Two step mechanism of phosphate release and the mechanism of force generation in chemically skinned fibers of rabbit psoas muscle
about
Poorly understood aspects of striated muscle contractionEffect of temperature on elementary steps of the cross-bridge cycle in rabbit soleus slow-twitch muscle fibresTemperature dependence of active tension in mammalian (rabbit psoas) muscle fibres: effect of inorganic phosphateEffects of substituting uridine triphosphate for ATP on the crossbridge cycle of rabbit muscleInterpreting cardiac muscle force-length dynamics using a novel functional modelKinetic differences at the single molecule level account for the functional diversity of rabbit cardiac myosin isoforms.Activation kinetics of skinned cardiac muscle by laser photolysis of nitrophenyl-EGTA.The biochemical kinetics underlying actin movement generated by one and many skeletal muscle myosin moleculesEndothermic force generation, temperature-jump experiments and effects of increased [MgADP] in rabbit psoas muscle fibres.Reconciling the working strokes of a single head of skeletal muscle myosin estimated from laser-trap experiments and crystal structures.Mechanism of tension generation in muscle: an analysis of the forward and reverse rate constants.Force generation examined by laser temperature-jumps in shortening and lengthening mammalian (rabbit psoas) muscle fibres.Phosphorylation of cMyBP-C affects contractile mechanisms in a site-specific mannerIndirect coupling of phosphate release to de novo tension generation during muscle contraction.Force generation and phosphate release steps in skinned rabbit soleus slow-twitch muscle fibers.Strain-dependent modulation of phosphate transients in rabbit skeletal muscle fibers.Phosphate release and force generation in cardiac myocytes investigated with caged phosphate and caged calciumKinetic and thermodynamic studies of the cross-bridge cycle in rabbit psoas muscle fibers.Cross-bridge scheme and force per cross-bridge state in skinned rabbit psoas muscle fibers.Effects of MgATP and MgADP on the cross-bridge kinetics of rabbit soleus slow-twitch muscle fibers.The effect of partial extraction of troponin C on the elementary steps of the cross-bridge cycle in rabbit psoas muscle fibersInitiation of the power stroke in muscle: insights from the phosphate analog AlF4The effect of the lattice spacing change on cross-bridge kinetics in chemically skinned rabbit psoas muscle fibers. II. Elementary steps affected by the spacing change.Force generation and temperature-jump and length-jump tension transients in muscle fibers.Does thin filament compliance diminish the cross-bridge kinetics? A study in rabbit psoas fibers.The ADP release step of the smooth muscle cross-bridge cycle is not directly associated with force generation.The smooth muscle cross-bridge cycle studied using sinusoidal length perturbations.Elementary steps of the cross-bridge cycle in bovine myocardium with and without regulatory proteins.The force exerted by a muscle cross-bridge depends directly on the strength of the actomyosin bond.Emerging complex pathways of the actomyosin powerstroke.Elementary steps of the cross-bridge cycle in fast-twitch fiber types from rabbit skeletal muscles.DCM-related tropomyosin mutants E40K/E54K over-inhibit the actomyosin interaction and lead to a decrease in the number of cycling cross-bridges.Cardiac myosin binding protein C phosphorylation affects cross-bridge cycle's elementary steps in a site-specific manner.Enhanced active cross-bridges during diastole: molecular pathogenesis of tropomyosin's HCM mutationsKinetics of cardiac myosin isoforms in mouse myocardium are affected differently by presence of myosin binding protein-CMeasuring myosin cross-bridge attachment time in activated muscle fibers using stochastic vs. sinusoidal length perturbation analysisThe role of tropomyosin isoforms and phosphorylation in force generation in thin-filament reconstituted bovine cardiac muscle fibres.Direct observation of phosphate inhibiting the force-generating capacity of a miniensemble of Myosin molecules.Temperature-dependence of isometric tension and cross-bridge kinetics of cardiac muscle fibers reconstituted with a tropomyosin internal deletion mutant.COOH-terminal truncation of flightin decreases myofilament lattice organization, cross-bridge binding, and power output in Drosophila indirect flight muscle.
P2860
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P2860
Two step mechanism of phosphate release and the mechanism of force generation in chemically skinned fibers of rabbit psoas muscle
description
1991 nî lūn-bûn
@nan
1991 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1991 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
name
Two step mechanism of phosphat ...... fibers of rabbit psoas muscle
@ast
Two step mechanism of phosphat ...... fibers of rabbit psoas muscle
@en
Two step mechanism of phosphat ...... fibers of rabbit psoas muscle
@nl
type
label
Two step mechanism of phosphat ...... fibers of rabbit psoas muscle
@ast
Two step mechanism of phosphat ...... fibers of rabbit psoas muscle
@en
Two step mechanism of phosphat ...... fibers of rabbit psoas muscle
@nl
prefLabel
Two step mechanism of phosphat ...... fibers of rabbit psoas muscle
@ast
Two step mechanism of phosphat ...... fibers of rabbit psoas muscle
@en
Two step mechanism of phosphat ...... fibers of rabbit psoas muscle
@nl
P2860
P1433
P1476
Two step mechanism of phosphat ...... fibers of rabbit psoas muscle
@en
P2093
H R Halvorson
P2860
P304
P356
10.1016/S0006-3495(91)82227-5
P407
P577
1991-02-01T00:00:00Z