Antagonism between Ena/VASP proteins and actin filament capping regulates fibroblast motility (Q29618423)

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10 November 2019

title

Antagonism between Ena/VASP proteins and actin filament capping regulates fibroblast motility (English)

2 references

PubMed

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30 April 2017

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10 November 2019

1 reference

3

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10 November 2019

John A Cooper

9

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10 November 2019

Gary Borisy

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10 November 2019

author name string

James E Bear

1

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10 November 2019

Tatyana M Svitkina

2

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10 November 2019

Dorothy A Schafer

4

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10 November 2019

Joseph J Loureiro

5

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10 November 2019

Geraldine A Strasser

6

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10 November 2019

Ivan V Maly

7

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10 November 2019

Oleg Y Chaga

8

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10 November 2019

Frank B Gertler

11

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10 November 2019

language of work or name

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30 April 2017

publication date

1 May 2002

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10 November 2019

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10 November 2019

volume

109

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10 November 2019

issue

4

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10 November 2019

page(s)

509-521

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The EVH2 domain of the vasodilator-stimulated phosphoprotein mediates tetramerization, F-actin binding, and actin bundle formation

10 November 2019

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Negative regulation of fibroblast motility by Ena/VASP proteins

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Regulating cellular actin assembly

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Listeria protein ActA mimics WASp family proteins: it activates filament barbed end branching by Arp2/3 complex

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Secrets of actin-based motility revealed by a bacterial pathogen

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Aromatic and basic residues within the EVH1 domain of VASP specify its interaction with proline-rich ligands

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Effects of cytochalasin and phalloidin on actin

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Pyrene actin: documentation of the validity of a sensitive assay for actin polymerization

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Mena, a relative of VASP and Drosophila Enabled, is implicated in the control of microfilament dynamics

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Quantifying Lamella Dynamics of Cultured Cells by SACED, a New Computer-Assisted Motion Analysis

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Characterization of the actin binding properties of the vasodilator-stimulated phosphoprotein VASP.

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cAMP-dependent protein kinase phosphorylation of EVL, a Mena/VASP relative, regulates its interaction with actin and SH3 domains

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Identification of two regions in the N-terminal domain of ActA involved in the actin comet tail formation by Listeria monocytogenes.

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Cell migration: a physically integrated molecular process

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Self-organization of a propulsive actin network as an evolutionary process

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Cell motility driven by actin polymerization

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A novel proline-rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the Ena/VASP family

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Interactions with PIP2, ADP-actin monomers, and capping protein regulate the activity and localization of yeast twinfilin

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7 January 2021

Actin-based motility: stop and go with Ena/VASP proteins

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[43] Correlative light and electron microscopy of the cytoskeleton of cultured cells

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Identifiers

DOI

2 references

Consolidated OpenCitations Corpus – April 2017

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12086607%20AND%20SRC:MED&resulttype=core&format=json

10 November 2019

1 reference

Consolidated OpenCitations Corpus – April 2017

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=12086607

3 references

30 April 2017

Consolidated OpenCitations Corpus – April 2017