Protein kinase C modulates in vitro phosphorylation of the smooth muscle heavy meromyosin by myosin light chain kinase.
Masakatsu Nishikawa(National Institutes of Health), Hisashi Hidaka(Kitasato University), Robert Adelstein(National Institutes of Health), James R. Sellers(National Heart Lung and Blood Institute)
Cited by 248
Related Papers
Inhibition of forskolin-induced neurite outgrowth and protein phosphorylation by a newly synthesized selective inhibitor of cyclic AMP-dependent protein kinase, N-[2-(p-bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide (H-89), of PC12D pheochromocytoma cells.
|Journal of Biological Chemistry|1990|1.5k
Mechanism of Blebbistatin Inhibition of Myosin II
|Journal of Biological Chemistry|2004|1k
KN-62, 1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenylpiperazi ne, a specific inhibitor of Ca2+/calmodulin-dependent protein kinase II.
|Journal of Biological Chemistry|1990|625
N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide, a calmodulin antagonist, inhibits cell proliferation.
|Proceedings of the National Academy of Sciences|1981|586
Selective inhibition of catalytic activity of smooth muscle myosin light chain kinase.
|Journal of Biological Chemistry|1987|513