Rabbit Skeletal Muscle Actin Behaves Differently Than Acanthamoeba Actin When Added to Solube Extracts of Acanthamoeba castellanii
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Cited by 6 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. Biochemical and functional characterization of the actin-binding activity of the B subunit of yeast vacuolar H+-ATPase;Journal of Experimental Biology;2008-04-01
2. Rho-family GTPases require the Arp2/3 complex to stimulate actin polymerizationin Acanthamoeba extracts;Current Biology;1999-04
3. Ca2+ bound to the high affinity divalent cation-binding site of actin enhances actophorin-induced depolymerization of muscle F-actin but inhibits actophorin-induced depolymerization of Acanthamoeba F-actin;Journal of Muscle Research and Cell Motility;1996-08
4. The bulk of unpolymerized actin in Xenopus egg extracts is ATP-bound.;Molecular Biology of the Cell;1995-02
5. Actobindin induces the accumulation of actin dimers that neither nucleate polymerization nor self-associate.;Journal of Biological Chemistry;1994-10
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