---
OA_place: repository
OA_type: green
_id: '14442'
abstract:
- lang: eng
text: In the presence of an obstacle, active particles condensate into a surface
“wetting” layer due to persistent motion. If the obstacle is asymmetric, a rectification
current arises in addition to wetting. Asymmetric geometries are therefore commonly
used to concentrate microorganisms like bacteria and sperms. However, most studies
neglect the fact that biological active matter is diverse, composed of individuals
with distinct self-propulsions. Using simulations, we study a mixture of “fast”
and “slow” active Brownian disks in two dimensions interacting with large half-disk
obstacles. With this prototypical obstacle geometry, we analyze how the stationary
collective behavior depends on the degree of self-propulsion “diversity,” defined
as proportional to the difference between the self-propulsion speeds, while keeping
the average self-propulsion speed fixed. A wetting layer rich in fast particles
arises. The rectification current is amplified by speed diversity due to a superlinear
dependence of rectification on self-propulsion speed, which arises from cooperative
effects. Thus, the total rectification current cannot be obtained from an effective
one-component active fluid with the same average self-propulsion speed, highlighting
the importance of considering diversity in active matter.
acknowledgement: MR-V and RS are supported by Fondecyt Grant No. 1220536 and Millennium
Science Initiative Program NCN19_170D of ANID, Chile. P.d.C. was supported by Scholarships
Nos. 2021/10139-2 and 2022/13872-5 and ICTP-SAIFR Grant No. 2021/14335-0, all granted
by São Paulo Research Foundation (FAPESP), Brazil.
article_number: '95'
article_processing_charge: No
article_type: original
arxiv: 1
author:
- first_name: Mauricio Nicolas
full_name: Rojas Vega, Mauricio Nicolas
id: 441e7207-f91f-11ec-b67c-9e6fe3d8fd6d
last_name: Rojas Vega
- first_name: Pablo
full_name: De Castro, Pablo
last_name: De Castro
- first_name: Rodrigo
full_name: Soto, Rodrigo
last_name: Soto
citation:
ama: Rojas Vega MN, De Castro P, Soto R. Mixtures of self-propelled particles interacting
with asymmetric obstacles. The European Physical Journal E. 2023;46(10).
doi:10.1140/epje/s10189-023-00354-y
apa: Rojas Vega, M. N., De Castro, P., & Soto, R. (2023). Mixtures of self-propelled
particles interacting with asymmetric obstacles. The European Physical Journal
E. Springer Nature. https://doi.org/10.1140/epje/s10189-023-00354-y
chicago: Rojas Vega, Mauricio Nicolas, Pablo De Castro, and Rodrigo Soto. “Mixtures
of Self-Propelled Particles Interacting with Asymmetric Obstacles.” The European
Physical Journal E. Springer Nature, 2023. https://doi.org/10.1140/epje/s10189-023-00354-y.
ieee: M. N. Rojas Vega, P. De Castro, and R. Soto, “Mixtures of self-propelled particles
interacting with asymmetric obstacles,” The European Physical Journal E,
vol. 46, no. 10. Springer Nature, 2023.
ista: Rojas Vega MN, De Castro P, Soto R. 2023. Mixtures of self-propelled particles
interacting with asymmetric obstacles. The European Physical Journal E. 46(10),
95.
mla: Rojas Vega, Mauricio Nicolas, et al. “Mixtures of Self-Propelled Particles
Interacting with Asymmetric Obstacles.” The European Physical Journal E,
vol. 46, no. 10, 95, Springer Nature, 2023, doi:10.1140/epje/s10189-023-00354-y.
short: M.N. Rojas Vega, P. De Castro, R. Soto, The European Physical Journal E 46
(2023).
corr_author: '1'
date_created: 2023-10-22T22:01:13Z
date_published: 2023-10-01T00:00:00Z
date_updated: 2025-09-09T13:08:14Z
day: '01'
department:
- _id: AnSa
doi: 10.1140/epje/s10189-023-00354-y
external_id:
arxiv:
- '2111.05952'
isi:
- '001187541900001'
pmid:
- '37819444'
fulldoi: https://doi.org/10.1140/epje/s10189-023-00354-y
intvolume: ' 46'
isi: 1
issue: '10'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: ' https://doi.org/10.48550/arXiv.2111.05952'
month: '10'
oa: 1
oa_version: Preprint
pmid: 1
publication: The European Physical Journal E
publication_identifier:
eissn:
- 1292-895X
issn:
- 1292-8941
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Mixtures of self-propelled particles interacting with asymmetric obstacles
type: journal_article
user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 46
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).
corr_author: '1'
date_created: 2023-10-30T16:38:32Z
date_published: 2023-10-31T00:00:00Z
date_updated: 2025-09-09T13:30:33Z
day: '31'
ddc:
- '570'
department:
- _id: AnSa
doi: 10.15479/AT:ISTA:14472
file:
- access_level: open_access
checksum: a18706e952e8660c51ede52a167270b7
content_type: application/zip
creator: ipalaia
date_created: 2023-10-30T16:31:08Z
date_updated: 2023-10-30T16:31:08Z
file_id: '14473'
file_name: SGporecondensation-main.zip
file_size: 62821432
relation: main_file
success: 1
- access_level: open_access
checksum: 389eab31c6509dbc05795017fb618758
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
relation: main_file
success: 1
file_date_updated: 2023-10-31T08:57:50Z
fulldoi: https://doi.org/10.15479/AT:ISTA:14472
has_accepted_license: '1'
license: https://creativecommons.org/publicdomain/zero/1.0/
month: '10'
oa: 1
oa_version: Published Version
publisher: Institute of Science and Technology Austria
related_material:
record:
- id: '14610'
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: '14610'
abstract:
- lang: eng
text: Endomembrane 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;623:1062-1069.
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, vol. 623. Springer Nature, pp. 1062–1069, 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. 623, 1062–1069.
mla: Bussi, Claudio, et al. “Stress Granules Plug and Stabilize Damaged Endolysosomal
Membranes.” Nature, vol. 623, Springer Nature, 2023, pp. 1062–69, 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 623 (2023) 1062–1069.
date_created: 2023-11-27T07:56:37Z
date_published: 2023-11-30T00:00:00Z
date_updated: 2025-09-09T13:30:34Z
day: '30'
ddc:
- '570'
department:
- _id: AnSa
doi: 10.1038/s41586-023-06726-w
external_id:
isi:
- '001105882300018'
pmid:
- '37968398'
file:
- access_level: open_access
checksum: b939a19e4c228fbf3beca298ac2ac014
content_type: application/pdf
creator: dernst
date_created: 2024-07-16T07:41:39Z
date_updated: 2024-07-16T07:41:39Z
file_id: '17248'
file_name: 2023_Nature_Bussi.pdf
file_size: 17047711
relation: main_file
success: 1
file_date_updated: 2024-07-16T07:41:39Z
fulldoi: https://doi.org/10.1038/s41586-023-06726-w
has_accepted_license: '1'
intvolume: ' 623'
isi: 1
language:
- iso: eng
month: '11'
oa: 1
oa_version: Published Version
page: 1062-1069
pmid: 1
publication: Nature
publication_identifier:
eissn:
- 1476-4687
issn:
- 0028-0836
publication_status: published
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
scopus_import: '1'
status: public
title: Stress granules plug and stabilize damaged endolysosomal membranes
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: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 623
year: '2023'
...
---
_id: '14655'
abstract:
- lang: eng
text: The kinetics of the assembly of semiflexible filaments through end-to-end
annealing is key to the structure of the cytoskeleton, but is not understood.
We analyze this problem through scaling theory and simulations, and uncover a
regime where filaments’ ends find each other through bending fluctuations without
the need for the whole filament to diffuse. This results in a very substantial
speedup of assembly in physiological regimes, and could help with understanding
the dynamics of actin and intermediate filaments in biological processes such
as wound healing and cell division.
acknowledgement: The authors thank C´ecile Leduc and Duc-Quang Tran for invaluable
help with understanding the experimental behavior of intermediate filaments, and
Raphael Voituriez, Nicolas Levernier, and Alexander Grosberg for fruitful discussion
on the theoretical model. V. S. also thanks Davide Michieletto, Maria Panoukidou,
and Lorenzo Rovigatti for very helpful suggestions on the simulation model. M. L.
was supported by Marie Curie Integration Grant No. PCIG12-GA-2012-334053, “Investissements
d’Avenir” LabEx PALM (ANR-10-LABX- 0039-PALM), ANR Grants No. ANR-15-CE13-0004-03,
No. ANR-21-CE11-0004-02 and No. ANR-22-CE30-0024, as well as ERC Starting Grant
No. 677532. M.L.’s group belongs to the CNRS consortium AQV. Part of this work was
performed using HPC resources from GENCI–IDRIS (Grants No. 2020-A0090712066 and
No. 2021-A0110712066).
article_number: '228401'
article_processing_charge: No
article_type: original
arxiv: 1
author:
- first_name: Valerio
full_name: Sorichetti, Valerio
id: ef8a92cb-c7b6-11ec-8bea-e1fd5847bc5b
last_name: Sorichetti
orcid: 0000-0002-9645-6576
- first_name: Martin
full_name: Lenz, Martin
last_name: Lenz
citation:
ama: Sorichetti V, Lenz M. Transverse fluctuations control the assembly of semiflexible
filaments. Physical Review Letters. 2023;131(22). doi:10.1103/PhysRevLett.131.228401
apa: Sorichetti, V., & Lenz, M. (2023). Transverse fluctuations control the
assembly of semiflexible filaments. Physical Review Letters. American Physical
Society. https://doi.org/10.1103/PhysRevLett.131.228401
chicago: Sorichetti, Valerio, and Martin Lenz. “Transverse Fluctuations Control
the Assembly of Semiflexible Filaments.” Physical Review Letters. American
Physical Society, 2023. https://doi.org/10.1103/PhysRevLett.131.228401.
ieee: V. Sorichetti and M. Lenz, “Transverse fluctuations control the assembly of
semiflexible filaments,” Physical Review Letters, vol. 131, no. 22. American
Physical Society, 2023.
ista: Sorichetti V, Lenz M. 2023. Transverse fluctuations control the assembly of
semiflexible filaments. Physical Review Letters. 131(22), 228401.
mla: Sorichetti, Valerio, and Martin Lenz. “Transverse Fluctuations Control the
Assembly of Semiflexible Filaments.” Physical Review Letters, vol. 131,
no. 22, 228401, American Physical Society, 2023, doi:10.1103/PhysRevLett.131.228401.
short: V. Sorichetti, M. Lenz, Physical Review Letters 131 (2023).
corr_author: '1'
date_created: 2023-12-10T23:00:57Z
date_published: 2023-12-01T00:00:00Z
date_updated: 2025-09-09T13:35:06Z
day: '01'
department:
- _id: AnSa
doi: 10.1103/PhysRevLett.131.228401
external_id:
arxiv:
- '2303.03088'
isi:
- '001163810200008'
pmid:
- '38101392'
fulldoi: https://doi.org/10.1103/PhysRevLett.131.228401
intvolume: ' 131'
isi: 1
issue: '22'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.48550/arXiv.2303.03088
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: Transverse fluctuations control the assembly of semiflexible filaments
type: journal_article
user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 131
year: '2023'
...
---
_id: '14782'
abstract:
- lang: eng
text: The actin cortex is a complex cytoskeletal machinery that drives and responds
to changes in cell shape. It must generate or adapt to plasma membrane curvature
to facilitate diverse functions such as cell division, migration, and phagocytosis.
Due to the complex molecular makeup of the actin cortex, it remains unclear whether
actin networks are inherently able to sense and generate membrane curvature, or
whether they rely on their diverse binding partners to accomplish this. Here,
we show that curvature sensing is an inherent capability of branched actin networks
nucleated by Arp2/3 and VCA. We develop a robust method to encapsulate actin inside
giant unilamellar vesicles (GUVs) and assemble an actin cortex at the inner surface
of the GUV membrane. We show that actin forms a uniform and thin cortical layer
when present at high concentration and distinct patches associated with negative
membrane curvature at low concentration. Serendipitously, we find that the GUV
production method also produces dumbbell-shaped GUVs, which we explain using mathematical
modeling in terms of membrane hemifusion of nested GUVs. We find that branched
actin networks preferentially assemble at the neck of the dumbbells, which possess
a micrometer-range convex curvature comparable with the curvature of the actin
patches found in spherical GUVs. Minimal branched actin networks can thus sense
membrane curvature, which may help mammalian cells to robustly recruit actin to
curved membranes to facilitate diverse cellular functions such as cytokinesis
and migration.
acknowledgement: We thank Jeffrey den Haan for protein purification, Kristina Ganzinger
(AMOLF) for providing the 10xHis VCA construct, David Kovar (University of Chicago)
for the CP constructs, and Michael Way (Crick Institute) for providing purified
human Arp2/3 proteins. We are grateful to Iris Lambert for early actin encapsulation
experiments that formed the basis for establishing the eDICE method, to Federico
Fanalista for acquiring images of dumbbell-shaped GUVs in samples produced by cDICE,
and to Tom Aarts for images of dumbbell-shaped GUVs produced by gel-assisted swelling.
Lennard van Buren is thanked for his help with image analysis to quantify actin
concentrations in GUVs. We thank Kristina Ganzinger (AMOLF) for hosting us to perform
pyrene assays in her lab, and Balász Antalicz (AMOLF) for technical assistance with
the spectrophotometer. The authors also thank Matthieu Piel and Daniel Fletcher
for insightful and inspiring discussions. We acknowledge financial support from
The Netherlands Organization of Scientific Research (NWO/OCW) Gravitation program
Building a Synthetic Cell (BaSyC) (024.003.019). F.F. gratefully acknowledges funding
from the Kavli Synergy program of the Kavli Institute of Nanoscience Delft.
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Lucia
full_name: Baldauf, Lucia
last_name: Baldauf
- first_name: Felix F
full_name: Frey, Felix F
id: a0270b37-8f1a-11ec-95c7-8e710c59a4f3
last_name: Frey
- first_name: Marcos
full_name: Arribas Perez, Marcos
last_name: Arribas Perez
- first_name: Timon
full_name: Idema, Timon
last_name: Idema
- first_name: Gijsje H.
full_name: Koenderink, Gijsje H.
last_name: Koenderink
citation:
ama: Baldauf L, Frey FF, Arribas Perez M, Idema T, Koenderink GH. Branched actin
cortices reconstituted in vesicles sense membrane curvature. Biophysical Journal.
2023;122(11):2311-2324. doi:10.1016/j.bpj.2023.02.018
apa: Baldauf, L., Frey, F. F., Arribas Perez, M., Idema, T., & Koenderink, G.
H. (2023). Branched actin cortices reconstituted in vesicles sense membrane curvature.
Biophysical Journal. Elsevier. https://doi.org/10.1016/j.bpj.2023.02.018
chicago: Baldauf, Lucia, Felix F Frey, Marcos Arribas Perez, Timon Idema, and Gijsje
H. Koenderink. “Branched Actin Cortices Reconstituted in Vesicles Sense Membrane
Curvature.” Biophysical Journal. Elsevier, 2023. https://doi.org/10.1016/j.bpj.2023.02.018.
ieee: L. Baldauf, F. F. Frey, M. Arribas Perez, T. Idema, and G. H. Koenderink,
“Branched actin cortices reconstituted in vesicles sense membrane curvature,”
Biophysical Journal, vol. 122, no. 11. Elsevier, pp. 2311–2324, 2023.
ista: Baldauf L, Frey FF, Arribas Perez M, Idema T, Koenderink GH. 2023. Branched
actin cortices reconstituted in vesicles sense membrane curvature. Biophysical
Journal. 122(11), 2311–2324.
mla: Baldauf, Lucia, et al. “Branched Actin Cortices Reconstituted in Vesicles Sense
Membrane Curvature.” Biophysical Journal, vol. 122, no. 11, Elsevier, 2023,
pp. 2311–24, doi:10.1016/j.bpj.2023.02.018.
short: L. Baldauf, F.F. Frey, M. Arribas Perez, T. Idema, G.H. Koenderink, Biophysical
Journal 122 (2023) 2311–2324.
date_created: 2024-01-10T09:45:48Z
date_published: 2023-06-06T00:00:00Z
date_updated: 2024-01-16T09:20:03Z
day: '06'
ddc:
- '570'
department:
- _id: AnSa
doi: 10.1016/j.bpj.2023.02.018
external_id:
isi:
- '001016792600001'
pmid:
- '36806830'
file:
- access_level: open_access
checksum: 70566e54cd95ea6df340909ad44c5cd5
content_type: application/pdf
creator: dernst
date_created: 2024-01-16T09:09:29Z
date_updated: 2024-01-16T09:09:29Z
file_id: '14807'
file_name: 2023_BiophysicalJournal_Baldauf.pdf
file_size: 3285810
relation: main_file
success: 1
file_date_updated: 2024-01-16T09:09:29Z
fulldoi: https://doi.org/10.1016/j.bpj.2023.02.018
has_accepted_license: '1'
intvolume: ' 122'
isi: 1
issue: '11'
keyword:
- Biophysics
language:
- iso: eng
license: https://creativecommons.org/licenses/by-nc-nd/4.0/
month: '06'
oa: 1
oa_version: Published Version
page: 2311-2324
pmid: 1
publication: Biophysical Journal
publication_identifier:
issn:
- 0006-3495
publication_status: published
publisher: Elsevier
quality_controlled: '1'
related_material:
link:
- relation: software
url: https://github.com/BioSoftMatterGroup/actin-curvature-sensing
status: public
title: Branched actin cortices reconstituted in vesicles sense membrane curvature
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: 122
year: '2023'
...
---
_id: '14788'
abstract:
- lang: eng
text: "Eukaryotic cells use clathrin-mediated endocytosis to take up a large range
of extracellular cargo. During endocytosis, a clathrin coat forms on the plasma
membrane, but it remains controversial when and how it is remodeled into a spherical
vesicle.\r\nHere, we use 3D superresolution microscopy to determine the precise
geometry of the clathrin coat at large numbers of endocytic sites. Through pseudo-temporal
sorting, we determine the average trajectory of clathrin remodeling during endocytosis.
We find that clathrin coats assemble first on flat membranes to 50% of the coat
area before they become rapidly and continuously bent, and this mechanism is confirmed
in three cell lines. We introduce the cooperative curvature model, which is based
on positive feedback for curvature generation. It accurately describes the measured
shapes and dynamics of the clathrin coat and could represent a general mechanism
for clathrin coat remodeling on the plasma membrane."
acknowledgement: We thank the entire Ries and Kaksonen labs for fruitful discussions
and support. This work was supported by the European Research Council (ERC CoG-724489
to J. Ries), the National Institutes of Health Common Fund 4D Nucleome Program (Grant
U01 to J. Ries), the Human Frontier Science Program (RGY0065/2017 to J. Ries), the
EMBL Interdisciplinary Postdoc Programme (EIPOD) under Marie Curie Actions COFUND
(Grant 229597 to O. Avinoam), the European Molecular Biology Laboratory (M. Mund,
A. Tschanz, Y.-L. Wu and J. Ries), and the Swiss National Science Foundation (grant
310030B_182825 and NCCR Chemical Biology to M. Kaksonen). O. Avinoam is an incumbent
of the Miriam Berman Presidential Development Chair.
article_number: e202206038
article_processing_charge: No
article_type: original
author:
- first_name: Markus
full_name: Mund, Markus
last_name: Mund
- first_name: Aline
full_name: Tschanz, Aline
last_name: Tschanz
- first_name: Yu-Le
full_name: Wu, Yu-Le
last_name: Wu
- first_name: Felix F
full_name: Frey, Felix F
id: a0270b37-8f1a-11ec-95c7-8e710c59a4f3
last_name: Frey
orcid: 0000-0001-8501-6017
- first_name: Johanna L.
full_name: Mehl, Johanna L.
last_name: Mehl
- first_name: Marko
full_name: Kaksonen, Marko
last_name: Kaksonen
- first_name: Ori
full_name: Avinoam, Ori
last_name: Avinoam
- first_name: Ulrich S.
full_name: Schwarz, Ulrich S.
last_name: Schwarz
- first_name: Jonas
full_name: Ries, Jonas
last_name: Ries
citation:
ama: Mund M, Tschanz A, Wu Y-L, et al. Clathrin coats partially preassemble and
subsequently bend during endocytosis. Journal of Cell Biology. 2023;222(3).
doi:10.1083/jcb.202206038
apa: Mund, M., Tschanz, A., Wu, Y.-L., Frey, F. F., Mehl, J. L., Kaksonen, M., …
Ries, J. (2023). Clathrin coats partially preassemble and subsequently bend during
endocytosis. Journal of Cell Biology. Rockefeller University Press. https://doi.org/10.1083/jcb.202206038
chicago: Mund, Markus, Aline Tschanz, Yu-Le Wu, Felix F Frey, Johanna L. Mehl, Marko
Kaksonen, Ori Avinoam, Ulrich S. Schwarz, and Jonas Ries. “Clathrin Coats Partially
Preassemble and Subsequently Bend during Endocytosis.” Journal of Cell Biology.
Rockefeller University Press, 2023. https://doi.org/10.1083/jcb.202206038.
ieee: M. Mund et al., “Clathrin coats partially preassemble and subsequently
bend during endocytosis,” Journal of Cell Biology, vol. 222, no. 3. Rockefeller
University Press, 2023.
ista: Mund M, Tschanz A, Wu Y-L, Frey FF, Mehl JL, Kaksonen M, Avinoam O, Schwarz
US, Ries J. 2023. Clathrin coats partially preassemble and subsequently bend during
endocytosis. Journal of Cell Biology. 222(3), e202206038.
mla: Mund, Markus, et al. “Clathrin Coats Partially Preassemble and Subsequently
Bend during Endocytosis.” Journal of Cell Biology, vol. 222, no. 3, e202206038,
Rockefeller University Press, 2023, doi:10.1083/jcb.202206038.
short: M. Mund, A. Tschanz, Y.-L. Wu, F.F. Frey, J.L. Mehl, M. Kaksonen, O. Avinoam,
U.S. Schwarz, J. Ries, Journal of Cell Biology 222 (2023).
date_created: 2024-01-10T10:45:55Z
date_published: 2023-02-03T00:00:00Z
date_updated: 2024-01-16T10:17:05Z
day: '03'
ddc:
- '570'
department:
- _id: AnSa
doi: 10.1083/jcb.202206038
external_id:
isi:
- '000978065000001'
pmid:
- '36734980'
file:
- access_level: open_access
checksum: 505d5cac36c14b073b68c7fed1a92bd3
content_type: application/pdf
creator: dernst
date_created: 2024-01-16T10:15:09Z
date_updated: 2024-01-16T10:15:09Z
file_id: '14811'
file_name: 2023_JCB_Mund.pdf
file_size: 5678069
relation: main_file
success: 1
file_date_updated: 2024-01-16T10:15:09Z
fulldoi: https://doi.org/10.1083/jcb.202206038
has_accepted_license: '1'
intvolume: ' 222'
isi: 1
issue: '3'
keyword:
- Cell Biology
language:
- iso: eng
month: '02'
oa: 1
oa_version: Published Version
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'
status: public
title: Clathrin coats partially preassemble and subsequently bend during endocytosis
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: 222
year: '2023'
...
---
_id: '14831'
abstract:
- lang: eng
text: Catalysis, the acceleration of product formation by a substance that is left
unchanged, typically results from multiple elementary processes, including diffusion
of the reactants toward the catalyst, chemical steps, and release of the products.
While efforts to design catalysts are often focused on accelerating the chemical
reaction on the catalyst, catalysis is a global property of the catalytic cycle
that involves all processes. These are controlled by both intrinsic parameters
such as the composition and shape of the catalyst and extrinsic parameters such
as the concentration of the chemical species at play. We examine here the conditions
that catalysis imposes on the different steps of a reaction cycle and the respective
role of intrinsic and extrinsic parameters of the system on the emergence of catalysis
by using an approach based on first-passage times. We illustrate this approach
for various decompositions of a catalytic cycle into elementary steps, including
non-Markovian decompositions, which are useful when the presence and nature of
intermediate states are a priori unknown. Our examples cover different types of
reactions and clarify the constraints on elementary steps and the impact of species
concentrations on catalysis.
acknowledgement: We acknowledge funding from ANR-22-CE06-0037-02. This work has received
funding from the European Unions Horizon 2020 research and innovation program under
the Marie Sklodowska-Curie grant agreement No. 754387.
article_processing_charge: No
article_type: original
arxiv: 1
author:
- first_name: Yann
full_name: Sakref, Yann
last_name: Sakref
- first_name: Maitane
full_name: Muñoz Basagoiti, Maitane
id: 1a8a7950-82cd-11ed-bd4f-9624c913a607
last_name: Muñoz Basagoiti
orcid: 0000-0003-1483-1457
- first_name: Zorana
full_name: Zeravcic, Zorana
last_name: Zeravcic
- first_name: Olivier
full_name: Rivoire, Olivier
last_name: Rivoire
citation:
ama: Sakref Y, Muñoz Basagoiti M, Zeravcic Z, Rivoire O. On kinetic constraints
that catalysis imposes on elementary processes. The Journal of Physical Chemistry
B. 2023;127(51):10950-10959. doi:10.1021/acs.jpcb.3c04627
apa: Sakref, Y., Muñoz Basagoiti, M., Zeravcic, Z., & Rivoire, O. (2023). On
kinetic constraints that catalysis imposes on elementary processes. The Journal
of Physical Chemistry B. American Chemical Society. https://doi.org/10.1021/acs.jpcb.3c04627
chicago: Sakref, Yann, Maitane Muñoz Basagoiti, Zorana Zeravcic, and Olivier Rivoire.
“On Kinetic Constraints That Catalysis Imposes on Elementary Processes.” The
Journal of Physical Chemistry B. American Chemical Society, 2023. https://doi.org/10.1021/acs.jpcb.3c04627.
ieee: Y. Sakref, M. Muñoz Basagoiti, Z. Zeravcic, and O. Rivoire, “On kinetic constraints
that catalysis imposes on elementary processes,” The Journal of Physical Chemistry
B, vol. 127, no. 51. American Chemical Society, pp. 10950–10959, 2023.
ista: Sakref Y, Muñoz Basagoiti M, Zeravcic Z, Rivoire O. 2023. On kinetic constraints
that catalysis imposes on elementary processes. The Journal of Physical Chemistry
B. 127(51), 10950–10959.
mla: Sakref, Yann, et al. “On Kinetic Constraints That Catalysis Imposes on Elementary
Processes.” The Journal of Physical Chemistry B, vol. 127, no. 51, American
Chemical Society, 2023, pp. 10950–59, doi:10.1021/acs.jpcb.3c04627.
short: Y. Sakref, M. Muñoz Basagoiti, Z. Zeravcic, O. Rivoire, The Journal of Physical
Chemistry B 127 (2023) 10950–10959.
date_created: 2024-01-18T07:47:11Z
date_published: 2023-12-13T00:00:00Z
date_updated: 2025-04-23T13:15:17Z
day: '13'
department:
- _id: AnSa
doi: 10.1021/acs.jpcb.3c04627
external_id:
arxiv:
- '2312.15940'
isi:
- '001134068000001'
pmid:
- '38091487'
fulldoi: https://doi.org/10.1021/acs.jpcb.3c04627
intvolume: ' 127'
isi: 1
issue: '51'
keyword:
- Materials Chemistry
- Surfaces
- Coatings and Films
- Physical and Theoretical Chemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.48550/arXiv.2312.15940
month: '12'
oa: 1
oa_version: Preprint
page: 10950-10959
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: On kinetic constraints that catalysis imposes on elementary processes
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 127
year: '2023'
...
---
OA_place: publisher
OA_type: gold
_id: '15027'
abstract:
- lang: eng
text: 'This data repository underpins the paper, published in PNAS (doi pending)
and bioarxiv (doi: https://doi.org/10.1101/2023.07.05.547777).'
article_processing_charge: No
author:
- first_name: Samo
full_name: Curk, Samo
id: 031eff0d-d481-11ee-8508-cd12a7a86e5b
last_name: Curk
orcid: 0000-0001-6160-9766
citation:
ama: Curk S. aggregation_data. 2023.
apa: Curk, S. (2023). aggregation_data. Figshare.
chicago: Curk, Samo. “Aggregation_data.” Figshare, 2023.
ieee: S. Curk, “aggregation_data.” Figshare, 2023.
ista: Curk S. 2023. aggregation_data, Figshare.
mla: Curk, Samo. Aggregation_data. Figshare, 2023.
short: S. Curk, (2023).
corr_author: '1'
date_created: 2024-02-26T08:37:57Z
date_published: 2023-12-13T00:00:00Z
date_updated: 2026-09-24T10:27:35Z
day: '13'
ddc:
- '570'
department:
- _id: AnSa
has_accepted_license: '1'
main_file_link:
- open_access: '1'
url: https://figshare.com/s/85798bba4ebc68d822ed
month: '12'
oa: 1
oa_version: Published Version
publisher: Figshare
related_material:
record:
- id: '15001'
relation: used_in_publication
status: public
status: public
title: aggregation_data
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_reference
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2023'
...
---
_id: '11340'
abstract:
- lang: eng
text: Like-charge attraction, driven by ionic correlations, challenges our understanding
of electrostatics both in soft and hard matter. For two charged planar surfaces
confining counterions and water, we prove that, even at relatively low correlation
strength, the relevant physics is the ground-state one, oblivious of fluctuations.
Based on this, we derive a simple and accurate interaction pressure that fulfills
known exact requirements and can be used as an effective potential. We test this
equation against implicit-solvent Monte Carlo simulations and against explicit-solvent
simulations of cement and several types of clays. We argue that water destructuring
under nanometric confinement drastically reduces dielectric screening, enhancing
ionic correlations. Our equation of state at reduced permittivity therefore explains
the exotic attractive regime reported for these materials, even in the absence
of multivalent counterions.
acknowledgement: We thank Martin Trulsson for useful discussions and for providing
us with simulation data. This work has received funding from the European Union’s
Horizon 2020 research and innovation programme under the Marie Sklodowska-Curie
grant agreement 674979-NANOTRANS. The support received from VEGA Grant No. 2/0092/21
is acknowledged.
article_processing_charge: No
article_type: original
arxiv: 1
author:
- first_name: Ivan
full_name: Palaia, Ivan
id: 9c805cd2-4b75-11ec-a374-db6dd0ed57fa
last_name: Palaia
orcid: ' 0000-0002-8843-9485 '
- first_name: Abhay
full_name: Goyal, Abhay
last_name: Goyal
- first_name: Emanuela
full_name: Del Gado, Emanuela
last_name: Del Gado
- first_name: Ladislav
full_name: Šamaj, Ladislav
last_name: Šamaj
- first_name: Emmanuel
full_name: Trizac, Emmanuel
last_name: Trizac
citation:
ama: 'Palaia I, Goyal A, Del Gado E, Šamaj L, Trizac E. Like-charge attraction at
the nanoscale: Ground-state correlations and water destructuring. Journal of
Physical Chemistry B. 2022;126(16):3143-3149. doi:10.1021/acs.jpcb.2c00028'
apa: 'Palaia, I., Goyal, A., Del Gado, E., Šamaj, L., & Trizac, E. (2022). Like-charge
attraction at the nanoscale: Ground-state correlations and water destructuring.
Journal of Physical Chemistry B. American Chemical Society. https://doi.org/10.1021/acs.jpcb.2c00028'
chicago: 'Palaia, Ivan, Abhay Goyal, Emanuela Del Gado, Ladislav Šamaj, and Emmanuel
Trizac. “Like-Charge Attraction at the Nanoscale: Ground-State Correlations and
Water Destructuring.” Journal of Physical Chemistry B. American Chemical
Society, 2022. https://doi.org/10.1021/acs.jpcb.2c00028.'
ieee: 'I. Palaia, A. Goyal, E. Del Gado, L. Šamaj, and E. Trizac, “Like-charge attraction
at the nanoscale: Ground-state correlations and water destructuring,” Journal
of Physical Chemistry B, vol. 126, no. 16. American Chemical Society, pp.
3143–3149, 2022.'
ista: 'Palaia I, Goyal A, Del Gado E, Šamaj L, Trizac E. 2022. Like-charge attraction
at the nanoscale: Ground-state correlations and water destructuring. Journal of
Physical Chemistry B. 126(16), 3143–3149.'
mla: 'Palaia, Ivan, et al. “Like-Charge Attraction at the Nanoscale: Ground-State
Correlations and Water Destructuring.” Journal of Physical Chemistry B,
vol. 126, no. 16, American Chemical Society, 2022, pp. 3143–49, doi:10.1021/acs.jpcb.2c00028.'
short: I. Palaia, A. Goyal, E. Del Gado, L. Šamaj, E. Trizac, Journal of Physical
Chemistry B 126 (2022) 3143–3149.
date_created: 2022-05-01T22:01:42Z
date_published: 2022-04-14T00:00:00Z
date_updated: 2025-06-11T13:34:36Z
day: '14'
department:
- _id: AnSa
doi: 10.1021/acs.jpcb.2c00028
external_id:
arxiv:
- '2203.10524'
isi:
- '000796953700022'
pmid:
- '35420420'
fulldoi: https://doi.org/10.1021/acs.jpcb.2c00028
intvolume: ' 126'
isi: 1
issue: '16'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: ' https://doi.org/10.48550/arXiv.2203.10524'
month: '04'
oa: 1
oa_version: Preprint
page: 3143-3149
pmid: 1
publication: 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: 'Like-charge attraction at the nanoscale: Ground-state correlations and water
destructuring'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 126
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).
corr_author: '1'
date_created: 2022-05-22T17:04:48Z
date_published: 2022-05-16T00:00:00Z
date_updated: 2025-06-11T14:00:32Z
day: '16'
ddc:
- '540'
department:
- _id: AnSa
doi: 10.1063/5.0087769
ec_funded: 1
external_id:
isi:
- '000797236000004'
pmid:
- '35597653'
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
fulldoi: https://doi.org/10.1063/5.0087769
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
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'
- _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'
scopus_import: '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: 2DF688A6-F248-11E8-B48F-1D18A9856A87
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. 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. 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. 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, 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: 2025-06-12T06:21:34Z
day: '28'
ddc:
- '570'
department:
- _id: AnSa
doi: 10.1073/pnas.2109718119
ec_funded: 1
external_id:
isi:
- '000903753500002'
pmid:
- '35901206'
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
fulldoi: https://doi.org/10.1073/pnas.2109718119
has_accepted_license: '1'
intvolume: ' 119'
isi: 1
issue: '31'
language:
- iso: eng
month: '07'
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
issn:
- 0027-8424
publication_status: published
publisher: 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: '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
orcid: 0000-0003-3441-1337
- 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).
corr_author: '1'
date_created: 2023-01-08T23:00:53Z
date_published: 2022-12-23T00:00:00Z
date_updated: 2025-04-14T07:54:53Z
day: '23'
department:
- _id: AnSa
doi: 10.1103/PhysRevLett.129.268101
ec_funded: 1
external_id:
isi:
- '000906721500001'
pmid:
- '36608212'
fulldoi: https://doi.org/10.1103/PhysRevLett.129.268101
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).
corr_author: '1'
date_created: 2023-01-12T12:08:10Z
date_published: 2022-10-17T00:00:00Z
date_updated: 2025-06-12T06:19:28Z
day: '17'
ddc:
- '570'
department:
- _id: AnSa
doi: 10.1371/journal.pcbi.1010586
ec_funded: 1
external_id:
isi:
- '000924885500005'
pmid:
- '36251703'
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
fulldoi: https://doi.org/10.1371/journal.pcbi.1010586
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
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'
- _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: 2DF688A6-F248-11E8-B48F-1D18A9856A87
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'
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title: Influence of denaturants on amyloid β42 aggregation kinetics
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