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- W2016538963 abstract "1) Myosin light chain kinases from smooth muscle and platelets can be phosphorylated by the catalytic subunit of cAMP-dependent protein kinase. 2) Phosphorylation of both kinases, in the absence of calmodulin, markedly decreases kinase activity. 3) The decrease in smooth muscle myosin kinase activity is due to a decreased affinity of the phosphorylated kinase for calmodulin. 4) Dephosphorylation of the smooth muscle kinase by a phosphatase isolated from smooth muscle restores the affinity of the kinase for calmodulin." @default.
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- W2016538963 date "1980-12-01" @default.
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- W2016538963 title "REGULATION OF MYOSIN LIGHT CHAIN KINASE BY REVERSIBLE PHOSPHORYLATION AND CALCIUM-CALMODULIN" @default.
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- W2016538963 doi "https://doi.org/10.1111/j.1749-6632.1980.tb29607.x" @default.
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