---
_id: '7572'
abstract:
- lang: eng
text: The polymerization–depolymerization dynamics of cytoskeletal proteins play
essential roles in the self-organization of cytoskeletal structures, in eukaryotic
as well as prokaryotic cells. While advances in fluorescence microscopy and in
vitro reconstitution experiments have helped to study the dynamic properties of
these complex systems, methods that allow to collect and analyze large quantitative
datasets of the underlying polymer dynamics are still missing. Here, we present
a novel image analysis workflow to study polymerization dynamics of active filaments
in a nonbiased, highly automated manner. Using treadmilling filaments of the bacterial
tubulin FtsZ as an example, we demonstrate that our method is able to specifically
detect, track and analyze growth and shrinkage of polymers, even in dense networks
of filaments. We believe that this automated method can facilitate the analysis
of a large variety of dynamic cytoskeletal systems, using standard time-lapse
movies obtained from experiments in vitro as well as in the living cell. Moreover,
we provide scripts implementing this method as supplementary material.
alternative_title:
- Methods in Cell Biology
article_processing_charge: No
author:
- first_name: Paulo R
full_name: Dos Santos Caldas, Paulo R
id: 38FCDB4C-F248-11E8-B48F-1D18A9856A87
last_name: Dos Santos Caldas
orcid: 0000-0001-6730-4461
- first_name: Philipp
full_name: Radler, Philipp
id: 40136C2A-F248-11E8-B48F-1D18A9856A87
last_name: Radler
orcid: '0000-0001-9198-2182 '
- first_name: Christoph M
full_name: Sommer, Christoph M
id: 4DF26D8C-F248-11E8-B48F-1D18A9856A87
last_name: Sommer
orcid: 0000-0003-1216-9105
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
citation:
ama: 'Dos Santos Caldas PR, Radler P, Sommer CM, Loose M. Computational analysis
of filament polymerization dynamics in cytoskeletal networks. In: Tran P, ed.
Methods in Cell Biology. Vol 158. Elsevier; 2020:145-161. doi:10.1016/bs.mcb.2020.01.006'
apa: Dos Santos Caldas, P. R., Radler, P., Sommer, C. M., & Loose, M. (2020).
Computational analysis of filament polymerization dynamics in cytoskeletal networks.
In P. Tran (Ed.), Methods in Cell Biology (Vol. 158, pp. 145–161). Elsevier.
https://doi.org/10.1016/bs.mcb.2020.01.006
chicago: Dos Santos Caldas, Paulo R, Philipp Radler, Christoph M Sommer, and Martin
Loose. “Computational Analysis of Filament Polymerization Dynamics in Cytoskeletal
Networks.” In Methods in Cell Biology, edited by Phong Tran, 158:145–61.
Elsevier, 2020. https://doi.org/10.1016/bs.mcb.2020.01.006.
ieee: P. R. Dos Santos Caldas, P. Radler, C. M. Sommer, and M. Loose, “Computational
analysis of filament polymerization dynamics in cytoskeletal networks,” in Methods
in Cell Biology, vol. 158, P. Tran, Ed. Elsevier, 2020, pp. 145–161.
ista: 'Dos Santos Caldas PR, Radler P, Sommer CM, Loose M. 2020.Computational analysis
of filament polymerization dynamics in cytoskeletal networks. In: Methods in Cell
Biology. Methods in Cell Biology, vol. 158, 145–161.'
mla: Dos Santos Caldas, Paulo R., et al. “Computational Analysis of Filament Polymerization
Dynamics in Cytoskeletal Networks.” Methods in Cell Biology, edited by
Phong Tran, vol. 158, Elsevier, 2020, pp. 145–61, doi:10.1016/bs.mcb.2020.01.006.
short: P.R. Dos Santos Caldas, P. Radler, C.M. Sommer, M. Loose, in:, P. Tran (Ed.),
Methods in Cell Biology, Elsevier, 2020, pp. 145–161.
date_created: 2020-03-08T23:00:47Z
date_published: 2020-02-27T00:00:00Z
date_updated: 2023-10-04T09:50:24Z
day: '27'
department:
- _id: MaLo
doi: 10.1016/bs.mcb.2020.01.006
ec_funded: 1
editor:
- first_name: 'Phong '
full_name: 'Tran, Phong '
last_name: Tran
external_id:
isi:
- '000611826500008'
intvolume: ' 158'
isi: 1
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1101/839571
month: '02'
oa: 1
oa_version: Preprint
page: 145-161
project:
- _id: 2595697A-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '679239'
name: Self-Organization of the Bacterial Cell
- _id: 260D98C8-B435-11E9-9278-68D0E5697425
name: Reconstitution of Bacterial Cell Division Using Purified Components
publication: Methods in Cell Biology
publication_identifier:
issn:
- 0091679X
publication_status: published
publisher: Elsevier
quality_controlled: '1'
related_material:
record:
- id: '8358'
relation: part_of_dissertation
status: public
scopus_import: '1'
status: public
title: Computational analysis of filament polymerization dynamics in cytoskeletal
networks
type: book_chapter
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 158
year: '2020'
...
---
_id: '7580'
abstract:
- lang: eng
text: The eukaryotic endomembrane system is controlled by small GTPases of the Rab
family, which are activated at defined times and locations in a switch-like manner.
While this switch is well understood for an individual protein, how regulatory
networks produce intracellular activity patterns is currently not known. Here,
we combine in vitro reconstitution experiments with computational modeling to
study a minimal Rab5 activation network. We find that the molecular interactions
in this system give rise to a positive feedback and bistable collective switching
of Rab5. Furthermore, we find that switching near the critical point is intrinsically
stochastic and provide evidence that controlling the inactive population of Rab5
on the membrane can shape the network response. Notably, we demonstrate that collective
switching can spread on the membrane surface as a traveling wave of Rab5 activation.
Together, our findings reveal how biochemical signaling networks control vesicle
trafficking pathways and how their nonequilibrium properties define the spatiotemporal
organization of the cell.
acknowledged_ssus:
- _id: Bio
- _id: LifeSc
article_processing_charge: No
article_type: original
author:
- first_name: Urban
full_name: Bezeljak, Urban
id: 2A58201A-F248-11E8-B48F-1D18A9856A87
last_name: Bezeljak
orcid: 0000-0003-1365-5631
- first_name: Hrushikesh
full_name: Loya, Hrushikesh
last_name: Loya
- first_name: Beata M
full_name: Kaczmarek, Beata M
id: 36FA4AFA-F248-11E8-B48F-1D18A9856A87
last_name: Kaczmarek
- first_name: Timothy E.
full_name: Saunders, Timothy E.
last_name: Saunders
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
citation:
ama: Bezeljak U, Loya H, Kaczmarek BM, Saunders TE, Loose M. Stochastic activation
and bistability in a Rab GTPase regulatory network. Proceedings of the National
Academy of Sciences. 2020;117(12):6504-6549. doi:10.1073/pnas.1921027117
apa: Bezeljak, U., Loya, H., Kaczmarek, B. M., Saunders, T. E., & Loose, M.
(2020). Stochastic activation and bistability in a Rab GTPase regulatory network.
Proceedings of the National Academy of Sciences. Proceedings of the National
Academy of Sciences. https://doi.org/10.1073/pnas.1921027117
chicago: Bezeljak, Urban, Hrushikesh Loya, Beata M Kaczmarek, Timothy E. Saunders,
and Martin Loose. “Stochastic Activation and Bistability in a Rab GTPase Regulatory
Network.” Proceedings of the National Academy of Sciences. Proceedings
of the National Academy of Sciences, 2020. https://doi.org/10.1073/pnas.1921027117.
ieee: U. Bezeljak, H. Loya, B. M. Kaczmarek, T. E. Saunders, and M. Loose, “Stochastic
activation and bistability in a Rab GTPase regulatory network,” Proceedings
of the National Academy of Sciences, vol. 117, no. 12. Proceedings of the
National Academy of Sciences, pp. 6504–6549, 2020.
ista: Bezeljak U, Loya H, Kaczmarek BM, Saunders TE, Loose M. 2020. Stochastic activation
and bistability in a Rab GTPase regulatory network. Proceedings of the National
Academy of Sciences. 117(12), 6504–6549.
mla: Bezeljak, Urban, et al. “Stochastic Activation and Bistability in a Rab GTPase
Regulatory Network.” Proceedings of the National Academy of Sciences, vol.
117, no. 12, Proceedings of the National Academy of Sciences, 2020, pp. 6504–49,
doi:10.1073/pnas.1921027117.
short: U. Bezeljak, H. Loya, B.M. Kaczmarek, T.E. Saunders, M. Loose, Proceedings
of the National Academy of Sciences 117 (2020) 6504–6549.
date_created: 2020-03-12T05:32:26Z
date_published: 2020-03-24T00:00:00Z
date_updated: 2023-09-07T13:17:06Z
day: '24'
department:
- _id: MaLo
- _id: CaBe
doi: 10.1073/pnas.1921027117
external_id:
isi:
- '000521821800040'
intvolume: ' 117'
isi: 1
issue: '12'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1101/776567
month: '03'
oa: 1
oa_version: Preprint
page: 6504-6549
project:
- _id: 2599F062-B435-11E9-9278-68D0E5697425
grant_number: RGY0083/2016
name: Reconstitution of cell polarity and axis determination in a cell-free system
publication: Proceedings of the National Academy of Sciences
publication_identifier:
eissn:
- 1091-6490
issn:
- 0027-8424
publication_status: published
publisher: Proceedings of the National Academy of Sciences
quality_controlled: '1'
related_material:
link:
- description: News on IST Homepage
relation: press_release
url: https://ist.ac.at/en/news/proteins-as-molecular-switches/
record:
- id: '8341'
relation: dissertation_contains
status: public
scopus_import: '1'
status: public
title: Stochastic activation and bistability in a Rab GTPase regulatory network
type: journal_article
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 117
year: '2020'
...
---
_id: '7663'
abstract:
- lang: eng
text: Wood, as the most abundant carbon dioxide storing bioresource, is currently
driven beyond its traditional use through creative innovations and nanotechnology.
For many properties the micro- and nanostructure plays a crucial role and one
key challenge is control and detection of chemical and physical processes in the
confined microstructure and nanopores of the wooden cell wall. In this study,
correlative Raman and atomic force microscopy show high potential for tracking
in situ molecular rearrangement of wood polymers during compression. More water
molecules (interpreted as wider cellulose microfibril distances) and disentangling
of hemicellulose chains are detected in the opened cell wall regions, whereas
an increase of lignin is revealed in the compressed areas. These results support
a new more “loose” cell wall model based on flexible lignin nanodomains and advance
our knowledge of the molecular reorganization during deformation of wood for optimized
processing and utilization.
article_processing_charge: No
article_type: original
author:
- first_name: Martin
full_name: Felhofer, Martin
last_name: Felhofer
- first_name: Peter
full_name: Bock, Peter
last_name: Bock
- first_name: Adya
full_name: Singh, Adya
last_name: Singh
- first_name: Batirtze
full_name: Prats Mateu, Batirtze
id: 299FE892-F248-11E8-B48F-1D18A9856A87
last_name: Prats Mateu
- first_name: Ronald
full_name: Zirbs, Ronald
last_name: Zirbs
- first_name: Notburga
full_name: Gierlinger, Notburga
last_name: Gierlinger
citation:
ama: Felhofer M, Bock P, Singh A, Prats Mateu B, Zirbs R, Gierlinger N. Wood deformation
leads to rearrangement of molecules at the nanoscale. Nano Letters. 2020;20(4):2647-2653.
doi:10.1021/acs.nanolett.0c00205
apa: Felhofer, M., Bock, P., Singh, A., Prats Mateu, B., Zirbs, R., & Gierlinger,
N. (2020). Wood deformation leads to rearrangement of molecules at the nanoscale.
Nano Letters. American Chemical Society. https://doi.org/10.1021/acs.nanolett.0c00205
chicago: Felhofer, Martin, Peter Bock, Adya Singh, Batirtze Prats Mateu, Ronald
Zirbs, and Notburga Gierlinger. “Wood Deformation Leads to Rearrangement of Molecules
at the Nanoscale.” Nano Letters. American Chemical Society, 2020. https://doi.org/10.1021/acs.nanolett.0c00205.
ieee: M. Felhofer, P. Bock, A. Singh, B. Prats Mateu, R. Zirbs, and N. Gierlinger,
“Wood deformation leads to rearrangement of molecules at the nanoscale,” Nano
Letters, vol. 20, no. 4. American Chemical Society, pp. 2647–2653, 2020.
ista: Felhofer M, Bock P, Singh A, Prats Mateu B, Zirbs R, Gierlinger N. 2020. Wood
deformation leads to rearrangement of molecules at the nanoscale. Nano Letters.
20(4), 2647–2653.
mla: Felhofer, Martin, et al. “Wood Deformation Leads to Rearrangement of Molecules
at the Nanoscale.” Nano Letters, vol. 20, no. 4, American Chemical Society,
2020, pp. 2647–53, doi:10.1021/acs.nanolett.0c00205.
short: M. Felhofer, P. Bock, A. Singh, B. Prats Mateu, R. Zirbs, N. Gierlinger,
Nano Letters 20 (2020) 2647–2653.
date_created: 2020-04-19T22:00:54Z
date_published: 2020-04-08T00:00:00Z
date_updated: 2023-08-21T06:12:09Z
day: '08'
ddc:
- '530'
department:
- _id: MaLo
doi: 10.1021/acs.nanolett.0c00205
external_id:
isi:
- '000526413400055'
pmid:
- '32196350'
file:
- access_level: open_access
checksum: fe46146a9c4c620592a1932a8599069e
content_type: application/pdf
creator: dernst
date_created: 2020-04-20T10:43:36Z
date_updated: 2020-07-14T12:48:01Z
file_id: '7667'
file_name: 2020_NanoLetters_Felhofer.pdf
file_size: 7108014
relation: main_file
file_date_updated: 2020-07-14T12:48:01Z
has_accepted_license: '1'
intvolume: ' 20'
isi: 1
issue: '4'
language:
- iso: eng
month: '04'
oa: 1
oa_version: Published Version
page: 2647-2653
pmid: 1
publication: Nano Letters
publication_identifier:
eissn:
- '15306992'
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Wood deformation leads to rearrangement of molecules at the nanoscale
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 20
year: '2020'
...
---
_id: '15036'
abstract:
- lang: eng
text: The assembly of a septin filament requires that homologous monomers must distinguish
between one another in establishing appropriate interfaces with their neighbors.
To understand this phenomenon at the molecular level, we present the first four
crystal structures of heterodimeric septin complexes. We describe in detail the
two distinct types of G-interface present within the octameric particles, which
must polymerize to form filaments. These are formed between SEPT2 and SEPT6 and
between SEPT7 and SEPT3, and their description permits an understanding of the
structural basis for the selectivity necessary for correct filament assembly.
By replacing SEPT6 by SEPT8 or SEPT11, it is possible to rationalize Kinoshita's
postulate, which predicts the exchangeability of septins from within a subgroup.
Switches I and II, which in classical small GTPases provide a mechanism for nucleotide-dependent
conformational change, have been repurposed in septins to play a fundamental role
in molecular recognition. Specifically, it is switch I which holds the key to
discriminating between the two different G-interfaces. Moreover, residues which
are characteristic for a given subgroup play subtle, but pivotal, roles in guaranteeing
that the correct interfaces are formed.
article_processing_charge: No
article_type: original
author:
- first_name: Higor Vinícius Dias
full_name: Rosa, Higor Vinícius Dias
last_name: Rosa
- first_name: Diego Antonio
full_name: Leonardo, Diego Antonio
last_name: Leonardo
- first_name: Gabriel
full_name: Brognara, Gabriel
id: D96FFDA0-A884-11E9-9968-DC26E6697425
last_name: Brognara
- first_name: José
full_name: Brandão-Neto, José
last_name: Brandão-Neto
- first_name: Humberto
full_name: D'Muniz Pereira, Humberto
last_name: D'Muniz Pereira
- first_name: Ana Paula Ulian
full_name: Araújo, Ana Paula Ulian
last_name: Araújo
- first_name: Richard Charles
full_name: Garratt, Richard Charles
last_name: Garratt
citation:
ama: 'Rosa HVD, Leonardo DA, Brognara G, et al. Molecular recognition at septin
interfaces: The switches hold the key. Journal of Molecular Biology. 2020;432(21):5784-5801.
doi:10.1016/j.jmb.2020.09.001'
apa: 'Rosa, H. V. D., Leonardo, D. A., Brognara, G., Brandão-Neto, J., D’Muniz Pereira,
H., Araújo, A. P. U., & Garratt, R. C. (2020). Molecular recognition at septin
interfaces: The switches hold the key. Journal of Molecular Biology. Elsevier.
https://doi.org/10.1016/j.jmb.2020.09.001'
chicago: 'Rosa, Higor Vinícius Dias, Diego Antonio Leonardo, Gabriel Brognara, José
Brandão-Neto, Humberto D’Muniz Pereira, Ana Paula Ulian Araújo, and Richard Charles
Garratt. “Molecular Recognition at Septin Interfaces: The Switches Hold the Key.”
Journal of Molecular Biology. Elsevier, 2020. https://doi.org/10.1016/j.jmb.2020.09.001.'
ieee: 'H. V. D. Rosa et al., “Molecular recognition at septin interfaces:
The switches hold the key,” Journal of Molecular Biology, vol. 432, no.
21. Elsevier, pp. 5784–5801, 2020.'
ista: 'Rosa HVD, Leonardo DA, Brognara G, Brandão-Neto J, D’Muniz Pereira H, Araújo
APU, Garratt RC. 2020. Molecular recognition at septin interfaces: The switches
hold the key. Journal of Molecular Biology. 432(21), 5784–5801.'
mla: 'Rosa, Higor Vinícius Dias, et al. “Molecular Recognition at Septin Interfaces:
The Switches Hold the Key.” Journal of Molecular Biology, vol. 432, no.
21, Elsevier, 2020, pp. 5784–801, doi:10.1016/j.jmb.2020.09.001.'
short: H.V.D. Rosa, D.A. Leonardo, G. Brognara, J. Brandão-Neto, H. D’Muniz Pereira,
A.P.U. Araújo, R.C. Garratt, Journal of Molecular Biology 432 (2020) 5784–5801.
date_created: 2024-02-28T08:50:34Z
date_published: 2020-10-02T00:00:00Z
date_updated: 2024-02-28T12:37:54Z
day: '02'
department:
- _id: MaLo
doi: 10.1016/j.jmb.2020.09.001
external_id:
pmid:
- '32910969'
intvolume: ' 432'
issue: '21'
keyword:
- Molecular Biology
- Structural Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.jmb.2020.09.001
month: '10'
oa: 1
oa_version: Published Version
page: 5784-5801
pmid: 1
publication: Journal of Molecular Biology
publication_identifier:
issn:
- 0022-2836
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: 'Molecular recognition at septin interfaces: The switches hold the key'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 432
year: '2020'
...
---
_id: '7010'
abstract:
- lang: eng
text: Numerous biophysical questions require the quantification of short-range interactions
between (functionalized) surfaces and synthetic or biological objects such as
cells. Here, we present an original, custom built setup for reflection interference
contrast microscopy that can assess distances between a substrate and a flowing
object at high speed with nanometric accuracy. We demonstrate its use to decipher
the complex biochemical and mechanical interplay regulating blood cell homing
at the vessel wall in the microcirculation using an in vitro approach. We show
that in the absence of specific biochemical interactions, flowing cells are repelled
from the soft layer lining the vessel wall, contributing to red blood cell repulsion
in vivo. In contrast, this so-called glycocalyx stabilizes rolling of cells under
flow in the presence of a specific receptor naturally present on activated leucocytes
and a number of cancer cell lines.
article_number: 110760V
article_processing_charge: No
author:
- first_name: Heather S.
full_name: Davies, Heather S.
last_name: Davies
- first_name: Natalia S.
full_name: Baranova, Natalia S.
id: 38661662-F248-11E8-B48F-1D18A9856A87
last_name: Baranova
orcid: 0000-0002-3086-9124
- first_name: Nouha
full_name: El Amri, Nouha
last_name: El Amri
- first_name: Liliane
full_name: Coche-Guérente, Liliane
last_name: Coche-Guérente
- first_name: Claude
full_name: Verdier, Claude
last_name: Verdier
- first_name: Lionel
full_name: Bureau, Lionel
last_name: Bureau
- first_name: Ralf P.
full_name: Richter, Ralf P.
last_name: Richter
- first_name: Delphine
full_name: Débarre, Delphine
last_name: Débarre
citation:
ama: 'Davies HS, Baranova NS, El Amri N, et al. Blood cell-vessel wall interactions
probed by reflection interference contrast microscopy. In: Advances in Microscopic
Imaging II. Vol 11076. SPIE; 2019. doi:10.1117/12.2527058'
apa: 'Davies, H. S., Baranova, N. S., El Amri, N., Coche-Guérente, L., Verdier,
C., Bureau, L., … Débarre, D. (2019). Blood cell-vessel wall interactions probed
by reflection interference contrast microscopy. In Advances in Microscopic
Imaging II (Vol. 11076). Munich, Germany: SPIE. https://doi.org/10.1117/12.2527058'
chicago: Davies, Heather S., Natalia S. Baranova, Nouha El Amri, Liliane Coche-Guérente,
Claude Verdier, Lionel Bureau, Ralf P. Richter, and Delphine Débarre. “Blood Cell-Vessel
Wall Interactions Probed by Reflection Interference Contrast Microscopy.” In Advances
in Microscopic Imaging II, Vol. 11076. SPIE, 2019. https://doi.org/10.1117/12.2527058.
ieee: H. S. Davies et al., “Blood cell-vessel wall interactions probed by
reflection interference contrast microscopy,” in Advances in Microscopic Imaging
II, Munich, Germany, 2019, vol. 11076.
ista: Davies HS, Baranova NS, El Amri N, Coche-Guérente L, Verdier C, Bureau L,
Richter RP, Débarre D. 2019. Blood cell-vessel wall interactions probed by reflection
interference contrast microscopy. Advances in Microscopic Imaging II. European
Conferences on Biomedical Optics vol. 11076, 110760V.
mla: Davies, Heather S., et al. “Blood Cell-Vessel Wall Interactions Probed by Reflection
Interference Contrast Microscopy.” Advances in Microscopic Imaging II,
vol. 11076, 110760V, SPIE, 2019, doi:10.1117/12.2527058.
short: H.S. Davies, N.S. Baranova, N. El Amri, L. Coche-Guérente, C. Verdier, L.
Bureau, R.P. Richter, D. Débarre, in:, Advances in Microscopic Imaging II, SPIE,
2019.
conference:
end_date: 2019-06-27
location: Munich, Germany
name: European Conferences on Biomedical Optics
start_date: 2019-06-26
date_created: 2019-11-12T15:10:18Z
date_published: 2019-07-22T00:00:00Z
date_updated: 2023-08-29T06:54:38Z
day: '22'
department:
- _id: MaLo
doi: 10.1117/12.2527058
external_id:
isi:
- '000535353000023'
intvolume: ' 11076'
isi: 1
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://hal.archives-ouvertes.fr/hal-02368135/file/110760V.pdf
month: '07'
oa: 1
oa_version: Published Version
publication: Advances in Microscopic Imaging II
publication_identifier:
isbn:
- '9781510628458'
issn:
- 1605-7422
publication_status: published
publisher: SPIE
quality_controlled: '1'
scopus_import: '1'
status: public
title: Blood cell-vessel wall interactions probed by reflection interference contrast
microscopy
type: conference
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 11076
year: '2019'
...
---
_id: '7197'
abstract:
- lang: eng
text: During bacterial cell division, the tubulin-homolog FtsZ forms a ring-like
structure at the center of the cell. This Z-ring not only organizes the division
machinery, but treadmilling of FtsZ filaments was also found to play a key role
in distributing proteins at the division site. What regulates the architecture,
dynamics and stability of the Z-ring is currently unknown, but FtsZ-associated
proteins are known to play an important role. Here, using an in vitro reconstitution
approach, we studied how the well-conserved protein ZapA affects FtsZ treadmilling
and filament organization into large-scale patterns. Using high-resolution fluorescence
microscopy and quantitative image analysis, we found that ZapA cooperatively increases
the spatial order of the filament network, but binds only transiently to FtsZ
filaments and has no effect on filament length and treadmilling velocity. Together,
our data provides a model for how FtsZ-associated proteins can increase the precision
and stability of the bacterial cell division machinery in a switch-like manner.
acknowledged_ssus:
- _id: LifeSc
- _id: Bio
article_number: '5744'
article_processing_charge: No
article_type: original
author:
- first_name: Paulo R
full_name: Dos Santos Caldas, Paulo R
id: 38FCDB4C-F248-11E8-B48F-1D18A9856A87
last_name: Dos Santos Caldas
orcid: 0000-0001-6730-4461
- first_name: Maria D
full_name: Lopez Pelegrin, Maria D
id: 319AA9CE-F248-11E8-B48F-1D18A9856A87
last_name: Lopez Pelegrin
- first_name: Daniel J. G.
full_name: Pearce, Daniel J. G.
last_name: Pearce
- first_name: Nazmi B
full_name: Budanur, Nazmi B
id: 3EA1010E-F248-11E8-B48F-1D18A9856A87
last_name: Budanur
orcid: 0000-0003-0423-5010
- first_name: Jan
full_name: Brugués, Jan
last_name: Brugués
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
citation:
ama: Dos Santos Caldas PR, Lopez Pelegrin MD, Pearce DJG, Budanur NB, Brugués J,
Loose M. Cooperative ordering of treadmilling filaments in cytoskeletal networks
of FtsZ and its crosslinker ZapA. Nature Communications. 2019;10. doi:10.1038/s41467-019-13702-4
apa: Dos Santos Caldas, P. R., Lopez Pelegrin, M. D., Pearce, D. J. G., Budanur,
N. B., Brugués, J., & Loose, M. (2019). Cooperative ordering of treadmilling
filaments in cytoskeletal networks of FtsZ and its crosslinker ZapA. Nature
Communications. Springer Nature. https://doi.org/10.1038/s41467-019-13702-4
chicago: Dos Santos Caldas, Paulo R, Maria D Lopez Pelegrin, Daniel J. G. Pearce,
Nazmi B Budanur, Jan Brugués, and Martin Loose. “Cooperative Ordering of Treadmilling
Filaments in Cytoskeletal Networks of FtsZ and Its Crosslinker ZapA.” Nature
Communications. Springer Nature, 2019. https://doi.org/10.1038/s41467-019-13702-4.
ieee: P. R. Dos Santos Caldas, M. D. Lopez Pelegrin, D. J. G. Pearce, N. B. Budanur,
J. Brugués, and M. Loose, “Cooperative ordering of treadmilling filaments in cytoskeletal
networks of FtsZ and its crosslinker ZapA,” Nature Communications, vol.
10. Springer Nature, 2019.
ista: Dos Santos Caldas PR, Lopez Pelegrin MD, Pearce DJG, Budanur NB, Brugués J,
Loose M. 2019. Cooperative ordering of treadmilling filaments in cytoskeletal
networks of FtsZ and its crosslinker ZapA. Nature Communications. 10, 5744.
mla: Dos Santos Caldas, Paulo R., et al. “Cooperative Ordering of Treadmilling Filaments
in Cytoskeletal Networks of FtsZ and Its Crosslinker ZapA.” Nature Communications,
vol. 10, 5744, Springer Nature, 2019, doi:10.1038/s41467-019-13702-4.
short: P.R. Dos Santos Caldas, M.D. Lopez Pelegrin, D.J.G. Pearce, N.B. Budanur,
J. Brugués, M. Loose, Nature Communications 10 (2019).
date_created: 2019-12-20T12:22:57Z
date_published: 2019-12-17T00:00:00Z
date_updated: 2023-09-07T13:18:51Z
day: '17'
ddc:
- '570'
department:
- _id: MaLo
- _id: BjHo
doi: 10.1038/s41467-019-13702-4
ec_funded: 1
external_id:
isi:
- '000503009300001'
file:
- access_level: open_access
checksum: a1b44b427ba341383197790d0e8789fa
content_type: application/pdf
creator: dernst
date_created: 2019-12-23T07:34:56Z
date_updated: 2020-07-14T12:47:53Z
file_id: '7208'
file_name: 2019_NatureComm_Caldas.pdf
file_size: 8488733
relation: main_file
file_date_updated: 2020-07-14T12:47:53Z
has_accepted_license: '1'
intvolume: ' 10'
isi: 1
language:
- iso: eng
month: '12'
oa: 1
oa_version: Published Version
project:
- _id: 2595697A-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '679239'
name: Self-Organization of the Bacterial Cell
- _id: 260D98C8-B435-11E9-9278-68D0E5697425
name: Reconstitution of Bacterial Cell Division Using Purified Components
publication: Nature Communications
publication_identifier:
issn:
- 2041-1723
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
related_material:
record:
- id: '8358'
relation: dissertation_contains
status: public
scopus_import: '1'
status: public
title: Cooperative ordering of treadmilling filaments in cytoskeletal networks of
FtsZ and its crosslinker ZapA
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 10
year: '2019'
...
---
_id: '6297'
abstract:
- lang: eng
text: Cell-cell and cell-glycocalyx interactions under flow are important for the
behaviour of circulating cells in blood and lymphatic vessels. However, such interactions
are not well understood due in part to a lack of tools to study them in defined
environments. Here, we develop a versatile in vitro platform for the study of
cell-glycocalyx interactions in well-defined physical and chemical settings under
flow. Our approach is demonstrated with the interaction between hyaluronan (HA,
a key component of the endothelial glycocalyx) and its cell receptor CD44. We
generate HA brushes in situ within a microfluidic device, and demonstrate the
tuning of their physical (thickness and softness) and chemical (density of CD44
binding sites) properties using characterisation with reflection interference
contrast microscopy (RICM) and application of polymer theory. We highlight the
interactions of HA brushes with CD44-displaying beads and cells under flow. Observations
of CD44+ beads on a HA brush with RICM enabled the 3-dimensional trajectories
to be generated, and revealed interactions in the form of stop and go phases with
reduced rolling velocity and reduced distance between the bead and the HA brush,
compared to uncoated beads. Combined RICM and bright-field microscopy of CD44+
AKR1 T-lymphocytes revealed complementary information about the dynamics of cell
rolling and cell morphology, and highlighted the formation of tethers and slings,
as they interacted with a HA brush under flow. This platform can readily incorporate
more complex models of the glycocalyx, and should permit the study of how mechanical
and biochemical factors are orchestrated to enable highly selective blood cell-vessel
wall interactions under flow.
article_processing_charge: No
article_type: original
author:
- first_name: Heather S.
full_name: Davies, Heather S.
last_name: Davies
- first_name: Natalia S.
full_name: Baranova, Natalia S.
id: 38661662-F248-11E8-B48F-1D18A9856A87
last_name: Baranova
orcid: 0000-0002-3086-9124
- first_name: Nouha
full_name: El Amri, Nouha
last_name: El Amri
- first_name: Liliane
full_name: Coche-Guérente, Liliane
last_name: Coche-Guérente
- first_name: Claude
full_name: Verdier, Claude
last_name: Verdier
- first_name: Lionel
full_name: Bureau, Lionel
last_name: Bureau
- first_name: Ralf P.
full_name: Richter, Ralf P.
last_name: Richter
- first_name: Delphine
full_name: Débarre, Delphine
last_name: Débarre
citation:
ama: Davies HS, Baranova NS, El Amri N, et al. An integrated assay to probe endothelial
glycocalyx-blood cell interactions under flow in mechanically and biochemically
well-defined environments. Matrix Biology. 2019;78-79:47-59. doi:10.1016/j.matbio.2018.12.002
apa: Davies, H. S., Baranova, N. S., El Amri, N., Coche-Guérente, L., Verdier, C.,
Bureau, L., … Débarre, D. (2019). An integrated assay to probe endothelial glycocalyx-blood
cell interactions under flow in mechanically and biochemically well-defined environments.
Matrix Biology. Elsevier. https://doi.org/10.1016/j.matbio.2018.12.002
chicago: Davies, Heather S., Natalia S. Baranova, Nouha El Amri, Liliane Coche-Guérente,
Claude Verdier, Lionel Bureau, Ralf P. Richter, and Delphine Débarre. “An Integrated
Assay to Probe Endothelial Glycocalyx-Blood Cell Interactions under Flow in Mechanically
and Biochemically Well-Defined Environments.” Matrix Biology. Elsevier,
2019. https://doi.org/10.1016/j.matbio.2018.12.002.
ieee: H. S. Davies et al., “An integrated assay to probe endothelial glycocalyx-blood
cell interactions under flow in mechanically and biochemically well-defined environments,”
Matrix Biology, vol. 78–79. Elsevier, pp. 47–59, 2019.
ista: Davies HS, Baranova NS, El Amri N, Coche-Guérente L, Verdier C, Bureau L,
Richter RP, Débarre D. 2019. An integrated assay to probe endothelial glycocalyx-blood
cell interactions under flow in mechanically and biochemically well-defined environments.
Matrix Biology. 78–79, 47–59.
mla: Davies, Heather S., et al. “An Integrated Assay to Probe Endothelial Glycocalyx-Blood
Cell Interactions under Flow in Mechanically and Biochemically Well-Defined Environments.”
Matrix Biology, vol. 78–79, Elsevier, 2019, pp. 47–59, doi:10.1016/j.matbio.2018.12.002.
short: H.S. Davies, N.S. Baranova, N. El Amri, L. Coche-Guérente, C. Verdier, L.
Bureau, R.P. Richter, D. Débarre, Matrix Biology 78–79 (2019) 47–59.
date_created: 2019-04-11T20:55:01Z
date_published: 2019-05-01T00:00:00Z
date_updated: 2023-08-25T10:11:28Z
day: '01'
ddc:
- '570'
department:
- _id: MaLo
doi: 10.1016/j.matbio.2018.12.002
external_id:
isi:
- '000468707600005'
file:
- access_level: open_access
checksum: 790878cd78bfc54a147ddcc7c8f286a0
content_type: application/pdf
creator: dernst
date_created: 2020-05-14T09:02:07Z
date_updated: 2020-07-14T12:47:27Z
file_id: '7825'
file_name: 2018_MatrixBiology_Davies.pdf
file_size: 4444339
relation: main_file
file_date_updated: 2020-07-14T12:47:27Z
has_accepted_license: '1'
isi: 1
language:
- iso: eng
month: '05'
oa: 1
oa_version: Submitted Version
page: 47-59
publication: Matrix Biology
publication_identifier:
issn:
- 0945-053X
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: An integrated assay to probe endothelial glycocalyx-blood cell interactions
under flow in mechanically and biochemically well-defined environments
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: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 78-79
year: '2019'
...
---
_id: '555'
abstract:
- lang: eng
text: Conventional wisdom has it that proteins fold and assemble into definite structures,
and that this defines their function. Glycosaminoglycans (GAGs) are different.
In most cases the structures they form have a low degree of order, even when interacting
with proteins. Here, we discuss how physical features common to all GAGs — hydrophilicity,
charge, linearity and semi-flexibility — underpin the overall properties of GAG-rich
matrices. By integrating soft matter physics concepts (e.g. polymer brushes and
phase separation) with our molecular understanding of GAG–protein interactions,
we can better comprehend how GAG-rich matrices assemble, what their properties
are, and how they function. Taking perineuronal nets (PNNs) — a GAG-rich matrix
enveloping neurons — as a relevant example, we propose that microphase separation
determines the holey PNN anatomy that is pivotal to PNN functions.
acknowledgement: "This work was supported by the European Research Council [Starting
Grant 306435 ‘JELLY’; to RPR], the Spanish Ministry of Competitiveness and Innovation
[MAT2014-54867-R, to RPR], the EPSRC Centre for Doctoral Training in Tissue Engineering
and Regenerative Medicine — Innovation in Medical and Biological Engineering [EP/L014823/1,
to JCFK], the Royal Society [RG160410, to JCFK], Wings for Life [WFL-UK-008/15,
to JCFK] and the European Union, the Operational Programme Research, Development
and Education in the framework of the project ‘Centre of Reconstructive Neuroscience’
[CZ.02.1.01/0.0./0.0/15_003/0000419, to JCFK]. AJD would like to thank Arthritis
Research UK [16539, 19489] and the MRC [76445, G0900538] for funding his work on
GAG–protein interactions.\r\n"
article_processing_charge: No
article_type: original
author:
- first_name: Ralf
full_name: Richter, Ralf
last_name: Richter
- first_name: Natalia
full_name: Baranova, Natalia
id: 38661662-F248-11E8-B48F-1D18A9856A87
last_name: Baranova
orcid: 0000-0002-3086-9124
- first_name: Anthony
full_name: Day, Anthony
last_name: Day
- first_name: Jessica
full_name: Kwok, Jessica
last_name: Kwok
citation:
ama: 'Richter R, Baranova NS, Day A, Kwok J. Glycosaminoglycans in extracellular
matrix organisation: Are concepts from soft matter physics key to understanding
the formation of perineuronal nets? Current Opinion in Structural Biology.
2018;50:65-74. doi:10.1016/j.sbi.2017.12.002'
apa: 'Richter, R., Baranova, N. S., Day, A., & Kwok, J. (2018). Glycosaminoglycans
in extracellular matrix organisation: Are concepts from soft matter physics key
to understanding the formation of perineuronal nets? Current Opinion in Structural
Biology. Elsevier. https://doi.org/10.1016/j.sbi.2017.12.002'
chicago: 'Richter, Ralf, Natalia S. Baranova, Anthony Day, and Jessica Kwok. “Glycosaminoglycans
in Extracellular Matrix Organisation: Are Concepts from Soft Matter Physics Key
to Understanding the Formation of Perineuronal Nets?” Current Opinion in Structural
Biology. Elsevier, 2018. https://doi.org/10.1016/j.sbi.2017.12.002.'
ieee: 'R. Richter, N. S. Baranova, A. Day, and J. Kwok, “Glycosaminoglycans in extracellular
matrix organisation: Are concepts from soft matter physics key to understanding
the formation of perineuronal nets?,” Current Opinion in Structural Biology,
vol. 50. Elsevier, pp. 65–74, 2018.'
ista: 'Richter R, Baranova NS, Day A, Kwok J. 2018. Glycosaminoglycans in extracellular
matrix organisation: Are concepts from soft matter physics key to understanding
the formation of perineuronal nets? Current Opinion in Structural Biology. 50,
65–74.'
mla: 'Richter, Ralf, et al. “Glycosaminoglycans in Extracellular Matrix Organisation:
Are Concepts from Soft Matter Physics Key to Understanding the Formation of Perineuronal
Nets?” Current Opinion in Structural Biology, vol. 50, Elsevier, 2018,
pp. 65–74, doi:10.1016/j.sbi.2017.12.002.'
short: R. Richter, N.S. Baranova, A. Day, J. Kwok, Current Opinion in Structural
Biology 50 (2018) 65–74.
date_created: 2018-12-11T11:47:09Z
date_published: 2018-06-01T00:00:00Z
date_updated: 2023-09-11T14:07:03Z
day: '01'
department:
- _id: MaLo
doi: 10.1016/j.sbi.2017.12.002
external_id:
isi:
- '000443661300011'
intvolume: ' 50'
isi: 1
language:
- iso: eng
main_file_link:
- open_access: '1'
url: http://eprints.whiterose.ac.uk/125524/
month: '06'
oa: 1
oa_version: Submitted Version
page: 65 - 74
publication: Current Opinion in Structural Biology
publication_status: published
publisher: Elsevier
publist_id: '7259'
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'Glycosaminoglycans in extracellular matrix organisation: Are concepts from
soft matter physics key to understanding the formation of perineuronal nets?'
type: journal_article
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 50
year: '2018'
...
---
_id: '7360'
abstract:
- lang: eng
text: Inflammation, which is a highly regulated host response against danger signals,
may be harmful if it is excessive and deregulated. Ideally, anti-inflammatory
therapy should autonomously commence as soon as possible after the onset of inflammation,
should be controllable by a physician, and should not systemically block beneficial
immune response in the long term. We describe a genetically encoded anti-inflammatory
mammalian cell device based on a modular engineered genetic circuit comprising
a sensor, an amplifier, a “thresholder” to restrict activation of a positive-feedback
loop, a combination of advanced clinically used biopharmaceutical proteins, and
orthogonal regulatory elements that linked modules into the functional device.
This genetic circuit was autonomously activated by inflammatory signals, including
endogenous cecal ligation and puncture (CLP)-induced inflammation in mice and
serum from a systemic juvenile idiopathic arthritis (sIJA) patient, and could
be reset externally by a chemical signal. The microencapsulated anti-inflammatory
device significantly reduced the pathology in dextran sodium sulfate (DSS)-induced
acute murine colitis, demonstrating a synthetic immunological approach for autonomous
anti-inflammatory therapy.
article_processing_charge: No
article_type: original
author:
- first_name: Anže
full_name: Smole, Anže
last_name: Smole
- first_name: Duško
full_name: Lainšček, Duško
last_name: Lainšček
- first_name: Urban
full_name: Bezeljak, Urban
id: 2A58201A-F248-11E8-B48F-1D18A9856A87
last_name: Bezeljak
orcid: 0000-0003-1365-5631
- first_name: Simon
full_name: Horvat, Simon
last_name: Horvat
- first_name: Roman
full_name: Jerala, Roman
last_name: Jerala
citation:
ama: Smole A, Lainšček D, Bezeljak U, Horvat S, Jerala R. A synthetic mammalian
therapeutic gene circuit for sensing and suppressing inflammation. Molecular
Therapy. 2017;25(1):102-119. doi:10.1016/j.ymthe.2016.10.005
apa: Smole, A., Lainšček, D., Bezeljak, U., Horvat, S., & Jerala, R. (2017).
A synthetic mammalian therapeutic gene circuit for sensing and suppressing inflammation.
Molecular Therapy. Elsevier. https://doi.org/10.1016/j.ymthe.2016.10.005
chicago: Smole, Anže, Duško Lainšček, Urban Bezeljak, Simon Horvat, and Roman Jerala.
“A Synthetic Mammalian Therapeutic Gene Circuit for Sensing and Suppressing Inflammation.”
Molecular Therapy. Elsevier, 2017. https://doi.org/10.1016/j.ymthe.2016.10.005.
ieee: A. Smole, D. Lainšček, U. Bezeljak, S. Horvat, and R. Jerala, “A synthetic
mammalian therapeutic gene circuit for sensing and suppressing inflammation,”
Molecular Therapy, vol. 25, no. 1. Elsevier, pp. 102–119, 2017.
ista: Smole A, Lainšček D, Bezeljak U, Horvat S, Jerala R. 2017. A synthetic mammalian
therapeutic gene circuit for sensing and suppressing inflammation. Molecular Therapy.
25(1), 102–119.
mla: Smole, Anže, et al. “A Synthetic Mammalian Therapeutic Gene Circuit for Sensing
and Suppressing Inflammation.” Molecular Therapy, vol. 25, no. 1, Elsevier,
2017, pp. 102–19, doi:10.1016/j.ymthe.2016.10.005.
short: A. Smole, D. Lainšček, U. Bezeljak, S. Horvat, R. Jerala, Molecular Therapy
25 (2017) 102–119.
date_created: 2020-01-25T15:55:39Z
date_published: 2017-01-01T00:00:00Z
date_updated: 2021-01-12T08:13:14Z
day: '01'
ddc:
- '570'
department:
- _id: MaLo
doi: 10.1016/j.ymthe.2016.10.005
external_id:
pmid:
- '28129106'
file:
- access_level: open_access
checksum: ea8b1b28606dd1edab7379ba4fa3641f
content_type: application/pdf
creator: dernst
date_created: 2020-03-03T10:55:13Z
date_updated: 2020-07-14T12:47:56Z
file_id: '7561'
file_name: 2017_MolecularTherapy_Smole.pdf
file_size: 3404806
relation: main_file
file_date_updated: 2020-07-14T12:47:56Z
has_accepted_license: '1'
intvolume: ' 25'
issue: '1'
language:
- iso: eng
month: '01'
oa: 1
oa_version: Published Version
page: 102-119
pmid: 1
publication: Molecular Therapy
publication_identifier:
issn:
- 1525-0016
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: A synthetic mammalian therapeutic gene circuit for sensing and suppressing
inflammation
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: 25
year: '2017'
...
---
_id: '629'
abstract:
- lang: eng
text: Even simple cells like bacteria have precisely regulated cellular anatomies,
which allow them to grow, divide and to respond to internal or external cues with
high fidelity. How spatial and temporal intracellular organization in prokaryotic
cells is achieved and maintained on the basis of locally interacting proteins
still remains largely a mystery. Bulk biochemical assays with purified components
and in vivo experiments help us to approach key cellular processes from two opposite
ends, in terms of minimal and maximal complexity. However, to understand how cellular
phenomena emerge, that are more than the sum of their parts, we have to assemble
cellular subsystems step by step from the bottom up. Here, we review recent in
vitro reconstitution experiments with proteins of the bacterial cell division
machinery and illustrate how they help to shed light on fundamental cellular mechanisms
that constitute spatiotemporal order and regulate cell division.
author:
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
- first_name: Katja
full_name: Zieske, Katja
last_name: Zieske
- first_name: Petra
full_name: Schwille, Petra
last_name: Schwille
citation:
ama: 'Loose M, Zieske K, Schwille P. Reconstitution of protein dynamics involved
in bacterial cell division. In: Prokaryotic Cytoskeletons. Vol 84. Sub-Cellular
Biochemistry. Springer; 2017:419-444. doi:10.1007/978-3-319-53047-5_15'
apa: Loose, M., Zieske, K., & Schwille, P. (2017). Reconstitution of protein
dynamics involved in bacterial cell division. In Prokaryotic Cytoskeletons
(Vol. 84, pp. 419–444). Springer. https://doi.org/10.1007/978-3-319-53047-5_15
chicago: Loose, Martin, Katja Zieske, and Petra Schwille. “Reconstitution of Protein
Dynamics Involved in Bacterial Cell Division.” In Prokaryotic Cytoskeletons,
84:419–44. Sub-Cellular Biochemistry. Springer, 2017. https://doi.org/10.1007/978-3-319-53047-5_15.
ieee: M. Loose, K. Zieske, and P. Schwille, “Reconstitution of protein dynamics
involved in bacterial cell division,” in Prokaryotic Cytoskeletons, vol.
84, Springer, 2017, pp. 419–444.
ista: 'Loose M, Zieske K, Schwille P. 2017.Reconstitution of protein dynamics involved
in bacterial cell division. In: Prokaryotic Cytoskeletons. vol. 84, 419–444.'
mla: Loose, Martin, et al. “Reconstitution of Protein Dynamics Involved in Bacterial
Cell Division.” Prokaryotic Cytoskeletons, vol. 84, Springer, 2017, pp.
419–44, doi:10.1007/978-3-319-53047-5_15.
short: M. Loose, K. Zieske, P. Schwille, in:, Prokaryotic Cytoskeletons, Springer,
2017, pp. 419–444.
date_created: 2018-12-11T11:47:35Z
date_published: 2017-05-13T00:00:00Z
date_updated: 2021-01-12T08:06:57Z
day: '13'
department:
- _id: MaLo
doi: 10.1007/978-3-319-53047-5_15
external_id:
pmid:
- '28500535'
intvolume: ' 84'
language:
- iso: eng
month: '05'
oa_version: None
page: 419 - 444
pmid: 1
publication: Prokaryotic Cytoskeletons
publication_identifier:
eisbn:
- 978-3-319-53047-5
publication_status: published
publisher: Springer
publist_id: '7165'
quality_controlled: '1'
scopus_import: 1
series_title: Sub-Cellular Biochemistry
status: public
title: Reconstitution of protein dynamics involved in bacterial cell division
type: book_chapter
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 84
year: '2017'
...
---
_id: '660'
abstract:
- lang: eng
text: Growing microtubules are protected from depolymerization by the presence of
a GTP or GDP/Pi cap. End-binding proteins of the EB1 family bind to the stabilizing
cap, allowing monitoring of its size in real time. The cap size has been shown
to correlate with instantaneous microtubule stability. Here we have quantitatively
characterized the properties of cap size fluctuations during steadystate growth
and have developed a theory predicting their timescale and amplitude from the
kinetics of microtubule growth and cap maturation. In contrast to growth speed
fluctuations, cap size fluctuations show a characteristic timescale, which is
defined by the lifetime of the cap sites. Growth fluctuations affect the amplitude
of cap size fluctuations; however, cap size does not affect growth speed, indicating
that microtubules are far from instability during most of their time of growth.
Our theory provides the basis for a quantitative understanding of microtubule
stability fluctuations during steady-state growth.
acknowledgement: We thank Philippe Cluzel for helpful discussions and Gunnar Pruessner
for data analysis advice. This work was supported by the Francis Crick Institute,
which receives its core funding from Cancer Research UK Grant FC001163, Medical
Research Council Grant FC001163, and Wellcome Trust Grant FC001163. This work was
also supported by European Research Council Advanced Grant Project 323042 (to C.D.
and T.S.).
author:
- first_name: Jamie
full_name: Rickman, Jamie
last_name: Rickman
- first_name: Christian F
full_name: Düllberg, Christian F
id: 459064DC-F248-11E8-B48F-1D18A9856A87
last_name: Düllberg
orcid: 0000-0001-6335-9748
- first_name: Nicholas
full_name: Cade, Nicholas
last_name: Cade
- first_name: Lewis
full_name: Griffin, Lewis
last_name: Griffin
- first_name: Thomas
full_name: Surrey, Thomas
last_name: Surrey
citation:
ama: Rickman J, Düllberg CF, Cade N, Griffin L, Surrey T. Steady state EB cap size
fluctuations are determined by stochastic microtubule growth and maturation. PNAS.
2017;114(13):3427-3432. doi:10.1073/pnas.1620274114
apa: Rickman, J., Düllberg, C. F., Cade, N., Griffin, L., & Surrey, T. (2017).
Steady state EB cap size fluctuations are determined by stochastic microtubule
growth and maturation. PNAS. National Academy of Sciences. https://doi.org/10.1073/pnas.1620274114
chicago: Rickman, Jamie, Christian F Düllberg, Nicholas Cade, Lewis Griffin, and
Thomas Surrey. “Steady State EB Cap Size Fluctuations Are Determined by Stochastic
Microtubule Growth and Maturation.” PNAS. National Academy of Sciences,
2017. https://doi.org/10.1073/pnas.1620274114.
ieee: J. Rickman, C. F. Düllberg, N. Cade, L. Griffin, and T. Surrey, “Steady state
EB cap size fluctuations are determined by stochastic microtubule growth and maturation,”
PNAS, vol. 114, no. 13. National Academy of Sciences, pp. 3427–3432, 2017.
ista: Rickman J, Düllberg CF, Cade N, Griffin L, Surrey T. 2017. Steady state EB
cap size fluctuations are determined by stochastic microtubule growth and maturation.
PNAS. 114(13), 3427–3432.
mla: Rickman, Jamie, et al. “Steady State EB Cap Size Fluctuations Are Determined
by Stochastic Microtubule Growth and Maturation.” PNAS, vol. 114, no. 13,
National Academy of Sciences, 2017, pp. 3427–32, doi:10.1073/pnas.1620274114.
short: J. Rickman, C.F. Düllberg, N. Cade, L. Griffin, T. Surrey, PNAS 114 (2017)
3427–3432.
date_created: 2018-12-11T11:47:46Z
date_published: 2017-03-28T00:00:00Z
date_updated: 2021-01-12T08:08:09Z
day: '28'
department:
- _id: MaLo
doi: 10.1073/pnas.1620274114
external_id:
pmid:
- '28280102'
intvolume: ' 114'
issue: '13'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5380103/
month: '03'
oa: 1
oa_version: Submitted Version
page: 3427 - 3432
pmid: 1
publication: PNAS
publication_identifier:
issn:
- '00278424'
publication_status: published
publisher: National Academy of Sciences
publist_id: '7073'
quality_controlled: '1'
scopus_import: 1
status: public
title: Steady state EB cap size fluctuations are determined by stochastic microtubule
growth and maturation
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 114
year: '2017'
...
---
_id: '960'
abstract:
- lang: eng
text: The human cerebral cortex is the seat of our cognitive abilities and composed
of an extraordinary number of neurons, organized in six distinct layers. The establishment
of specific morphological and physiological features in individual neurons needs
to be regulated with high precision. Impairments in the sequential developmental
programs instructing corticogenesis lead to alterations in the cortical cytoarchitecture
which is thought to represent the major underlying cause for several neurological
disorders including neurodevelopmental and psychiatric diseases. In this review
we discuss the role of cell polarity at sequential stages during cortex development.
We first provide an overview of morphological cell polarity features in cortical
neural stem cells and newly-born postmitotic neurons. We then synthesize a conceptual
molecular and biochemical framework how cell polarity is established at the cellular
level through a break in symmetry in nascent cortical projection neurons. Lastly
we provide a perspective how the molecular mechanisms applying to single cells
could be probed and integrated in an in vivo and tissue-wide context.
article_number: '176'
article_processing_charge: Yes
author:
- first_name: Andi H
full_name: Hansen, Andi H
id: 38853E16-F248-11E8-B48F-1D18A9856A87
last_name: Hansen
- first_name: Christian F
full_name: Düllberg, Christian F
id: 459064DC-F248-11E8-B48F-1D18A9856A87
last_name: Düllberg
orcid: 0000-0001-6335-9748
- first_name: Christine
full_name: Mieck, Christine
id: 34CAE85C-F248-11E8-B48F-1D18A9856A87
last_name: Mieck
orcid: 0000-0003-1919-7416
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
- first_name: Simon
full_name: Hippenmeyer, Simon
id: 37B36620-F248-11E8-B48F-1D18A9856A87
last_name: Hippenmeyer
orcid: 0000-0003-2279-1061
citation:
ama: Hansen AH, Düllberg CF, Mieck C, Loose M, Hippenmeyer S. Cell polarity in cerebral
cortex development - cellular architecture shaped by biochemical networks. Frontiers
in Cellular Neuroscience. 2017;11. doi:10.3389/fncel.2017.00176
apa: Hansen, A. H., Düllberg, C. F., Mieck, C., Loose, M., & Hippenmeyer, S.
(2017). Cell polarity in cerebral cortex development - cellular architecture shaped
by biochemical networks. Frontiers in Cellular Neuroscience. Frontiers
Research Foundation. https://doi.org/10.3389/fncel.2017.00176
chicago: Hansen, Andi H, Christian F Düllberg, Christine Mieck, Martin Loose, and
Simon Hippenmeyer. “Cell Polarity in Cerebral Cortex Development - Cellular Architecture
Shaped by Biochemical Networks.” Frontiers in Cellular Neuroscience. Frontiers
Research Foundation, 2017. https://doi.org/10.3389/fncel.2017.00176.
ieee: A. H. Hansen, C. F. Düllberg, C. Mieck, M. Loose, and S. Hippenmeyer, “Cell
polarity in cerebral cortex development - cellular architecture shaped by biochemical
networks,” Frontiers in Cellular Neuroscience, vol. 11. Frontiers Research
Foundation, 2017.
ista: Hansen AH, Düllberg CF, Mieck C, Loose M, Hippenmeyer S. 2017. Cell polarity
in cerebral cortex development - cellular architecture shaped by biochemical networks.
Frontiers in Cellular Neuroscience. 11, 176.
mla: Hansen, Andi H., et al. “Cell Polarity in Cerebral Cortex Development - Cellular
Architecture Shaped by Biochemical Networks.” Frontiers in Cellular Neuroscience,
vol. 11, 176, Frontiers Research Foundation, 2017, doi:10.3389/fncel.2017.00176.
short: A.H. Hansen, C.F. Düllberg, C. Mieck, M. Loose, S. Hippenmeyer, Frontiers
in Cellular Neuroscience 11 (2017).
date_created: 2018-12-11T11:49:25Z
date_published: 2017-06-28T00:00:00Z
date_updated: 2024-03-25T23:30:23Z
day: '28'
ddc:
- '570'
department:
- _id: SiHi
- _id: MaLo
doi: 10.3389/fncel.2017.00176
ec_funded: 1
external_id:
isi:
- '000404486700001'
file:
- access_level: open_access
checksum: dc1f5a475b918d09a0f9f587400b1626
content_type: application/pdf
creator: system
date_created: 2018-12-12T10:09:40Z
date_updated: 2020-07-14T12:48:16Z
file_id: '4764'
file_name: IST-2017-830-v1+1_2017_Hansen_CellPolarity.pdf
file_size: 2153858
relation: main_file
file_date_updated: 2020-07-14T12:48:16Z
has_accepted_license: '1'
intvolume: ' 11'
isi: 1
language:
- iso: eng
month: '06'
oa: 1
oa_version: Published Version
project:
- _id: 25D61E48-B435-11E9-9278-68D0E5697425
call_identifier: FP7
grant_number: '618444'
name: Molecular Mechanisms of Cerebral Cortex Development
- _id: 25D7962E-B435-11E9-9278-68D0E5697425
grant_number: RGP0053/2014
name: Quantitative Structure-Function Analysis of Cerebral Cortex Assembly at Clonal
Level
- _id: 25681D80-B435-11E9-9278-68D0E5697425
call_identifier: FP7
grant_number: '291734'
name: International IST Postdoc Fellowship Programme
- _id: 25985A36-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: T00817-B21
name: The biochemical basis of PAR polarization
publication: Frontiers in Cellular Neuroscience
publication_identifier:
issn:
- '16625102'
publication_status: published
publisher: Frontiers Research Foundation
publist_id: '6445'
pubrep_id: '830'
quality_controlled: '1'
related_material:
record:
- id: '9962'
relation: dissertation_contains
status: public
scopus_import: '1'
status: public
title: Cell polarity in cerebral cortex development - cellular architecture shaped
by biochemical networks
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 11
year: '2017'
...
---
_id: '1213'
abstract:
- lang: eng
text: Bacterial cytokinesis is commonly initiated by the Z-ring, a dynamic cytoskeletal
structure that assembles at the site of division. Its primary component is FtsZ,
a tubulin-like GTPase, that like its eukaryotic relative forms protein filaments
in the presence of GTP. Since the discovery of the Z-ring 25 years ago, various
models for the role of FtsZ have been suggested. However, important information
about the architecture and dynamics of FtsZ filaments during cytokinesis is still
missing. One reason for this lack of knowledge has been the small size of bacteria,
which has made it difficult to resolve the orientation and dynamics of individual
FtsZ filaments in the Z-ring. While superresolution microscopy experiments have
helped to gain more information about the organization of the Z-ring in the dividing
cell, they were not yet able to elucidate a mechanism of how FtsZ filaments reorganize
during assembly and disassembly of the Z-ring. In this chapter, we explain how
to use an in vitro reconstitution approach to investigate the self-organization
of FtsZ filaments recruited to a biomimetic lipid bilayer by its membrane anchor
FtsA. We show how to perform single-molecule experiments to study the behavior
of individual FtsZ monomers during the constant reorganization of the FtsZ-FtsA
filament network. We describe how to analyze the dynamics of single molecules
and explain why this information can help to shed light onto possible mechanism
of Z-ring constriction. We believe that similar experimental approaches will be
useful to study the mechanism of membrane-based polymerization of other cytoskeletal
systems, not only from prokaryotic but also eukaryotic origin.
acknowledged_ssus:
- _id: Bio
acknowledgement: Natalia Baranova is supported by an EMBO Long-Term Fellowship (EMBO
ALTF 1163-2015) and Martin Loose by an ERC Starting Grant (ERCStG-2015-SelfOrganiCell).
alternative_title:
- Methods in Cell Biology
article_processing_charge: No
author:
- first_name: Natalia
full_name: Baranova, Natalia
id: 38661662-F248-11E8-B48F-1D18A9856A87
last_name: Baranova
orcid: 0000-0002-3086-9124
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
citation:
ama: 'Baranova NS, Loose M. Single-molecule measurements to study polymerization
dynamics of FtsZ-FtsA copolymers. In: Echard A, ed. Cytokinesis. Vol 137.
Academic Press; 2017:355-370. doi:10.1016/bs.mcb.2016.03.036'
apa: Baranova, N. S., & Loose, M. (2017). Single-molecule measurements to study
polymerization dynamics of FtsZ-FtsA copolymers. In A. Echard (Ed.), Cytokinesis
(Vol. 137, pp. 355–370). Academic Press. https://doi.org/10.1016/bs.mcb.2016.03.036
chicago: Baranova, Natalia S., and Martin Loose. “Single-Molecule Measurements to
Study Polymerization Dynamics of FtsZ-FtsA Copolymers.” In Cytokinesis,
edited by Arnaud Echard, 137:355–70. Academic Press, 2017. https://doi.org/10.1016/bs.mcb.2016.03.036.
ieee: N. S. Baranova and M. Loose, “Single-molecule measurements to study polymerization
dynamics of FtsZ-FtsA copolymers,” in Cytokinesis, vol. 137, A. Echard,
Ed. Academic Press, 2017, pp. 355–370.
ista: 'Baranova NS, Loose M. 2017.Single-molecule measurements to study polymerization
dynamics of FtsZ-FtsA copolymers. In: Cytokinesis. Methods in Cell Biology, vol.
137, 355–370.'
mla: Baranova, Natalia S., and Martin Loose. “Single-Molecule Measurements to Study
Polymerization Dynamics of FtsZ-FtsA Copolymers.” Cytokinesis, edited by
Arnaud Echard, vol. 137, Academic Press, 2017, pp. 355–70, doi:10.1016/bs.mcb.2016.03.036.
short: N.S. Baranova, M. Loose, in:, A. Echard (Ed.), Cytokinesis, Academic Press,
2017, pp. 355–370.
date_created: 2018-12-11T11:50:45Z
date_published: 2017-12-01T00:00:00Z
date_updated: 2023-09-20T11:16:30Z
day: '01'
department:
- _id: MaLo
doi: 10.1016/bs.mcb.2016.03.036
ec_funded: 1
editor:
- first_name: 'Arnaud '
full_name: 'Echard, Arnaud '
last_name: Echard
external_id:
isi:
- '000403542900022'
intvolume: ' 137'
isi: 1
language:
- iso: eng
month: '12'
oa_version: None
page: 355 - 370
project:
- _id: 2596EAB6-B435-11E9-9278-68D0E5697425
grant_number: ALTF 2015-1163
name: Synthesis of bacterial cell wall
- _id: 25681D80-B435-11E9-9278-68D0E5697425
call_identifier: FP7
grant_number: '291734'
name: International IST Postdoc Fellowship Programme
publication: Cytokinesis
publication_identifier:
issn:
- 0091679X
publication_status: published
publisher: Academic Press
publist_id: '6134'
quality_controlled: '1'
scopus_import: '1'
status: public
title: Single-molecule measurements to study polymerization dynamics of FtsZ-FtsA
copolymers
type: book_chapter
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 137
year: '2017'
...
---
_id: '453'
abstract:
- lang: eng
text: Most kinesin motors move in only one direction along microtubules. Members
of the kinesin-5 subfamily were initially described as unidirectional plus-end-directed
motors and shown to produce piconewton forces. However, some fungal kinesin-5
motors are bidirectional. The force production of a bidirectional kinesin-5 has
not yet been measured. Therefore, it remains unknown whether the mechanism of
the unconventional minus-end-directed motility differs fundamentally from that
of plus-end-directed stepping. Using force spectroscopy, we have measured here
the forces that ensembles of purified budding yeast kinesin-5 Cin8 produce in
microtubule gliding assays in both plus- and minus-end direction. Correlation
analysis of pause forces demonstrated that individual Cin8 molecules produce additive
forces in both directions of movement. In ensembles, Cin8 motors were able to
produce single-motor forces up to a magnitude of ∼1.5 pN. Hence, these properties
appear to be conserved within the kinesin-5 subfamily. Force production was largely
independent of the directionality of movement, indicating similarities between
the motility mechanisms for both directions. These results provide constraints
for the development of models for the bidirectional motility mechanism of fission
yeast kinesin-5 and provide insight into the function of this mitotic motor.
acknowledgement: 'The plasmid for full-length kinesin-1 was a gift from G. Holzwarth
and J. Macosko with permission from J. Howard. We thank I. Lueke and N. I. Cade
for technical assistance. G.P. thanks the Francis Crick Institute, and in particular
the Surrey and Salbreux groups, for their hospitality during his sabbatical stay,
as well as Imperial College London for making it possible. This work was supported
by the Francis Crick Institute, which receives its core funding from Cancer Research
UK (FC001163), the United Kingdom Medical Research Council (FC001163), and the Wellcome
Trust (FC001163), and by Imperial College London. J.R. was also supported by a Sir
Henry Wellcome Postdoctoral Fellowship (100145/Z/12/Z) and T.S. by the European
Research Council (Advanced Grant, project 323042). '
article_processing_charge: No
article_type: original
author:
- first_name: Todd
full_name: Fallesen, Todd
last_name: Fallesen
- first_name: Johanna
full_name: Roostalu, Johanna
last_name: Roostalu
- first_name: Christian F
full_name: Düllberg, Christian F
id: 459064DC-F248-11E8-B48F-1D18A9856A87
last_name: Düllberg
orcid: 0000-0001-6335-9748
- first_name: Gunnar
full_name: Pruessner, Gunnar
last_name: Pruessner
- first_name: Thomas
full_name: Surrey, Thomas
last_name: Surrey
citation:
ama: Fallesen T, Roostalu J, Düllberg CF, Pruessner G, Surrey T. Ensembles of bidirectional
kinesin Cin8 produce additive forces in both directions of movement. Biophysical
Journal. 2017;113(9):2055-2067. doi:10.1016/j.bpj.2017.09.006
apa: Fallesen, T., Roostalu, J., Düllberg, C. F., Pruessner, G., & Surrey, T.
(2017). Ensembles of bidirectional kinesin Cin8 produce additive forces in both
directions of movement. Biophysical Journal. Biophysical Society. https://doi.org/10.1016/j.bpj.2017.09.006
chicago: Fallesen, Todd, Johanna Roostalu, Christian F Düllberg, Gunnar Pruessner,
and Thomas Surrey. “Ensembles of Bidirectional Kinesin Cin8 Produce Additive Forces
in Both Directions of Movement.” Biophysical Journal. Biophysical Society,
2017. https://doi.org/10.1016/j.bpj.2017.09.006.
ieee: T. Fallesen, J. Roostalu, C. F. Düllberg, G. Pruessner, and T. Surrey, “Ensembles
of bidirectional kinesin Cin8 produce additive forces in both directions of movement,”
Biophysical Journal, vol. 113, no. 9. Biophysical Society, pp. 2055–2067,
2017.
ista: Fallesen T, Roostalu J, Düllberg CF, Pruessner G, Surrey T. 2017. Ensembles
of bidirectional kinesin Cin8 produce additive forces in both directions of movement.
Biophysical Journal. 113(9), 2055–2067.
mla: Fallesen, Todd, et al. “Ensembles of Bidirectional Kinesin Cin8 Produce Additive
Forces in Both Directions of Movement.” Biophysical Journal, vol. 113,
no. 9, Biophysical Society, 2017, pp. 2055–67, doi:10.1016/j.bpj.2017.09.006.
short: T. Fallesen, J. Roostalu, C.F. Düllberg, G. Pruessner, T. Surrey, Biophysical
Journal 113 (2017) 2055–2067.
date_created: 2018-12-11T11:46:33Z
date_published: 2017-11-07T00:00:00Z
date_updated: 2021-01-12T07:59:28Z
day: '07'
ddc:
- '570'
department:
- _id: MaLo
doi: 10.1016/j.bpj.2017.09.006
file:
- access_level: open_access
checksum: 99a2474088e20ac74b1882c4fbbb45b1
content_type: application/pdf
creator: system
date_created: 2018-12-12T10:14:03Z
date_updated: 2020-07-14T12:46:31Z
file_id: '5052'
file_name: IST-2018-965-v1+1_2017_Duellberg_Ensembles_of.pdf
file_size: 977192
relation: main_file
file_date_updated: 2020-07-14T12:46:31Z
has_accepted_license: '1'
intvolume: ' 113'
issue: '9'
language:
- iso: eng
month: '11'
oa: 1
oa_version: Published Version
page: 2055 - 2067
publication: Biophysical Journal
publication_status: published
publisher: Biophysical Society
publist_id: '7369'
pubrep_id: '965'
quality_controlled: '1'
status: public
title: Ensembles of bidirectional kinesin Cin8 produce additive forces in both directions
of movement
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: 113
year: '2017'
...
---
_id: '1544'
abstract:
- lang: eng
text: 'Cell division in prokaryotes and eukaryotes is commonly initiated by the
well-controlled binding of proteins to the cytoplasmic side of the cell membrane.
However, a precise characterization of the spatiotemporal dynamics of membrane-bound
proteins is often difficult to achieve in vivo. Here, we present protocols for
the use of supported lipid bilayers to rebuild the cytokinetic machineries of
cells with greatly different dimensions: the bacterium Escherichia coli and eggs
of the vertebrate Xenopus laevis. Combined with total internal reflection fluorescence
microscopy, these experimental setups allow for precise quantitative analyses
of membrane-bound proteins. The protocols described to obtain glass-supported
membranes from bacterial and vertebrate lipids can be used as starting points
for other reconstitution experiments. We believe that similar biochemical assays
will be instrumental to study the biochemistry and biophysics underlying a variety
of complex cellular tasks, such as signaling, vesicle trafficking, and cell motility.'
author:
- first_name: Phuong
full_name: Nguyen, Phuong
last_name: Nguyen
- first_name: Christine
full_name: Field, Christine
last_name: Field
- first_name: Aaron
full_name: Groen, Aaron
last_name: Groen
- first_name: Timothy
full_name: Mitchison, Timothy
last_name: Mitchison
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
citation:
ama: 'Nguyen P, Field C, Groen A, Mitchison T, Loose M. Using supported bilayers
to study the spatiotemporal organization of membrane-bound proteins. In: Building
a Cell from Its Components Parts. Vol 128. Academic Press; 2015:223-241. doi:10.1016/bs.mcb.2015.01.007'
apa: Nguyen, P., Field, C., Groen, A., Mitchison, T., & Loose, M. (2015). Using
supported bilayers to study the spatiotemporal organization of membrane-bound
proteins. In Building a Cell from its Components Parts (Vol. 128, pp. 223–241).
Academic Press. https://doi.org/10.1016/bs.mcb.2015.01.007
chicago: Nguyen, Phuong, Christine Field, Aaron Groen, Timothy Mitchison, and Martin
Loose. “Using Supported Bilayers to Study the Spatiotemporal Organization of Membrane-Bound
Proteins.” In Building a Cell from Its Components Parts, 128:223–41. Academic
Press, 2015. https://doi.org/10.1016/bs.mcb.2015.01.007.
ieee: P. Nguyen, C. Field, A. Groen, T. Mitchison, and M. Loose, “Using supported
bilayers to study the spatiotemporal organization of membrane-bound proteins,”
in Building a Cell from its Components Parts, vol. 128, Academic Press,
2015, pp. 223–241.
ista: 'Nguyen P, Field C, Groen A, Mitchison T, Loose M. 2015.Using supported bilayers
to study the spatiotemporal organization of membrane-bound proteins. In: Building
a Cell from its Components Parts. vol. 128, 223–241.'
mla: Nguyen, Phuong, et al. “Using Supported Bilayers to Study the Spatiotemporal
Organization of Membrane-Bound Proteins.” Building a Cell from Its Components
Parts, vol. 128, Academic Press, 2015, pp. 223–41, doi:10.1016/bs.mcb.2015.01.007.
short: P. Nguyen, C. Field, A. Groen, T. Mitchison, M. Loose, in:, Building a Cell
from Its Components Parts, Academic Press, 2015, pp. 223–241.
date_created: 2018-12-11T11:52:38Z
date_published: 2015-04-08T00:00:00Z
date_updated: 2021-01-12T06:51:30Z
day: '08'
department:
- _id: MaLo
doi: 10.1016/bs.mcb.2015.01.007
external_id:
pmid:
- '25997350'
intvolume: ' 128'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4578691/
month: '04'
oa: 1
oa_version: Submitted Version
page: 223 - 241
pmid: 1
publication: Building a Cell from its Components Parts
publication_status: published
publisher: Academic Press
publist_id: '5627'
quality_controlled: '1'
scopus_import: 1
status: public
title: Using supported bilayers to study the spatiotemporal organization of membrane-bound
proteins
type: book_chapter
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 128
year: '2015'
...