How a single residue in individual β-thymosin/WH2 domains controls their functions in actin assembly-Reference-Cited by-同舟云学术

How a single residue in individual β-thymosin/WH2 domains controls their functions in actin assembly

Published:2011-12-23 Issue:4 Volume:31 Page:1000-1013
ISSN:0261-4189
Container-title:The EMBO Journal
language:en
Short-container-title:

Author:

Didry Dominique¹,Cantrelle Francois-Xavier²,Husson Clotilde¹,Roblin Pierre¹³,Moorthy Anna M Eswara¹,Perez Javier³,Le Clainche Christophe¹,Hertzog Maud¹,Guittet Eric²,Carlier Marie-France¹,van Heijenoort Carine²,Renault Louis¹

Affiliation:

1. Laboratoire d'Enzymologie et Biochimie Structurales, Centre de Recherche de Gif, CNRS; Gif-sur-Yvette France

2. Institut de Chimie des Substances Naturelles, Centre de Recherche de Gif, CNRS; Gif-sur-Yvette France

3. Synchrotron SOLEIL; Gif-sur-Yvette France

Publisher

Wiley

Subject

General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,Molecular Biology,General Neuroscience

Reference45 articles.

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2. Widely distributed residues in thymosin beta4 are critical for actin binding;Au;Biochemistry,2008

3. Clustering of VASP actively drives processive, WH2 domain-mediated actin filament elongation;Breitsprecher;EMBO J,2008

4. Molecular mechanism of Ena/VASP-mediated actin-filament elongation;Breitsprecher;EMBO J,2011

5. A nucleator arms race: cellular control of actin assembly;Campellone;Nat Rev Mol Cell Biol,2010

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