---
_id: '10867'
abstract:
- lang: eng
text: In this paper we find a tight estimate for Gromov’s waist of the balls in
spaces of constant curvature, deduce the estimates for the balls in Riemannian
manifolds with upper bounds on the curvature (CAT(ϰ)-spaces), and establish similar
result for normed spaces.
acknowledgement: ' Supported by the Russian Foundation for Basic Research grant 18-01-00036.'
article_processing_charge: No
article_type: original
arxiv: 1
author:
- first_name: Arseniy
full_name: Akopyan, Arseniy
id: 430D2C90-F248-11E8-B48F-1D18A9856A87
last_name: Akopyan
orcid: 0000-0002-2548-617X
- first_name: Roman
full_name: Karasev, Roman
last_name: Karasev
citation:
ama: Akopyan A, Karasev R. Waist of balls in hyperbolic and spherical spaces. International
Mathematics Research Notices. 2020;2020(3):669-697. doi:10.1093/imrn/rny037
apa: Akopyan, A., & Karasev, R. (2020). Waist of balls in hyperbolic and spherical
spaces. International Mathematics Research Notices. Oxford University Press.
https://doi.org/10.1093/imrn/rny037
chicago: Akopyan, Arseniy, and Roman Karasev. “Waist of Balls in Hyperbolic and
Spherical Spaces.” International Mathematics Research Notices. Oxford University
Press, 2020. https://doi.org/10.1093/imrn/rny037.
ieee: A. Akopyan and R. Karasev, “Waist of balls in hyperbolic and spherical spaces,”
International Mathematics Research Notices, vol. 2020, no. 3. Oxford University
Press, pp. 669–697, 2020.
ista: Akopyan A, Karasev R. 2020. Waist of balls in hyperbolic and spherical spaces.
International Mathematics Research Notices. 2020(3), 669–697.
mla: Akopyan, Arseniy, and Roman Karasev. “Waist of Balls in Hyperbolic and Spherical
Spaces.” International Mathematics Research Notices, vol. 2020, no. 3,
Oxford University Press, 2020, pp. 669–97, doi:10.1093/imrn/rny037.
short: A. Akopyan, R. Karasev, International Mathematics Research Notices 2020 (2020)
669–697.
date_created: 2022-03-18T11:39:30Z
date_published: 2020-02-01T00:00:00Z
date_updated: 2023-08-24T14:19:55Z
day: '01'
department:
- _id: HeEd
doi: 10.1093/imrn/rny037
external_id:
arxiv:
- '1702.07513'
isi:
- '000522852700002'
intvolume: ' 2020'
isi: 1
issue: '3'
keyword:
- General Mathematics
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1702.07513
month: '02'
oa: 1
oa_version: Preprint
page: 669-697
publication: International Mathematics Research Notices
publication_identifier:
eissn:
- 1687-0247
issn:
- 1073-7928
publication_status: published
publisher: Oxford University Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: Waist of balls in hyperbolic and spherical spaces
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 2020
year: '2020'
...
---
_id: '11054'
abstract:
- lang: eng
text: In recent years, the nuclear pore complex (NPC) has emerged as a key player
in genome regulation and cellular homeostasis. New discoveries have revealed that
the NPC has multiple cellular functions besides mediating the molecular exchange
between the nucleus and the cytoplasm. In this review, we discuss non-transport
aspects of the NPC focusing on the NPC-genome interaction, the extreme longevity
of the NPC proteins, and NPC dysfunction in age-related diseases. The examples
summarized herein demonstrate that the NPC, which first evolved to enable the
biochemical communication between the nucleus and the cytoplasm, now doubles as
the gatekeeper of cellular identity and aging.
article_processing_charge: No
article_type: review
author:
- first_name: Ukrae H.
full_name: Cho, Ukrae H.
last_name: Cho
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: 'Cho UH, Hetzer M. Nuclear periphery takes center stage: The role of nuclear
pore complexes in cell identity and aging. Neuron. 2020;106(6):899-911.
doi:10.1016/j.neuron.2020.05.031'
apa: 'Cho, U. H., & Hetzer, M. (2020). Nuclear periphery takes center stage:
The role of nuclear pore complexes in cell identity and aging. Neuron.
Elsevier. https://doi.org/10.1016/j.neuron.2020.05.031'
chicago: 'Cho, Ukrae H., and Martin Hetzer. “Nuclear Periphery Takes Center Stage:
The Role of Nuclear Pore Complexes in Cell Identity and Aging.” Neuron.
Elsevier, 2020. https://doi.org/10.1016/j.neuron.2020.05.031.'
ieee: 'U. H. Cho and M. Hetzer, “Nuclear periphery takes center stage: The role
of nuclear pore complexes in cell identity and aging,” Neuron, vol. 106,
no. 6. Elsevier, pp. 899–911, 2020.'
ista: 'Cho UH, Hetzer M. 2020. Nuclear periphery takes center stage: The role of
nuclear pore complexes in cell identity and aging. Neuron. 106(6), 899–911.'
mla: 'Cho, Ukrae H., and Martin Hetzer. “Nuclear Periphery Takes Center Stage: The
Role of Nuclear Pore Complexes in Cell Identity and Aging.” Neuron, vol.
106, no. 6, Elsevier, 2020, pp. 899–911, doi:10.1016/j.neuron.2020.05.031.'
short: U.H. Cho, M. Hetzer, Neuron 106 (2020) 899–911.
date_created: 2022-04-07T07:43:36Z
date_published: 2020-06-17T00:00:00Z
date_updated: 2024-10-14T11:15:26Z
day: '17'
doi: 10.1016/j.neuron.2020.05.031
extern: '1'
external_id:
pmid:
- '32553207'
intvolume: ' 106'
issue: '6'
keyword:
- General Neuroscience
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.neuron.2020.05.031
month: '06'
oa: 1
oa_version: Published Version
page: 899-911
pmid: 1
publication: Neuron
publication_identifier:
issn:
- 0896-6273
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'Nuclear periphery takes center stage: The role of nuclear pore complexes in
cell identity and aging'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 106
year: '2020'
...
---
_id: '11055'
abstract:
- lang: eng
text: Vascular dysfunctions are a common feature of multiple age-related diseases.
However, modeling healthy and pathological aging of the human vasculature represents
an unresolved experimental challenge. Here, we generated induced vascular endothelial
cells (iVECs) and smooth muscle cells (iSMCs) by direct reprogramming of healthy
human fibroblasts from donors of different ages and Hutchinson-Gilford Progeria
Syndrome (HGPS) patients. iVECs induced from old donors revealed upregulation
of GSTM1 and PALD1, genes linked to oxidative stress, inflammation and endothelial
junction stability, as vascular aging markers. A functional assay performed on
PALD1 KD VECs demonstrated a recovery in vascular permeability. We found that
iSMCs from HGPS donors overexpressed bone morphogenetic protein (BMP)−4, which
plays a key role in both vascular calcification and endothelial barrier damage
observed in HGPS. Strikingly, BMP4 concentrations are higher in serum from HGPS
vs. age-matched mice. Furthermore, targeting BMP4 with blocking antibody recovered
the functionality of the vascular barrier in vitro, hence representing a potential
future therapeutic strategy to limit cardiovascular dysfunction in HGPS. These
results show that iVECs and iSMCs retain disease-related signatures, allowing
modeling of vascular aging and HGPS in vitro.
article_number: e54383
article_processing_charge: No
article_type: original
author:
- first_name: Simone
full_name: Bersini, Simone
last_name: Bersini
- first_name: Roberta
full_name: Schulte, Roberta
last_name: Schulte
- first_name: Ling
full_name: Huang, Ling
last_name: Huang
- first_name: Hannah
full_name: Tsai, Hannah
last_name: Tsai
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Bersini S, Schulte R, Huang L, Tsai H, Hetzer M. Direct reprogramming of human
smooth muscle and vascular endothelial cells reveals defects associated with aging
and Hutchinson-Gilford progeria syndrome. eLife. 2020;9. doi:10.7554/elife.54383
apa: Bersini, S., Schulte, R., Huang, L., Tsai, H., & Hetzer, M. (2020). Direct
reprogramming of human smooth muscle and vascular endothelial cells reveals defects
associated with aging and Hutchinson-Gilford progeria syndrome. ELife.
eLife Sciences Publications. https://doi.org/10.7554/elife.54383
chicago: Bersini, Simone, Roberta Schulte, Ling Huang, Hannah Tsai, and Martin Hetzer.
“Direct Reprogramming of Human Smooth Muscle and Vascular Endothelial Cells Reveals
Defects Associated with Aging and Hutchinson-Gilford Progeria Syndrome.” ELife.
eLife Sciences Publications, 2020. https://doi.org/10.7554/elife.54383.
ieee: S. Bersini, R. Schulte, L. Huang, H. Tsai, and M. Hetzer, “Direct reprogramming
of human smooth muscle and vascular endothelial cells reveals defects associated
with aging and Hutchinson-Gilford progeria syndrome,” eLife, vol. 9. eLife
Sciences Publications, 2020.
ista: Bersini S, Schulte R, Huang L, Tsai H, Hetzer M. 2020. Direct reprogramming
of human smooth muscle and vascular endothelial cells reveals defects associated
with aging and Hutchinson-Gilford progeria syndrome. eLife. 9, e54383.
mla: Bersini, Simone, et al. “Direct Reprogramming of Human Smooth Muscle and Vascular
Endothelial Cells Reveals Defects Associated with Aging and Hutchinson-Gilford
Progeria Syndrome.” ELife, vol. 9, e54383, eLife Sciences Publications,
2020, doi:10.7554/elife.54383.
short: S. Bersini, R. Schulte, L. Huang, H. Tsai, M. Hetzer, ELife 9 (2020).
date_created: 2022-04-07T07:43:48Z
date_published: 2020-09-08T00:00:00Z
date_updated: 2024-10-14T11:17:02Z
day: '08'
ddc:
- '570'
doi: 10.7554/elife.54383
extern: '1'
external_id:
pmid:
- '32896271'
file:
- access_level: open_access
checksum: f8b3821349a194050be02570d8fe7d4b
content_type: application/pdf
creator: dernst
date_created: 2022-04-08T06:53:10Z
date_updated: 2022-04-08T06:53:10Z
file_id: '11132'
file_name: 2020_eLife_Bersini.pdf
file_size: 4399825
relation: main_file
success: 1
file_date_updated: 2022-04-08T06:53:10Z
has_accepted_license: '1'
intvolume: ' 9'
keyword:
- General Immunology and Microbiology
- General Biochemistry
- Genetics and Molecular Biology
- General Medicine
- General Neuroscience
language:
- iso: eng
month: '09'
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: Direct reprogramming of human smooth muscle and vascular endothelial cells
reveals defects associated with aging and Hutchinson-Gilford progeria syndrome
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: 9
year: '2020'
...
---
_id: '11056'
abstract:
- lang: eng
text: Aging of the circulatory system correlates with the pathogenesis of a large
spectrum of diseases. However, it is largely unknown which factors drive the age-dependent
or pathological decline of the vasculature and how vascular defects relate to
tissue aging. The goal of the study is to design a multianalytical approach to
identify how the cellular microenvironment (i.e., fibroblasts) and serum from
healthy donors of different ages or Alzheimer disease (AD) patients can modulate
the functionality of organ-specific vascular endothelial cells (VECs). Long-living
human microvascular networks embedding VECs and fibroblasts from skin biopsies
are generated. RNA-seq, secretome analyses, and microfluidic assays demonstrate
that fibroblasts from young donors restore the functionality of aged endothelial
cells, an effect also achieved by serum from young donors. New biomarkers of vascular
aging are validated in human biopsies and it is shown that young serum induces
angiopoietin-like-4, which can restore compromised vascular barriers. This strategy
is then employed to characterize transcriptional/functional changes induced on
the blood–brain barrier by AD serum, demonstrating the importance of PTP4A3 in
the regulation of permeability. Features of vascular degeneration during aging
and AD are recapitulated, and a tool to identify novel biomarkers that can be
exploited to develop future therapeutics modulating vascular function is established.
article_number: '2000044'
article_processing_charge: No
article_type: original
author:
- first_name: Simone
full_name: Bersini, Simone
last_name: Bersini
- first_name: Rafael
full_name: Arrojo e Drigo, Rafael
last_name: Arrojo e Drigo
- first_name: Ling
full_name: Huang, Ling
last_name: Huang
- first_name: Maxim N.
full_name: Shokhirev, Maxim N.
last_name: Shokhirev
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Bersini S, Arrojo e Drigo R, Huang L, Shokhirev MN, Hetzer M. Transcriptional
and functional changes of the human microvasculature during physiological aging
and Alzheimer disease. Advanced Biosystems. 2020;4(5). doi:10.1002/adbi.202000044
apa: Bersini, S., Arrojo e Drigo, R., Huang, L., Shokhirev, M. N., & Hetzer,
M. (2020). Transcriptional and functional changes of the human microvasculature
during physiological aging and Alzheimer disease. Advanced Biosystems.
Wiley. https://doi.org/10.1002/adbi.202000044
chicago: Bersini, Simone, Rafael Arrojo e Drigo, Ling Huang, Maxim N. Shokhirev,
and Martin Hetzer. “Transcriptional and Functional Changes of the Human Microvasculature
during Physiological Aging and Alzheimer Disease.” Advanced Biosystems.
Wiley, 2020. https://doi.org/10.1002/adbi.202000044.
ieee: S. Bersini, R. Arrojo e Drigo, L. Huang, M. N. Shokhirev, and M. Hetzer, “Transcriptional
and functional changes of the human microvasculature during physiological aging
and Alzheimer disease,” Advanced Biosystems, vol. 4, no. 5. Wiley, 2020.
ista: Bersini S, Arrojo e Drigo R, Huang L, Shokhirev MN, Hetzer M. 2020. Transcriptional
and functional changes of the human microvasculature during physiological aging
and Alzheimer disease. Advanced Biosystems. 4(5), 2000044.
mla: Bersini, Simone, et al. “Transcriptional and Functional Changes of the Human
Microvasculature during Physiological Aging and Alzheimer Disease.” Advanced
Biosystems, vol. 4, no. 5, 2000044, Wiley, 2020, doi:10.1002/adbi.202000044.
short: S. Bersini, R. Arrojo e Drigo, L. Huang, M.N. Shokhirev, M. Hetzer, Advanced
Biosystems 4 (2020).
date_created: 2022-04-07T07:43:57Z
date_published: 2020-05-01T00:00:00Z
date_updated: 2024-10-14T11:18:07Z
day: '01'
ddc:
- '570'
doi: 10.1002/adbi.202000044
extern: '1'
external_id:
pmid:
- '32402127'
file:
- access_level: open_access
checksum: 5584d9a1609812dc75c02ce1e35d2ec0
content_type: application/pdf
creator: dernst
date_created: 2022-04-08T07:06:05Z
date_updated: 2022-04-08T07:06:05Z
file_id: '11134'
file_name: 2020_AdvancedBiosystems_Bersini.pdf
file_size: 2490829
relation: main_file
success: 1
file_date_updated: 2022-04-08T07:06:05Z
has_accepted_license: '1'
intvolume: ' 4'
issue: '5'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
- Biomedical Engineering
- Biomaterials
language:
- iso: eng
month: '05'
oa: 1
oa_version: Published Version
pmid: 1
publication: Advanced Biosystems
publication_identifier:
issn:
- 2366-7478
- 2366-7478
publication_status: published
publisher: Wiley
quality_controlled: '1'
scopus_import: '1'
status: public
title: Transcriptional and functional changes of the human microvasculature during
physiological aging and Alzheimer disease
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: 4
year: '2020'
...
---
_id: '11057'
abstract:
- lang: eng
text: During mitosis, transcription of genomic DNA is dramatically reduced, before
it is reactivated during nuclear reformation in anaphase/telophase. Many aspects
of the underlying principles that mediate transcriptional memory and reactivation
in the daughter cells remain unclear. Here, we used ChIP-seq on synchronized cells
at different stages after mitosis to generate genome-wide maps of histone modifications.
Combined with EU-RNA-seq and Hi-C analyses, we found that during prometaphase,
promoters, enhancers, and insulators retain H3K4me3 and H3K4me1, while losing
H3K27ac. Enhancers globally retaining mitotic H3K4me1 or locally retaining mitotic
H3K27ac are associated with cell type-specific genes and their transcription factors
for rapid transcriptional activation. As cells exit mitosis, promoters regain
H3K27ac, which correlates with transcriptional reactivation. Insulators also gain
H3K27ac and CCCTC-binding factor (CTCF) in anaphase/telophase. This increase of
H3K27ac in anaphase/telophase is required for posttranscriptional activation and
may play a role in the establishment of topologically associating domains (TADs).
Together, our results suggest that the genome is reorganized in a sequential order,
in which histone methylations occur first in prometaphase, histone acetylation,
and CTCF in anaphase/telophase, transcription in cytokinesis, and long-range chromatin
interactions in early G1. We thus provide insights into the histone modification
landscape that allows faithful reestablishment of the transcriptional program
and TADs during cell division.
article_processing_charge: No
article_type: original
author:
- first_name: Hyeseon
full_name: Kang, Hyeseon
last_name: Kang
- first_name: Maxim N.
full_name: Shokhirev, Maxim N.
last_name: Shokhirev
- first_name: Zhichao
full_name: Xu, Zhichao
last_name: Xu
- first_name: Sahaana
full_name: Chandran, Sahaana
last_name: Chandran
- first_name: Jesse R.
full_name: Dixon, Jesse R.
last_name: Dixon
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Kang H, Shokhirev MN, Xu Z, Chandran S, Dixon JR, Hetzer M. Dynamic regulation
of histone modifications and long-range chromosomal interactions during postmitotic
transcriptional reactivation. Genes & Development. 2020;34(13-14):913-930.
doi:10.1101/gad.335794.119
apa: Kang, H., Shokhirev, M. N., Xu, Z., Chandran, S., Dixon, J. R., & Hetzer,
M. (2020). Dynamic regulation of histone modifications and long-range chromosomal
interactions during postmitotic transcriptional reactivation. Genes & Development.
Cold Spring Harbor Laboratory Press. https://doi.org/10.1101/gad.335794.119
chicago: Kang, Hyeseon, Maxim N. Shokhirev, Zhichao Xu, Sahaana Chandran, Jesse
R. Dixon, and Martin Hetzer. “Dynamic Regulation of Histone Modifications and
Long-Range Chromosomal Interactions during Postmitotic Transcriptional Reactivation.”
Genes & Development. Cold Spring Harbor Laboratory Press, 2020. https://doi.org/10.1101/gad.335794.119.
ieee: H. Kang, M. N. Shokhirev, Z. Xu, S. Chandran, J. R. Dixon, and M. Hetzer,
“Dynamic regulation of histone modifications and long-range chromosomal interactions
during postmitotic transcriptional reactivation,” Genes & Development,
vol. 34, no. 13–14. Cold Spring Harbor Laboratory Press, pp. 913–930, 2020.
ista: Kang H, Shokhirev MN, Xu Z, Chandran S, Dixon JR, Hetzer M. 2020. Dynamic
regulation of histone modifications and long-range chromosomal interactions during
postmitotic transcriptional reactivation. Genes & Development. 34(13–14),
913–930.
mla: Kang, Hyeseon, et al. “Dynamic Regulation of Histone Modifications and Long-Range
Chromosomal Interactions during Postmitotic Transcriptional Reactivation.” Genes
& Development, vol. 34, no. 13–14, Cold Spring Harbor Laboratory Press,
2020, pp. 913–30, doi:10.1101/gad.335794.119.
short: H. Kang, M.N. Shokhirev, Z. Xu, S. Chandran, J.R. Dixon, M. Hetzer, Genes
& Development 34 (2020) 913–930.
date_created: 2022-04-07T07:44:09Z
date_published: 2020-04-28T00:00:00Z
date_updated: 2024-10-14T11:18:25Z
day: '28'
ddc:
- '570'
doi: 10.1101/gad.335794.119
extern: '1'
external_id:
pmid:
- '32499403'
file:
- access_level: open_access
checksum: 84e92d40e67936c739628315c238daf9
content_type: application/pdf
creator: dernst
date_created: 2022-04-08T07:12:33Z
date_updated: 2022-04-08T07:12:33Z
file_id: '11136'
file_name: 2020_GenesDevelopment_Kang.pdf
file_size: 4406772
relation: main_file
success: 1
file_date_updated: 2022-04-08T07:12:33Z
has_accepted_license: '1'
intvolume: ' 34'
issue: 13-14
keyword:
- Developmental Biology
- Genetics
language:
- iso: eng
month: '04'
oa: 1
oa_version: Published Version
page: 913-930
pmid: 1
publication: Genes & Development
publication_identifier:
issn:
- 0890-9369
- 1549-5477
publication_status: published
publisher: Cold Spring Harbor Laboratory Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: Dynamic regulation of histone modifications and long-range chromosomal interactions
during postmitotic transcriptional reactivation
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: 34
year: '2020'
...
---
_id: '11058'
abstract:
- lang: eng
text: Nucleoporin 93 (Nup93) expression inversely correlates with the survival of
triple-negative breast cancer patients. However, our knowledge of Nup93 function
in breast cancer besides its role as structural component of the nuclear pore
complex is not understood. Combination of functional assays and genetic analyses
suggested that chromatin interaction of Nup93 partially modulates the expression
of genes associated with actin cytoskeleton remodeling and epithelial to mesenchymal
transition, resulting in impaired invasion of triple-negative, claudin-low breast
cancer cells. Nup93 depletion induced stress fiber formation associated with reduced
cell migration/proliferation and impaired expression of mesenchymal-like genes.
Silencing LIMCH1, a gene responsible for actin cytoskeleton remodeling and up-regulated
upon Nup93 depletion, partially restored the invasive phenotype of cancer cells.
Loss of Nup93 led to significant defects in tumor establishment/propagation in
vivo, whereas patient samples revealed that high Nup93 and low LIMCH1 expression
correlate with late tumor stage. Our approach identified Nup93 as contributor
of triple-negative, claudin-low breast cancer cell invasion and paves the way
to study the role of nuclear envelope proteins during breast cancer tumorigenesis.
article_number: e201900623
article_processing_charge: No
article_type: original
author:
- first_name: Simone
full_name: Bersini, Simone
last_name: Bersini
- first_name: Nikki K
full_name: Lytle, Nikki K
last_name: Lytle
- first_name: Roberta
full_name: Schulte, Roberta
last_name: Schulte
- first_name: Ling
full_name: Huang, Ling
last_name: Huang
- first_name: Geoffrey M
full_name: Wahl, Geoffrey M
last_name: Wahl
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Bersini S, Lytle NK, Schulte R, Huang L, Wahl GM, Hetzer M. Nup93 regulates
breast tumor growth by modulating cell proliferation and actin cytoskeleton remodeling.
Life Science Alliance. 2020;3(1). doi:10.26508/lsa.201900623
apa: Bersini, S., Lytle, N. K., Schulte, R., Huang, L., Wahl, G. M., & Hetzer,
M. (2020). Nup93 regulates breast tumor growth by modulating cell proliferation
and actin cytoskeleton remodeling. Life Science Alliance. Life Science
Alliance. https://doi.org/10.26508/lsa.201900623
chicago: Bersini, Simone, Nikki K Lytle, Roberta Schulte, Ling Huang, Geoffrey M
Wahl, and Martin Hetzer. “Nup93 Regulates Breast Tumor Growth by Modulating Cell
Proliferation and Actin Cytoskeleton Remodeling.” Life Science Alliance.
Life Science Alliance, 2020. https://doi.org/10.26508/lsa.201900623.
ieee: S. Bersini, N. K. Lytle, R. Schulte, L. Huang, G. M. Wahl, and M. Hetzer,
“Nup93 regulates breast tumor growth by modulating cell proliferation and actin
cytoskeleton remodeling,” Life Science Alliance, vol. 3, no. 1. Life Science
Alliance, 2020.
ista: Bersini S, Lytle NK, Schulte R, Huang L, Wahl GM, Hetzer M. 2020. Nup93 regulates
breast tumor growth by modulating cell proliferation and actin cytoskeleton remodeling.
Life Science Alliance. 3(1), e201900623.
mla: Bersini, Simone, et al. “Nup93 Regulates Breast Tumor Growth by Modulating
Cell Proliferation and Actin Cytoskeleton Remodeling.” Life Science Alliance,
vol. 3, no. 1, e201900623, Life Science Alliance, 2020, doi:10.26508/lsa.201900623.
short: S. Bersini, N.K. Lytle, R. Schulte, L. Huang, G.M. Wahl, M. Hetzer, Life
Science Alliance 3 (2020).
date_created: 2022-04-07T07:44:18Z
date_published: 2020-01-01T00:00:00Z
date_updated: 2024-10-14T11:18:41Z
day: '01'
ddc:
- '570'
doi: 10.26508/lsa.201900623
extern: '1'
external_id:
pmid:
- '31959624'
file:
- access_level: open_access
checksum: 3bf33e7e93bef7823287807206b69b38
content_type: application/pdf
creator: dernst
date_created: 2022-04-08T07:33:01Z
date_updated: 2022-04-08T07:33:01Z
file_id: '11137'
file_name: 2020_LifeScienceAlliance_Bersini.pdf
file_size: 2653960
relation: main_file
success: 1
file_date_updated: 2022-04-08T07:33:01Z
has_accepted_license: '1'
intvolume: ' 3'
issue: '1'
keyword:
- Health
- Toxicology and Mutagenesis
- Plant Science
- Biochemistry
- Genetics and Molecular Biology (miscellaneous)
- Ecology
language:
- iso: eng
month: '01'
oa: 1
oa_version: Published Version
pmid: 1
publication: Life Science Alliance
publication_identifier:
issn:
- 2575-1077
publication_status: published
publisher: Life Science Alliance
quality_controlled: '1'
scopus_import: '1'
status: public
title: Nup93 regulates breast tumor growth by modulating cell proliferation and actin
cytoskeleton remodeling
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: 3
year: '2020'
...
---
_id: '10328'
abstract:
- lang: eng
text: We discus noise channels in coherent electro-optic up-conversion between microwave
and optical fields, in particular due to optical heating. We also report on a
novel configuration, which promises to be flexible and highly efficient.
alternative_title:
- OSA Technical Digest
article_number: QTu8A.1
article_processing_charge: No
author:
- first_name: Nicholas J.
full_name: Lambert, Nicholas J.
last_name: Lambert
- first_name: Sonia
full_name: Mobassem, Sonia
last_name: Mobassem
- first_name: Alfredo R
full_name: Rueda Sanchez, Alfredo R
id: 3B82B0F8-F248-11E8-B48F-1D18A9856A87
last_name: Rueda Sanchez
orcid: 0000-0001-6249-5860
- first_name: Harald G.L.
full_name: Schwefel, Harald G.L.
last_name: Schwefel
citation:
ama: 'Lambert NJ, Mobassem S, Rueda Sanchez AR, Schwefel HGL. New designs and noise
channels in electro-optic microwave to optical up-conversion. In: OSA Quantum
2.0 Conference. Optica Publishing Group; 2020. doi:10.1364/QUANTUM.2020.QTu8A.1'
apa: 'Lambert, N. J., Mobassem, S., Rueda Sanchez, A. R., & Schwefel, H. G.
L. (2020). New designs and noise channels in electro-optic microwave to optical
up-conversion. In OSA Quantum 2.0 Conference. Washington, DC, United States:
Optica Publishing Group. https://doi.org/10.1364/QUANTUM.2020.QTu8A.1'
chicago: Lambert, Nicholas J., Sonia Mobassem, Alfredo R Rueda Sanchez, and Harald
G.L. Schwefel. “New Designs and Noise Channels in Electro-Optic Microwave to Optical
up-Conversion.” In OSA Quantum 2.0 Conference. Optica Publishing Group,
2020. https://doi.org/10.1364/QUANTUM.2020.QTu8A.1.
ieee: N. J. Lambert, S. Mobassem, A. R. Rueda Sanchez, and H. G. L. Schwefel, “New
designs and noise channels in electro-optic microwave to optical up-conversion,”
in OSA Quantum 2.0 Conference, Washington, DC, United States, 2020.
ista: 'Lambert NJ, Mobassem S, Rueda Sanchez AR, Schwefel HGL. 2020. New designs
and noise channels in electro-optic microwave to optical up-conversion. OSA Quantum
2.0 Conference. OSA: Optical Society of America, OSA Technical Digest, , QTu8A.1.'
mla: Lambert, Nicholas J., et al. “New Designs and Noise Channels in Electro-Optic
Microwave to Optical up-Conversion.” OSA Quantum 2.0 Conference, QTu8A.1,
Optica Publishing Group, 2020, doi:10.1364/QUANTUM.2020.QTu8A.1.
short: N.J. Lambert, S. Mobassem, A.R. Rueda Sanchez, H.G.L. Schwefel, in:, OSA
Quantum 2.0 Conference, Optica Publishing Group, 2020.
conference:
end_date: 2020-09-17
location: Washington, DC, United States
name: 'OSA: Optical Society of America'
start_date: 2020-09-14
date_created: 2021-11-21T23:01:31Z
date_published: 2020-01-01T00:00:00Z
date_updated: 2023-10-18T08:32:34Z
day: '01'
department:
- _id: JoFi
doi: 10.1364/QUANTUM.2020.QTu8A.1
language:
- iso: eng
month: '01'
oa_version: None
publication: OSA Quantum 2.0 Conference
publication_identifier:
isbn:
- 9-781-5575-2820-9
publication_status: published
publisher: Optica Publishing Group
quality_controlled: '1'
scopus_import: '1'
status: public
title: New designs and noise channels in electro-optic microwave to optical up-conversion
type: conference
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2020'
...
---
_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'
...
---
OA_place: publisher
OA_type: hybrid
_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: 2024-10-16T12:53:17Z
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: 0043cee0-e5fc-11ee-9736-f83bc23afbf0
volume: 16
year: '2020'
...
---
DOAJ_listed: '1'
OA_place: publisher
OA_type: gold
_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: 2024-10-16T12:56:52Z
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: 0043cee0-e5fc-11ee-9736-f83bc23afbf0
volume: 6
year: '2020'
...
---
OA_place: publisher
OA_type: hybrid
_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: 2024-10-16T12:59:57Z
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: 0043cee0-e5fc-11ee-9736-f83bc23afbf0
volume: 125
year: '2020'
...
---
OA_place: publisher
OA_type: hybrid
_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: 2024-10-16T13:05:34Z
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: 0043cee0-e5fc-11ee-9736-f83bc23afbf0
volume: 119
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: '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: '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: '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
license: https://creativecommons.org/licenses/by-nc/3.0/
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: '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: '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'
...
---
OA_place: publisher
OA_type: hybrid
_id: '21083'
abstract:
- lang: eng
text: Helically folded aromatic oligoamide foldamers have a size and geometrical
parameters very distinct from those of α‐helices and are not obvious candidates
for α‐helix mimicry. Nevertheless, they offer multiple sites for attaching side
chains. It was found that some arrays of side chains at the surface of an aromatic
helix make it possible to mimic extended α‐helical surfaces. Synthetic methods
were developed to produce quinoline monomers suitably functionalized for solid
phase synthesis. A dodecamer was prepared. Its crystal structure validated the
initial design and showed helix bundling involving the α‐helix‐like interface.
These results open up new uses of aromatic helices to recognize protein surfaces
and to program helix bundling in water.
article_processing_charge: No
article_type: original
author:
- first_name: Márton
full_name: Zwillinger, Márton
last_name: Zwillinger
- first_name: Post Sai
full_name: Reddy, Post Sai
last_name: Reddy
- first_name: Barbara
full_name: Wicher, Barbara
last_name: Wicher
- first_name: Pradeep K
full_name: Mandal, Pradeep K
id: 6a3def15-d4b4-11ef-9fa9-a24c1f545ec3
last_name: Mandal
orcid: 0000-0001-5996-956X
- first_name: Márton
full_name: Csékei, Márton
last_name: Csékei
- first_name: Lucile
full_name: Fischer, Lucile
last_name: Fischer
- first_name: András
full_name: Kotschy, András
last_name: Kotschy
- first_name: Ivan
full_name: Huc, Ivan
last_name: Huc
citation:
ama: Zwillinger M, Reddy PS, Wicher B, et al. Aromatic foldamer helices as α‐helix
extended surface mimetics. Chemistry – A European Journal. 2020;26(72):17366-17370.
doi:10.1002/chem.202004064
apa: Zwillinger, M., Reddy, P. S., Wicher, B., Mandal, P. K., Csékei, M., Fischer,
L., … Huc, I. (2020). Aromatic foldamer helices as α‐helix extended surface mimetics.
Chemistry – A European Journal. Wiley. https://doi.org/10.1002/chem.202004064
chicago: Zwillinger, Márton, Post Sai Reddy, Barbara Wicher, Pradeep K Mandal, Márton
Csékei, Lucile Fischer, András Kotschy, and Ivan Huc. “Aromatic Foldamer Helices
as Α‐helix Extended Surface Mimetics.” Chemistry – A European Journal.
Wiley, 2020. https://doi.org/10.1002/chem.202004064.
ieee: M. Zwillinger et al., “Aromatic foldamer helices as α‐helix extended
surface mimetics,” Chemistry – A European Journal, vol. 26, no. 72. Wiley,
pp. 17366–17370, 2020.
ista: Zwillinger M, Reddy PS, Wicher B, Mandal PK, Csékei M, Fischer L, Kotschy
A, Huc I. 2020. Aromatic foldamer helices as α‐helix extended surface mimetics.
Chemistry – A European Journal. 26(72), 17366–17370.
mla: Zwillinger, Márton, et al. “Aromatic Foldamer Helices as Α‐helix Extended Surface
Mimetics.” Chemistry – A European Journal, vol. 26, no. 72, Wiley, 2020,
pp. 17366–70, doi:10.1002/chem.202004064.
short: M. Zwillinger, P.S. Reddy, B. Wicher, P.K. Mandal, M. Csékei, L. Fischer,
A. Kotschy, I. Huc, Chemistry – A European Journal 26 (2020) 17366–17370.
date_created: 2026-01-29T15:31:13Z
date_published: 2020-09-10T00:00:00Z
date_updated: 2026-02-20T06:53:53Z
day: '10'
ddc:
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doi: 10.1002/chem.202004064
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url: https://doi.org/10.1002/chem.202004064
month: '09'
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oa_version: Published Version
page: 17366-17370
publication: Chemistry – A European Journal
publication_identifier:
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issn:
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publication_status: published
publisher: Wiley
quality_controlled: '1'
status: public
title: Aromatic foldamer helices as α‐helix extended surface mimetics
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