The purification and characterization of a globular subfragment of Acanthamoeba myosin II that is fully active when cross-linked to F-actin.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference31 articles.
1. Acanthamoeba myosin II.
2. Characterization of a second myosin from Acanthamoeba castellanii
3. Structure and polymerization of Acanthamoeba myosin-II filaments.
4. Comparison of the actin binding and filament formation properties of phosphorylated and dephosphorylated Acanthamoeba myosin II
5. Actin activation of Ca2+-sensitive Mg2+-ATPase activity of Acanthamoeba myosin II is enhanced by dephosphorylation of its heavy chains.
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1. Phenylglyoxal Reveals Phosphorylation-Dependent Difference in the Conformation of Acanthamoeba Myosin II Active Site;Archives of Biochemistry and Biophysics;2000-12
2. Thermal unfolding of Acanthamoeba myosin II and skeletal muscle myosin;Biophysical Chemistry;1996-04
3. Effects of phosphorylation and nucleotides on the conformation of myosin II from Acanthamoeba castellanii.;Journal of Biological Chemistry;1994-05
4. A structural difference between filaments of phosphorylated and dephosphorylated Acanthamoeba myosin II revealed by electric birefringence.;Journal of Biological Chemistry;1993-03
5. Regulation of the actin-activated ATPase and in vitro motility activities of monomeric and filamentous Acanthamoeba myosin II.;Journal of Biological Chemistry;1992-10
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