Localization of the three phosphorylation sites on each heavy chain of Acanthamoeba myosin II to a segment at the end of the tail.
Open Access
- 1 April 1982
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 257 (8) , 4529-4534
- https://doi.org/10.1016/s0021-9258(18)34755-0
Abstract
No abstract availableThis publication has 14 references indexed in Scilit:
- Identification of three phosphorylation sites on each heavy chain of Acanthamoeba myosin II.Journal of Biological Chemistry, 1981
- Dictyostelium myosin: characterization of chymotryptic fragments and localization of the heavy-chain phosphorylation site.The Journal of cell biology, 1981
- Purification and characterization of actin-activatable, Ca2+-sensitive myosin II from Acanthamoeba.Journal of Biological Chemistry, 1981
- Direct photoaffinity labeling by nucleotides of the apparent catalytic site on the heavy chains of smooth muscle and Acanthamoeba myosins.Journal of Biological Chemistry, 1981
- Regulation of myosin self-assembly: phosphorylation of Dictyostelium heavy chain inhibits formation of thick filaments.Proceedings of the National Academy of Sciences, 1980
- Dissociation of the actin.subfragment 1 complex by adenyl-5'-yl imidodiphosphate, ADP, and PPi.Journal of Biological Chemistry, 1980
- Characterization of a second myosin from Acanthamoeba castellaniiJournal of Biological Chemistry, 1978
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Electrophoretic analysis of the major polypeptides of the human erythrocyte membraneBiochemistry, 1971
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970