Widely Distributed Residues in Thymosin β4 Are Critical for Actin Binding-Reference-Cited by-同舟云学术

Widely Distributed Residues in Thymosin β4 Are Critical for Actin Binding

Published:2008-03-08 Issue:13 Volume:47 Page:4181-4188
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Au Joshua K.¹,Olivares Adrian O.¹,Henn Arnon¹,Cao Wenxiang¹,Safer Daniel¹,De La Cruz Enrique M.¹

Affiliation:

1. Department of Molecular Biophysics and Biochemistry, Yale University, 260 Whitney Avenue, New Haven, Connecticut 06520, and Pennsylvania Muscle Institute and Department of Physiology, University of Pennsylvania, School of Medicine, Philadelphia, Pennsylvania 19104

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi701769u

Reference23 articles.

1. Cellular Motility Driven by Assembly and Disassembly of Actin Filaments

2. Actin-based motility: from molecules to movement

3. Distribution of thymosin β4 in vertebrate classes

4. Thymosin β: actin-sequestering protein moonlights to repair injured tissues

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1. Prediction and Dissection of Widely-Varying Association Rate Constants of Actin-Binding Proteins;PLoS Computational Biology;2012-10-04

2. How a single residue in individual β-thymosin/WH2 domains controls their functions in actin assembly;The EMBO Journal;2011-12-23

3. Control of Actin Assembly by the WH2 Domains and Their Multifunctional Tandem Repeats in Spire and Cordon-Bleu;International Review of Cell and Molecular Biology;2011

4. Multifunctionality of the β-thymosin/WH2 module: G-actin sequestration, actin filament growth, nucleation, and severing;Annals of the New York Academy of Sciences;2010-05

5. The β-thymosins: Intracellular and extracellular activities of a versatile actin binding protein family;Cell Motility and the Cytoskeleton;2009-10