Kinetic studies of the cooperative binding of subfragment 1 to regulated actin
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Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filamentAltered cardiac troponin T in vitro function in the presence of a mutation implicated in familial hypertrophic cardiomyopathyEffects of a cardiomyopathy-causing troponin t mutation on thin filament function and structure.Force spectroscopy reveals multiple "closed states" of the muscle thin filament.Regulation of actin-myosin interaction by conserved periodic sites of tropomyosin.Striated muscle regulation of isometric tension by multiple equilibria.Kinetics of cardiac thin-filament activation probed by fluorescence polarization of rhodamine-labeled troponin C in skinned guinea pig trabeculaeSingle-myosin crossbridge interactions with actin filaments regulated by troponin-tropomyosin.Kinetics of regulated actin transitions measured by probes on tropomyosin.Modulation of cross-bridge affinity for MgGTP by Ca2+ in skinned fibers of rabbit psoas muscle.Characterizations of cross-bridges in the presence of saturating concentrations of MgAMP-PNP in rabbit permeabilized psoas muscle.Kinetics of thin filament activation probed by fluorescence of N-((2-(iodoacetoxy)ethyl)-N-methyl)amino-7-nitrobenz-2-oxa-1,3-diazole-labeled troponin I incorporated into skinned fibers of rabbit psoas muscle: implications for regulation of muscle cTransient kinetics of the interaction of actin with myosin subfragment-1 in the absence of nucleotide.Calcium alone does not fully activate the thin filament for S1 binding to rigor myofibrils.Activation of skeletal S-1 ATPase activity by actin-tropomyosin-troponin. Effect of Ca++ on the fluorescence transient.Equilibrium muscle cross-bridge behavior. Theoretical considerations. II. Model describing the behavior of strongly-binding cross-bridges when both heads of myosin bind to the actin filament.Subsarcomeric distribution of calcium in demembranated fibers of rabbit psoas muscle.Inhibition of actomyosin ATPase activity by troponin-tropomyosin without blocking the binding of myosin to actin.Distinct molecular processes associated with isometric force generation and rapid tension recovery after quick release.Parallel inhibition of active force and relaxed fiber stiffness by caldesmon fragments at physiological ionic strength and temperature conditions: additional evidence that weak cross-bridge binding to actin is an essential intermediate for force genTroponin-tropomyosin: an allosteric switch or a steric blocker?Distributions of calcium in A and I bands of skinned vertebrate muscle fibers stretched to beyond filament overlapThin filament activation probed by fluorescence of N-((2-(iodoacetoxy)ethyl)-N-methyl)amino-7-nitrobenz-2-oxa-1,3-diazole-labeled troponin I incorporated into skinned fibers of rabbit psoas muscle.Ising model of cardiac thin filament activation with nearest-neighbor cooperative interactionsCooperative regulation of myosin-actin interactions by a continuous flexible chain I: actin-tropomyosin systems.Ca2+ and ionic strength dependencies of S1-ADP binding to actin-tropomyosin-troponin: regulatory implications.Theoretical models for cooperative steady-state ATPase activity of myosin subfragment-1 on regulated actin.Kinetics of actin-myosin binding. I. An exactly soluble one-variable model.Kinetics of actin-myosin binding. II. Two-variable model and actin gelation.A model of force production that explains the lag between crossbridge attachment and force after electrical stimulation of striated muscle fibersDual regulatory functions of the thin filament revealed by replacement of the troponin I inhibitory peptide with a linkerEffects of actin-myosin kinetics on the calcium sensitivity of regulated thin filaments.Kinetic model for the interaction of myosin subfragment 1 with regulated actin.Interaction between troponin and myosin enhances contractile activity of myosin in cardiac muscle.Understanding the cooperative interaction between myosin II and actin cross-linkers mediated by actin filaments during mechanosensationA Spatially Detailed Model of Isometric Contraction Based on Competitive Binding of Troponin I Explains Cooperative Interactions between Tropomyosin and Crossbridges.The Hill model for binding myosin S1 to regulated actin is not equivalent to the McKillop-Geeves modelThe C-terminus of troponin T is essential for maintaining the inactive state of regulated actinThe rates of Ca2+ dissociation and cross-bridge detachment from ventricular myofibrils as reported by a fluorescent cardiac troponin C.Regulation of binding of subfragment 1 in isolated rigor myofibrils.
P2860
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P2860
Kinetic studies of the cooperative binding of subfragment 1 to regulated actin
description
1980 nî lūn-bûn
@nan
1980年の論文
@ja
1980年学术文章
@wuu
1980年学术文章
@zh-cn
1980年学术文章
@zh-hans
1980年学术文章
@zh-my
1980年学术文章
@zh-sg
1980年學術文章
@yue
1980年學術文章
@zh
1980年學術文章
@zh-hant
name
Kinetic studies of the cooperative binding of subfragment 1 to regulated actin
@ast
Kinetic studies of the cooperative binding of subfragment 1 to regulated actin
@en
type
label
Kinetic studies of the cooperative binding of subfragment 1 to regulated actin
@ast
Kinetic studies of the cooperative binding of subfragment 1 to regulated actin
@en
prefLabel
Kinetic studies of the cooperative binding of subfragment 1 to regulated actin
@ast
Kinetic studies of the cooperative binding of subfragment 1 to regulated actin
@en
P2860
P356
P1476
Kinetic studies of the cooperative binding of subfragment 1 to regulated actin
@en
P2093
E W Taylor
K M Trybus
P2860
P304
P356
10.1073/PNAS.77.12.7209
P407
P577
1980-12-01T00:00:00Z