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Purified rabbit brain protein kinase C relaxes skinned vascular smooth muscle and phosphorylates myosin light chain

Data up to Jan 2025

Published1987
Citations58
References22

Total Citations Per Year

Abstract

References (22)

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1983 • 174 citations

Phosphorylation of smooth muscle myosin light chain kinase by protein kinase C. Comparative study of the phosphorylated sites.

1985 • 145 citations

Serotonin secretion from human platelets may be modified by Ca2+-activated, phospholipid-dependent myosin phosphorylation.

1984 • 143 citations

Phosphorylation of smooth muscle myosin light chain kinase by Ca2+-activated, phospholipid-dependent protein kinase.

1985 • 128 citations

N-(2-Aminoethyl)-5-isoquinolinesulfonamide, a newly synthesized protein kinase inhibitor, functions as a ligand in affinity chromatography. Purification of Ca2+-activated, phospholipid-dependent and other protein kinases.

1985 • 122 citations

Calcium-independent myosin light chain kinase of smooth muscle. Preparation by limited chymotryptic digestion of the calcium ion dependent enzyme, purification and characterization

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Extraterrestrial platinum group nuggets in deep-sea sediments

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Tension responses of chemically skinned fibre bundles of the guinea‐pig taenia caeci under varied ionic environments

1981 • 96 citations

Phosphorylation-dependent activated tension in skinned gizzard muscle fibers in the absence of Ca2+.

1982 • 91 citations

Phorbol ester contracts rabbit thoracic aorta by increasing intracellular calcium and by activating calcium influx

1986 • 91 citations

Ca2+-phospholipid dependent phosphorylation of smooth muscle myosin

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Purified rabbit brain protein kinase C relaxes skinned vascular smooth muscle and… (1987) – Archives of Biochemistry and Biophysics | Metascience Observatory Explorer