publication_identifier:
eissn:
- 2041-6539
issn:
- 2041-6520
publication_status: published
publisher: Royal Society of Chemistry
quality_controlled: '1'
scopus_import: '1'
status: public
title: Identification of on- and off-pathway oligomers in amyloid fibril formation
tmp:
image: /images/cc_by_nc.png
legal_code_url: https://creativecommons.org/licenses/by-nc/3.0/legalcode
name: Creative Commons Attribution-NonCommercial 3.0 Unported (CC BY-NC 3.0)
short: CC BY-NC (3.0)
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 11
year: '2020'
...
---
_id: '10349'
abstract:
- lang: eng
text: Sulfolobus acidocaldarius is the closest experimentally tractable archaeal
relative of eukaryotes and, despite lacking obvious cyclin-dependent kinase and
cyclin homologs, has an ordered eukaryote-like cell cycle with distinct phases
of DNA replication and division. Here, in exploring the mechanism of cell division
in S. acidocaldarius, we identify a role for the archaeal proteasome in regulating
the transition from the end of one cell cycle to the beginning of the next. Further,
we identify the archaeal ESCRT-III homolog, CdvB, as a key target of the proteasome
and show that its degradation triggers division by allowing constriction of the
CdvB1:CdvB2 ESCRT-III division ring. These findings offer a minimal mechanism
for ESCRT-III–mediated membrane remodeling and point to a conserved role for the
proteasome in eukaryotic and archaeal cell cycle control.
acknowledgement: "We thank the MRC LMCB at UCL for their support; the flow cytometry
STP at the Francis Crick Institute for assistance, with special thanks to S. Purewal
and D. Davis; C. Bertoli for mentorship\r\nand advice; J. M. Garcia-Arcos for help
early on in this project; the entire Baum lab for their input throughout the project;
the Albers lab for advice and reagents, with special thanks to M. Van Wolferen and
S. Albers; the members of the Wellcome consortium for archaeal cytoskeleton studies
for advice and comments; and J. Löwe, S. Oliferenko, M. Balasubramanian, and D.
Gerlich for discussions and advice on the manuscript. N.P.R. and S.B. would like
to thank N. Rzechorzek, A. Simon, and S. Anjum for discussion and advice."
article_processing_charge: No
article_type: original
author:
- first_name: Gabriel
full_name: Tarrason Risa, Gabriel
last_name: Tarrason Risa
- first_name: Fredrik
full_name: Hurtig, Fredrik
last_name: Hurtig
- first_name: Sian
full_name: Bray, Sian
last_name: Bray
- first_name: Anne E.
full_name: Hafner, Anne E.
last_name: Hafner
- first_name: Lena
full_name: Harker-Kirschneck, Lena
last_name: Harker-Kirschneck
- first_name: Peter
full_name: Faull, Peter
last_name: Faull
- first_name: Colin
full_name: Davis, Colin
last_name: Davis
- first_name: Dimitra
full_name: Papatziamou, Dimitra
last_name: Papatziamou
- first_name: Delyan R.
full_name: Mutavchiev, Delyan R.
last_name: Mutavchiev
- first_name: Catherine
full_name: Fan, Catherine
last_name: Fan
- first_name: Leticia
full_name: Meneguello, Leticia
last_name: Meneguello
- first_name: Andre
full_name: Arashiro Pulschen, Andre
last_name: Arashiro Pulschen
- first_name: Gautam
full_name: Dey, Gautam
last_name: Dey
- first_name: Siân
full_name: Culley, Siân
last_name: Culley
- first_name: Mairi
full_name: Kilkenny, Mairi
last_name: Kilkenny
- first_name: Diorge P.
full_name: Souza, Diorge P.
last_name: Souza
- first_name: Luca
full_name: Pellegrini, Luca
last_name: Pellegrini
- first_name: Robertus A. M.
full_name: de Bruin, Robertus A. M.
last_name: de Bruin
- first_name: Ricardo
full_name: Henriques, Ricardo
last_name: Henriques
- first_name: Ambrosius P.
full_name: Snijders, Ambrosius P.
last_name: Snijders
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Ann-Christin
full_name: Lindås, Ann-Christin
last_name: Lindås
- first_name: Nicholas P.
full_name: Robinson, Nicholas P.
last_name: Robinson
- first_name: Buzz
full_name: Baum, Buzz
last_name: Baum
citation:
ama: Tarrason Risa G, Hurtig F, Bray S, et al. The proteasome controls ESCRT-III–mediated
cell division in an archaeon. Science. 2020;369(6504). doi:10.1126/science.aaz2532
apa: Tarrason Risa, G., Hurtig, F., Bray, S., Hafner, A. E., Harker-Kirschneck,
L., Faull, P., … Baum, B. (2020). The proteasome controls ESCRT-III–mediated cell
division in an archaeon. Science. American Association for the Advancement
of Science. https://doi.org/10.1126/science.aaz2532
chicago: Tarrason Risa, Gabriel, Fredrik Hurtig, Sian Bray, Anne E. Hafner, Lena
Harker-Kirschneck, Peter Faull, Colin Davis, et al. “The Proteasome Controls ESCRT-III–Mediated
Cell Division in an Archaeon.” Science. American Association for the Advancement
of Science, 2020. https://doi.org/10.1126/science.aaz2532.
ieee: G. Tarrason Risa et al., “The proteasome controls ESCRT-III–mediated
cell division in an archaeon,” Science, vol. 369, no. 6504. American Association
for the Advancement of Science, 2020.
ista: Tarrason Risa G, Hurtig F, Bray S, Hafner AE, Harker-Kirschneck L, Faull P,
Davis C, Papatziamou D, Mutavchiev DR, Fan C, Meneguello L, Arashiro Pulschen
A, Dey G, Culley S, Kilkenny M, Souza DP, Pellegrini L, de Bruin RAM, Henriques
R, Snijders AP, Šarić A, Lindås A-C, Robinson NP, Baum B. 2020. The proteasome
controls ESCRT-III–mediated cell division in an archaeon. Science. 369(6504).
mla: Tarrason Risa, Gabriel, et al. “The Proteasome Controls ESCRT-III–Mediated
Cell Division in an Archaeon.” Science, vol. 369, no. 6504, American Association
for the Advancement of Science, 2020, doi:10.1126/science.aaz2532.
short: G. Tarrason Risa, F. Hurtig, S. Bray, A.E. Hafner, L. Harker-Kirschneck,
P. Faull, C. Davis, D. Papatziamou, D.R. Mutavchiev, C. Fan, L. Meneguello, A.
Arashiro Pulschen, G. Dey, S. Culley, M. Kilkenny, D.P. Souza, L. Pellegrini,
R.A.M. de Bruin, R. Henriques, A.P. Snijders, A. Šarić, A.-C. Lindås, N.P. Robinson,
B. Baum, Science 369 (2020).
date_created: 2021-11-26T08:21:34Z
date_published: 2020-08-07T00:00:00Z
date_updated: 2021-11-26T08:58:33Z
day: '07'
doi: 10.1126/science.aaz2532
extern: '1'
external_id:
pmid:
- '32764038'
intvolume: ' 369'
issue: '6504'
keyword:
- multidisciplinary
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.biorxiv.org/content/10.1101/774273v1
month: '08'
oa: 1
oa_version: Preprint
pmid: 1
publication: Science
publication_identifier:
eissn:
- 1095-9203
issn:
- 0036-8075
publication_status: published
publisher: American Association for the Advancement of Science
quality_controlled: '1'
scopus_import: '1'
status: public
title: The proteasome controls ESCRT-III–mediated cell division in an archaeon
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 369
year: '2020'
...
---
_id: '10347'
abstract:
- lang: eng
text: Understanding the mechanism of action of compounds capable of inhibiting amyloid-fibril
formation is critical to the development of potential therapeutics against protein-misfolding
diseases. A fundamental challenge for progress is the range of possible target
species and the disparate timescales involved, since the aggregating proteins
are simultaneously the reactants, products, intermediates, and catalysts of the
reaction. It is a complex problem, therefore, to choose the states of the aggregating
proteins that should be bound by the compounds to achieve the most potent inhibition.
We present here a comprehensive kinetic theory of amyloid-aggregation inhibition
that reveals the fundamental thermodynamic and kinetic signatures characterizing
effective inhibitors by identifying quantitative relationships between the aggregation
and binding rate constants. These results provide general physical laws to guide
the design and optimization of inhibitors of amyloid-fibril formation, revealing
in particular the important role of on-rates in the binding of the inhibitors.
acknowledgement: We acknowledge support from Peterhouse, Cambridge (T.C.T.M.); the
Swiss National Science Foundation (T.C.T.M.); the Royal Society (A.S. and S.C.);
the Academy of Medical Sciences (A.S.); Sidney Sussex College, Cambridge (G.M.);
Newnham College, Cambridge (G.T.H.); the Wellcome Trust (T.P.J.K.); the Cambridge
Center for Misfolding Diseases (T.P.J.K. and M.V.); the Biotechnology and Biological
Sciences Research Council (T.P.J.K.); the Frances and Augustus Newman Foundation
(T.P.J.K.); and the Synapsis Foundation for Alzheimer’s disease (P.A.). The research
leading to these results has received funding from the European Research Council
(ERC) under the European Union’s Seventh Framework Program (FP7/2007-2013) through
the ERC Grant PhysProt (Agreement 337969).
article_processing_charge: No
article_type: original
author:
- first_name: Thomas C. T.
full_name: Michaels, Thomas C. T.
last_name: Michaels
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Georg
full_name: Meisl, Georg
last_name: Meisl
- first_name: Gabriella T.
full_name: Heller, Gabriella T.
last_name: Heller
- first_name: Samo
full_name: Curk, Samo
last_name: Curk
- first_name: Paolo
full_name: Arosio, Paolo
last_name: Arosio
- first_name: Sara
full_name: Linse, Sara
last_name: Linse
- first_name: Christopher M.
full_name: Dobson, Christopher M.
last_name: Dobson
- first_name: Michele
full_name: Vendruscolo, Michele
last_name: Vendruscolo
- first_name: Tuomas P. J.
full_name: Knowles, Tuomas P. J.
last_name: Knowles
citation:
ama: Michaels TCT, Šarić A, Meisl G, et al. Thermodynamic and kinetic design principles
for amyloid-aggregation inhibitors. Proceedings of the National Academy of
Sciences. 2020;117(39):24251-24257. doi:10.1073/pnas.2006684117
apa: Michaels, T. C. T., Šarić, A., Meisl, G., Heller, G. T., Curk, S., Arosio,
P., … Knowles, T. P. J. (2020). Thermodynamic and kinetic design principles for
amyloid-aggregation inhibitors. Proceedings of the National Academy of Sciences.
National Academy of Sciences. https://doi.org/10.1073/pnas.2006684117
chicago: Michaels, Thomas C. T., Anđela Šarić, Georg Meisl, Gabriella T. Heller,
Samo Curk, Paolo Arosio, Sara Linse, Christopher M. Dobson, Michele Vendruscolo,
and Tuomas P. J. Knowles. “Thermodynamic and Kinetic Design Principles for Amyloid-Aggregation
Inhibitors.” Proceedings of the National Academy of Sciences. National
Academy of Sciences, 2020. https://doi.org/10.1073/pnas.2006684117.
ieee: T. C. T. Michaels et al., “Thermodynamic and kinetic design principles
for amyloid-aggregation inhibitors,” Proceedings of the National Academy of
Sciences, vol. 117, no. 39. National Academy of Sciences, pp. 24251–24257,
2020.
ista: Michaels TCT, Šarić A, Meisl G, Heller GT, Curk S, Arosio P, Linse S, Dobson
CM, Vendruscolo M, Knowles TPJ. 2020. Thermodynamic and kinetic design principles
for amyloid-aggregation inhibitors. Proceedings of the National Academy of Sciences.
117(39), 24251–24257.
mla: Michaels, Thomas C. T., et al. “Thermodynamic and Kinetic Design Principles
for Amyloid-Aggregation Inhibitors.” Proceedings of the National Academy of
Sciences, vol. 117, no. 39, National Academy of Sciences, 2020, pp. 24251–57,
doi:10.1073/pnas.2006684117.
short: T.C.T. Michaels, A. Šarić, G. Meisl, G.T. Heller, S. Curk, P. Arosio, S.
Linse, C.M. Dobson, M. Vendruscolo, T.P.J. Knowles, Proceedings of the National
Academy of Sciences 117 (2020) 24251–24257.
date_created: 2021-11-26T07:48:27Z
date_published: 2020-09-14T00:00:00Z
date_updated: 2021-11-26T08:59:06Z
day: '14'
doi: 10.1073/pnas.2006684117
extern: '1'
external_id:
pmid:
- '32929030'
intvolume: ' 117'
issue: '39'
keyword:
- multidisciplinary
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.biorxiv.org/content/10.1101/2020.02.22.960716
month: '09'
oa: 1
oa_version: Published Version
page: 24251-24257
pmid: 1
publication: Proceedings of the National Academy of Sciences
publication_identifier:
eissn:
- 1091-6490
issn:
- 0027-8424
publication_status: published
publisher: National Academy of Sciences
quality_controlled: '1'
scopus_import: '1'
status: public
title: Thermodynamic and kinetic design principles for amyloid-aggregation inhibitors
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 117
year: '2020'
...
---
_id: '10351'
abstract:
- lang: eng
text: Oligomeric species populated during the aggregation of the Aβ42 peptide have
been identified as potent cytotoxins linked to Alzheimer’s disease, but the fundamental
molecular pathways that control their dynamics have yet to be elucidated. By developing
a general approach that combines theory, experiment and simulation, we reveal,
in molecular detail, the mechanisms of Aβ42 oligomer dynamics during amyloid fibril
formation. Even though all mature amyloid fibrils must originate as oligomers,
we found that most Aβ42 oligomers dissociate into their monomeric precursors without
forming new fibrils. Only a minority of oligomers converts into fibrillar structures.
Moreover, the heterogeneous ensemble of oligomeric species interconverts on timescales
comparable to those of aggregation. Our results identify fundamentally new steps
that could be targeted by therapeutic interventions designed to combat protein
misfolding diseases.
acknowledgement: We acknowledge support from Peterhouse (T.C.T.M.), the Swiss National
Science foundation (T.C.T.M.), the Royal Society (A.Š.), the Academy of Medical
Sciences (A.Š.), the UCL Institute for the Physics of Living Systems (S.C.), Sidney
Sussex College (G.M.), the Wellcome Trust (A.Š., M.V., C.M.D. and T.P.J.K.), the
Schiff Foundation (A.J.D.), the Cambridge Centre for Misfolding Diseases (M.V.,
C.M.D. and T.P.J.K.), the BBSRC (C.M.D. and T.P.J.K.), the Frances and Augustus
Newman Foundation (T.P.J.K.), the Swedish Research Council (S.L.) and the ERC grant
MAMBA (S.L., agreement no. 340890). The research that led to these results received
funding from the European Research Council under the European Union’s Seventh Framework
Programme (FP7/2007-2013) through the ERC grant PhysProt (agreement no. 337969).
article_processing_charge: No
article_type: original
author:
- first_name: Thomas C. T.
full_name: Michaels, Thomas C. T.
last_name: Michaels
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Samo
full_name: Curk, Samo
last_name: Curk
- first_name: Katja
full_name: Bernfur, Katja
last_name: Bernfur
- first_name: Paolo
full_name: Arosio, Paolo
last_name: Arosio
- first_name: Georg
full_name: Meisl, Georg
last_name: Meisl
- first_name: Alexander J.
full_name: Dear, Alexander J.
last_name: Dear
- first_name: Samuel I. A.
full_name: Cohen, Samuel I. A.
last_name: Cohen
- first_name: Christopher M.
full_name: Dobson, Christopher M.
last_name: Dobson
- first_name: Michele
full_name: Vendruscolo, Michele
last_name: Vendruscolo
- first_name: Sara
full_name: Linse, Sara
last_name: Linse
- first_name: Tuomas P. J.
full_name: Knowles, Tuomas P. J.
last_name: Knowles
citation:
ama: Michaels TCT, Šarić A, Curk S, et al. Dynamics of oligomer populations formed
during the aggregation of Alzheimer’s Aβ42 peptide. Nature Chemistry. 2020;12(5):445-451.
doi:10.1038/s41557-020-0452-1
apa: Michaels, T. C. T., Šarić, A., Curk, S., Bernfur, K., Arosio, P., Meisl, G.,
… Knowles, T. P. J. (2020). Dynamics of oligomer populations formed during the
aggregation of Alzheimer’s Aβ42 peptide. Nature Chemistry. Springer Nature.
https://doi.org/10.1038/s41557-020-0452-1
chicago: Michaels, Thomas C. T., Anđela Šarić, Samo Curk, Katja Bernfur, Paolo Arosio,
Georg Meisl, Alexander J. Dear, et al. “Dynamics of Oligomer Populations Formed
during the Aggregation of Alzheimer’s Aβ42 Peptide.” Nature Chemistry.
Springer Nature, 2020. https://doi.org/10.1038/s41557-020-0452-1.
ieee: T. C. T. Michaels et al., “Dynamics of oligomer populations formed
during the aggregation of Alzheimer’s Aβ42 peptide,” Nature Chemistry,
vol. 12, no. 5. Springer Nature, pp. 445–451, 2020.
ista: Michaels TCT, Šarić A, Curk S, Bernfur K, Arosio P, Meisl G, Dear AJ, Cohen
SIA, Dobson CM, Vendruscolo M, Linse S, Knowles TPJ. 2020. Dynamics of oligomer
populations formed during the aggregation of Alzheimer’s Aβ42 peptide. Nature
Chemistry. 12(5), 445–451.
mla: Michaels, Thomas C. T., et al. “Dynamics of Oligomer Populations Formed during
the Aggregation of Alzheimer’s Aβ42 Peptide.” Nature Chemistry, vol. 12,
no. 5, Springer Nature, 2020, pp. 445–51, doi:10.1038/s41557-020-0452-1.
short: T.C.T. Michaels, A. Šarić, S. Curk, K. Bernfur, P. Arosio, G. Meisl, A.J.
Dear, S.I.A. Cohen, C.M. Dobson, M. Vendruscolo, S. Linse, T.P.J. Knowles, Nature
Chemistry 12 (2020) 445–451.
date_created: 2021-11-26T09:15:13Z
date_published: 2020-04-13T00:00:00Z
date_updated: 2021-11-26T11:21:08Z
day: '13'
doi: 10.1038/s41557-020-0452-1
extern: '1'
external_id:
pmid:
- '32303714'
intvolume: ' 12'
issue: '5'
keyword:
- general chemical engineering
- general chemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.biorxiv.org/content/10.1101/2020.01.08.897488
month: '04'
oa: 1
oa_version: None
page: 445-451
pmid: 1
publication: Nature Chemistry
publication_identifier:
eissn:
- 1755-4349
issn:
- 1755-4330
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
related_material:
link:
- relation: erratum
url: https://doi.org/10.1038/s41557-020-0468-6
scopus_import: '1'
status: public
title: Dynamics of oligomer populations formed during the aggregation of Alzheimer’s
Aβ42 peptide
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 12
year: '2020'
...
---
_id: '10348'
abstract:
- lang: eng
text: The endosomal sorting complex required for transport-III (ESCRT-III) catalyzes
membrane fission from within membrane necks, a process that is essential for many
cellular functions, from cell division to lysosome degradation and autophagy.
How it breaks membranes, though, remains unknown. Here, we characterize a sequential
polymerization of ESCRT-III subunits that, driven by a recruitment cascade and
by continuous subunit-turnover powered by the ATPase Vps4, induces membrane deformation
and fission. During this process, the exchange of Vps24 for Did2 induces a tilt
in the polymer-membrane interface, which triggers transition from flat spiral
polymers to helical filament to drive the formation of membrane protrusions, and
ends with the formation of a highly constricted Did2-Ist1 co-polymer that we show
is competent to promote fission when bound on the inside of membrane necks. Overall,
our results suggest a mechanism of stepwise changes in ESCRT-III filament structure
and mechanical properties via exchange of the filament subunits to catalyze ESCRT-III
activity.
acknowledgement: The authors thank Nicolas Chiaruttini, Jean Gruenberg, and Lena Harker-Kirschneck
for careful correction of this manuscript and helpful discussions. The authors want
to thank the NCCR Chemical Biology for constant support during this project. A.R.
acknowledges funding from the Swiss National Fund for Research (31003A_130520, 31003A_149975,
and 31003A_173087) and the European Research Council Consolidator (311536). A.Š.
acknowledges the European Research Council (802960). B.B. thanks the BBSRC (BB/K009001/1)
and Wellcome Trust (203276/Z/16/Z) for support. J.M.v.F. acknowledges funding through
an EMBO Long-Term Fellowship (ALTF 1065-2015), the European Commission FP7 (Marie
Curie Actions, LTFCOFUND2013, and GA-2013-609409), and a Transitional Postdoc fellowship
(2015/345) from the Swiss SystemsX.ch initiative, evaluated by the Swiss National
Science Foundation and Swiss National Science Foundation Research (SNSF SINERGIA
160728/1 [leader, Sophie Martin]).
article_processing_charge: No
article_type: original
author:
- first_name: Anna-Katharina
full_name: Pfitzner, Anna-Katharina
last_name: Pfitzner
- first_name: Vincent
full_name: Mercier, Vincent
last_name: Mercier
- first_name: Xiuyun
full_name: Jiang, Xiuyun
last_name: Jiang
- first_name: Joachim
full_name: Moser von Filseck, Joachim
last_name: Moser von Filseck
- first_name: Buzz
full_name: Baum, Buzz
last_name: Baum
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Aurélien
full_name: Roux, Aurélien
last_name: Roux
citation:
ama: Pfitzner A-K, Mercier V, Jiang X, et al. An ESCRT-III polymerization sequence
drives membrane deformation and fission. Cell. 2020;182(5):1140-1155.e18.
doi:10.1016/j.cell.2020.07.021
apa: Pfitzner, A.-K., Mercier, V., Jiang, X., Moser von Filseck, J., Baum, B., Šarić,
A., & Roux, A. (2020). An ESCRT-III polymerization sequence drives membrane
deformation and fission. Cell. Elsevier. https://doi.org/10.1016/j.cell.2020.07.021
chicago: Pfitzner, Anna-Katharina, Vincent Mercier, Xiuyun Jiang, Joachim Moser
von Filseck, Buzz Baum, Anđela Šarić, and Aurélien Roux. “An ESCRT-III Polymerization
Sequence Drives Membrane Deformation and Fission.” Cell. Elsevier, 2020.
https://doi.org/10.1016/j.cell.2020.07.021.
ieee: A.-K. Pfitzner et al., “An ESCRT-III polymerization sequence drives
membrane deformation and fission,” Cell, vol. 182, no. 5. Elsevier, p.
1140–1155.e18, 2020.
ista: Pfitzner A-K, Mercier V, Jiang X, Moser von Filseck J, Baum B, Šarić A, Roux
A. 2020. An ESCRT-III polymerization sequence drives membrane deformation and
fission. Cell. 182(5), 1140–1155.e18.
mla: Pfitzner, Anna-Katharina, et al. “An ESCRT-III Polymerization Sequence Drives
Membrane Deformation and Fission.” Cell, vol. 182, no. 5, Elsevier, 2020,
p. 1140–1155.e18, doi:10.1016/j.cell.2020.07.021.
short: A.-K. Pfitzner, V. Mercier, X. Jiang, J. Moser von Filseck, B. Baum, A. Šarić,
A. Roux, Cell 182 (2020) 1140–1155.e18.
date_created: 2021-11-26T08:02:27Z
date_published: 2020-08-18T00:00:00Z
date_updated: 2021-11-26T08:58:37Z
day: '18'
doi: 10.1016/j.cell.2020.07.021
extern: '1'
external_id:
pmid:
- '32814015'
intvolume: ' 182'
issue: '5'
keyword:
- general biochemistry
- genetics and molecular biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.sciencedirect.com/science/article/pii/S0092867420309296
month: '08'
oa: 1
oa_version: Published Version
page: 1140-1155.e18
pmid: 1
publication: Cell
publication_identifier:
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: An ESCRT-III polymerization sequence drives membrane deformation and fission
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 182
year: '2020'
...
---
_id: '10352'
abstract:
- lang: eng
text: In the nuclear pore complex, intrinsically disordered nuclear pore proteins
(FG Nups) form a selective barrier for transport into and out of the cell nucleus,
in a way that remains poorly understood. The collective FG Nup behavior has long
been conceptualized either as a polymer brush, dominated by entropic and excluded-volume
(repulsive) interactions, or as a hydrogel, dominated by cohesive (attractive)
interactions between FG Nups. Here we compare mesoscale computational simulations
with a wide range of experimental data to demonstrate that FG Nups are at the
crossover point between these two regimes. Specifically, we find that repulsive
and attractive interactions are balanced, resulting in morphologies and dynamics
that are close to those of ideal polymer chains. We demonstrate that this property
of FG Nups yields sufficient cohesion to seal the transport barrier, and yet maintains
fast dynamics at the molecular scale, permitting the rapid polymer rearrangements
needed for transport events.
acknowledgement: We thank Dino Osmanović (MIT), Roy Beck (Tel-Aviv), Larissa Kapinos
(Basel), Roderick Lim (Basel), Ralf Richter (Leeds), and Anton Zilman (Toronto)
for discussions. This work was funded by the Royal Society (A.Š.) and the UK Engineering
and Physical Sciences Research Council (EP/L504889/1, B.W.H.).
article_number: '022420'
article_processing_charge: No
article_type: original
author:
- first_name: Luke K.
full_name: Davis, Luke K.
last_name: Davis
- first_name: Ian J.
full_name: Ford, Ian J.
last_name: Ford
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Bart W.
full_name: Hoogenboom, Bart W.
last_name: Hoogenboom
citation:
ama: Davis LK, Ford IJ, Šarić A, Hoogenboom BW. Intrinsically disordered nuclear
pore proteins show ideal-polymer morphologies and dynamics. Physical Review
E. 2020;101(2). doi:10.1103/physreve.101.022420
apa: Davis, L. K., Ford, I. J., Šarić, A., & Hoogenboom, B. W. (2020). Intrinsically
disordered nuclear pore proteins show ideal-polymer morphologies and dynamics.
Physical Review E. American Physical Society. https://doi.org/10.1103/physreve.101.022420
chicago: Davis, Luke K., Ian J. Ford, Anđela Šarić, and Bart W. Hoogenboom. “Intrinsically
Disordered Nuclear Pore Proteins Show Ideal-Polymer Morphologies and Dynamics.”
Physical Review E. American Physical Society, 2020. https://doi.org/10.1103/physreve.101.022420.
ieee: L. K. Davis, I. J. Ford, A. Šarić, and B. W. Hoogenboom, “Intrinsically disordered
nuclear pore proteins show ideal-polymer morphologies and dynamics,” Physical
Review E, vol. 101, no. 2. American Physical Society, 2020.
ista: Davis LK, Ford IJ, Šarić A, Hoogenboom BW. 2020. Intrinsically disordered
nuclear pore proteins show ideal-polymer morphologies and dynamics. Physical Review
E. 101(2), 022420.
mla: Davis, Luke K., et al. “Intrinsically Disordered Nuclear Pore Proteins Show
Ideal-Polymer Morphologies and Dynamics.” Physical Review E, vol. 101,
no. 2, 022420, American Physical Society, 2020, doi:10.1103/physreve.101.022420.
short: L.K. Davis, I.J. Ford, A. Šarić, B.W. Hoogenboom, Physical Review E 101 (2020).
date_created: 2021-11-26T09:41:04Z
date_published: 2020-02-28T00:00:00Z
date_updated: 2021-11-26T11:21:16Z
day: '28'
doi: 10.1103/physreve.101.022420
extern: '1'
external_id:
pmid:
- '32168597'
intvolume: ' 101'
issue: '2'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.biorxiv.org/content/10.1101/571687
month: '02'
oa: 1
oa_version: Preprint
pmid: 1
publication: Physical Review E
publication_identifier:
eissn:
- 2470-0053
issn:
- 2470-0045
publication_status: published
publisher: American Physical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Intrinsically disordered nuclear pore proteins show ideal-polymer morphologies
and dynamics
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 101
year: '2020'
...
---
_id: '10353'
abstract:
- lang: eng
text: Experiments have suggested that bacterial mechanosensitive channels separate
into 2D clusters, the role of which is unclear. By developing a coarse-grained
computer model we find that clustering promotes the channel closure, which is
highly dependent on the channel concentration and membrane stress. This behaviour
yields a tightly regulated gating system, whereby at high tensions channels gate
individually, and at lower tensions the channels spontaneously aggregate and inactivate.
We implement this positive feedback into the model for cell volume regulation,
and find that the channel clustering protects the cell against excessive loss
of cytoplasmic content.
acknowledgement: We thank Samantha Miller, Bert Poolman, and the members of Šarić
and Pilizota laboratories for useful discussion. We acknowledge support from the
Engineering and Physical Sciences Research Council (A.P. and A.Š.), the UCL Institute
for the Physics of Living Systems (A.P. and A.Š.), Darwin Trust of University of
Edinburgh (H.S.), Industrial Biotechnology Innovation Centre (H.S. and T.P.), BBSRC
Council Crossing Biological Membrane Network (H.S. and T.P.), BBSRC/EPSRC/MRC Synthetic
Biology Research Centre (T.P.), and the Royal Society (A.Š.).
article_number: '048102'
article_processing_charge: No
article_type: original
author:
- first_name: Alexandru
full_name: Paraschiv, Alexandru
last_name: Paraschiv
- first_name: Smitha
full_name: Hegde, Smitha
last_name: Hegde
- first_name: Raman
full_name: Ganti, Raman
last_name: Ganti
- first_name: Teuta
full_name: Pilizota, Teuta
last_name: Pilizota
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
citation:
ama: Paraschiv A, Hegde S, Ganti R, Pilizota T, Šarić A. Dynamic clustering regulates
activity of mechanosensitive membrane channels. Physical Review Letters.
2020;124(4). doi:10.1103/physrevlett.124.048102
apa: Paraschiv, A., Hegde, S., Ganti, R., Pilizota, T., & Šarić, A. (2020).
Dynamic clustering regulates activity of mechanosensitive membrane channels. Physical
Review Letters. American Physical Society. https://doi.org/10.1103/physrevlett.124.048102
chicago: Paraschiv, Alexandru, Smitha Hegde, Raman Ganti, Teuta Pilizota, and Anđela
Šarić. “Dynamic Clustering Regulates Activity of Mechanosensitive Membrane Channels.”
Physical Review Letters. American Physical Society, 2020. https://doi.org/10.1103/physrevlett.124.048102.
ieee: A. Paraschiv, S. Hegde, R. Ganti, T. Pilizota, and A. Šarić, “Dynamic clustering
regulates activity of mechanosensitive membrane channels,” Physical Review
Letters, vol. 124, no. 4. American Physical Society, 2020.
ista: Paraschiv A, Hegde S, Ganti R, Pilizota T, Šarić A. 2020. Dynamic clustering
regulates activity of mechanosensitive membrane channels. Physical Review Letters.
124(4), 048102.
mla: Paraschiv, Alexandru, et al. “Dynamic Clustering Regulates Activity of Mechanosensitive
Membrane Channels.” Physical Review Letters, vol. 124, no. 4, 048102, American
Physical Society, 2020, doi:10.1103/physrevlett.124.048102.
short: A. Paraschiv, S. Hegde, R. Ganti, T. Pilizota, A. Šarić, Physical Review
Letters 124 (2020).
date_created: 2021-11-26T09:57:01Z
date_published: 2020-01-31T00:00:00Z
date_updated: 2021-11-26T11:21:12Z
day: '31'
doi: 10.1103/physrevlett.124.048102
extern: '1'
external_id:
pmid:
- '32058787'
intvolume: ' 124'
issue: '4'
keyword:
- general physics and astronomy
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.biorxiv.org/content/10.1101/553248
month: '01'
oa: 1
oa_version: Preprint
pmid: 1
publication: Physical Review Letters
publication_identifier:
eissn:
- 1079-7114
issn:
- 0031-9007
publication_status: published
publisher: American Physical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Dynamic clustering regulates activity of mechanosensitive membrane channels
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 124
year: '2020'
...
---
_id: '10354'
abstract:
- lang: eng
text: "Background\r\nESCRT-III is a membrane remodelling filament with the unique
ability to cut membranes from the inside of the membrane neck. It is essential
for the final stage of cell division, the formation of vesicles, the release of
viruses, and membrane repair. Distinct from other cytoskeletal filaments, ESCRT-III
filaments do not consume energy themselves, but work in conjunction with another
ATP-consuming complex. Despite rapid progress in describing the cell biology of
ESCRT-III, we lack an understanding of the physical mechanisms behind its force
production and membrane remodelling.\r\nResults\r\nHere we present a minimal coarse-grained
model that captures all the experimentally reported cases of ESCRT-III driven
membrane sculpting, including the formation of downward and upward cones and tubules.
This model suggests that a change in the geometry of membrane bound ESCRT-III
filaments—from a flat spiral to a 3D helix—drives membrane deformation. We then
show that such repetitive filament geometry transitions can induce the fission
of cargo-containing vesicles.\r\nConclusions\r\nOur model provides a general physical
mechanism that explains the full range of ESCRT-III-dependent membrane remodelling
and scission events observed in cells. This mechanism for filament force production
is distinct from the mechanisms described for other cytoskeletal elements discovered
so far. The mechanistic principles revealed here suggest new ways of manipulating
ESCRT-III-driven processes in cells and could be used to guide the engineering
of synthetic membrane-sculpting systems."
acknowledgement: We thank Jeremy Carlton, Mike Staddon, Geraint Harker, and the Wellcome
Trust Consortium “Archaeal Origins of Eukaryotic Cell Organisation” for fruitful
conversations. We thank Peter Wirnsberger and Tine Curk for discussions about the
membrane model implementation.
article_number: '82'
article_processing_charge: No
article_type: original
author:
- first_name: Lena
full_name: Harker-Kirschneck, Lena
last_name: Harker-Kirschneck
- first_name: Buzz
full_name: Baum, Buzz
last_name: Baum
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
citation:
ama: Harker-Kirschneck L, Baum B, Šarić A. Changes in ESCRT-III filament geometry
drive membrane remodelling and fission in silico. BMC Biology. 2019;17(1).
doi:10.1186/s12915-019-0700-2
apa: Harker-Kirschneck, L., Baum, B., & Šarić, A. (2019). Changes in ESCRT-III
filament geometry drive membrane remodelling and fission in silico. BMC Biology.
Springer Nature. https://doi.org/10.1186/s12915-019-0700-2
chicago: Harker-Kirschneck, Lena, Buzz Baum, and Anđela Šarić. “Changes in ESCRT-III
Filament Geometry Drive Membrane Remodelling and Fission in Silico.” BMC Biology.
Springer Nature, 2019. https://doi.org/10.1186/s12915-019-0700-2.
ieee: L. Harker-Kirschneck, B. Baum, and A. Šarić, “Changes in ESCRT-III filament
geometry drive membrane remodelling and fission in silico,” BMC Biology,
vol. 17, no. 1. Springer Nature, 2019.
ista: Harker-Kirschneck L, Baum B, Šarić A. 2019. Changes in ESCRT-III filament
geometry drive membrane remodelling and fission in silico. BMC Biology. 17(1),
82.
mla: Harker-Kirschneck, Lena, et al. “Changes in ESCRT-III Filament Geometry Drive
Membrane Remodelling and Fission in Silico.” BMC Biology, vol. 17, no.
1, 82, Springer Nature, 2019, doi:10.1186/s12915-019-0700-2.
short: L. Harker-Kirschneck, B. Baum, A. Šarić, BMC Biology 17 (2019).
date_created: 2021-11-26T11:25:03Z
date_published: 2019-10-22T00:00:00Z
date_updated: 2021-11-26T11:54:29Z
day: '22'
ddc:
- '570'
doi: 10.1186/s12915-019-0700-2
extern: '1'
external_id:
pmid:
- '31640700'
file:
- access_level: open_access
checksum: 31d8bae55a376d30925f53f7e1a02396
content_type: application/pdf
creator: cchlebak
date_created: 2021-11-26T11:37:54Z
date_updated: 2021-11-26T11:37:54Z
file_id: '10356'
file_name: 2019_BMCBio_Harker_Kirschneck.pdf
file_size: 1648926
relation: main_file
success: 1
file_date_updated: 2021-11-26T11:37:54Z
has_accepted_license: '1'
intvolume: ' 17'
issue: '1'
keyword:
- cell biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.biorxiv.org/content/10.1101/559898
month: '10'
oa: 1
oa_version: Published Version
pmid: 1
publication: BMC Biology
publication_identifier:
issn:
- 1741-7007
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Changes in ESCRT-III filament geometry drive membrane remodelling and fission
in silico
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 17
year: '2019'
...
---
_id: '10355'
abstract:
- lang: eng
text: The molecular machinery of life is largely created via self-organisation of
individual molecules into functional assemblies. Minimal coarse-grained models,
in which a whole macromolecule is represented by a small number of particles,
can be of great value in identifying the main driving forces behind self-organisation
in cell biology. Such models can incorporate data from both molecular and continuum
scales, and their results can be directly compared to experiments. Here we review
the state of the art of models for studying the formation and biological function
of macromolecular assemblies in living organisms. We outline the key ingredients
of each model and their main findings. We illustrate the contribution of this
class of simulations to identifying the physical mechanisms behind life and diseases,
and discuss their future developments.
acknowledgement: We acknowledge funding from EPSRC (A.E.H. and A.Š.), the Academy
of Medical Sciences (J.K. and A.Š.), the Wellcome Trust (J.K. and A.Š.), and the
Royal Society (A.Š.). We thank Shiladitya Banerjee and Nikola Ojkic for critically
reading the manuscript, and Claudia Flandoli for helping us with figures and illustrations.
article_processing_charge: No
article_type: original
author:
- first_name: Anne E
full_name: Hafner, Anne E
last_name: Hafner
- first_name: Johannes
full_name: Krausser, Johannes
last_name: Krausser
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
citation:
ama: Hafner AE, Krausser J, Šarić A. Minimal coarse-grained models for molecular
self-organisation in biology. Current Opinion in Structural Biology. 2019;58:43-52.
doi:10.1016/j.sbi.2019.05.018
apa: Hafner, A. E., Krausser, J., & Šarić, A. (2019). Minimal coarse-grained
models for molecular self-organisation in biology. Current Opinion in Structural
Biology. Elsevier. https://doi.org/10.1016/j.sbi.2019.05.018
chicago: Hafner, Anne E, Johannes Krausser, and Anđela Šarić. “Minimal Coarse-Grained
Models for Molecular Self-Organisation in Biology.” Current Opinion in Structural
Biology. Elsevier, 2019. https://doi.org/10.1016/j.sbi.2019.05.018.
ieee: A. E. Hafner, J. Krausser, and A. Šarić, “Minimal coarse-grained models for
molecular self-organisation in biology,” Current Opinion in Structural Biology,
vol. 58. Elsevier, pp. 43–52, 2019.
ista: Hafner AE, Krausser J, Šarić A. 2019. Minimal coarse-grained models for molecular
self-organisation in biology. Current Opinion in Structural Biology. 58, 43–52.
mla: Hafner, Anne E., et al. “Minimal Coarse-Grained Models for Molecular Self-Organisation
in Biology.” Current Opinion in Structural Biology, vol. 58, Elsevier,
2019, pp. 43–52, doi:10.1016/j.sbi.2019.05.018.
short: A.E. Hafner, J. Krausser, A. Šarić, Current Opinion in Structural Biology
58 (2019) 43–52.
date_created: 2021-11-26T11:33:21Z
date_published: 2019-06-18T00:00:00Z
date_updated: 2021-11-26T11:54:25Z
day: '18'
doi: 10.1016/j.sbi.2019.05.018
extern: '1'
external_id:
pmid:
- '31226513'
intvolume: ' 58'
keyword:
- molecular biology
- structural biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1906.09349
month: '06'
oa: 1
oa_version: Preprint
page: 43-52
pmid: 1
publication: Current Opinion in Structural Biology
publication_identifier:
issn:
- 0959-440X
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Minimal coarse-grained models for molecular self-organisation in biology
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 58
year: '2019'
...
---
_id: '10362'
abstract:
- lang: eng
text: Nuclear pore complexes (NPCs) form gateways that control molecular exchange
between the nucleus and the cytoplasm. They impose a diffusion barrier to macromolecules
and enable the selective transport of nuclear transport receptors with bound cargo.
The underlying mechanisms that establish these permeability properties remain
to be fully elucidated but require unstructured nuclear pore proteins rich in
Phe-Gly (FG)-repeat domains of different types, such as FxFG and GLFG. While physical
modeling and in vitro approaches have provided a framework for explaining how
the FG network contributes to the barrier and transport properties of the NPC,
it remains unknown whether the number and/or the spatial positioning of different
FG-domains along a cylindrical, ∼40 nm diameter transport channel contributes
to their collective properties and function. To begin to answer these questions,
we have used DNA origami to build a cylinder that mimics the dimensions of the
central transport channel and can house a specified number of FG-domains at specific
positions with easily tunable design parameters, such as grafting density and
topology. We find the overall morphology of the FG-domain assemblies to be dependent
on their chemical composition, determined by the type and density of FG-repeat,
and on their architectural confinement provided by the DNA cylinder, largely consistent
with here presented molecular dynamics simulations based on a coarse-grained polymer
model. In addition, high-speed atomic force microscopy reveals local and reversible
FG-domain condensation that transiently occludes the lumen of the DNA central
channel mimics, suggestive of how the NPC might establish its permeability properties.
acknowledgement: We thank J. Edel and members of the Lusk, Lin and Hoogenboom lab
for discussion and acknowledge A. Pyne and R. Thorogate for support carrying out
the AFM experiments. This work was funded by the NIH (R21GM109466 to CPL, CL and
TJM, DP2GM114830 to CL, RO1GM105672 to CPL, and T32GM007223 to PDEF) and the UK
Engineering and Physical Sciences Research Council (EP/L015277/1, EP/L504889/1,
and EP/M028100/1).
article_processing_charge: No
article_type: original
author:
- first_name: Patrick D. Ellis
full_name: Fisher, Patrick D. Ellis
last_name: Fisher
- first_name: Qi
full_name: Shen, Qi
last_name: Shen
- first_name: Bernice
full_name: Akpinar, Bernice
last_name: Akpinar
- first_name: Luke K.
full_name: Davis, Luke K.
last_name: Davis
- first_name: Kenny Kwok Hin
full_name: Chung, Kenny Kwok Hin
last_name: Chung
- first_name: David
full_name: Baddeley, David
last_name: Baddeley
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Thomas J.
full_name: Melia, Thomas J.
last_name: Melia
- first_name: Bart W.
full_name: Hoogenboom, Bart W.
last_name: Hoogenboom
- first_name: Chenxiang
full_name: Lin, Chenxiang
last_name: Lin
- first_name: C. Patrick
full_name: Lusk, C. Patrick
last_name: Lusk
citation:
ama: Fisher PDE, Shen Q, Akpinar B, et al. A Programmable DNA origami platform for
organizing intrinsically disordered nucleoporins within nanopore confinement.
ACS Nano. 2018;12(2):1508-1518. doi:10.1021/acsnano.7b08044
apa: Fisher, P. D. E., Shen, Q., Akpinar, B., Davis, L. K., Chung, K. K. H., Baddeley,
D., … Lusk, C. P. (2018). A Programmable DNA origami platform for organizing intrinsically
disordered nucleoporins within nanopore confinement. ACS Nano. American
Chemical Society. https://doi.org/10.1021/acsnano.7b08044
chicago: Fisher, Patrick D. Ellis, Qi Shen, Bernice Akpinar, Luke K. Davis, Kenny
Kwok Hin Chung, David Baddeley, Anđela Šarić, et al. “A Programmable DNA Origami
Platform for Organizing Intrinsically Disordered Nucleoporins within Nanopore
Confinement.” ACS Nano. American Chemical Society, 2018. https://doi.org/10.1021/acsnano.7b08044.
ieee: P. D. E. Fisher et al., “A Programmable DNA origami platform for organizing
intrinsically disordered nucleoporins within nanopore confinement,” ACS Nano,
vol. 12, no. 2. American Chemical Society, pp. 1508–1518, 2018.
ista: Fisher PDE, Shen Q, Akpinar B, Davis LK, Chung KKH, Baddeley D, Šarić A, Melia
TJ, Hoogenboom BW, Lin C, Lusk CP. 2018. A Programmable DNA origami platform for
organizing intrinsically disordered nucleoporins within nanopore confinement.
ACS Nano. 12(2), 1508–1518.
mla: Fisher, Patrick D. Ellis, et al. “A Programmable DNA Origami Platform for Organizing
Intrinsically Disordered Nucleoporins within Nanopore Confinement.” ACS Nano,
vol. 12, no. 2, American Chemical Society, 2018, pp. 1508–18, doi:10.1021/acsnano.7b08044.
short: P.D.E. Fisher, Q. Shen, B. Akpinar, L.K. Davis, K.K.H. Chung, D. Baddeley,
A. Šarić, T.J. Melia, B.W. Hoogenboom, C. Lin, C.P. Lusk, ACS Nano 12 (2018) 1508–1518.
date_created: 2021-11-26T15:15:00Z
date_published: 2018-01-19T00:00:00Z
date_updated: 2021-11-26T15:57:02Z
day: '19'
doi: 10.1021/acsnano.7b08044
extern: '1'
external_id:
pmid:
- '29350911'
intvolume: ' 12'
issue: '2'
keyword:
- general physics and astronomy
language:
- iso: eng
month: '01'
oa_version: None
page: 1508-1518
pmid: 1
publication: ACS Nano
publication_identifier:
eissn:
- 1936-086X
issn:
- 1936-0851
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: A Programmable DNA origami platform for organizing intrinsically disordered
nucleoporins within nanopore confinement
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 12
year: '2018'
...
---
_id: '10360'
abstract:
- lang: eng
text: Mapping free-energy landscapes has proved to be a powerful tool for studying
reaction mechanisms. Many complex biomolecular assembly processes, however, have
remained challenging to access using this approach, including the aggregation
of peptides and proteins into amyloid fibrils implicated in a range of disorders.
Here, we generalize the strategy used to probe free-energy landscapes in protein
folding to determine the activation energies and entropies that characterize each
of the molecular steps in the aggregation of the amyloid-β peptide (Aβ42), which
is associated with Alzheimer’s disease. Our results reveal that interactions between
monomeric Aβ42 and amyloid fibrils during fibril-dependent secondary nucleation
fundamentally reverse the thermodynamic signature of this process relative to
primary nucleation, even though both processes generate aggregates from soluble
peptides. By mapping the energetic and entropic contributions along the reaction
trajectories, we show that the catalytic efficiency of Aβ42 fibril surfaces results
from the enthalpic stabilization of adsorbing peptides in conformations amenable
to nucleation, resulting in a dramatic lowering of the activation energy for nucleation.
acknowledgement: We thank B. Jönsson and I. André for helpful discussions. We acknowledge
financial support from the Schiff Foundation (S.I.A.C.), St John’s College, Cambridge
(S.I.A.C.), the Royal Physiographic Society (R.C.), the Research School FLÄK of
Lund University (S.L., R.C.), the Swedish Research Council (S.L.) and its Linneaus
Centre Organizing Molecular Matter (S.L.), the Crafoord Foundation (S.L.), Alzheimerfonden
(S.L.), the European Research Council (S.L.), NanoLund (S.L.), Knut and Alice Wallenberg
Foundation (S.L.), Peterhouse, Cambridge (T.C.T.M.), the Swiss National Science
Foundation (T.C.T.M.), Magdalene College, Cambridge (A.K.B.), the Leverhulme Trust
(A.K.B.), the Royal Society (A.Š.), the Academy of Medical Sciences (A.Š.), the
Wellcome Trust (C.M.D., T.P.J.K., A.Š.), and the Centre for Misfolding Diseases
(C.M.D., T.P.J.K, M.V.). A.K.B. thanks the Alzheimer Forschung Initiative (AFI).
article_processing_charge: No
article_type: original
author:
- first_name: Samuel I. A.
full_name: Cohen, Samuel I. A.
last_name: Cohen
- first_name: Risto
full_name: Cukalevski, Risto
last_name: Cukalevski
- first_name: Thomas C. T.
full_name: Michaels, Thomas C. T.
last_name: Michaels
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Mattias
full_name: Törnquist, Mattias
last_name: Törnquist
- first_name: Michele
full_name: Vendruscolo, Michele
last_name: Vendruscolo
- first_name: Christopher M.
full_name: Dobson, Christopher M.
last_name: Dobson
- first_name: Alexander K.
full_name: Buell, Alexander K.
last_name: Buell
- first_name: Tuomas P. J.
full_name: Knowles, Tuomas P. J.
last_name: Knowles
- first_name: Sara
full_name: Linse, Sara
last_name: Linse
citation:
ama: Cohen SIA, Cukalevski R, Michaels TCT, et al. Distinct thermodynamic signatures
of oligomer generation in the aggregation of the amyloid-β peptide. Nature
Chemistry. 2018;10(5):523-531. doi:10.1038/s41557-018-0023-x
apa: Cohen, S. I. A., Cukalevski, R., Michaels, T. C. T., Šarić, A., Törnquist,
M., Vendruscolo, M., … Linse, S. (2018). Distinct thermodynamic signatures of
oligomer generation in the aggregation of the amyloid-β peptide. Nature Chemistry.
Springer Nature. https://doi.org/10.1038/s41557-018-0023-x
chicago: Cohen, Samuel I. A., Risto Cukalevski, Thomas C. T. Michaels, Anđela Šarić,
Mattias Törnquist, Michele Vendruscolo, Christopher M. Dobson, Alexander K. Buell,
Tuomas P. J. Knowles, and Sara Linse. “Distinct Thermodynamic Signatures of Oligomer
Generation in the Aggregation of the Amyloid-β Peptide.” Nature Chemistry.
Springer Nature, 2018. https://doi.org/10.1038/s41557-018-0023-x.
ieee: S. I. A. Cohen et al., “Distinct thermodynamic signatures of oligomer
generation in the aggregation of the amyloid-β peptide,” Nature Chemistry,
vol. 10, no. 5. Springer Nature, pp. 523–531, 2018.
ista: Cohen SIA, Cukalevski R, Michaels TCT, Šarić A, Törnquist M, Vendruscolo M,
Dobson CM, Buell AK, Knowles TPJ, Linse S. 2018. Distinct thermodynamic signatures
of oligomer generation in the aggregation of the amyloid-β peptide. Nature Chemistry.
10(5), 523–531.
mla: Cohen, Samuel I. A., et al. “Distinct Thermodynamic Signatures of Oligomer
Generation in the Aggregation of the Amyloid-β Peptide.” Nature Chemistry,
vol. 10, no. 5, Springer Nature, 2018, pp. 523–31, doi:10.1038/s41557-018-0023-x.
short: S.I.A. Cohen, R. Cukalevski, T.C.T. Michaels, A. Šarić, M. Törnquist, M.
Vendruscolo, C.M. Dobson, A.K. Buell, T.P.J. Knowles, S. Linse, Nature Chemistry
10 (2018) 523–531.
date_created: 2021-11-26T12:41:38Z
date_published: 2018-03-26T00:00:00Z
date_updated: 2021-11-26T15:14:00Z
day: '26'
doi: 10.1038/s41557-018-0023-x
extern: '1'
external_id:
pmid:
- '29581486'
intvolume: ' 10'
issue: '5'
keyword:
- general chemical engineering
- general chemistry
language:
- iso: eng
month: '03'
oa_version: None
page: 523-531
pmid: 1
publication: Nature Chemistry
publication_identifier:
eissn:
- 1755-4349
issn:
- 1755-4330
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Distinct thermodynamic signatures of oligomer generation in the aggregation
of the amyloid-β peptide
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 10
year: '2018'
...
---
_id: '10357'
abstract:
- lang: eng
text: The misfolding and aggregation of proteins into linear fibrils is widespread
in human biology, for example, in connection with amyloid formation and the pathology
of neurodegenerative disorders such as Alzheimer’s and Parkinson’s diseases. The
oligomeric species that are formed in the early stages of protein aggregation
are of great interest, having been linked with the cellular toxicity associated
with these conditions. However, these species are not characterized in any detail
experimentally, and their properties are not well understood. Many of these species
have been found to have approximately spherical morphology and to be held together
by hydrophobic interactions. We present here an analytical statistical mechanical
model of globular oligomer formation from simple idealized amphiphilic protein
monomers and show that this correlates well with Monte Carlo simulations of oligomer
formation. We identify the controlling parameters of the model, which are closely
related to simple quantities that may be fitted directly from experiment. We predict
that globular oligomers are unlikely to form at equilibrium in many polypeptide
systems but instead form transiently in the early stages of amyloid formation.
We contrast the globular model of oligomer formation to a well-established model
of linear oligomer formation, highlighting how the differing ensemble properties
of linear and globular oligomers offer a potential strategy for characterizing
oligomers from experimental measurements.
acknowledgement: We acknowledge support from the Schiff Foundation (A.J.D.), the Royal
Society (A.Š.), the Academy of Medical Sciences and Wellcome Trust (A.Š.), Peterhouse,
Cambridge (T.C.T.M.), the Swiss National Science foundation (T.C.T.M.), the Wellcome
Trust (T.P.J.K.), the Cambridge Centre for Misfolding Diseases (T.P.J.K.), the BBSRC
(T.P.J.K.), the Frances and Augustus Newman foundation (T.P.J.K.). The research
leading to these results has received funding from the European Research Council
under the European Union’s Seventh Framework Programme (Grant FP7/2007-2013) through
the ERC Grant PhysProt (Agreement No. 337969). We thank Daan Frenkel for several
useful discussions.
article_processing_charge: No
article_type: original
author:
- first_name: Alexander J.
full_name: Dear, Alexander J.
last_name: Dear
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Thomas C. T.
full_name: Michaels, Thomas C. T.
last_name: Michaels
- first_name: Christopher M.
full_name: Dobson, Christopher M.
last_name: Dobson
- first_name: Tuomas P. J.
full_name: Knowles, Tuomas P. J.
last_name: Knowles
citation:
ama: Dear AJ, Šarić A, Michaels TCT, Dobson CM, Knowles TPJ. Statistical mechanics
of globular oligomer formation by protein molecules. The Journal of Physical
Chemistry B. 2018;122(49):11721-11730. doi:10.1021/acs.jpcb.8b07805
apa: Dear, A. J., Šarić, A., Michaels, T. C. T., Dobson, C. M., & Knowles, T.
P. J. (2018). Statistical mechanics of globular oligomer formation by protein
molecules. The Journal of Physical Chemistry B. American Chemical Society.
https://doi.org/10.1021/acs.jpcb.8b07805
chicago: Dear, Alexander J., Anđela Šarić, Thomas C. T. Michaels, Christopher M.
Dobson, and Tuomas P. J. Knowles. “Statistical Mechanics of Globular Oligomer
Formation by Protein Molecules.” The Journal of Physical Chemistry B. American
Chemical Society, 2018. https://doi.org/10.1021/acs.jpcb.8b07805.
ieee: A. J. Dear, A. Šarić, T. C. T. Michaels, C. M. Dobson, and T. P. J. Knowles,
“Statistical mechanics of globular oligomer formation by protein molecules,” The
Journal of Physical Chemistry B, vol. 122, no. 49. American Chemical Society,
pp. 11721–11730, 2018.
ista: Dear AJ, Šarić A, Michaels TCT, Dobson CM, Knowles TPJ. 2018. Statistical
mechanics of globular oligomer formation by protein molecules. The Journal of
Physical Chemistry B. 122(49), 11721–11730.
mla: Dear, Alexander J., et al. “Statistical Mechanics of Globular Oligomer Formation
by Protein Molecules.” The Journal of Physical Chemistry B, vol. 122, no.
49, American Chemical Society, 2018, pp. 11721–30, doi:10.1021/acs.jpcb.8b07805.
short: A.J. Dear, A. Šarić, T.C.T. Michaels, C.M. Dobson, T.P.J. Knowles, The Journal
of Physical Chemistry B 122 (2018) 11721–11730.
date_created: 2021-11-26T11:55:12Z
date_published: 2018-10-18T00:00:00Z
date_updated: 2021-11-26T12:40:02Z
day: '18'
doi: 10.1021/acs.jpcb.8b07805
extern: '1'
external_id:
pmid:
- '30336667'
intvolume: ' 122'
issue: '49'
keyword:
- materials chemistry
language:
- iso: eng
month: '10'
oa_version: None
page: 11721-11730
pmid: 1
publication: The Journal of Physical Chemistry B
publication_identifier:
eissn:
- 1520-5207
issn:
- 1520-6106
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Statistical mechanics of globular oligomer formation by protein molecules
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 122
year: '2018'
...
---
_id: '10359'
abstract:
- lang: eng
text: Biological membranes typically contain a large number of different components
dispersed in small concentrations in the main membrane phase, including proteins,
sugars, and lipids of varying geometrical properties. Most of these components
do not bind the cargo. Here, we show that such “inert” components can be crucial
for the precise control of cross-membrane trafficking. Using a statistical mechanics
model and molecular dynamics simulations, we demonstrate that the presence of
inert membrane components of small isotropic curvatures dramatically influences
cargo endocytosis, even if the total spontaneous curvature of such a membrane
remains unchanged. Curved lipids, such as cholesterol, as well as asymmetrically
included proteins and tethered sugars can, therefore, actively participate in
the control of the membrane trafficking of nanoscopic cargo. We find that even
a low-level expression of curved inert membrane components can determine the membrane
selectivity toward the cargo size and can be used to selectively target membranes
of certain compositions. Our results suggest a robust and general method of controlling
cargo trafficking by adjusting the membrane composition without needing to alter
the concentration of receptors or the average membrane curvature. This study indicates
that cells can prepare for any trafficking event by incorporating curved inert
components in either of the membrane leaflets.
acknowledgement: We acknowledge discussions with Giuseppe Battaglia as well as support
from the Herchel Smith scholarship (T.C.), the CAS PIFI fellowship (T.C.), the UCL
Institute for the Physics of Living Systems (T.C. and A.Š.), the Austrian Academy
of Sciences through a DOC fellowship (P.W.), the European Union Horizon 2020 programme
under ETN grant no. 674979-NANOTRANS and FET grant no. 766972-NANOPHLOW (J.D. and
D.F.), the Engineering and Physical Sciences Research Council (D.F. and A.Š.), the
Academy of Medical Sciences and Wellcome Trust (A.Š.), and the Royal Society (A.Š.).
We thank Claudia Flandoli for help with Figure 1.
article_processing_charge: No
article_type: original
author:
- first_name: Tine
full_name: Curk, Tine
last_name: Curk
- first_name: Peter
full_name: Wirnsberger, Peter
last_name: Wirnsberger
- first_name: Jure
full_name: Dobnikar, Jure
last_name: Dobnikar
- first_name: Daan
full_name: Frenkel, Daan
last_name: Frenkel
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
citation:
ama: Curk T, Wirnsberger P, Dobnikar J, Frenkel D, Šarić A. Controlling cargo trafficking
in multicomponent membranes. Nano Letters. 2018;18(9):5350-5356. doi:10.1021/acs.nanolett.8b00786
apa: Curk, T., Wirnsberger, P., Dobnikar, J., Frenkel, D., & Šarić, A. (2018).
Controlling cargo trafficking in multicomponent membranes. Nano Letters.
American Chemical Society. https://doi.org/10.1021/acs.nanolett.8b00786
chicago: Curk, Tine, Peter Wirnsberger, Jure Dobnikar, Daan Frenkel, and Anđela
Šarić. “Controlling Cargo Trafficking in Multicomponent Membranes.” Nano Letters.
American Chemical Society, 2018. https://doi.org/10.1021/acs.nanolett.8b00786.
ieee: T. Curk, P. Wirnsberger, J. Dobnikar, D. Frenkel, and A. Šarić, “Controlling
cargo trafficking in multicomponent membranes,” Nano Letters, vol. 18,
no. 9. American Chemical Society, pp. 5350–5356, 2018.
ista: Curk T, Wirnsberger P, Dobnikar J, Frenkel D, Šarić A. 2018. Controlling cargo
trafficking in multicomponent membranes. Nano Letters. 18(9), 5350–5356.
mla: Curk, Tine, et al. “Controlling Cargo Trafficking in Multicomponent Membranes.”
Nano Letters, vol. 18, no. 9, American Chemical Society, 2018, pp. 5350–56,
doi:10.1021/acs.nanolett.8b00786.
short: T. Curk, P. Wirnsberger, J. Dobnikar, D. Frenkel, A. Šarić, Nano Letters
18 (2018) 5350–5356.
date_created: 2021-11-26T12:15:47Z
date_published: 2018-04-18T00:00:00Z
date_updated: 2021-11-26T15:14:08Z
day: '18'
doi: 10.1021/acs.nanolett.8b00786
extern: '1'
external_id:
pmid:
- '29667410'
intvolume: ' 18'
issue: '9'
keyword:
- mechanical engineering
- condensed matter physics
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1712.10147
month: '04'
oa: 1
oa_version: Preprint
page: 5350-5356
pmid: 1
publication: Nano Letters
publication_identifier:
eissn:
- 1530-6992
issn:
- 1530-6984
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Controlling cargo trafficking in multicomponent membranes
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 18
year: '2018'
...
---
_id: '10358'
abstract:
- lang: eng
text: Probing reaction mechanisms of supramolecular processes in soft and biological
matter, such as protein aggregation, is inherently challenging. This is because
these processes involve multiple molecular mechanisms that are associated with
the rearrangement of large numbers of weak bonds, resulting in complex free energy
landscapes with many kinetic barriers. Reaction rate measurements at different
temperatures can offer unprecedented insights into the underlying molecular mechanisms.
However, to be able to interpret such measurements, a key challenge is to establish
which properties of the complex free energy landscapes are probed by the reaction
rate. Here, we present a reaction rate theory for supramolecular kinetics based
on Kramers theory of diffusive reactions over multiple kinetic barriers. We find
that reaction rates for protein aggregation are of the Arrhenius–Eyring type and
that the associated activation energies probe only one relevant barrier along
the respective free energy landscapes. We apply this advancement to interpret,
in experiments and in coarse-grained computer simulations, reaction rates of amyloid
aggregation in terms of molecular mechanisms and associated thermodynamic signatures.
These results suggest a practical extension of the concept of rate-determining
steps for complex supramolecular processes and establish a general platform for
probing the underlying energy landscape using kinetic measurements.
acknowledgement: We thank Claudia Flandoli for the help with illustrations.
article_processing_charge: No
article_type: original
author:
- first_name: Thomas C. T.
full_name: Michaels, Thomas C. T.
last_name: Michaels
- first_name: Lucie X.
full_name: Liu, Lucie X.
last_name: Liu
- first_name: Samo
full_name: Curk, Samo
last_name: Curk
- first_name: Peter G.
full_name: Bolhuis, Peter G.
last_name: Bolhuis
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Tuomas P. J.
full_name: Knowles, Tuomas P. J.
last_name: Knowles
citation:
ama: 'Michaels TCT, Liu LX, Curk S, Bolhuis PG, Šarić A, Knowles TPJ. Reaction rate
theory for supramolecular kinetics: application to protein aggregation. Molecular
Physics. 2018;116(21-22):3055-3065. doi:10.1080/00268976.2018.1474280'
apa: 'Michaels, T. C. T., Liu, L. X., Curk, S., Bolhuis, P. G., Šarić, A., &
Knowles, T. P. J. (2018). Reaction rate theory for supramolecular kinetics: application
to protein aggregation. Molecular Physics. Taylor & Francis. https://doi.org/10.1080/00268976.2018.1474280'
chicago: 'Michaels, Thomas C. T., Lucie X. Liu, Samo Curk, Peter G. Bolhuis, Anđela
Šarić, and Tuomas P. J. Knowles. “Reaction Rate Theory for Supramolecular Kinetics:
Application to Protein Aggregation.” Molecular Physics. Taylor & Francis,
2018. https://doi.org/10.1080/00268976.2018.1474280.'
ieee: 'T. C. T. Michaels, L. X. Liu, S. Curk, P. G. Bolhuis, A. Šarić, and T. P.
J. Knowles, “Reaction rate theory for supramolecular kinetics: application to
protein aggregation,” Molecular Physics, vol. 116, no. 21–22. Taylor &
Francis, pp. 3055–3065, 2018.'
ista: 'Michaels TCT, Liu LX, Curk S, Bolhuis PG, Šarić A, Knowles TPJ. 2018. Reaction
rate theory for supramolecular kinetics: application to protein aggregation. Molecular
Physics. 116(21–22), 3055–3065.'
mla: 'Michaels, Thomas C. T., et al. “Reaction Rate Theory for Supramolecular Kinetics:
Application to Protein Aggregation.” Molecular Physics, vol. 116, no. 21–22,
Taylor & Francis, 2018, pp. 3055–65, doi:10.1080/00268976.2018.1474280.'
short: T.C.T. Michaels, L.X. Liu, S. Curk, P.G. Bolhuis, A. Šarić, T.P.J. Knowles,
Molecular Physics 116 (2018) 3055–3065.
date_created: 2021-11-26T12:08:02Z
date_published: 2018-05-24T00:00:00Z
date_updated: 2021-11-26T12:39:58Z
day: '24'
doi: 10.1080/00268976.2018.1474280
extern: '1'
external_id:
arxiv:
- '1803.04851'
intvolume: ' 116'
issue: 21-22
keyword:
- physical chemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1803.04851
month: '05'
oa: 1
oa_version: Preprint
page: 3055-3065
publication: Molecular Physics
publication_identifier:
eissn:
- 1362-3028
issn:
- 0026-8976
publication_status: published
publisher: Taylor & Francis
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'Reaction rate theory for supramolecular kinetics: application to protein aggregation'
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 116
year: '2018'
...
---
_id: '10361'
abstract:
- lang: eng
text: Understanding how normally soluble peptides and proteins aggregate to form
amyloid fibrils is central to many areas of modern biomolecular science, ranging
from the development of functional biomaterials to the design of rational therapeutic
strategies against increasingly prevalent medical conditions such as Alzheimer's
and Parkinson's diseases. As such, there is a great need to develop models to
mechanistically describe how amyloid fibrils are formed from precursor peptides
and proteins. Here we review and discuss how ideas and concepts from chemical
reaction kinetics can help to achieve this objective. In particular, we show how
a combination of theory, experiments, and computer simulations, based on chemical
kinetics, provides a general formalism for uncovering, at the molecular level,
the mechanistic steps that underlie the phenomenon of amyloid fibril formation.
acknowledgement: "We acknowledge support from the Swiss National Science Foundation
(T.C.T.M.); Peterhouse,\r\nCambridge (T.C.T.M.); the Royal Society (A.S.); the Academy
of Medical Sciences (A.S.); the\r\nWellcome Trust (A.S., M.V., C.M.D., T.P.J.K.);
the Cambridge Centre for Misfolding Diseases\r\n(M.V., C.M.D., T.P.J.K.); the Biotechnology
and Biological Sciences Research Council (C.M.D.,\r\nT.P.J.K.); and the Frances
and Augustus Newman Foundation (T.P.J.K.). The research leading\r\nto these results
has received funding from the European Research Council (ERC) under the\r\nEuropean
Union’s Seventh Framework Programme (FP7/2007-2013) through the ERC grant\r\nPhysProt
(337969)."
article_processing_charge: No
article_type: original
author:
- first_name: Thomas C.T.
full_name: Michaels, Thomas C.T.
last_name: Michaels
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Johnny
full_name: Habchi, Johnny
last_name: Habchi
- first_name: Sean
full_name: Chia, Sean
last_name: Chia
- first_name: Georg
full_name: Meisl, Georg
last_name: Meisl
- first_name: Michele
full_name: Vendruscolo, Michele
last_name: Vendruscolo
- first_name: Christopher M.
full_name: Dobson, Christopher M.
last_name: Dobson
- first_name: Tuomas P.J.
full_name: Knowles, Tuomas P.J.
last_name: Knowles
citation:
ama: Michaels TCT, Šarić A, Habchi J, et al. Chemical kinetics for bridging molecular
mechanisms and macroscopic measurements of amyloid fibril formation. Annual
Review of Physical Chemistry. 2018;69(1):273-298. doi:10.1146/annurev-physchem-050317-021322
apa: Michaels, T. C. T., Šarić, A., Habchi, J., Chia, S., Meisl, G., Vendruscolo,
M., … Knowles, T. P. J. (2018). Chemical kinetics for bridging molecular mechanisms
and macroscopic measurements of amyloid fibril formation. Annual Review of
Physical Chemistry. Annual Reviews. https://doi.org/10.1146/annurev-physchem-050317-021322
chicago: Michaels, Thomas C.T., Anđela Šarić, Johnny Habchi, Sean Chia, Georg Meisl,
Michele Vendruscolo, Christopher M. Dobson, and Tuomas P.J. Knowles. “Chemical
Kinetics for Bridging Molecular Mechanisms and Macroscopic Measurements of Amyloid
Fibril Formation.” Annual Review of Physical Chemistry. Annual Reviews,
2018. https://doi.org/10.1146/annurev-physchem-050317-021322.
ieee: T. C. T. Michaels et al., “Chemical kinetics for bridging molecular
mechanisms and macroscopic measurements of amyloid fibril formation,” Annual
Review of Physical Chemistry, vol. 69, no. 1. Annual Reviews, pp. 273–298,
2018.
ista: Michaels TCT, Šarić A, Habchi J, Chia S, Meisl G, Vendruscolo M, Dobson CM,
Knowles TPJ. 2018. Chemical kinetics for bridging molecular mechanisms and macroscopic
measurements of amyloid fibril formation. Annual Review of Physical Chemistry.
69(1), 273–298.
mla: Michaels, Thomas C. T., et al. “Chemical Kinetics for Bridging Molecular Mechanisms
and Macroscopic Measurements of Amyloid Fibril Formation.” Annual Review of
Physical Chemistry, vol. 69, no. 1, Annual Reviews, 2018, pp. 273–98, doi:10.1146/annurev-physchem-050317-021322.
short: T.C.T. Michaels, A. Šarić, J. Habchi, S. Chia, G. Meisl, M. Vendruscolo,
C.M. Dobson, T.P.J. Knowles, Annual Review of Physical Chemistry 69 (2018) 273–298.
date_created: 2021-11-26T12:52:12Z
date_published: 2018-02-28T00:00:00Z
date_updated: 2021-11-26T15:58:19Z
day: '28'
doi: 10.1146/annurev-physchem-050317-021322
extern: '1'
external_id:
pmid:
- '29490200'
intvolume: ' 69'
issue: '1'
keyword:
- physical and theoretical chemistry
language:
- iso: eng
month: '02'
oa_version: None
page: 273-298
pmid: 1
publication: Annual Review of Physical Chemistry
publication_identifier:
eissn:
- 1545-1593
issn:
- 0066-426X
publication_status: published
publisher: Annual Reviews
quality_controlled: '1'
scopus_import: '1'
status: public
title: Chemical kinetics for bridging molecular mechanisms and macroscopic measurements
of amyloid fibril formation
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 69
year: '2018'
...
---
_id: '10126'
article_number: 391a
article_processing_charge: No
article_type: letter_note
author:
- first_name: Afshin
full_name: Vahid Belarghou, Afshin
last_name: Vahid Belarghou
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Timon
full_name: Idema, Timon
last_name: Idema
citation:
ama: Vahid Belarghou A, Šarić A, Idema T. Curvature mediated interactions in highly
curved membranes. Biophysical Journal. 2017;112(3). doi:10.1016/j.bpj.2016.11.2123
apa: Vahid Belarghou, A., Šarić, A., & Idema, T. (2017). Curvature mediated
interactions in highly curved membranes. Biophysical Journal. Elsevier
. https://doi.org/10.1016/j.bpj.2016.11.2123
chicago: Vahid Belarghou, Afshin, Anđela Šarić, and Timon Idema. “Curvature Mediated
Interactions in Highly Curved Membranes.” Biophysical Journal. Elsevier
, 2017. https://doi.org/10.1016/j.bpj.2016.11.2123.
ieee: A. Vahid Belarghou, A. Šarić, and T. Idema, “Curvature mediated interactions
in highly curved membranes,” Biophysical Journal, vol. 112, no. 3. Elsevier
, 2017.
ista: Vahid Belarghou A, Šarić A, Idema T. 2017. Curvature mediated interactions
in highly curved membranes. Biophysical Journal. 112(3), 391a.
mla: Vahid Belarghou, Afshin, et al. “Curvature Mediated Interactions in Highly
Curved Membranes.” Biophysical Journal, vol. 112, no. 3, 391a, Elsevier
, 2017, doi:10.1016/j.bpj.2016.11.2123.
short: A. Vahid Belarghou, A. Šarić, T. Idema, Biophysical Journal 112 (2017).
date_created: 2021-10-12T07:47:55Z
date_published: 2017-02-03T00:00:00Z
date_updated: 2021-11-03T10:02:45Z
day: '03'
doi: 10.1016/j.bpj.2016.11.2123
extern: '1'
intvolume: ' 112'
issue: '3'
keyword:
- biophysics
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.cell.com/biophysj/fulltext/S0006-3495(16)33153-8
month: '02'
oa: 1
oa_version: Published Version
publication: Biophysical Journal
publication_identifier:
issn:
- 0006-3495
publication_status: published
publisher: 'Elsevier '
quality_controlled: '1'
status: public
title: Curvature mediated interactions in highly curved membranes
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 112
year: '2017'
...
---
_id: '10370'
abstract:
- lang: eng
text: Eukaryotic cells are densely packed with macromolecular complexes and intertwining
organelles, continually transported and reshaped. Intriguingly, organelles avoid
clashing and entangling with each other in such limited space. Mitochondria form
extensive networks constantly remodeled by fission and fusion. Here, we show that
mitochondrial fission is triggered by mechanical forces. Mechano-stimulation of
mitochondria – via encounter with motile intracellular pathogens, via external
pressure applied by an atomic force microscope, or via cell migration across uneven
microsurfaces – results in the recruitment of the mitochondrial fission machinery,
and subsequent division. We propose that MFF, owing to affinity for narrow mitochondria,
acts as a membrane-bound force sensor to recruit the fission machinery to mechanically
strained sites. Thus, mitochondria adapt to the environment by sensing and responding
to biomechanical cues. Our findings that mechanical triggers can be coupled to
biochemical responses in membrane dynamics may explain how organelles orderly
cohabit in the crowded cytoplasm.
article_number: e30292
article_processing_charge: No
article_type: original
author:
- first_name: Sebastian Carsten Johannes
full_name: Helle, Sebastian Carsten Johannes
last_name: Helle
- first_name: Qian
full_name: Feng, Qian
last_name: Feng
- first_name: Mathias J
full_name: Aebersold, Mathias J
last_name: Aebersold
- first_name: Luca
full_name: Hirt, Luca
last_name: Hirt
- first_name: Raphael R
full_name: Grüter, Raphael R
last_name: Grüter
- first_name: Afshin
full_name: Vahid, Afshin
last_name: Vahid
- first_name: Andrea
full_name: Sirianni, Andrea
last_name: Sirianni
- first_name: Serge
full_name: Mostowy, Serge
last_name: Mostowy
- first_name: Jess G
full_name: Snedeker, Jess G
last_name: Snedeker
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Timon
full_name: Idema, Timon
last_name: Idema
- first_name: Tomaso
full_name: Zambelli, Tomaso
last_name: Zambelli
- first_name: Benoît
full_name: Kornmann, Benoît
last_name: Kornmann
citation:
ama: Helle SCJ, Feng Q, Aebersold MJ, et al. Mechanical force induces mitochondrial
fission. eLife. 2017;6. doi:10.7554/elife.30292
apa: Helle, S. C. J., Feng, Q., Aebersold, M. J., Hirt, L., Grüter, R. R., Vahid,
A., … Kornmann, B. (2017). Mechanical force induces mitochondrial fission. ELife.
eLife Sciences Publications. https://doi.org/10.7554/elife.30292
chicago: Helle, Sebastian Carsten Johannes, Qian Feng, Mathias J Aebersold, Luca
Hirt, Raphael R Grüter, Afshin Vahid, Andrea Sirianni, et al. “Mechanical Force
Induces Mitochondrial Fission.” ELife. eLife Sciences Publications, 2017.
https://doi.org/10.7554/elife.30292.
ieee: S. C. J. Helle et al., “Mechanical force induces mitochondrial fission,”
eLife, vol. 6. eLife Sciences Publications, 2017.
ista: Helle SCJ, Feng Q, Aebersold MJ, Hirt L, Grüter RR, Vahid A, Sirianni A, Mostowy
S, Snedeker JG, Šarić A, Idema T, Zambelli T, Kornmann B. 2017. Mechanical force
induces mitochondrial fission. eLife. 6, e30292.
mla: Helle, Sebastian Carsten Johannes, et al. “Mechanical Force Induces Mitochondrial
Fission.” ELife, vol. 6, e30292, eLife Sciences Publications, 2017, doi:10.7554/elife.30292.
short: S.C.J. Helle, Q. Feng, M.J. Aebersold, L. Hirt, R.R. Grüter, A. Vahid, A.
Sirianni, S. Mostowy, J.G. Snedeker, A. Šarić, T. Idema, T. Zambelli, B. Kornmann,
ELife 6 (2017).
date_created: 2021-11-29T08:51:38Z
date_published: 2017-11-09T00:00:00Z
date_updated: 2021-11-29T09:28:14Z
day: '09'
ddc:
- '572'
doi: 10.7554/elife.30292
extern: '1'
external_id:
pmid:
- '29119945'
file:
- access_level: open_access
checksum: c35f42dcfb007f6d6c761a27e24c26d3
content_type: application/pdf
creator: cchlebak
date_created: 2021-11-29T09:07:41Z
date_updated: 2021-11-29T09:07:41Z
file_id: '10372'
file_name: 2017_eLife_Helle.pdf
file_size: 6120157
relation: main_file
success: 1
file_date_updated: 2021-11-29T09:07:41Z
has_accepted_license: '1'
intvolume: ' 6'
keyword:
- general immunology and microbiology
- general biochemistry
- genetics and molecular biology
- general medicine
- general neuroscience
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://elifesciences.org/articles/30292
month: '11'
oa: 1
oa_version: Published Version
pmid: 1
publication: eLife
publication_identifier:
issn:
- 2050-084X
publication_status: published
publisher: eLife Sciences Publications
quality_controlled: '1'
scopus_import: '1'
status: public
title: Mechanical force induces mitochondrial fission
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 6
year: '2017'
...
---
_id: '10369'
abstract:
- lang: eng
text: Biological membranes have a central role in mediating the organization of
membrane-curving proteins, a dynamic process that has proven to be challenging
to probe experimentally. Using atomic force microscopy, we capture the hierarchically
organized assemblies of Bin/amphiphysin/Rvs (BAR) proteins on supported lipid
membranes. Their structure reveals distinct long linear aggregates of proteins,
regularly spaced by up to 300 nm. Employing accurate free-energy calculations
from large-scale coarse-grained computer simulations, we found that the membrane
mediates the interaction among protein filaments as a combination of short- and
long-ranged interactions. The long-ranged component acts at strikingly long distances,
giving rise to a variety of micron-sized ordered patterns. This mechanism may
contribute to the long-ranged spatiotemporal control of membrane remodeling by
proteins in the cell.
acknowledgement: M.S. and G.A.V. acknowledge their research reported in this publication
as being supported by the National Institute of General Medical Sciences of the
National Institutes of Health under Award Number R01-GM063796. Computational resources
were provided to M.S. and G.A.V. by the National Science Foundation through XSEDE
(Grant TG-MCA94P017, supercomputers Stampede and Gordon), and also by the Blue Waters
computing project at the National Center for Supercomputing Applications (University
of Illinois at Urbana–Champaign, NSF Awards OCI-0725070 and ACI-1238993). A.Š. acknowledges
support from the Human Frontier Science Program and Royal Society. J.M.H. and K.Y.C.L.
acknowledge the support from the National Science Foundation (Grant MCB-1413613)
and the NSF-supported MRSEC program at the University of Chicago (Grant DMR-1420709).
We are grateful to Carsten Mim and Vinzenz Unger of Northwestern University for
generously providing us with the protein. We thank all the members of the Voth group
for fruitful discussions, especially John M. A. Grime.
article_processing_charge: No
article_type: original
author:
- first_name: Mijo
full_name: Simunovic, Mijo
last_name: Simunovic
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: J. Michael
full_name: Henderson, J. Michael
last_name: Henderson
- first_name: Ka Yee C.
full_name: Lee, Ka Yee C.
last_name: Lee
- first_name: Gregory A.
full_name: Voth, Gregory A.
last_name: Voth
citation:
ama: Simunovic M, Šarić A, Henderson JM, Lee KYC, Voth GA. Long-range organization
of membrane-curving proteins. ACS Central Science. 2017;3(12):1246-1253.
doi:10.1021/acscentsci.7b00392
apa: Simunovic, M., Šarić, A., Henderson, J. M., Lee, K. Y. C., & Voth, G. A.
(2017). Long-range organization of membrane-curving proteins. ACS Central Science.
American Chemical Society. https://doi.org/10.1021/acscentsci.7b00392
chicago: Simunovic, Mijo, Anđela Šarić, J. Michael Henderson, Ka Yee C. Lee, and
Gregory A. Voth. “Long-Range Organization of Membrane-Curving Proteins.” ACS
Central Science. American Chemical Society, 2017. https://doi.org/10.1021/acscentsci.7b00392.
ieee: M. Simunovic, A. Šarić, J. M. Henderson, K. Y. C. Lee, and G. A. Voth, “Long-range
organization of membrane-curving proteins,” ACS Central Science, vol. 3,
no. 12. American Chemical Society, pp. 1246–1253, 2017.
ista: Simunovic M, Šarić A, Henderson JM, Lee KYC, Voth GA. 2017. Long-range organization
of membrane-curving proteins. ACS Central Science. 3(12), 1246–1253.
mla: Simunovic, Mijo, et al. “Long-Range Organization of Membrane-Curving Proteins.”
ACS Central Science, vol. 3, no. 12, American Chemical Society, 2017, pp.
1246–53, doi:10.1021/acscentsci.7b00392.
short: M. Simunovic, A. Šarić, J.M. Henderson, K.Y.C. Lee, G.A. Voth, ACS Central
Science 3 (2017) 1246–1253.
date_created: 2021-11-29T08:49:50Z
date_published: 2017-11-21T00:00:00Z
date_updated: 2021-11-29T09:28:06Z
day: '21'
ddc:
- '540'
doi: 10.1021/acscentsci.7b00392
extern: '1'
external_id:
pmid:
- '29296664'
file:
- access_level: open_access
checksum: 1cf3e5e5342f2d728f47560acc3ec560
content_type: application/pdf
creator: cchlebak
date_created: 2021-11-29T09:00:40Z
date_updated: 2021-11-29T09:00:40Z
file_id: '10371'
file_name: 2017_ACSCentSci_Simunovic.pdf
file_size: 2635263
relation: main_file
success: 1
file_date_updated: 2021-11-29T09:00:40Z
has_accepted_license: '1'
intvolume: ' 3'
issue: '12'
keyword:
- general chemical engineering
- general chemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://pubs.acs.org/doi/10.1021/acscentsci.7b00392
month: '11'
oa: 1
oa_version: Published Version
page: 1246-1253
pmid: 1
publication: ACS Central Science
publication_identifier:
eissn:
- 2374-7951
issn:
- 2374-7943
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Long-range organization of membrane-curving proteins
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 3
year: '2017'
...
---
_id: '10373'
abstract:
- lang: eng
text: 'Electric charges are conserved. The same would be expected to hold for magnetic
charges, yet magnetic monopoles have never been observed. It is therefore surprising
that the laws of nonequilibrium thermodynamics, combined with Maxwell’s equations,
suggest that colloidal particles heated or cooled in certain polar or paramagnetic
solvents may behave as if they carry an electric/magnetic charge. Here, we present
numerical simulations that show that the field distribution around a pair of such
heated/cooled colloidal particles agrees quantitatively with the theoretical predictions
for a pair of oppositely charged electric or magnetic monopoles. However, in other
respects, the nonequilibrium colloidal particles do not behave as monopoles: They
cannot be moved by a homogeneous applied field. The numerical evidence for the
monopole-like fields around heated/cooled colloidal particles is crucial because
the experimental and numerical determination of forces between such colloidal
particles would be complicated by the presence of other effects, such as thermophoresis.'
acknowledgement: P.W. acknowledges many invaluable discussions with Martin Neumann,
Chao Zhang, Michiel Sprik, Aleks Reinhardt, Carl Pölking, and Tine Curk. We acknowledge
financial support from the Austrian Academy of Sciences through a doctoral (DOC)
fellowship (to P.W.), the Austrian Science Fund (FWF) within the Spezialforschungsbereich
Vienna Computational Materials Laboratory (Project F41) (C.D.), and the European
Union Early Training Network NANOTRANS (Grant 674979 to D. Frenkel). The results
presented here have been achieved in part using the Vienna Scientific Cluster.
article_processing_charge: No
article_type: original
author:
- first_name: Peter
full_name: Wirnsberger, Peter
last_name: Wirnsberger
- first_name: Domagoj
full_name: Fijan, Domagoj
last_name: Fijan
- first_name: Roger A.
full_name: Lightwood, Roger A.
last_name: Lightwood
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Christoph
full_name: Dellago, Christoph
last_name: Dellago
- first_name: Daan
full_name: Frenkel, Daan
last_name: Frenkel
citation:
ama: Wirnsberger P, Fijan D, Lightwood RA, Šarić A, Dellago C, Frenkel D. Numerical
evidence for thermally induced monopoles. Proceedings of the National Academy
of Sciences. 2017;114(19):4911-4914. doi:10.1073/pnas.1621494114
apa: Wirnsberger, P., Fijan, D., Lightwood, R. A., Šarić, A., Dellago, C., &
Frenkel, D. (2017). Numerical evidence for thermally induced monopoles. Proceedings
of the National Academy of Sciences. National Academy of Sciences. https://doi.org/10.1073/pnas.1621494114
chicago: Wirnsberger, Peter, Domagoj Fijan, Roger A. Lightwood, Anđela Šarić, Christoph
Dellago, and Daan Frenkel. “Numerical Evidence for Thermally Induced Monopoles.”
Proceedings of the National Academy of Sciences. National Academy of Sciences,
2017. https://doi.org/10.1073/pnas.1621494114.
ieee: P. Wirnsberger, D. Fijan, R. A. Lightwood, A. Šarić, C. Dellago, and D. Frenkel,
“Numerical evidence for thermally induced monopoles,” Proceedings of the National
Academy of Sciences, vol. 114, no. 19. National Academy of Sciences, pp. 4911–4914,
2017.
ista: Wirnsberger P, Fijan D, Lightwood RA, Šarić A, Dellago C, Frenkel D. 2017.
Numerical evidence for thermally induced monopoles. Proceedings of the National
Academy of Sciences. 114(19), 4911–4914.
mla: Wirnsberger, Peter, et al. “Numerical Evidence for Thermally Induced Monopoles.”
Proceedings of the National Academy of Sciences, vol. 114, no. 19, National
Academy of Sciences, 2017, pp. 4911–14, doi:10.1073/pnas.1621494114.
short: P. Wirnsberger, D. Fijan, R.A. Lightwood, A. Šarić, C. Dellago, D. Frenkel,
Proceedings of the National Academy of Sciences 114 (2017) 4911–4914.
date_created: 2021-11-29T09:28:24Z
date_published: 2017-04-24T00:00:00Z
date_updated: 2021-11-29T09:59:12Z
day: '24'
doi: 10.1073/pnas.1621494114
extern: '1'
external_id:
arxiv:
- '1610.06840'
pmid:
- '28439003'
intvolume: ' 114'
issue: '19'
keyword:
- multidisciplinary
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.pnas.org/content/114/19/4911
month: '04'
oa: 1
oa_version: Published Version
page: 4911-4914
pmid: 1
publication: Proceedings of the National Academy of Sciences
publication_identifier:
eissn:
- 1091-6490
issn:
- 0027-8424
publication_status: published
publisher: National Academy of Sciences
quality_controlled: '1'
scopus_import: '1'
status: public
title: Numerical evidence for thermally induced monopoles
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 114
year: '2017'
...
---
_id: '10374'
abstract:
- lang: eng
text: The formation of filaments from naturally occurring protein molecules is a
process at the core of a range of functional and aberrant biological phenomena,
such as the assembly of the cytoskeleton or the appearance of aggregates in Alzheimer's
disease. The macroscopic behaviour associated with such processes is remarkably
diverse, ranging from simple nucleated growth to highly cooperative processes
with a well-defined lagtime. Thus, conventionally, different molecular mechanisms
have been used to explain the self-assembly of different proteins. Here we show
that this range of behaviour can be quantitatively captured by a single unifying
Petri net that describes filamentous growth in terms of aggregate number and aggregate
mass concentrations. By considering general features associated with a particular
network connectivity, we are able to establish directly the rate-determining steps
of the overall aggregation reaction from the system's scaling behaviour. We illustrate
the power of this framework on a range of different experimental and simulated
aggregating systems. The approach is general and will be applicable to any future
extensions of the reaction network of filamentous self-assembly.
acknowledgement: The research leading to these results has received funding from the
European Research Council under the European Union's Seventh Framework Programme
(FP7/2007-2013) through the ERC grant PhysProt (agreement no. 337969) (SL, TPJK),
Sidney Sussex College Cambridge (GM), the Frances and Augusta Newman Foundation
(TPJK), the Biotechnology and Biological Science Research Council (TPJK), the Swedish
Research Council (SL), the Academy of Medical Sciences (AŠ), Wellcome Trust (AŠ),
and the Cambridge Centre for Misfolding Diseases (CMD, TPJK, MV).
article_processing_charge: No
article_type: original
author:
- first_name: Georg
full_name: Meisl, Georg
last_name: Meisl
- first_name: Luke
full_name: Rajah, Luke
last_name: Rajah
- first_name: Samuel A. I.
full_name: Cohen, Samuel A. I.
last_name: Cohen
- first_name: Manuela
full_name: Pfammatter, Manuela
last_name: Pfammatter
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Erik
full_name: Hellstrand, Erik
last_name: Hellstrand
- first_name: Alexander K.
full_name: Buell, Alexander K.
last_name: Buell
- first_name: Adriano
full_name: Aguzzi, Adriano
last_name: Aguzzi
- first_name: Sara
full_name: Linse, Sara
last_name: Linse
- first_name: Michele
full_name: Vendruscolo, Michele
last_name: Vendruscolo
- first_name: Christopher M.
full_name: Dobson, Christopher M.
last_name: Dobson
- first_name: Tuomas P. J.
full_name: Knowles, Tuomas P. J.
last_name: Knowles
citation:
ama: Meisl G, Rajah L, Cohen SAI, et al. Scaling behaviour and rate-determining
steps in filamentous self-assembly. Chemical Science. 2017;8(10):7087-7097.
doi:10.1039/c7sc01965c
apa: Meisl, G., Rajah, L., Cohen, S. A. I., Pfammatter, M., Šarić, A., Hellstrand,
E., … Knowles, T. P. J. (2017). Scaling behaviour and rate-determining steps in
filamentous self-assembly. Chemical Science. Royal Society of Chemistry.
https://doi.org/10.1039/c7sc01965c
chicago: Meisl, Georg, Luke Rajah, Samuel A. I. Cohen, Manuela Pfammatter, Anđela
Šarić, Erik Hellstrand, Alexander K. Buell, et al. “Scaling Behaviour and Rate-Determining
Steps in Filamentous Self-Assembly.” Chemical Science. Royal Society of
Chemistry, 2017. https://doi.org/10.1039/c7sc01965c.
ieee: G. Meisl et al., “Scaling behaviour and rate-determining steps in filamentous
self-assembly,” Chemical Science, vol. 8, no. 10. Royal Society of Chemistry,
pp. 7087–7097, 2017.
ista: Meisl G, Rajah L, Cohen SAI, Pfammatter M, Šarić A, Hellstrand E, Buell AK,
Aguzzi A, Linse S, Vendruscolo M, Dobson CM, Knowles TPJ. 2017. Scaling behaviour
and rate-determining steps in filamentous self-assembly. Chemical Science. 8(10),
7087–7097.
mla: Meisl, Georg, et al. “Scaling Behaviour and Rate-Determining Steps in Filamentous
Self-Assembly.” Chemical Science, vol. 8, no. 10, Royal Society of Chemistry,
2017, pp. 7087–97, doi:10.1039/c7sc01965c.
short: G. Meisl, L. Rajah, S.A.I. Cohen, M. Pfammatter, A. Šarić, E. Hellstrand,
A.K. Buell, A. Aguzzi, S. Linse, M. Vendruscolo, C.M. Dobson, T.P.J. Knowles,
Chemical Science 8 (2017) 7087–7097.
date_created: 2021-11-29T09:29:31Z
date_published: 2017-08-31T00:00:00Z
date_updated: 2021-11-29T10:00:00Z
day: '31'
ddc:
- '540'
doi: 10.1039/c7sc01965c
extern: '1'
external_id:
pmid:
- '29147538'
intvolume: ' 8'
issue: '10'
keyword:
- general chemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://pubs.rsc.org/en/content/articlelanding/2017/SC/C7SC01965C
month: '08'
oa: 1
oa_version: Published Version
page: 7087-7097
pmid: 1
publication: Chemical Science
publication_identifier:
eissn:
- 2041-6539
issn:
- 2041-6520
publication_status: published
publisher: Royal Society of Chemistry
quality_controlled: '1'
scopus_import: '1'
status: public
title: Scaling behaviour and rate-determining steps in filamentous self-assembly
tmp:
image: /images/cc_by_nc.png
legal_code_url: https://creativecommons.org/licenses/by-nc/3.0/legalcode
name: Creative Commons Attribution-NonCommercial 3.0 Unported (CC BY-NC 3.0)
short: CC BY-NC (3.0)
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 8
year: '2017'
...
---
_id: '10375'
abstract:
- lang: eng
text: 'Cellular membranes exhibit a large variety of shapes, strongly coupled to
their function. Many biological processes involve dynamic reshaping of membranes,
usually mediated by proteins. This interaction works both ways: while proteins
influence the membrane shape, the membrane shape affects the interactions between
the proteins. To study these membrane-mediated interactions on closed and anisotropically
curved membranes, we use colloids adhered to ellipsoidal membrane vesicles as
a model system. We find that two particles on a closed system always attract each
other, and tend to align with the direction of largest curvature. Multiple particles
form arcs, or, at large enough numbers, a complete ring surrounding the vesicle
in its equatorial plane. The resulting vesicle shape resembles a snowman. Our
results indicate that these physical interactions on membranes with anisotropic
shapes can be exploited by cells to drive macromolecules to preferred regions
of cellular or intracellular membranes, and utilized to initiate dynamic processes
such as cell division. The same principle could be used to find the midplane of
an artificial vesicle, as a first step towards dividing it into two equal parts.'
acknowledgement: This work was supported by the Netherlands Organisation for Scientific
Research (NWO/OCW), as part of the Frontiers of Nanoscience program.
article_processing_charge: No
article_type: original
author:
- first_name: Afshin
full_name: Vahid, Afshin
last_name: Vahid
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Timon
full_name: Idema, Timon
last_name: Idema
citation:
ama: Vahid A, Šarić A, Idema T. Curvature variation controls particle aggregation
on fluid vesicles. Soft Matter. 2017;13(28):4924-4930. doi:10.1039/c7sm00433h
apa: Vahid, A., Šarić, A., & Idema, T. (2017). Curvature variation controls
particle aggregation on fluid vesicles. Soft Matter. Royal Society of Chemistry.
https://doi.org/10.1039/c7sm00433h
chicago: Vahid, Afshin, Anđela Šarić, and Timon Idema. “Curvature Variation Controls
Particle Aggregation on Fluid Vesicles.” Soft Matter. Royal Society of
Chemistry, 2017. https://doi.org/10.1039/c7sm00433h.
ieee: A. Vahid, A. Šarić, and T. Idema, “Curvature variation controls particle aggregation
on fluid vesicles,” Soft Matter, vol. 13, no. 28. Royal Society of Chemistry,
pp. 4924–4930, 2017.
ista: Vahid A, Šarić A, Idema T. 2017. Curvature variation controls particle aggregation
on fluid vesicles. Soft Matter. 13(28), 4924–4930.
mla: Vahid, Afshin, et al. “Curvature Variation Controls Particle Aggregation on
Fluid Vesicles.” Soft Matter, vol. 13, no. 28, Royal Society of Chemistry,
2017, pp. 4924–30, doi:10.1039/c7sm00433h.
short: A. Vahid, A. Šarić, T. Idema, Soft Matter 13 (2017) 4924–4930.
date_created: 2021-11-29T10:00:39Z
date_published: 2017-06-15T00:00:00Z
date_updated: 2021-11-29T10:33:36Z
day: '15'
doi: 10.1039/c7sm00433h
extern: '1'
external_id:
arxiv:
- '1703.00776'
pmid:
- '28677712'
intvolume: ' 13'
issue: '28'
keyword:
- condensed matter physics
- general chemistry
language:
- iso: eng
license: https://creativecommons.org/licenses/by/3.0/
main_file_link:
- open_access: '1'
url: https://pubs.rsc.org/en/content/articlelanding/2017/SM/C7SM00433H
month: '06'
oa: 1
oa_version: Published Version
page: 4924-4930
pmid: 1
publication: Soft Matter
publication_identifier:
eissn:
- 1744-6848
issn:
- 1744-683X
publication_status: published
publisher: Royal Society of Chemistry
quality_controlled: '1'
scopus_import: '1'
status: public
title: Curvature variation controls particle aggregation on fluid vesicles
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/3.0/legalcode
name: Creative Commons Attribution 3.0 Unported (CC BY 3.0)
short: CC BY (3.0)
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 13
year: '2017'
...
---
_id: '10377'
abstract:
- lang: eng
text: The interplay of membrane proteins is vital for many biological processes,
such as cellular transport, cell division, and signal transduction between nerve
cells. Theoretical considerations have led to the idea that the membrane itself
mediates protein self-organization in these processes through minimization of
membrane curvature energy. Here, we present a combined experimental and numerical
study in which we quantify these interactions directly for the first time. In
our experimental model system we control the deformation of a lipid membrane by
adhering colloidal particles. Using confocal microscopy, we establish that these
membrane deformations cause an attractive interaction force leading to reversible
binding. The attraction extends over 2.5 times the particle diameter and has a
strength of three times the thermal energy (−3.3 kBT). Coarse-grained Monte-Carlo
simulations of the system are in excellent agreement with the experimental results
and prove that the measured interaction is independent of length scale. Our combined
experimental and numerical results reveal membrane curvature as a common physical
origin for interactions between any membrane-deforming objects, from nanometre-sized
proteins to micrometre-sized particles.
acknowledgement: This work was supported by the Netherlands Organisation for Scientific
Research (NWO/OCW), as part of the Frontiers of Nanoscience program and VENI grant
680-47-431. We thank Jeroen Appel and Wim Pomp for advice on the protocol design
and Marcel Winter and Ruben Verweij for experimental support.
article_number: '32825'
article_processing_charge: No
article_type: original
author:
- first_name: Casper
full_name: van der Wel, Casper
last_name: van der Wel
- first_name: Afshin
full_name: Vahid, Afshin
last_name: Vahid
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Timon
full_name: Idema, Timon
last_name: Idema
- first_name: Doris
full_name: Heinrich, Doris
last_name: Heinrich
- first_name: Daniela J.
full_name: Kraft, Daniela J.
last_name: Kraft
citation:
ama: van der Wel C, Vahid A, Šarić A, Idema T, Heinrich D, Kraft DJ. Lipid membrane-mediated
attraction between curvature inducing objects. Scientific Reports. 2016;6(1).
doi:10.1038/srep32825
apa: van der Wel, C., Vahid, A., Šarić, A., Idema, T., Heinrich, D., & Kraft,
D. J. (2016). Lipid membrane-mediated attraction between curvature inducing objects.
Scientific Reports. Springer Nature. https://doi.org/10.1038/srep32825
chicago: Wel, Casper van der, Afshin Vahid, Anđela Šarić, Timon Idema, Doris Heinrich,
and Daniela J. Kraft. “Lipid Membrane-Mediated Attraction between Curvature Inducing
Objects.” Scientific Reports. Springer Nature, 2016. https://doi.org/10.1038/srep32825.
ieee: C. van der Wel, A. Vahid, A. Šarić, T. Idema, D. Heinrich, and D. J. Kraft,
“Lipid membrane-mediated attraction between curvature inducing objects,” Scientific
Reports, vol. 6, no. 1. Springer Nature, 2016.
ista: van der Wel C, Vahid A, Šarić A, Idema T, Heinrich D, Kraft DJ. 2016. Lipid
membrane-mediated attraction between curvature inducing objects. Scientific Reports.
6(1), 32825.
mla: van der Wel, Casper, et al. “Lipid Membrane-Mediated Attraction between Curvature
Inducing Objects.” Scientific Reports, vol. 6, no. 1, 32825, Springer Nature,
2016, doi:10.1038/srep32825.
short: C. van der Wel, A. Vahid, A. Šarić, T. Idema, D. Heinrich, D.J. Kraft, Scientific
Reports 6 (2016).
date_created: 2021-11-29T10:34:08Z
date_published: 2016-09-13T00:00:00Z
date_updated: 2021-11-29T11:08:15Z
day: '13'
ddc:
- '540'
doi: 10.1038/srep32825
extern: '1'
external_id:
arxiv:
- '1603.04644'
pmid:
- '27618764'
file:
- access_level: open_access
checksum: d6cf16dd511e15726b001e7cc287cf1d
content_type: application/pdf
creator: cchlebak
date_created: 2021-11-29T10:50:00Z
date_updated: 2021-11-29T10:50:00Z
file_id: '10379'
file_name: 2016_SciRep_vanderWel.pdf
file_size: 1598289
relation: main_file
success: 1
file_date_updated: 2021-11-29T10:50:00Z
has_accepted_license: '1'
intvolume: ' 6'
issue: '1'
keyword:
- multidisciplinary
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.nature.com/articles/srep32825
month: '09'
oa: 1
oa_version: Published Version
pmid: 1
publication: Scientific Reports
publication_identifier:
issn:
- 2045-2322
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
related_material:
link:
- relation: erratum
url: https://doi.org/10.1038/srep37382
scopus_import: '1'
status: public
title: Lipid membrane-mediated attraction between curvature inducing objects
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 6
year: '2016'
...
---
_id: '10376'
abstract:
- lang: eng
text: Nucleation processes are at the heart of a large number of phenomena, from
cloud formation to protein crystallization. A recently emerging area where nucleation
is highly relevant is the initiation of filamentous protein self-assembly, a process
that has broad implications in many research areas ranging from medicine to nanotechnology.
As such, spontaneous nucleation of protein fibrils has received much attention
in recent years with many theoretical and experimental studies focusing on the
underlying physical principles. In this paper we make a step forward in this direction
and explore the early time behaviour of filamentous protein growth in the context
of nucleation theory. We first provide an overview of the thermodynamics and kinetics
of spontaneous nucleation of protein filaments in the presence of one relevant
degree of freedom, namely the cluster size. In this case, we review how key kinetic
observables, such as the reaction order of spontaneous nucleation, are directly
related to the physical size of the critical nucleus. We then focus on the increasingly
prominent case of filament nucleation that includes a conformational conversion
of the nucleating building-block as an additional slow step in the nucleation
process. Using computer simulations, we study the concentration dependence of
the nucleation rate. We find that, under these circumstances, the reaction order
of spontaneous nucleation with respect to the free monomer does no longer relate
to the overall physical size of the nucleating aggregate but rather to the portion
of the aggregate that actively participates in the conformational conversion.
Our results thus provide a novel interpretation of the common kinetic descriptors
of protein filament formation, including the reaction order of the nucleation
step or the scaling exponent of lag times, and put into perspective current theoretical
descriptions of protein aggregation.
acknowledgement: We acknowledge support from the Human Frontier Science Program and
Emmanuel College (A.Š.), St John’s and Peterhouse Colleges (T.C.T.M.), the Swiss
National Science Foundation (T.C.T.M.), the Biotechnology and Biological Sciences
Research Council (T.P.J.K.), the Frances and Augustus Newman Foundation (T.P.J.K.),
the European Research Council (T.C.T.M., T.P.J.K., and D.F.), and the Engineering
and Physical Sciences Research Council (D.F.).
article_number: '211926'
article_processing_charge: No
article_type: original
author:
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Thomas C. T.
full_name: Michaels, Thomas C. T.
last_name: Michaels
- first_name: Alessio
full_name: Zaccone, Alessio
last_name: Zaccone
- first_name: Tuomas P. J.
full_name: Knowles, Tuomas P. J.
last_name: Knowles
- first_name: Daan
full_name: Frenkel, Daan
last_name: Frenkel
citation:
ama: 'Šarić A, Michaels TCT, Zaccone A, Knowles TPJ, Frenkel D. Kinetics of spontaneous
filament nucleation via oligomers: Insights from theory and simulation. The
Journal of Chemical Physics. 2016;145(21). doi:10.1063/1.4965040'
apa: 'Šarić, A., Michaels, T. C. T., Zaccone, A., Knowles, T. P. J., & Frenkel,
D. (2016). Kinetics of spontaneous filament nucleation via oligomers: Insights
from theory and simulation. The Journal of Chemical Physics. American Institute
of Physics. https://doi.org/10.1063/1.4965040'
chicago: 'Šarić, Anđela, Thomas C. T. Michaels, Alessio Zaccone, Tuomas P. J. Knowles,
and Daan Frenkel. “Kinetics of Spontaneous Filament Nucleation via Oligomers:
Insights from Theory and Simulation.” The Journal of Chemical Physics.
American Institute of Physics, 2016. https://doi.org/10.1063/1.4965040.'
ieee: 'A. Šarić, T. C. T. Michaels, A. Zaccone, T. P. J. Knowles, and D. Frenkel,
“Kinetics of spontaneous filament nucleation via oligomers: Insights from theory
and simulation,” The Journal of Chemical Physics, vol. 145, no. 21. American
Institute of Physics, 2016.'
ista: 'Šarić A, Michaels TCT, Zaccone A, Knowles TPJ, Frenkel D. 2016. Kinetics
of spontaneous filament nucleation via oligomers: Insights from theory and simulation.
The Journal of Chemical Physics. 145(21), 211926.'
mla: 'Šarić, Anđela, et al. “Kinetics of Spontaneous Filament Nucleation via Oligomers:
Insights from Theory and Simulation.” The Journal of Chemical Physics,
vol. 145, no. 21, 211926, American Institute of Physics, 2016, doi:10.1063/1.4965040.'
short: A. Šarić, T.C.T. Michaels, A. Zaccone, T.P.J. Knowles, D. Frenkel, The Journal
of Chemical Physics 145 (2016).
date_created: 2021-11-29T10:01:57Z
date_published: 2016-12-01T00:00:00Z
date_updated: 2021-11-29T10:33:11Z
day: '01'
doi: 10.1063/1.4965040
extern: '1'
external_id:
arxiv:
- '1610.02320'
pmid:
- '28799382'
intvolume: ' 145'
issue: '21'
keyword:
- physical and theoretical chemistry
- general physics and astronomy
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1610.02320
month: '12'
oa: 1
oa_version: Preprint
pmid: 1
publication: The Journal of Chemical Physics
publication_identifier:
eissn:
- 1089-7690
issn:
- 0021-9606
publication_status: published
publisher: American Institute of Physics
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'Kinetics of spontaneous filament nucleation via oligomers: Insights from theory
and simulation'
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 145
year: '2016'
...
---
_id: '10380'
abstract:
- lang: eng
text: Using non-equilibrium molecular dynamics simulations, it has been recently
demonstrated that water molecules align in response to an imposed temperature
gradient, resulting in an effective electric field. Here, we investigate how thermally
induced fields depend on the underlying treatment of long-ranged interactions.
For the short-ranged Wolf method and Ewald summation, we find the peak strength
of the field to range between 2 × 107 and 5 × 107 V/m for a temperature gradient
of 5.2 K/Å. Our value for the Wolf method is therefore an order of magnitude lower
than the literature value [J. A. Armstrong and F. Bresme, J. Chem. Phys. 139,
014504 (2013); J. Armstrong et al., J. Chem. Phys. 143, 036101 (2015)]. We show
that this discrepancy can be traced back to the use of an incorrect kernel in
the calculation of the electrostatic field. More seriously, we find that the Wolf
method fails to predict correct molecular orientations, resulting in dipole densities
with opposite sign to those computed using Ewald summation. By considering two
different multipole expansions, we show that, for inhomogeneous polarisations,
the quadrupole contribution can be significant and even outweigh the dipole contribution
to the field. Finally, we propose a more accurate way of calculating the electrostatic
potential and the field. In particular, we show that averaging the microscopic
field analytically to obtain the macroscopic Maxwell field reduces the error bars
by up to an order of magnitude. As a consequence, the simulation times required
to reach a given statistical accuracy decrease by up to two orders of magnitude.
acknowledgement: The authors should like to dedicate this paper to the memory of Simon
de Leeuw, who was a pioneer in the calculation of Coulomb effects in simulations.
P.W. would like to thank the Austrian Academy of Sciences for financial support
through a DOC Fellowship, and for covering the travel expenses for the CECAM workshop
in Zaragoza in May 2015, where these results were first presented. P.W. would also
like to thank Chao Zhang for pointing out the equivalence of the two expressions
for the electric field discussed in Sec. VI D, Michiel Sprik for emphasising the
importance of the quadrupole contribution in experimental studies of interfacial
systems, as well as Aleks Reinhardt and other members of the Frenkel and Dellago
groups for their advice. We further acknowledge support from the Federation of Austrian
Industry (IV) Carinthia (P.W.), the University of Zagreb and Erasmus SMP (D. Fijan),
the Human Frontier Science Program and Emmanuel College (A.Š.), the Austrian Science
Fund FWF within the SFB Vicom project F41 (C.D.), and the Engineering and Physical
Sciences Research Council Programme Grant No. EP/I001352/1 (D.F.). Additional data
related to this publication are available at the University of Cambridge data repository
(http://dx.doi.org/10.17863/CAM.118).
article_number: '224102'
article_processing_charge: No
article_type: original
author:
- first_name: P.
full_name: Wirnsberger, P.
last_name: Wirnsberger
- first_name: D.
full_name: Fijan, D.
last_name: Fijan
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: M.
full_name: Neumann, M.
last_name: Neumann
- first_name: C.
full_name: Dellago, C.
last_name: Dellago
- first_name: D.
full_name: Frenkel, D.
last_name: Frenkel
citation:
ama: Wirnsberger P, Fijan D, Šarić A, Neumann M, Dellago C, Frenkel D. Non-equilibrium
simulations of thermally induced electric fields in water. The Journal of Chemical
Physics. 2016;144(22). doi:10.1063/1.4953036
apa: Wirnsberger, P., Fijan, D., Šarić, A., Neumann, M., Dellago, C., & Frenkel,
D. (2016). Non-equilibrium simulations of thermally induced electric fields in
water. The Journal of Chemical Physics. American Institute of Physics.
https://doi.org/10.1063/1.4953036
chicago: Wirnsberger, P., D. Fijan, Anđela Šarić, M. Neumann, C. Dellago, and D.
Frenkel. “Non-Equilibrium Simulations of Thermally Induced Electric Fields in
Water.” The Journal of Chemical Physics. American Institute of Physics,
2016. https://doi.org/10.1063/1.4953036.
ieee: P. Wirnsberger, D. Fijan, A. Šarić, M. Neumann, C. Dellago, and D. Frenkel,
“Non-equilibrium simulations of thermally induced electric fields in water,” The
Journal of Chemical Physics, vol. 144, no. 22. American Institute of Physics,
2016.
ista: Wirnsberger P, Fijan D, Šarić A, Neumann M, Dellago C, Frenkel D. 2016. Non-equilibrium
simulations of thermally induced electric fields in water. The Journal of Chemical
Physics. 144(22), 224102.
mla: Wirnsberger, P., et al. “Non-Equilibrium Simulations of Thermally Induced Electric
Fields in Water.” The Journal of Chemical Physics, vol. 144, no. 22, 224102,
American Institute of Physics, 2016, doi:10.1063/1.4953036.
short: P. Wirnsberger, D. Fijan, A. Šarić, M. Neumann, C. Dellago, D. Frenkel, The
Journal of Chemical Physics 144 (2016).
date_created: 2021-11-29T11:08:52Z
date_published: 2016-06-10T00:00:00Z
date_updated: 2021-11-29T13:09:08Z
day: '10'
doi: 10.1063/1.4953036
extern: '1'
external_id:
arxiv:
- '1602.02734'
pmid:
- '27305991'
intvolume: ' 144'
issue: '22'
keyword:
- physical and theoretical chemistry
- general physics and astronomy
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1602.02734
month: '06'
oa: 1
oa_version: Preprint
pmid: 1
publication: The Journal of Chemical Physics
publication_identifier:
eissn:
- 1089-7690
issn:
- 0021-9606
publication_status: published
publisher: American Institute of Physics
quality_controlled: '1'
scopus_import: '1'
status: public
title: Non-equilibrium simulations of thermally induced electric fields in water
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 144
year: '2016'
...
---
_id: '10381'
abstract:
- lang: eng
text: We study phase behaviour of lipid-bilayer vesicles functionalised by ligand–receptor
complexes made of synthetic DNA by introducing a modelling framework and a dedicated
experimental platform. In particular, we perform Monte Carlo simulations that
combine a coarse grained description of the lipid bilayer with state of art analytical
models for multivalent ligand–receptor interactions. Using density of state calculations,
we derive the partition function in pairs of vesicles and compute the number of
ligand–receptor bonds as a function of temperature. Numerical results are compared
to microscopy and fluorimetry experiments on large unilamellar vesicles decorated
by DNA linkers carrying complementary overhangs. We find that vesicle aggregation
is suppressed when the total number of linkers falls below a threshold value.
Within the model proposed here, this is due to the higher configurational costs
required to form inter-vesicle bridges as compared to intra-vesicle loops, which
are in turn related to membrane deformability. Our findings and our numerical/experimental
methodologies are applicable to the rational design of liposomes used as functional
materials and drug delivery applications, as well as to study inter-membrane interactions
in living systems, such as cell adhesion.
article_processing_charge: No
article_type: original
author:
- first_name: Stephan Jan
full_name: Bachmann, Stephan Jan
last_name: Bachmann
- first_name: Jurij
full_name: Kotar, Jurij
last_name: Kotar
- first_name: Lucia
full_name: Parolini, Lucia
last_name: Parolini
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Pietro
full_name: Cicuta, Pietro
last_name: Cicuta
- first_name: Lorenzo
full_name: Di Michele, Lorenzo
last_name: Di Michele
- first_name: Bortolo Matteo
full_name: Mognetti, Bortolo Matteo
last_name: Mognetti
citation:
ama: Bachmann SJ, Kotar J, Parolini L, et al. Melting transition in lipid vesicles
functionalised by mobile DNA linkers. Soft Matter. 2016;12(37):7804-7817.
doi:10.1039/c6sm01515h
apa: Bachmann, S. J., Kotar, J., Parolini, L., Šarić, A., Cicuta, P., Di Michele,
L., & Mognetti, B. M. (2016). Melting transition in lipid vesicles functionalised
by mobile DNA linkers. Soft Matter. Royal Society of Chemistry. https://doi.org/10.1039/c6sm01515h
chicago: Bachmann, Stephan Jan, Jurij Kotar, Lucia Parolini, Anđela Šarić, Pietro
Cicuta, Lorenzo Di Michele, and Bortolo Matteo Mognetti. “Melting Transition in
Lipid Vesicles Functionalised by Mobile DNA Linkers.” Soft Matter. Royal
Society of Chemistry, 2016. https://doi.org/10.1039/c6sm01515h.
ieee: S. J. Bachmann et al., “Melting transition in lipid vesicles functionalised
by mobile DNA linkers,” Soft Matter, vol. 12, no. 37. Royal Society of
Chemistry, pp. 7804–7817, 2016.
ista: Bachmann SJ, Kotar J, Parolini L, Šarić A, Cicuta P, Di Michele L, Mognetti
BM. 2016. Melting transition in lipid vesicles functionalised by mobile DNA linkers.
Soft Matter. 12(37), 7804–7817.
mla: Bachmann, Stephan Jan, et al. “Melting Transition in Lipid Vesicles Functionalised
by Mobile DNA Linkers.” Soft Matter, vol. 12, no. 37, Royal Society of
Chemistry, 2016, pp. 7804–17, doi:10.1039/c6sm01515h.
short: S.J. Bachmann, J. Kotar, L. Parolini, A. Šarić, P. Cicuta, L. Di Michele,
B.M. Mognetti, Soft Matter 12 (2016) 7804–7817.
date_created: 2021-11-29T11:09:55Z
date_published: 2016-08-19T00:00:00Z
date_updated: 2021-11-29T13:09:00Z
day: '19'
doi: 10.1039/c6sm01515h
extern: '1'
external_id:
arxiv:
- '1608.05788'
pmid:
- '27722701'
intvolume: ' 12'
issue: '37'
keyword:
- condensed matter physics
- general chemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1608.05788
month: '08'
oa: 1
oa_version: Preprint
page: 7804-7817
pmid: 1
publication: Soft Matter
publication_identifier:
eissn:
- 1744-6848
issn:
- 1744-683X
publication_status: published
publisher: Royal Society of Chemistry
quality_controlled: '1'
scopus_import: '1'
status: public
title: Melting transition in lipid vesicles functionalised by mobile DNA linkers
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 12
year: '2016'
...
---
_id: '10378'
abstract:
- lang: eng
text: The ability of biological molecules to replicate themselves is the foundation
of life, requiring a complex cellular machinery. However, a range of aberrant
processes involve the self-replication of pathological protein structures without
any additional assistance. One example is the autocatalytic generation of pathological
protein aggregates, including amyloid fibrils, involved in neurodegenerative disorders.
Here, we use computer simulations to identify the necessary requirements for the
self-replication of fibrillar assemblies of proteins. We establish that a key
physical determinant for this process is the affinity of proteins for the surfaces
of fibrils. We find that self-replication can take place only in a very narrow
regime of inter-protein interactions, implying a high level of sensitivity to
system parameters and experimental conditions. We then compare our theoretical
predictions with kinetic and biosensor measurements of fibrils formed from the
Aβ peptide associated with Alzheimer’s disease. Our results show a quantitative
connection between the kinetics of self-replication and the surface coverage of
fibrils by monomeric proteins. These findings reveal the fundamental physical
requirements for the formation of supra-molecular structures able to replicate
themselves, and shed light on mechanisms in play in the proliferation of protein
aggregates in nature.
acknowledgement: We acknowledge support from the Human Frontier Science Program and
Emmanuel College (A.Š.), the Leverhulme Trust and Magdalene College (A.K.B.), St
John’s College (T.C.T.M.), the Biotechnology and Biological Sciences Research Council
(T.P.J.K. and C.M.D.), the Frances and Augustus Newman Foundation (T.P.J.K.), the
European Research Council (T.P.J.K., T.C.T.M., S.L. and D.F.), and the Engineering
and Physical Sciences Research Council (D.F.).
article_processing_charge: No
article_type: original
author:
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Alexander K.
full_name: Buell, Alexander K.
last_name: Buell
- first_name: Georg
full_name: Meisl, Georg
last_name: Meisl
- first_name: Thomas C. T.
full_name: Michaels, Thomas C. T.
last_name: Michaels
- first_name: Christopher M.
full_name: Dobson, Christopher M.
last_name: Dobson
- first_name: Sara
full_name: Linse, Sara
last_name: Linse
- first_name: Tuomas P. J.
full_name: Knowles, Tuomas P. J.
last_name: Knowles
- first_name: Daan
full_name: Frenkel, Daan
last_name: Frenkel
citation:
ama: Šarić A, Buell AK, Meisl G, et al. Physical determinants of the self-replication
of protein fibrils. Nature Physics. 2016;12(9):874-880. doi:10.1038/nphys3828
apa: Šarić, A., Buell, A. K., Meisl, G., Michaels, T. C. T., Dobson, C. M., Linse,
S., … Frenkel, D. (2016). Physical determinants of the self-replication of protein
fibrils. Nature Physics. Springer Nature. https://doi.org/10.1038/nphys3828
chicago: Šarić, Anđela, Alexander K. Buell, Georg Meisl, Thomas C. T. Michaels,
Christopher M. Dobson, Sara Linse, Tuomas P. J. Knowles, and Daan Frenkel. “Physical
Determinants of the Self-Replication of Protein Fibrils.” Nature Physics.
Springer Nature, 2016. https://doi.org/10.1038/nphys3828.
ieee: A. Šarić et al., “Physical determinants of the self-replication of
protein fibrils,” Nature Physics, vol. 12, no. 9. Springer Nature, pp.
874–880, 2016.
ista: Šarić A, Buell AK, Meisl G, Michaels TCT, Dobson CM, Linse S, Knowles TPJ,
Frenkel D. 2016. Physical determinants of the self-replication of protein fibrils.
Nature Physics. 12(9), 874–880.
mla: Šarić, Anđela, et al. “Physical Determinants of the Self-Replication of Protein
Fibrils.” Nature Physics, vol. 12, no. 9, Springer Nature, 2016, pp. 874–80,
doi:10.1038/nphys3828.
short: A. Šarić, A.K. Buell, G. Meisl, T.C.T. Michaels, C.M. Dobson, S. Linse, T.P.J.
Knowles, D. Frenkel, Nature Physics 12 (2016) 874–880.
date_created: 2021-11-29T10:36:11Z
date_published: 2016-07-18T00:00:00Z
date_updated: 2021-11-29T11:07:25Z
day: '18'
doi: 10.1038/nphys3828
extern: '1'
external_id:
pmid:
- '31031819'
intvolume: ' 12'
issue: '9'
keyword:
- general physics and astronomy
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://discovery.ucl.ac.uk/id/eprint/1517406/
month: '07'
oa: 1
oa_version: Preprint
page: 874-880
pmid: 1
publication: Nature Physics
publication_identifier:
eissn:
- 1745-2481
issn:
- 1745-2473
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Physical determinants of the self-replication of protein fibrils
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 12
year: '2016'
...
---
_id: '10382'
abstract:
- lang: eng
text: 'Protein oligomers have been implicated as toxic agents in a wide range of
amyloid-related diseases. However, it has remained unsolved whether the oligomers
are a necessary step in the formation of amyloid fibrils or just a dangerous byproduct.
Analogously, it has not been resolved if the amyloid nucleation process is a classical
one-step nucleation process or a two-step process involving prenucleation clusters.
We use coarse-grained computer simulations to study the effect of nonspecific
attractions between peptides on the primary nucleation process underlying amyloid
fibrillization. We find that, for peptides that do not attract, the classical
one-step nucleation mechanism is possible but only at nonphysiologically high
peptide concentrations. At low peptide concentrations, which mimic the physiologically
relevant regime, attractive interpeptide interactions are essential for fibril
formation. Nucleation then inevitably takes place through a two-step mechanism
involving prefibrillar oligomers. We show that oligomers not only help peptides
meet each other but also, create an environment that facilitates the conversion
of monomers into the β-sheet–rich form characteristic of fibrils. Nucleation typically
does not proceed through the most prevalent oligomers but through an oligomer
size that is only observed in rare fluctuations, which is why such aggregates
might be hard to capture experimentally. Finally, we find that the nucleation
of amyloid fibrils cannot be described by classical nucleation theory: in the
two-step mechanism, the critical nucleus size increases with increases in both
concentration and interpeptide interactions, which is in direct contrast with
predictions from classical nucleation theory.'
acknowledgement: We thank Michele Vendruscolo, Iskra Staneva, and William M. Jacobs,
for helpful discussions. A.Š. acknowledges support from the Human Frontier Science
Program and Emmanuel College. Y.C.C. and D.F. are supported by Engineering and Physical
Sciences Research Council Programme Grant EP/I001352/1. T.P.J.K. acknowledges the
Frances and Augustus Newman Foundation, the European Research Council, and the Biotechnology
and Biological Sciences Research Council. D.F. acknowledges European Research Council
Advanced Grant 227758.
article_processing_charge: No
article_type: original
author:
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Yassmine C.
full_name: Chebaro, Yassmine C.
last_name: Chebaro
- first_name: Tuomas P. J.
full_name: Knowles, Tuomas P. J.
last_name: Knowles
- first_name: Daan
full_name: Frenkel, Daan
last_name: Frenkel
citation:
ama: Šarić A, Chebaro YC, Knowles TPJ, Frenkel D. Crucial role of nonspecific interactions
in amyloid nucleation. Proceedings of the National Academy of Sciences.
2014;111(50):17869-17874. doi:10.1073/pnas.1410159111
apa: Šarić, A., Chebaro, Y. C., Knowles, T. P. J., & Frenkel, D. (2014). Crucial
role of nonspecific interactions in amyloid nucleation. Proceedings of the
National Academy of Sciences. National Academy of Sciences. https://doi.org/10.1073/pnas.1410159111
chicago: Šarić, Anđela, Yassmine C. Chebaro, Tuomas P. J. Knowles, and Daan Frenkel.
“Crucial Role of Nonspecific Interactions in Amyloid Nucleation.” Proceedings
of the National Academy of Sciences. National Academy of Sciences, 2014. https://doi.org/10.1073/pnas.1410159111.
ieee: A. Šarić, Y. C. Chebaro, T. P. J. Knowles, and D. Frenkel, “Crucial role of
nonspecific interactions in amyloid nucleation,” Proceedings of the National
Academy of Sciences, vol. 111, no. 50. National Academy of Sciences, pp. 17869–17874,
2014.
ista: Šarić A, Chebaro YC, Knowles TPJ, Frenkel D. 2014. Crucial role of nonspecific
interactions in amyloid nucleation. Proceedings of the National Academy of Sciences.
111(50), 17869–17874.
mla: Šarić, Anđela, et al. “Crucial Role of Nonspecific Interactions in Amyloid
Nucleation.” Proceedings of the National Academy of Sciences, vol. 111,
no. 50, National Academy of Sciences, 2014, pp. 17869–74, doi:10.1073/pnas.1410159111.
short: A. Šarić, Y.C. Chebaro, T.P.J. Knowles, D. Frenkel, Proceedings of the National
Academy of Sciences 111 (2014) 17869–17874.
date_created: 2021-11-29T13:09:53Z
date_published: 2014-12-01T00:00:00Z
date_updated: 2021-11-29T13:29:05Z
day: '01'
doi: 10.1073/pnas.1410159111
extern: '1'
external_id:
arxiv:
- '1412.0897'
pmid:
- '25453085'
intvolume: ' 111'
issue: '50'
keyword:
- multidisciplinary
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.pnas.org/content/111/50/17869
month: '12'
oa: 1
oa_version: Published Version
page: 17869-17874
pmid: 1
publication: Proceedings of the National Academy of Sciences
publication_identifier:
eissn:
- 1091-6490
issn:
- 0027-8424
publication_status: published
publisher: National Academy of Sciences
quality_controlled: '1'
scopus_import: '1'
status: public
title: Crucial role of nonspecific interactions in amyloid nucleation
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 111
year: '2014'
...
---
_id: '10383'
abstract:
- lang: eng
text: We use numerical simulations to compute the equation of state of a suspension
of spherical self-propelled nanoparticles in two and three dimensions. We study
in detail the effect of excluded volume interactions and confinement as a function
of the system's temperature, concentration, and strength of the propulsion. We
find a striking nonmonotonic dependence of the pressure on the temperature and
provide simple scaling arguments to predict and explain the occurrence of such
anomalous behavior. We explicitly show how our results have important implications
for the effective forces on passive components suspended in a bath of active particles.
article_number: '052303'
article_processing_charge: No
article_type: original
author:
- first_name: S. A.
full_name: Mallory, S. A.
last_name: Mallory
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: C.
full_name: Valeriani, C.
last_name: Valeriani
- first_name: A.
full_name: Cacciuto, A.
last_name: Cacciuto
citation:
ama: Mallory SA, Šarić A, Valeriani C, Cacciuto A. Anomalous thermomechanical properties
of a self-propelled colloidal fluid. Physical Review E. 2014;89(5). doi:10.1103/physreve.89.052303
apa: Mallory, S. A., Šarić, A., Valeriani, C., & Cacciuto, A. (2014). Anomalous
thermomechanical properties of a self-propelled colloidal fluid. Physical Review
E. American Physical Society. https://doi.org/10.1103/physreve.89.052303
chicago: Mallory, S. A., Anđela Šarić, C. Valeriani, and A. Cacciuto. “Anomalous
Thermomechanical Properties of a Self-Propelled Colloidal Fluid.” Physical
Review E. American Physical Society, 2014. https://doi.org/10.1103/physreve.89.052303.
ieee: S. A. Mallory, A. Šarić, C. Valeriani, and A. Cacciuto, “Anomalous thermomechanical
properties of a self-propelled colloidal fluid,” Physical Review E, vol.
89, no. 5. American Physical Society, 2014.
ista: Mallory SA, Šarić A, Valeriani C, Cacciuto A. 2014. Anomalous thermomechanical
properties of a self-propelled colloidal fluid. Physical Review E. 89(5), 052303.
mla: Mallory, S. A., et al. “Anomalous Thermomechanical Properties of a Self-Propelled
Colloidal Fluid.” Physical Review E, vol. 89, no. 5, 052303, American Physical
Society, 2014, doi:10.1103/physreve.89.052303.
short: S.A. Mallory, A. Šarić, C. Valeriani, A. Cacciuto, Physical Review E 89 (2014).
date_created: 2021-11-29T13:10:33Z
date_published: 2014-05-06T00:00:00Z
date_updated: 2021-11-29T13:29:01Z
day: '06'
doi: 10.1103/physreve.89.052303
extern: '1'
external_id:
arxiv:
- '1310.0826'
pmid:
- '25353796'
intvolume: ' 89'
issue: '5'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1310.0826
month: '05'
oa: 1
oa_version: Preprint
pmid: 1
publication: Physical Review E
publication_identifier:
eissn:
- 1550-2376
issn:
- 1539-3755
publication_status: published
publisher: American Physical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Anomalous thermomechanical properties of a self-propelled colloidal fluid
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 89
year: '2014'
...
---
_id: '10384'
abstract:
- lang: eng
text: 'Recent studies aimed at investigating artificial analogs of bacterial colonies
have shown that low-density suspensions of self-propelled particles confined in
two dimensions can assemble into finite aggregates that merge and split, but have
a typical size that remains constant (living clusters). In this Letter, we address
the problem of the formation of living clusters and crystals of active particles
in three dimensions. We study two systems: self-propelled particles interacting
via a generic attractive potential and colloids that can move toward each other
as a result of active agents (e.g., by molecular motors). In both cases, fluidlike
“living” clusters form. We explain this general feature in terms of the balance
between active forces and regression to thermodynamic equilibrium. This balance
can be quantified in terms of a dimensionless number that allows us to collapse
the observed clustering behavior onto a universal curve. We also discuss how active
motion affects the kinetics of crystal formation.'
acknowledgement: This work was supported by the ERC Advanced Grant 227758, the National
Science Foundation under Career Grant No. DMR-0846426, the Wolfson Merit Award 2007/R3
of the Royal Society of London and the EPSRC Programme Grant EP/I001352/1. BMM acknowledge
T. Curk and A. Ballard for useful discussions. C. V. acknowledges financial support
from a Juan de la Cierva Fellowship, from the Marie Curie Integration Grant PCIG-GA-2011-303941
ANISOKINEQ, and from the National Project FIS2010- 16159. S. A-U acknowledges support
from the Alexander von Humboldt Foundation.
article_number: '245702'
article_processing_charge: No
article_type: original
author:
- first_name: B. M.
full_name: Mognetti, B. M.
last_name: Mognetti
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: S.
full_name: Angioletti-Uberti, S.
last_name: Angioletti-Uberti
- first_name: A.
full_name: Cacciuto, A.
last_name: Cacciuto
- first_name: C.
full_name: Valeriani, C.
last_name: Valeriani
- first_name: D.
full_name: Frenkel, D.
last_name: Frenkel
citation:
ama: Mognetti BM, Šarić A, Angioletti-Uberti S, Cacciuto A, Valeriani C, Frenkel
D. Living clusters and crystals from low-density suspensions of active colloids.
Physical Review Letters. 2013;111(24). doi:10.1103/physrevlett.111.245702
apa: Mognetti, B. M., Šarić, A., Angioletti-Uberti, S., Cacciuto, A., Valeriani,
C., & Frenkel, D. (2013). Living clusters and crystals from low-density suspensions
of active colloids. Physical Review Letters. American Physical Society.
https://doi.org/10.1103/physrevlett.111.245702
chicago: Mognetti, B. M., Anđela Šarić, S. Angioletti-Uberti, A. Cacciuto, C. Valeriani,
and D. Frenkel. “Living Clusters and Crystals from Low-Density Suspensions of
Active Colloids.” Physical Review Letters. American Physical Society, 2013.
https://doi.org/10.1103/physrevlett.111.245702.
ieee: B. M. Mognetti, A. Šarić, S. Angioletti-Uberti, A. Cacciuto, C. Valeriani,
and D. Frenkel, “Living clusters and crystals from low-density suspensions of
active colloids,” Physical Review Letters, vol. 111, no. 24. American Physical
Society, 2013.
ista: Mognetti BM, Šarić A, Angioletti-Uberti S, Cacciuto A, Valeriani C, Frenkel
D. 2013. Living clusters and crystals from low-density suspensions of active colloids.
Physical Review Letters. 111(24), 245702.
mla: Mognetti, B. M., et al. “Living Clusters and Crystals from Low-Density Suspensions
of Active Colloids.” Physical Review Letters, vol. 111, no. 24, 245702,
American Physical Society, 2013, doi:10.1103/physrevlett.111.245702.
short: B.M. Mognetti, A. Šarić, S. Angioletti-Uberti, A. Cacciuto, C. Valeriani,
D. Frenkel, Physical Review Letters 111 (2013).
date_created: 2021-11-29T13:29:31Z
date_published: 2013-12-11T00:00:00Z
date_updated: 2021-11-29T14:05:19Z
day: '11'
doi: 10.1103/physrevlett.111.245702
extern: '1'
external_id:
arxiv:
- '1311.4681'
pmid:
- '24483677'
intvolume: ' 111'
issue: '24'
keyword:
- general physics and astronomy
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1311.4681
month: '12'
oa: 1
oa_version: Preprint
pmid: 1
publication: Physical Review Letters
publication_identifier:
eissn:
- 1079-7114
issn:
- 0031-9007
publication_status: published
publisher: American Physical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Living clusters and crystals from low-density suspensions of active colloids
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 111
year: '2013'
...
---
_id: '10386'
abstract:
- lang: eng
text: In this paper we review recent numerical and theoretical developments of particle
self-assembly on fluid and elastic membranes and compare them to available experimental
realizations. We discuss the problem and its applications in biology and materials
science, and give an overview of numerical models and strategies to study these
systems across all length-scales. As this is a very broad field, this review focuses
exclusively on surface-driven aggregation of nanoparticles that are at least one
order of magnitude larger than the surface thickness and are adsorbed onto it.
In this regime, all chemical details of the surface can be ignored in favor of
a coarse-grained representation, and the collective behavior of many particles
can be monitored and analyzed. We review the existing literature on how the mechanical
properties and the geometry of the surface affect the structure of the particle
aggregates and how these can drive shape deformation on the surface.
acknowledgement: This work was supported by the National Science Foundation under
Career Grant No. DMR 0846426. The authors thank J. C. Pàmies for many fruitful discussions
on the subject.
article_number: '6677'
article_processing_charge: No
article_type: original
author:
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Angelo
full_name: Cacciuto, Angelo
last_name: Cacciuto
citation:
ama: Šarić A, Cacciuto A. Self-assembly of nanoparticles adsorbed on fluid and elastic
membranes. Soft Matter. 2013;9(29). doi:10.1039/c3sm50188d
apa: Šarić, A., & Cacciuto, A. (2013). Self-assembly of nanoparticles adsorbed
on fluid and elastic membranes. Soft Matter. Royal Society of Chemistry.
https://doi.org/10.1039/c3sm50188d
chicago: Šarić, Anđela, and Angelo Cacciuto. “Self-Assembly of Nanoparticles Adsorbed
on Fluid and Elastic Membranes.” Soft Matter. Royal Society of Chemistry,
2013. https://doi.org/10.1039/c3sm50188d.
ieee: A. Šarić and A. Cacciuto, “Self-assembly of nanoparticles adsorbed on fluid
and elastic membranes,” Soft Matter, vol. 9, no. 29. Royal Society of Chemistry,
2013.
ista: Šarić A, Cacciuto A. 2013. Self-assembly of nanoparticles adsorbed on fluid
and elastic membranes. Soft Matter. 9(29), 6677.
mla: Šarić, Anđela, and Angelo Cacciuto. “Self-Assembly of Nanoparticles Adsorbed
on Fluid and Elastic Membranes.” Soft Matter, vol. 9, no. 29, 6677, Royal
Society of Chemistry, 2013, doi:10.1039/c3sm50188d.
short: A. Šarić, A. Cacciuto, Soft Matter 9 (2013).
date_created: 2021-11-29T14:06:32Z
date_published: 2013-05-03T00:00:00Z
date_updated: 2021-11-29T14:29:31Z
day: '03'
doi: 10.1039/c3sm50188d
extern: '1'
intvolume: ' 9'
issue: '29'
keyword:
- condensed matter physics
- general chemistry
language:
- iso: eng
main_file_link:
- url: https://pubs.rsc.org/en/content/articlehtml/2013/sm/c3sm50188d
month: '05'
oa_version: None
publication: Soft Matter
publication_identifier:
eissn:
- 1744-6848
issn:
- 1744-683X
publication_status: published
publisher: Royal Society of Chemistry
quality_controlled: '1'
scopus_import: '1'
status: public
title: Self-assembly of nanoparticles adsorbed on fluid and elastic membranes
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 9
year: '2013'
...
---
_id: '10385'
abstract:
- lang: eng
text: We show how self-assembly of sticky nanoparticles can drive radial collapse
of thin-walled nanotubes. Using numerical simulations, we study the transition
as a function of the geometric and elastic parameters of the nanotube and the
binding strength of the nanoparticles. We find that it is possible to derive a
simple scaling law relating all these parameters, and estimate bounds for the
onset conditions leading to the collapse of the nanotube. We also study the reverse
process – the nanoparticle release from the folded state – and find that the stability
of the collapsed state can be greatly improved by increasing the bending rigidity
of the nanotubes. Our results suggest ways to strengthen the mechanical properties
of nanotubes, but also indicate that the control of nanoparticle self-assembly
on these nanotubes can lead to nanoparticle-laden responsive materials.
acknowledgement: This work was supported by the National Science Foundation under
Career Grant no. DMR-0846426.
article_processing_charge: No
article_type: original
author:
- first_name: Joseph A.
full_name: Napoli, Joseph A.
last_name: Napoli
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Angelo
full_name: Cacciuto, Angelo
last_name: Cacciuto
citation:
ama: Napoli JA, Šarić A, Cacciuto A. Collapsing nanoparticle-laden nanotubes. Soft
Matter. 2013;9(37):8881-8886. doi:10.1039/c3sm51495a
apa: Napoli, J. A., Šarić, A., & Cacciuto, A. (2013). Collapsing nanoparticle-laden
nanotubes. Soft Matter. Royal Society of Chemistry. https://doi.org/10.1039/c3sm51495a
chicago: Napoli, Joseph A., Anđela Šarić, and Angelo Cacciuto. “Collapsing Nanoparticle-Laden
Nanotubes.” Soft Matter. Royal Society of Chemistry, 2013. https://doi.org/10.1039/c3sm51495a.
ieee: J. A. Napoli, A. Šarić, and A. Cacciuto, “Collapsing nanoparticle-laden nanotubes,”
Soft Matter, vol. 9, no. 37. Royal Society of Chemistry, pp. 8881–8886,
2013.
ista: Napoli JA, Šarić A, Cacciuto A. 2013. Collapsing nanoparticle-laden nanotubes.
Soft Matter. 9(37), 8881–8886.
mla: Napoli, Joseph A., et al. “Collapsing Nanoparticle-Laden Nanotubes.” Soft
Matter, vol. 9, no. 37, Royal Society of Chemistry, 2013, pp. 8881–86, doi:10.1039/c3sm51495a.
short: J.A. Napoli, A. Šarić, A. Cacciuto, Soft Matter 9 (2013) 8881–8886.
date_created: 2021-11-29T13:31:24Z
date_published: 2013-08-08T00:00:00Z
date_updated: 2021-11-29T14:05:23Z
day: '08'
doi: 10.1039/c3sm51495a
extern: '1'
intvolume: ' 9'
issue: '37'
keyword:
- condensed matter physics
- general chemistry
language:
- iso: eng
month: '08'
oa_version: None
page: 8881-8886
publication: Soft Matter
publication_identifier:
eissn:
- 1744-6848
issn:
- 1744-683X
publication_status: published
publisher: Royal Society of Chemistry
quality_controlled: '1'
scopus_import: '1'
status: public
title: Collapsing nanoparticle-laden nanotubes
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 9
year: '2013'
...
---
_id: '10387'
abstract:
- lang: eng
text: We report numerical simulations of membrane tubulation driven by large colloidal
particles. Using Monte Carlo simulations we study how the process depends on particle
size and binding strength, and present accurate free energy calculations to sort
out how tube formation compares with the competing budding process. We find that
tube formation is a result of the collective behavior of the particles adhering
on the surface, and it occurs for binding strengths that are smaller than those
required for budding. We also find that long linear aggregates of particles forming
on the membrane surface act as nucleation seeds for tubulation by lowering the
free energy barrier associated to the process.
article_number: '188101'
article_processing_charge: No
article_type: original
author:
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Angelo
full_name: Cacciuto, Angelo
last_name: Cacciuto
citation:
ama: Šarić A, Cacciuto A. Mechanism of membrane tube formation induced by adhesive
nanocomponents. Physical Review Letters. 2012;109(18). doi:10.1103/physrevlett.109.188101
apa: Šarić, A., & Cacciuto, A. (2012). Mechanism of membrane tube formation
induced by adhesive nanocomponents. Physical Review Letters. American Physical
Society. https://doi.org/10.1103/physrevlett.109.188101
chicago: Šarić, Anđela, and Angelo Cacciuto. “Mechanism of Membrane Tube Formation
Induced by Adhesive Nanocomponents.” Physical Review Letters. American
Physical Society, 2012. https://doi.org/10.1103/physrevlett.109.188101.
ieee: A. Šarić and A. Cacciuto, “Mechanism of membrane tube formation induced by
adhesive nanocomponents,” Physical Review Letters, vol. 109, no. 18. American
Physical Society, 2012.
ista: Šarić A, Cacciuto A. 2012. Mechanism of membrane tube formation induced by
adhesive nanocomponents. Physical Review Letters. 109(18), 188101.
mla: Šarić, Anđela, and Angelo Cacciuto. “Mechanism of Membrane Tube Formation Induced
by Adhesive Nanocomponents.” Physical Review Letters, vol. 109, no. 18,
188101, American Physical Society, 2012, doi:10.1103/physrevlett.109.188101.
short: A. Šarić, A. Cacciuto, Physical Review Letters 109 (2012).
date_created: 2021-11-29T14:08:00Z
date_published: 2012-10-31T00:00:00Z
date_updated: 2021-11-29T14:29:25Z
day: '31'
doi: 10.1103/physrevlett.109.188101
extern: '1'
external_id:
arxiv:
- '1206.3528'
pmid:
- '23215334'
intvolume: ' 109'
issue: '18'
keyword:
- general physics and astronomy
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1206.3528
month: '10'
oa: 1
oa_version: Preprint
pmid: 1
publication: Physical Review Letters
publication_identifier:
eissn:
- 1079-7114
issn:
- 0031-9007
publication_status: published
publisher: American Physical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Mechanism of membrane tube formation induced by adhesive nanocomponents
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 109
year: '2012'
...
---
_id: '10388'
abstract:
- lang: eng
text: Using computer simulations, we show that lipid membranes can mediate linear
aggregation of spherical nanoparticles binding to it for a wide range of biologically
relevant bending rigidities. This result is in net contrast with the isotropic
aggregation of nanoparticles on fluid interfaces or the expected clustering of
isotropic insertions in biological membranes. We present a phase diagram indicating
where linear aggregation is expected and compute explicitly the free-energy barriers
associated with linear and isotropic aggregation. Finally, we provide simple scaling
arguments to explain this phenomenology.
acknowledgement: "This work was supported by the National Science Foundation under
Career Grant No. DMR-0846426.\r\n"
article_number: '118101'
article_processing_charge: No
article_type: original
author:
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Angelo
full_name: Cacciuto, Angelo
last_name: Cacciuto
citation:
ama: Šarić A, Cacciuto A. Fluid membranes can drive linear aggregation of adsorbed
spherical nanoparticles. Physical Review Letters. 2012;108(11). doi:10.1103/physrevlett.108.118101
apa: Šarić, A., & Cacciuto, A. (2012). Fluid membranes can drive linear aggregation
of adsorbed spherical nanoparticles. Physical Review Letters. American
Physical Society. https://doi.org/10.1103/physrevlett.108.118101
chicago: Šarić, Anđela, and Angelo Cacciuto. “Fluid Membranes Can Drive Linear Aggregation
of Adsorbed Spherical Nanoparticles.” Physical Review Letters. American
Physical Society, 2012. https://doi.org/10.1103/physrevlett.108.118101.
ieee: A. Šarić and A. Cacciuto, “Fluid membranes can drive linear aggregation of
adsorbed spherical nanoparticles,” Physical Review Letters, vol. 108, no.
11. American Physical Society, 2012.
ista: Šarić A, Cacciuto A. 2012. Fluid membranes can drive linear aggregation of
adsorbed spherical nanoparticles. Physical Review Letters. 108(11), 118101.
mla: Šarić, Anđela, and Angelo Cacciuto. “Fluid Membranes Can Drive Linear Aggregation
of Adsorbed Spherical Nanoparticles.” Physical Review Letters, vol. 108,
no. 11, 118101, American Physical Society, 2012, doi:10.1103/physrevlett.108.118101.
short: A. Šarić, A. Cacciuto, Physical Review Letters 108 (2012).
date_created: 2021-11-29T14:30:05Z
date_published: 2012-03-14T00:00:00Z
date_updated: 2021-11-29T15:12:13Z
day: '14'
doi: 10.1103/physrevlett.108.118101
extern: '1'
external_id:
arxiv:
- '1201.0036'
pmid:
- '22540513'
intvolume: ' 108'
issue: '11'
keyword:
- general physics and astronomy
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1201.0036
month: '03'
oa: 1
oa_version: Preprint
pmid: 1
publication: Physical Review Letters
publication_identifier:
eissn:
- 1079-7114
issn:
- 0031-9007
publication_status: published
publisher: American Physical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Fluid membranes can drive linear aggregation of adsorbed spherical nanoparticles
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 108
year: '2012'
...
---
_id: '10389'
abstract:
- lang: eng
text: We perform numerical simulations to study self-assembly of nanoparticles mediated
by an elastic planar surface. We show how the nontrivial elastic response to deformations
of these surfaces leads to anisotropic interactions between the particles resulting
in aggregates having different geometrical features. The morphology of the patterns
can be controlled by the mechanical properties of the surface and the strength
of the particle adhesion. We use simple scaling arguments to understand the formation
of the different structures, and we show how the adhering particles can cause
the underlying elastic substrate to wrinkle if two of its opposite edges are clamped.
Finally, we discuss the implications of our results and suggest how elastic surfaces
could be used in nanofabrication.
acknowledgement: This work was supported by the National Science Foundation under
Career Grant No. DMR-0846426. We thank Josep C. Pàmies and William L. Miller for
helpful discussions.
article_number: '8324'
article_processing_charge: No
article_type: original
author:
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Angelo
full_name: Cacciuto, Angelo
last_name: Cacciuto
citation:
ama: Šarić A, Cacciuto A. Soft elastic surfaces as a platform for particle self-assembly.
Soft Matter. 2011;7(18). doi:10.1039/c1sm05773a
apa: Šarić, A., & Cacciuto, A. (2011). Soft elastic surfaces as a platform for
particle self-assembly. Soft Matter. Royal Society of Chemistry. https://doi.org/10.1039/c1sm05773a
chicago: Šarić, Anđela, and Angelo Cacciuto. “Soft Elastic Surfaces as a Platform
for Particle Self-Assembly.” Soft Matter. Royal Society of Chemistry, 2011.
https://doi.org/10.1039/c1sm05773a.
ieee: A. Šarić and A. Cacciuto, “Soft elastic surfaces as a platform for particle
self-assembly,” Soft Matter, vol. 7, no. 18. Royal Society of Chemistry,
2011.
ista: Šarić A, Cacciuto A. 2011. Soft elastic surfaces as a platform for particle
self-assembly. Soft Matter. 7(18), 8324.
mla: Šarić, Anđela, and Angelo Cacciuto. “Soft Elastic Surfaces as a Platform for
Particle Self-Assembly.” Soft Matter, vol. 7, no. 18, 8324, Royal Society
of Chemistry, 2011, doi:10.1039/c1sm05773a.
short: A. Šarić, A. Cacciuto, Soft Matter 7 (2011).
date_created: 2021-11-29T14:33:18Z
date_published: 2011-08-08T00:00:00Z
date_updated: 2021-11-29T15:12:10Z
day: '08'
doi: 10.1039/c1sm05773a
extern: '1'
external_id:
arxiv:
- '1106.2995'
intvolume: ' 7'
issue: '18'
keyword:
- condensed matter physics
- general chemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1106.2995
month: '08'
oa: 1
oa_version: Preprint
publication: Soft Matter
publication_identifier:
eissn:
- 1744-6848
issn:
- 1744-683X
publication_status: published
publisher: Royal Society of Chemistry
quality_controlled: '1'
scopus_import: '1'
status: public
title: Soft elastic surfaces as a platform for particle self-assembly
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 7
year: '2011'
...
---
_id: '10128'
abstract:
- lang: eng
text: 'An extensive computational study of the conformational preferences of three
capped dipeptides: Ac-Xxx-Phe-NH2, Xxx = Gly, Ala, Val is reported. On the basis
of local second-order Møller–Plesset perturbation theory (LMP2) and DFT computations
we were able to identify the experimentally observed conformers as γL–γL(g−) and
β-turn I(g+) in Ac-Gly-Phe-NH2, and Ac-Ala-Phe-NH2, and as the closely related
γL(g+)–γL(g−) and β-turn I(a,g+) in Ac-Val-Phe-NH2. In contrast to the experimental
observation that peptides with bulky side chain have a propensity for β-turns,
we show that in Ac-Val-Phe-NH2 the minimum energy structure corresponds to the
experimentally non detected β-strand.'
acknowledgement: This work has been supported by the MZOŠ projects 098-0352851-2921
and 119-1191342-2959.
article_processing_charge: No
article_type: original
author:
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: T.
full_name: Hrenar, T.
last_name: Hrenar
- first_name: M.
full_name: Mališ, M.
last_name: Mališ
- first_name: N.
full_name: Došlić, N.
last_name: Došlić
citation:
ama: Šarić A, Hrenar T, Mališ M, Došlić N. Quantum mechanical study of secondary
structure formation in protected dipeptides. Physical Chemistry Chemical Physics.
2010;12(18):4678-4685. doi:10.1039/b923041f
apa: Šarić, A., Hrenar, T., Mališ, M., & Došlić, N. (2010). Quantum mechanical
study of secondary structure formation in protected dipeptides. Physical Chemistry
Chemical Physics. Royal Society of Chemistry . https://doi.org/10.1039/b923041f
chicago: Šarić, Anđela, T. Hrenar, M. Mališ, and N. Došlić. “Quantum Mechanical
Study of Secondary Structure Formation in Protected Dipeptides.” Physical Chemistry
Chemical Physics. Royal Society of Chemistry , 2010. https://doi.org/10.1039/b923041f.
ieee: A. Šarić, T. Hrenar, M. Mališ, and N. Došlić, “Quantum mechanical study of
secondary structure formation in protected dipeptides,” Physical Chemistry
Chemical Physics, vol. 12, no. 18. Royal Society of Chemistry , pp. 4678–4685,
2010.
ista: Šarić A, Hrenar T, Mališ M, Došlić N. 2010. Quantum mechanical study of secondary
structure formation in protected dipeptides. Physical Chemistry Chemical Physics.
12(18), 4678–4685.
mla: Šarić, Anđela, et al. “Quantum Mechanical Study of Secondary Structure Formation
in Protected Dipeptides.” Physical Chemistry Chemical Physics, vol. 12,
no. 18, Royal Society of Chemistry , 2010, pp. 4678–85, doi:10.1039/b923041f.
short: A. Šarić, T. Hrenar, M. Mališ, N. Došlić, Physical Chemistry Chemical Physics
12 (2010) 4678–4685.
date_created: 2021-10-12T08:44:34Z
date_published: 2010-03-16T00:00:00Z
date_updated: 2021-10-12T09:49:22Z
day: '16'
doi: 10.1039/b923041f
extern: '1'
external_id:
pmid:
- '20428547'
intvolume: ' 12'
issue: '18'
keyword:
- Physical and Theoretical Chemistry
- General Physics and Astronomy
language:
- iso: eng
main_file_link:
- url: https://europepmc.org/article/med/20428547
month: '03'
oa_version: None
page: 4678-4685
pmid: 1
publication: Physical Chemistry Chemical Physics
publication_identifier:
issn:
- 1463-9076
- 1463-9084
publication_status: published
publisher: 'Royal Society of Chemistry '
quality_controlled: '1'
status: public
title: Quantum mechanical study of secondary structure formation in protected dipeptides
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 12
year: '2010'
...
---
_id: '10127'
abstract:
- lang: eng
text: We use numerical simulations to show how noninteracting hard particles binding
to a deformable elastic shell may self-assemble into a variety of linear patterns.
This is a result of the nontrivial elastic response to deformations of shells.
The morphology of the patterns can be controlled by the mechanical properties
of the surface, and can be fine-tuned by varying the binding energy of the particles.
We also repeat our calculations for a fully flexible chain and find that the chain
conformations follow patterns similar to those formed by the nanoparticles under
analogous conditions. We propose a simple way of understanding and sorting the
different structures and relate it to the underlying shape transition of the shell.
Finally, we discuss the implications of our results.
acknowledgement: This work was supported by the National Science Foundation under
Career Grant No. DMR-0846426. We thank Josep C. Pàmies for helpful discussions.
article_processing_charge: No
article_type: original
author:
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Angelo
full_name: Cacciuto, Angelo
last_name: Cacciuto
citation:
ama: Šarić A, Cacciuto A. Particle self-assembly on soft elastic shells. Soft
Matter. 2010;7(5):1874-1878. doi:10.1039/c0sm01143f
apa: Šarić, A., & Cacciuto, A. (2010). Particle self-assembly on soft elastic
shells. Soft Matter. Royal Society of Chemistry (RSC). https://doi.org/10.1039/c0sm01143f
chicago: Šarić, Anđela, and Angelo Cacciuto. “Particle Self-Assembly on Soft Elastic
Shells.” Soft Matter. Royal Society of Chemistry (RSC), 2010. https://doi.org/10.1039/c0sm01143f.
ieee: A. Šarić and A. Cacciuto, “Particle self-assembly on soft elastic shells,”
Soft Matter, vol. 7, no. 5. Royal Society of Chemistry (RSC), pp. 1874–1878,
2010.
ista: Šarić A, Cacciuto A. 2010. Particle self-assembly on soft elastic shells.
Soft Matter. 7(5), 1874–1878.
mla: Šarić, Anđela, and Angelo Cacciuto. “Particle Self-Assembly on Soft Elastic
Shells.” Soft Matter, vol. 7, no. 5, Royal Society of Chemistry (RSC),
2010, pp. 1874–78, doi:10.1039/c0sm01143f.
short: A. Šarić, A. Cacciuto, Soft Matter 7 (2010) 1874–1878.
date_created: 2021-10-12T08:34:23Z
date_published: 2010-12-23T00:00:00Z
date_updated: 2021-10-12T09:49:27Z
day: '23'
doi: 10.1039/c0sm01143f
extern: '1'
external_id:
arxiv:
- '1010.2453'
intvolume: ' 7'
issue: '5'
keyword:
- condensed matter physics
- general chemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1010.2453
month: '12'
oa: 1
oa_version: Preprint
page: 1874-1878
publication: Soft Matter
publication_identifier:
issn:
- 1744-683X
- 1744-6848
publication_status: published
publisher: Royal Society of Chemistry (RSC)
quality_controlled: '1'
status: public
title: Particle self-assembly on soft elastic shells
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 7
year: '2010'
...
---
_id: '10390'
abstract:
- lang: eng
text: 'We use numerical simulations to study the phase behavior of a system of purely
repulsive soft dumbbells as a function of size ratio of the two components and
their relative degree of deformability. We find a plethora of different phases,
which includes most of the mesophases observed in self-assembly of block copolymers
but also crystalline structures formed by asymmetric, hard binary mixtures. Our
results detail the phenomenological behavior of these systems when softness is
introduced in terms of two different classes of interparticle interactions: (a)
the elastic Hertz potential, which has a finite energy cost for complete overlap
of any two components, and (b) a generic power-law repulsion with tunable exponent.
We discuss how simple geometric arguments can be used to account for the large
structural variety observed in these systems and detail the similarities and differences
in the phase behavior for the two classes of potentials under consideration.'
acknowledgement: This work was supported by the National Science Foundation under
CAREER Grant No. DMR-0846426 and partly by Columbia University.
article_processing_charge: No
article_type: original
author:
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Behnaz
full_name: Bozorgui, Behnaz
last_name: Bozorgui
- first_name: Angelo
full_name: Cacciuto, Angelo
last_name: Cacciuto
citation:
ama: Šarić A, Bozorgui B, Cacciuto A. Packing of soft asymmetric dumbbells. The
Journal of Physical Chemistry B. 2010;115(22):7182-7189. doi:10.1021/jp107545w
apa: Šarić, A., Bozorgui, B., & Cacciuto, A. (2010). Packing of soft asymmetric
dumbbells. The Journal of Physical Chemistry B. American Chemical Society.
https://doi.org/10.1021/jp107545w
chicago: Šarić, Anđela, Behnaz Bozorgui, and Angelo Cacciuto. “Packing of Soft Asymmetric
Dumbbells.” The Journal of Physical Chemistry B. American Chemical Society,
2010. https://doi.org/10.1021/jp107545w.
ieee: A. Šarić, B. Bozorgui, and A. Cacciuto, “Packing of soft asymmetric dumbbells,”
The Journal of Physical Chemistry B, vol. 115, no. 22. American Chemical
Society, pp. 7182–7189, 2010.
ista: Šarić A, Bozorgui B, Cacciuto A. 2010. Packing of soft asymmetric dumbbells.
The Journal of Physical Chemistry B. 115(22), 7182–7189.
mla: Šarić, Anđela, et al. “Packing of Soft Asymmetric Dumbbells.” The Journal
of Physical Chemistry B, vol. 115, no. 22, American Chemical Society, 2010,
pp. 7182–89, doi:10.1021/jp107545w.
short: A. Šarić, B. Bozorgui, A. Cacciuto, The Journal of Physical Chemistry B 115
(2010) 7182–7189.
date_created: 2021-11-29T15:13:17Z
date_published: 2010-10-15T00:00:00Z
date_updated: 2021-11-29T16:20:29Z
day: '15'
doi: 10.1021/jp107545w
extern: '1'
external_id:
arxiv:
- '1010.2458'
pmid:
- '20949934'
intvolume: ' 115'
issue: '22'
keyword:
- materials chemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1010.2458
month: '10'
oa: 1
oa_version: Preprint
page: 7182-7189
pmid: 1
publication: The Journal of Physical Chemistry B
publication_identifier:
eissn:
- 1520-5207
issn:
- 1520-6106
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Packing of soft asymmetric dumbbells
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 115
year: '2010'
...
---
_id: '10391'
abstract:
- lang: eng
text: We use numerical simulations to show how a fully flexible filament binding
to a deformable cylindrical surface may acquire a macroscopic persistence length
and a helical conformation. This is a result of the nontrivial elastic response
to deformations of elastic sheets. We find that the filament’s helical pitch is
completely determined by the mechanical properties of the surface, and can be
easily tuned by varying the surface stretching rigidity. We propose simple scaling
arguments to understand the physical mechanism behind this phenomenon and present
a phase diagram indicating under what conditions one should expect a fully flexible
chain to behave as a helical semiflexible filament. Finally, we discuss the implications
of our results.
acknowledgement: This work was supported by the National Science Foundation under
Career Grant No. DMR-0846426.
article_number: '226101'
article_processing_charge: No
article_type: original
author:
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Josep C.
full_name: Pàmies, Josep C.
last_name: Pàmies
- first_name: Angelo
full_name: Cacciuto, Angelo
last_name: Cacciuto
citation:
ama: Šarić A, Pàmies JC, Cacciuto A. Effective elasticity of a flexible filament
bound to a deformable cylindrical surface. Physical Review Letters. 2010;104(22).
doi:10.1103/physrevlett.104.226101
apa: Šarić, A., Pàmies, J. C., & Cacciuto, A. (2010). Effective elasticity of
a flexible filament bound to a deformable cylindrical surface. Physical Review
Letters. American Physical Society. https://doi.org/10.1103/physrevlett.104.226101
chicago: Šarić, Anđela, Josep C. Pàmies, and Angelo Cacciuto. “Effective Elasticity
of a Flexible Filament Bound to a Deformable Cylindrical Surface.” Physical
Review Letters. American Physical Society, 2010. https://doi.org/10.1103/physrevlett.104.226101.
ieee: A. Šarić, J. C. Pàmies, and A. Cacciuto, “Effective elasticity of a flexible
filament bound to a deformable cylindrical surface,” Physical Review Letters,
vol. 104, no. 22. American Physical Society, 2010.
ista: Šarić A, Pàmies JC, Cacciuto A. 2010. Effective elasticity of a flexible filament
bound to a deformable cylindrical surface. Physical Review Letters. 104(22), 226101.
mla: Šarić, Anđela, et al. “Effective Elasticity of a Flexible Filament Bound to
a Deformable Cylindrical Surface.” Physical Review Letters, vol. 104, no.
22, 226101, American Physical Society, 2010, doi:10.1103/physrevlett.104.226101.
short: A. Šarić, J.C. Pàmies, A. Cacciuto, Physical Review Letters 104 (2010).
date_created: 2021-11-29T15:14:33Z
date_published: 2010-06-03T00:00:00Z
date_updated: 2021-11-30T08:11:19Z
day: '03'
doi: 10.1103/physrevlett.104.226101
extern: '1'
external_id:
arxiv:
- '1005.2429'
pmid:
- '20867183'
intvolume: ' 104'
issue: '22'
keyword:
- general physics and astronomy
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1005.2429
month: '06'
oa: 1
oa_version: Preprint
pmid: 1
publication: Physical Review Letters
publication_identifier:
eissn:
- 1079-7114
issn:
- 0031-9007
publication_status: published
publisher: American Physical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Effective elasticity of a flexible filament bound to a deformable cylindrical
surface
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 104
year: '2010'
...
---
_id: '10392'
abstract:
- lang: eng
text: Protonated formylmetallocenes [M(C5H5)(C5H4-CHOH)]+ (M = Fe, Ru) and their
isomers have been studied at the BP86 and B3LYP levels of density functional theory.
Oxygen-protonated isomers are the most stable forms in each case, with a plethora
of ring- or metal-protonated species at least ca. 14 and 10 kcal/mol higher in
energy for M = Fe and Ru, respectively. The computed rotational barriers around
the C−C bond connecting the cyclopentadienyl and protonated formyl moieties, ca.
18 kcal/mol, are indicative of substantial conjugation between these moieties.
Some of the ring- and iron-protonated species are models for possible intermediates
in Friedel–Crafts acylation of ferrocene, and the computations provide further
evidence that exo attack is clearly favored over endo attack of the electrophile
in this reaction. The structures of the most stable mono- and diprotonated formylferrocenes
are corroborated by the good agreement between GIAO-B3LYP-computed and experimental
NMR chemical shifts.
acknowledgement: M.B. wishes to thank Prof. W. Thiel and the Max-Planck-Institut für
Kohlenforschung for continuing support. A Humboldt fellowship for V.V. is gratefully
acknowledged. Computations were performed on Compaq XP1000 and ES40 workstations
as well as on an Intel Xeon PC cluster at the MPI Mülheim. A.S. thanks the Computing
Center of the University of Zagreb SRCE for allocating computer time on the Isabella
cluster.
article_processing_charge: No
article_type: original
author:
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Valerije
full_name: Vrček, Valerije
last_name: Vrček
- first_name: Michael
full_name: Bühl, Michael
last_name: Bühl
citation:
ama: Šarić A, Vrček V, Bühl M. Density functional study of protonated formylmetallocenes.
Organometallics. 2008;27(3):394-401. doi:10.1021/om700916f
apa: Šarić, A., Vrček, V., & Bühl, M. (2008). Density functional study of protonated
formylmetallocenes. Organometallics. American Chemical Society. https://doi.org/10.1021/om700916f
chicago: Šarić, Anđela, Valerije Vrček, and Michael Bühl. “Density Functional Study
of Protonated Formylmetallocenes.” Organometallics. American Chemical Society,
2008. https://doi.org/10.1021/om700916f.
ieee: A. Šarić, V. Vrček, and M. Bühl, “Density functional study of protonated formylmetallocenes,”
Organometallics, vol. 27, no. 3. American Chemical Society, pp. 394–401,
2008.
ista: Šarić A, Vrček V, Bühl M. 2008. Density functional study of protonated formylmetallocenes.
Organometallics. 27(3), 394–401.
mla: Šarić, Anđela, et al. “Density Functional Study of Protonated Formylmetallocenes.”
Organometallics, vol. 27, no. 3, American Chemical Society, 2008, pp. 394–401,
doi:10.1021/om700916f.
short: A. Šarić, V. Vrček, M. Bühl, Organometallics 27 (2008) 394–401.
date_created: 2021-11-29T15:31:06Z
date_published: 2008-01-15T00:00:00Z
date_updated: 2021-11-30T08:04:44Z
day: '15'
doi: 10.1021/om700916f
extern: '1'
intvolume: ' 27'
issue: '3'
keyword:
- Inorganic Chemistry
- Organic Chemistry
- Physical and Theoretical Chemistry
language:
- iso: eng
main_file_link:
- url: https://pubs.acs.org/doi/10.1021/om700916f
month: '01'
oa_version: None
page: 394-401
publication: Organometallics
publication_identifier:
eissn:
- 1520-6041
issn:
- 0276-7333
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Density functional study of protonated formylmetallocenes
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 27
year: '2008'
...