Proteolytic separation of the actin-activatable ATPase site from the phosphorylation site on the heavy chain of Acanthamoeba myosin IA.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference16 articles.
1. Acanthamoeba cofactor protein is a heavy chain kinase required for actin activation of the Mg2+-ATPase activity of Acanthamoeba myosin I
2. The isolated heavy chain of an Acanthamoeba myosin contains full enzymatic activity.
3. Direct photoaffinity labeling by nucleotides of the apparent catalytic site on the heavy chains of smooth muscle and Acanthamoeba myosins.
4. Regulation and Kinetics of the Actin-Myosin-ATP Interaction
5. Actin activation of Ca2+-sensitive Mg2+-ATPase activity of Acanthamoeba myosin II is enhanced by dephosphorylation of its heavy chains.
Cited by 15 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. Role of Calcium/Calmodulin-Mediated Processes in Protozoa;International Review of Cytology;1992
2. Chapter 2 Acanthamoeba Myosin I: Past, Present, and Future;Ordering the Membrane-Cytoskeleton Trilayer;1991
3. Contractile Proteins of Smooth Muscle;Physiology and Pathophysiology of the Heart;1989
4. Amino acid sequence of the calcium-binding light chain of myosin from the lower eukaryote, Physarum polycephalum.;Journal of Biological Chemistry;1988-01
5. Isolation and characterization of myosin from amoebae of Physarum polycephalum.;Journal of Biological Chemistry;1986-06
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