Comparison of the actin binding and filament formation properties of phosphorylated and dephosphorylated Acanthamoeba myosin II
- 1 December 1982
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 21 (26), 6910-6915
- https://doi.org/10.1021/bi00269a045
Abstract
No abstract availableThis publication has 10 references indexed in Scilit:
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- Regulation of myosin self-assembly: phosphorylation of Dictyostelium heavy chain inhibits formation of thick filaments.Proceedings of the National Academy of Sciences, 1980
- Actin activation of Ca2+-sensitive Mg2+-ATPase activity of Acanthamoeba myosin II is enhanced by dephosphorylation of its heavy chains.Journal of Biological Chemistry, 1980
- Regulation of non-muscle myosin assembly by calmodulin-dependent light chain kinaseNature, 1980
- Chymotryptic heavy meromyosin from gizzard myosin: A proteolytic fragment with the regulatory properties of the intact myosinBiochemical and Biophysical Research Communications, 1978
- Characterization of a second myosin from Acanthamoeba castellaniiJournal of Biological Chemistry, 1978
- ACANTHAMOEBA MYOSIN-II1977
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976