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- W2014956239 abstract "The primary signal for smooth-muscle contraction is an increase in sarcoplasmic free Ca2+ concentration ([Ca2+]i). This triggers activation of calmodulin-dependent myosin light-chain kinase, which catalyses myosin phosphorylation, thereby activating crossbridge cycling and the development of force or contraction of the muscle cell. Restoration of resting [Ca2+]i deactivates the kinase; myosin is dephosphorylated by myosin light-chain phosphatase and the muscle relaxes. Recent evidence suggests that other signal-transduction pathways can modulate the contractile state of a smooth-muscle cell by affecting specific steps in the myosin phosphorylation-dephosphorylation mechanism." @default.
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- W2014956239 date "1994-09-01" @default.
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- W2014956239 title "The biochemical basis of the regulation of smooth-muscle contraction" @default.
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- W2014956239 doi "https://doi.org/10.1016/0968-0004(94)90112-0" @default.
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