about
X-ray structures of the Dictyostelium discoideum myosin motor domain with six non-nucleotide analogsCrystallographic findings on the internally uncoupled and near-rigor states of myosin: further insights into the mechanics of the motor.The myosin power strokeThe structural basis of the myosin ATPase activityEffects of sarcomere length and temperature on the rate of ATP utilisation by rabbit psoas muscle fibresStructural changes in muscle crossbridges accompanying force generation.The biochemical kinetics underlying actin movement generated by one and many skeletal muscle myosin moleculesATP consumption and efficiency of human single muscle fibers with different myosin isoform compositionATPase and shortening rates in frog fast skeletal myofibrils by time-resolved measurements of protein-bound and free Pi.Kinetics of force generation and phosphate release in skinned rabbit soleus muscle fibers.Spontaneous oscillation of tension and sarcomere length in skeletal myofibrils. Microscopic measurement and analysisA metabolite-sensitive, thermodynamically constrained model of cardiac cross-bridge cycling: implications for force development during ischemia.Relaxation of muscle fibers with adenosine 5'-[gamma-thio]triphosphate (ATP[gamma S]) and by laser photolysis of caged ATP[gamma S]: evidence for Ca2+-dependent affinity of rapidly detaching zero-force cross-bridges.Indirect coupling of phosphate release to de novo tension generation during muscle contraction.Measurement of nucleotide release kinetics in single skeletal muscle myofibrils during isometric and isovelocity contractions using fluorescence microscopyIn vitro actin filament sliding velocities produced by mixtures of different types of myosin.Nucleotide-dependent contractile properties of Ca(2+)-activated fast and slow skeletal muscle fibers.Effects of phosphate and ADP on shortening velocity during maximal and submaximal calcium activation of the thin filament in skeletal muscle fibers.Flash and smash: rapid freezing of muscle fibers activated by photolysis of caged ATP.Mechanical characterization of skeletal muscle myofibrils.Sliding distance per ATP molecule hydrolyzed by myosin heads during isotonic shortening of skinned muscle fibersRelaxation from rigor of skinned trabeculae of the guinea pig induced by laser photolysis of caged ATP.Two step mechanism of phosphate release and the mechanism of force generation in chemically skinned fibers of rabbit psoas muscleMuscle cross-bridges bound to actin are disordered in the presence of 2,3-butanedione monoxime.Characterization of single actomyosin rigor bonds: load dependence of lifetime and mechanical properties.Multiple structures of thick filaments in resting cardiac muscle and their influence on cross-bridge interactions.At physiological temperatures the ATPase rates of shortening soleus and psoas myofibrils are similar.Cross-bridge number, position, and angle in target zones of cryofixed isometrically active insect flight muscle.The force exerted by a muscle cross-bridge depends directly on the strength of the actomyosin bond.Heat changes during transient tension responses to small releases in active frog muscleRole of MgATP and MgADP in the cross-bridge kinetics in chemically skinned rabbit psoas fibers. Study of a fast exponential process (C)Force generation in single conventional actomyosin complexes under high dynamic loadKinetics of force generation by single kinesin molecules activated by laser photolysis of caged ATP.Regulation of binding of subfragment 1 in isolated rigor myofibrils.Cross-bridge kinetics, cooperativity, and negatively strained cross-bridges in vertebrate smooth muscle. A laser-flash photolysis study.Tension transients initiated by photogeneration of MgADP in skinned skeletal muscle fibersA one-headed class V myosin molecule develops multiple large (approximately 32-nm) steps successively.ATPase kinetics on activation of rabbit and frog permeabilized isometric muscle fibres: a real time phosphate assay.Temperature dependent measurements reveal similarities between muscle and non-muscle myosin motility.The dynamics of actin and myosin association and the crossbridge model of muscle contraction.
P2860
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P2860
description
1987 nî lūn-bûn
@nan
1987年の論文
@ja
1987年学术文章
@wuu
1987年学术文章
@zh-cn
1987年学术文章
@zh-hans
1987年学术文章
@zh-my
1987年学术文章
@zh-sg
1987年學術文章
@yue
1987年學術文章
@zh
1987年學術文章
@zh-hant
name
Kinetics of the actomyosin ATPase in muscle fibers.
@en
Kinetics of the actomyosin ATPase in muscle fibers.
@nl
type
label
Kinetics of the actomyosin ATPase in muscle fibers.
@en
Kinetics of the actomyosin ATPase in muscle fibers.
@nl
prefLabel
Kinetics of the actomyosin ATPase in muscle fibers.
@en
Kinetics of the actomyosin ATPase in muscle fibers.
@nl
P1476
Kinetics of the actomyosin ATPase in muscle fibers.
@en
P2093
Goldman YE
P304
P356
10.1146/ANNUREV.PH.49.030187.003225
P577
1987-01-01T00:00:00Z