about
A novel pressure-jump apparatus for the microvolume analysis of protein-ligand and protein-protein interactions: its application to nucleotide binding to skeletal-muscle and smooth-muscle myosin subfragment-1Diffusion of myosin light chain kinase on actin: A mechanism to enhance myosin phosphorylation rates in smooth muscle.The kinesin-1 motor protein is regulated by a direct interaction of its head and tailBroad disorder and the allosteric mechanism of myosin II regulation by phosphorylation.Velocities of unloaded muscle filaments are not limited by drag forces imposed by myosin cross-bridges.The N-terminal lobes of both regulatory light chains interact with the tail domain in the 10 S-inhibited conformation of smooth muscle myosin.The kinetics underlying the velocity of smooth muscle myosin filament sliding on actin filaments in vitro.Two heads are required for phosphorylation-dependent regulation of smooth muscle myosin.Effects of actin-myosin kinetics on the calcium sensitivity of regulated thin filaments.Direct evidence for functional smooth muscle myosin II in the 10S self-inhibited monomeric conformation in airway smooth muscle cellsHSP20 phosphorylation and airway smooth muscle relaxation.Photochemical mapping of the active site of myosin.Modification of interface between regulatory and essential light chains hampers phosphorylation-dependent activation of smooth muscle myosinRole of the tail in the regulated state of myosin 2.Characterization of tightly associated smooth muscle myosin-myosin light-chain kinase-calmodulin complexes.Kinetic and motor functions mediated by distinct regions of the regulatory light chain of smooth muscle myosin.Regulatory and catalytic domain dynamics of smooth muscle myosin filaments.Kinetics of myosin light chain kinase activation of smooth muscle myosin in an in vitro model system.Biochemistry of smooth muscle myosin light chain kinase.Sucrose increases the activation energy barrier for actin-myosin strong binding.Synthesis and spectral characterization of sulfhydryl-reactive fluorescent probes.Myosin light chain kinase steady-state kinetics: comparison of smooth muscle myosin II and nonmuscle myosin IIB as substrates.Actin Sliding Velocities are Influenced by the Driving Forces of Actin-Myosin Binding.Phosphorylation-dependent regulation is absent in a nonmuscle heavy meromyosin construct with one complete head and one head lacking the motor domain.Photocleavage of myosin subfragment 1 by vanadate.2'-Deoxy-3'-O-(4-benzoylbenzoyl)- and 3'(2')-O-(4-benzoylbenzoyl)-1,N6-ethenoadenosine 5'-diphosphate, fluorescent photoaffinity analogues of adenosine 5'-diphosphate. Synthesis, characterization, and interaction with myosin subfragment 1.Direct chemical evidence that serine 180 in the glycine-rich loop of myosin binds to ATP.Both heads of tissue-derived smooth muscle heavy meromyosin bind to actin in the presence of ADP.Vanadate-mediated photocleavage of myosin.ADP release produces a rotation of the neck region of smooth myosin but not skeletal myosin.A mixed-kinetic model describes unloaded velocities of smooth, skeletal, and cardiac muscle myosin filaments in vitro.The myosin duty ratio tunes the calcium sensitivity and cooperative activation of the thin filament.Photoaffinity ADP analogs as covalently attached reporter groups of the active site of myosin subfragment 1.Kinetics of smooth muscle heavy meromyosin with one thiophosphorylated headUsing the SpyTag SpyCatcher system to label smooth muscle myosin II filaments with a quantum dot on the regulatory light chain
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description
biochemist
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wetenschapper
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name
Christine R Cremo
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Christine R Cremo
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Christine R Cremo
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Christine R Cremo
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Christine R Cremo
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Christine R Cremo
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Christine R Cremo
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Christine R Cremo
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Christine R Cremo
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Christine R Cremo
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Christine R Cremo
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Christine R Cremo
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Christine R Cremo
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Christine R Cremo
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Christine R Cremo
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Christine R Cremo
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Christine R Cremo
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Christine R Cremo
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P1153
7003820572
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P2381
P31
P496
0000-0001-5516-5222