Supramolecular regulation of the actin-activated ATPase activity of filaments of Acanthamoeba Myosin II.
Open Access
- 1 May 1983
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 258 (10) , 6011-6014
- https://doi.org/10.1016/s0021-9258(18)32364-0
Abstract
No abstract availableKeywords
This publication has 11 references indexed in Scilit:
- Structure and polymerization of Acanthamoeba myosin-II filaments.The Journal of cell biology, 1982
- Comparison of the actin binding and filament formation properties of phosphorylated and dephosphorylated Acanthamoeba myosin IIBiochemistry, 1982
- A bent monomeric conformation of myosin from smooth muscle.Proceedings of the National Academy of Sciences, 1982
- Localization of the three phosphorylation sites on each heavy chain of Acanthamoeba myosin II to a segment at the end of the tail.Journal of Biological Chemistry, 1982
- Identification of three phosphorylation sites on each heavy chain of Acanthamoeba myosin II.Journal of Biological Chemistry, 1981
- Purification and characterization of actin-activatable, Ca2+-sensitive myosin II from Acanthamoeba.Journal of Biological Chemistry, 1981
- 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
- Multiple forms of Acanthamoeba myosin I.Journal of Biological Chemistry, 1979
- Characterization of a second myosin from Acanthamoeba castellaniiJournal of Biological Chemistry, 1978
- Interaction between Acanthamoeba actin and rabbit skeletal muscle tropomyosin.Journal of Biological Chemistry, 1977