The relationship between calmodulin binding and phosphorylation of smooth muscle myosin kinase by the catalytic subunit of 3‘:5‘ cAMP-dependent protein kinase.
Open Access
- 1 April 1981
- journal article
- abstracts
- Published by Elsevier
- Vol. 256 (7) , 3178-3181
- https://doi.org/10.1016/s0021-9258(19)69586-4
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- Activation of skeletal muscle myosin light chain kinase by calcium(2+) and calmodulinBiochemistry, 1980
- A Ca2+- and modulator-dependent myosin light chain kinase from non-muscle cellsBiochemical and Biophysical Research Communications, 1978
- Roles of calcium and phosphorylation in the regulation of the activity of gizzard myosinBiochemistry, 1978
- Modulator protein as a component of the myosin light chain kinase from chicken gizzardBiochemistry, 1978
- Myoblast myosin phosphorylation is a prerequisite for actin-activationNature, 1977
- Regulation of the actin-myosin interaction in vertebrate smooth muscle: Activation via a myosin light-chain kinase and the effect of tropomyosinJournal of Molecular Biology, 1977
- Conformational transition accompanying the binding of calcium(2+) ion to the protein activator of 3',5'-cyclic adenosine monophosphate phosphodiesteraseBiochemistry, 1977
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Phosphorylation of platelet myosin increases actin-activated myosin ATPase activityNature, 1975
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970