M
Ming C. Gong
Researcher at University of Kentucky
Publications - 65
Citations - 3619
Ming C. Gong is an academic researcher from University of Kentucky. The author has contributed to research in topics: Vascular smooth muscle & Circadian rhythm. The author has an hindex of 33, co-authored 59 publications receiving 3323 citations. Previous affiliations of Ming C. Gong include University of Virginia & Southern Medical University.
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Journal ArticleDOI
Role of guanine nucleotide-binding proteins--ras-family or trimeric proteins or both--in Ca2+ sensitization of smooth muscle
Ming C. Gong,K. Iizuka,Graeme Nixon,J P Browne,A Hall,J F Eccleston,M Sugai,S Kobayashi,Avril V. Somlyo,Andrew P. Somlyo +9 more
TL;DR: It is concluded that p21rho may play a role in physiological Ca2+ sensitization as a cofactor with other messengers, rather than as a sole direct inhibitor of smooth muscle MLC20 phosphatase.
Journal ArticleDOI
Arachidonic acid inhibits myosin light chain phosphatase and sensitizes smooth muscle to calcium
Ming C. Gong,A. Fuglsang,Dario R. Alessi,S. Kobayashi,P. Cohen,Avril V. Somlyo,Andrew P. Somlyo +6 more
TL;DR: It is concluded that AA may act as a messenger-promoting protein phosphorylation through direct inhibition of the form of protein phosphatase(s) that dephosphorylate MLC20 in vivo.
Journal ArticleDOI
Translocation of rhoA Associated with Ca2+ Sensitization of Smooth Muscle
TL;DR: It is concluded that translocation of rhoA plays a causal role in Ca2+ sensitization, and membrane-boundrhoA can exist in two or more states and be a good substrate for in vitroADP-ribosylation.
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The effects of the Rho‐kinase inhibitor Y‐27632 on arachidonic acid‐, GTPγS‐, and phorbol ester‐induced Ca2+‐sensitization of smooth muscle
TL;DR: It is concluded that AA induces Ca2+‐sensitization through dual mechanisms, one mediated by Rho‐kinase (or a related kinase), and (ii) Rho'kinase is not required for phorbol ester‐induced Ca2‐s Sensitization.
Journal ArticleDOI
Myosin light chain phosphatase activities and the effects of phosphatase inhibitors in tonic and phasic smooth muscle.
Ming C. Gong,P. Cohen,Toshio Kitazawa,M. Ikebe,Masatoshi Masuo,Andrew P. Somlyo,Avril V. Somlyo +6 more
TL;DR: The results suggest that the HMMosphatases of smooth muscle have properties common to type 1 protein phosphatases, but are inhibited only partially by high concentrations of inhibitor-2, and that the lower HMM phosphatase activity of tonic smooth muscle may contribute to its greater sensitivity toosphatase inhibitors and its slower rate of relaxation.