The relationship between calmodulin binding and phosphorylation of smooth muscle myosin kinase by the catalytic subunit of 3‘:5‘ cAMP-dependent protein kinase.-Reference-Cited by-同舟云学术

The relationship between calmodulin binding and phosphorylation of smooth muscle myosin kinase by the catalytic subunit of 3‘:5‘ cAMP-dependent protein kinase.

Published:1981-04 Issue:7 Volume:256 Page:3178-3181
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Conti M.A.,Adelstein R.S.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference28 articles.

1. Dephosphorylation of the 20,000-dalton light chain of myosin by two different phosphatases from smooth muscle.

2. Roles of calcium and phosphorylation in the regulation of the activity of gizzard myosin

3. Regulation of the actin-myosin interaction in vertebrate smooth muscle: Activation via a myosin light-chain kinase and the effect of tropomyosin

4. Effect of phosphorylation of smooth muscle myosin on actin activation and Ca2+ regulation.

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