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Chi-Ming Hai
Researcher at Brown University
Publications - 59
Citations - 2197
Chi-Ming Hai is an academic researcher from Brown University. The author has contributed to research in topics: Muscle contraction & Myosin. The author has an hindex of 23, co-authored 59 publications receiving 2138 citations. Previous affiliations of Chi-Ming Hai include University of Virginia & Austrian Academy of Sciences.
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Journal ArticleDOI
Cross-bridge phosphorylation and regulation of latch state in smooth muscle
Chi-Ming Hai,Richard A. Murphy +1 more
TL;DR: A minimum kinetic model for cross-bridge interactions with the thin filament in smooth muscle predicted a hyperbolic dependence of steady-state stress on myosin phosphorylation, which corresponded with the experimental observation of high values of stress with low levels of phosphate in intact tissues.
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Ca2+ Crossbridge Phosphorylation, and Contraction
Chi-Ming Hai,Richard A. Murphy +1 more
TL;DR: This review attempts to answer a specific question: Can Ca2+ -calmodulin dependent MLCK activa tion, per se, explain the steady-state and transient changes in crossbridge phosphorylation, isometric stress, and isotonic shortening velocity during smooth muscle contraction?
Journal ArticleDOI
Regulation of shortening velocity by cross-bridge phosphorylation in smooth muscle.
Chi-Ming Hai,Richard A. Murphy +1 more
TL;DR: A model that incorporates a dephosphorylated "latch bridge" to explain the mechanics and energetics of smooth muscle and predicts the latch state: stress maintenance with reduced phosphorylation, cross-bridge cycling rates, and ATP consumption is proposed.
Journal ArticleDOI
Conventional protein kinase C mediates phorbol-dibutyrate-induced cytoskeletal remodeling in a7r5 smooth muscle cells.
TL;DR: Findings suggest that conventional PKCs mediate PDBu-induced formation of dynamic podosome-like structures in A7r5 cells, and Rho-kinase is unlikely to be the underlying mechanism.
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F-actin disruption attenuates agonist-induced [Ca2+], myosin phosphorylation, and force in smooth muscle
TL;DR: The results suggest that actin filaments in smooth muscle cells are dynamic and may be an integral component of Ca2+ regulation and/or signal transduction in receptor-coupled mechanisms.