Purification and characterization of an ATP-sensitive actin gelation protein from Acanthamoeba castellanii.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference16 articles.
1. Purification from Acanthamoeba castellanii of proteins that induce gelation and syneresis of F-actin.
2. Purification of a calcium-sensitive actin gelation protein from Acanthamoeba.
3. Purification of a high molecular weight actin filament gelation protein from Acanthamoeba that shares antigenic determinants with vertebrate spectrins.
4. Regulation of the actin-activated ATPase activity of Acanthamoeba myosin I by cross-linking actin filaments.
5. Viscometric analysis of the gelation of Acanthamoeba extracts and purification of two gelation factors.
Cited by 3 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. 2E4 (Kaptin): A novel actin-associated protein from human blood platelets found in lamellipodia and the tips of the stereocilia of the inner ear;European Journal of Cell Biology;1999-02
2. The Polyelectrolyte Nature of F-actin and the Mechanism of Actin Bundle Formation;Journal of Biological Chemistry;1996-04
3. Inhibition of an early stage of actin polymerization by actobindin.;Journal of Biological Chemistry;1988-09
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