Phosphorylation of the 20,000-dalton light chain of smooth muscle myosin by the calcium-activated, phospholipid-dependent protein kinase. Phosphorylation sites and effects of phosphorylation.-Reference-Cited by-同舟云学术

Phosphorylation of the 20,000-dalton light chain of smooth muscle myosin by the calcium-activated, phospholipid-dependent protein kinase. Phosphorylation sites and effects of phosphorylation.

Published:1987-07 Issue:20 Volume:262 Page:9569-9573
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Ikebe M,Hartshorne D J,Elzinga M

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference26 articles.

1. Calcium and Cell Function;Walsh,1982

2. Identification, phosphorylation, and dephosphorylation of a second site for myosin light chain kinase on the 20,000-dalton light chain of smooth muscle myosin.

3. Phosphorylation of smooth muscle myosin at two distinct sites by myosin light chain kinase.

4. Linear relationship between diphosphorylation of 20 kDa light chain of gizzard myosin and the actin-activated myosin ATPase activity

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