Thymosin β4serves as a glutaminyl substrate of transglutaminase. Labeling with fluorescent dansylcadaverine does not abolish interaction with G-actin1-Reference-Cited by-同舟云学术

Thymosin β4serves as a glutaminyl substrate of transglutaminase. Labeling with fluorescent dansylcadaverine does not abolish interaction with G-actin1

Published:1999-12-20 Issue:1-2 Volume:464 Page:14-20
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Huff Thomas,Ballweber Edda,Humeny Andreas,Bonk Thomas,Becker Cord-Michael,Müller Christian S.G.,Mannherz Hans Georg,Hannappel Ewald

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/S0014-5793(99)01670-1/fullpdf

Reference44 articles.

1. ACTIN AND ACTIN-BINDING PROTEINS. A CRITICAL EVALUATION OF MECHANISMS AND FUNCTIONS

2. Actin assembly in response to extracellular signals: role of capping proteins, thymosin β4 and profilin

3. Determination of thymosin β4 in human blood cells and serum

4. Complete amino acid sequence of bovine thymosin beta 4: a thymic hormone that induces terminal deoxynucleotidyl transferase activity in thymocyte populations.

5. Chemical characterization of thymosin beta 4.

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4. Peptide labeling with photoactivatable trifunctional cadaverine derivative and identification of interacting partners by biotin transfer;Analytical Biochemistry;2014-07

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