Isometric force redevelopment of skinned muscle fibers from rabbit activated with and without Ca2+
about
Basal myosin light chain phosphorylation is a determinant of Ca2+ sensitivity of force and activation dependence of the kinetics of myocardial force developmentInfluence of length on force and activation-dependent changes in troponin c structure in skinned cardiac and fast skeletal muscle.Ablation of the cardiac-specific gene leucine-rich repeat containing 10 (Lrrc10) results in dilated cardiomyopathyPKA accelerates rate of force development in murine skinned myocardium expressing alpha- or beta-tropomyosinEffect of viscosity on mechanics of single, skinned fibers from rabbit psoas muscle.Sarcomere lattice geometry influences cooperative myosin binding in muscle.A new experimental model to study force depression: the Drosophila jump muscleMyosin regulatory light chain modulates the Ca2+ dependence of the kinetics of tension development in skeletal muscle fibers.Influence of Ca2+ on force redevelopment kinetics in skinned rat myocardiumCalmidazolium alters Ca2+ regulation of tension redevelopment rate in skinned skeletal muscleForce regulation by Ca2+ in skinned single cardiac myocytes of frogCalcium regulation of tension redevelopment kinetics with 2-deoxy-ATP or low [ATP] in rabbit skeletal muscle.The effect of ATP analogs on posthydrolytic and force development steps in skinned skeletal muscle fibers.Ca2+ and cross-bridge-induced changes in troponin C in skinned skeletal muscle fibers: effects of force inhibition.Regulation of skeletal muscle tension redevelopment by troponin C constructs with different Ca2+ affinities.Ca2+ regulation of rabbit skeletal muscle thin filament sliding: role of cross-bridge number.Cross-bridge versus thin filament contributions to the level and rate of force development in cardiac muscle.Contractile properties of muscle fibers from the deep and superficial digital flexors of horses.Effect of Ca2+ binding properties of troponin C on rate of skeletal muscle force redevelopment.Tension recovery in permeabilized rat soleus muscle fibers after rapid shortening and restretch.Frequency dependence of power and its implications for contractile function of muscle fibers from the digital flexors of horses.Positive inotropic effects of low dATP/ATP ratios on mechanics and kinetics of porcine cardiac muscleSlowed Dynamics of Thin Filament Regulatory Units Reduces Ca(2+)-Sensitivity of Cardiac Biomechanical Function.A re-interpretation of the rate of tension redevelopment (k(TR)) in active muscle.Relaxation kinetics following sudden Ca(2+) reduction in single myofibrils from skeletal muscle.Cardiac length dependence of force and force redevelopment kinetics with altered cross-bridge cycling.Tropomyosin flexural rigidity and single ca(2+) regulatory unit dynamics: implications for cooperative regulation of cardiac muscle contraction and cardiomyocyte hypertrophy.Altered Right Ventricular Mechanical Properties Are Afterload Dependent in a Rodent Model of Bronchopulmonary Dysplasia.Contractile effects of the exchange of cardiac troponin for fast skeletal troponin in rabbit psoas single myofibrils.Modulation of contractile activation in skeletal muscle by a calcium-insensitive troponin C mutant.cTnT1, a cardiac troponin T isoform, decreases myofilament tension and affects the left ventricular pressure waveform.Kinetics of muscle contraction and actomyosin NTP hydrolysis from rabbit using a series of metal-nucleotide substrates.Modulation of Skeletal Muscle Contraction by Myosin Phosphorylation.Kinetics of force recovery following length changes in active skinned single fibres from rabbit psoas muscle: analysis and modelling of the late recovery phase.Thin-filament regulation of force redevelopment kinetics in rabbit skeletal muscle fibres.Nitric oxide impairs Ca2+ activation and slows cross-bridge cycling kinetics in skeletal muscle.Contractile responses of the rat gastrocnemius and soleus muscles to isotonic resistance exercise.Role of calcium and cross bridges in determining rate of force development in frog muscle fibers.Differential roles of regulatory light chain and myosin binding protein-C phosphorylations in the modulation of cardiac force development.
P2860
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P2860
Isometric force redevelopment of skinned muscle fibers from rabbit activated with and without Ca2+
description
1994 nî lūn-bûn
@nan
1994 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Isometric force redevelopment ...... ctivated with and without Ca2+
@ast
Isometric force redevelopment ...... ctivated with and without Ca2+
@en
Isometric force redevelopment ...... ctivated with and without Ca2+
@nl
type
label
Isometric force redevelopment ...... ctivated with and without Ca2+
@ast
Isometric force redevelopment ...... ctivated with and without Ca2+
@en
Isometric force redevelopment ...... ctivated with and without Ca2+
@nl
prefLabel
Isometric force redevelopment ...... ctivated with and without Ca2+
@ast
Isometric force redevelopment ...... ctivated with and without Ca2+
@en
Isometric force redevelopment ...... ctivated with and without Ca2+
@nl
P2860
P1433
P1476
Isometric force redevelopment ...... ctivated with and without Ca2+
@en
P2093
D A Martyn
J D Hannon
P2860
P304
P356
10.1016/S0006-3495(94)80682-4
P407
P577
1994-11-01T00:00:00Z