Coupling of Folding and Binding of Thymosin β4 upon Interaction with Monomeric Actin Monitored by Nuclear Magnetic Resonance-Reference-Cited by-同舟云学术

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Coupling of Folding and Binding of Thymosin β4 upon Interaction with Monomeric Actin Monitored by Nuclear Magnetic Resonance

Published:2004-05 Issue:22 Volume:279 Page:23637-23645
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Domanski Michael,Hertzog Maud,Coutant Jérôme,Gutsche-Perelroizen Irina,Bontems François,Carlier Marie-France,Guittet Eric,van Heijenoort Carine

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference67 articles.

1. Actin Binding Proteins: Regulation of Cytoskeletal Microfilaments

2. Thymosin β4 and Fx, an actin-sequestering peptide, are indistinguishable

3. Interaction of thymosin .beta.4 with muscle and platelet actin: implications for actin sequestration in resting platelets

4. Thymosin beta 4 sequesters the majority of G-actin in resting human polymorphonuclear leukocytes.

5. Use of bimanyl actin derivative (TMB-actin) for studying complexation of β-thymosins

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