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pro vyhledávání: '"Sheila Reardon"'
Publikováno v:
Journal of Biological Chemistry. 274:30122-30126
Myosin regulatory light chain (RLC) is phosphorylated at various sites at its N-terminal region, and heterotrimeric myosin light chain phosphatase (MLCP) has been assigned as a physiological phosphatase that dephosphorylates myosin in vivo. Specifici
Publikováno v:
Proceedings of the National Academy of Sciences. 91:9096-9100
The segment of smooth muscle regulatory light chain essential for the phosphorylation dependent activation of actomyosin motor activity and the binding of myosin heavy chain was identified. The C-terminal domain of the 20-kDa light chain, which is le
Publikováno v:
The Journal of General Physiology
Mechanisms of Ca2+ sensitization of both myosin light chain (MLC) phosphorylation and force development by protein kinase C (PKC) were studied in permeabilized tonic smooth muscle obtained from the rabbit femoral artery. For comparison, the Ca2+ sens
Publikováno v:
Biochemistry. 29(51)
Previously, it was reported that smooth muscle caldesmon is a protein kinase and is autophosphorylated [Scott-Woo, G. C., & Walsh, M. P. (1988) Biochem. J. 252, 463-472]. We separated a Ca 2+ /calmodulin-dependent protein kinase from caldesmon in the
Autor:
Sheila Reardon, Mitsuo Ikebe
Publikováno v:
Biochemistry. 29(11)
Bovine platelet myosin is phosphorylated by protein kinase C at multiple sites. Most of the phosphate is incorporated in the 20,000-dalton light chain although some phosphate is incorporated in the heavy chain. Phosphorylation of the 20,000-dalton li
Publikováno v:
FEBS Letters. (2-3):245-248
Myosin light chain kinase (MLCK) contains the autoinhibitor sequence right next to the N-terminus side of the calmodulin binding region. In this paper, the structural requirement of the inhibition of MLCK activity was studied using synthetic peptide