Kinetic differences at the single molecule level account for the functional diversity of rabbit cardiac myosin isoforms.
about
Human actin mutations associated with hypertrophic and dilated cardiomyopathies demonstrate distinct thin filament regulatory properties in vitroSkeletal muscle myofilament adaptations to aging, disease, and disuse and their effects on whole muscle performance in older adult humansThe cell biology of disease: cellular mechanisms of cardiomyopathy.Molecular mechanics of mouse cardiac myosin isoformsThe myosin power strokeAltered cross-bridge characteristics following haemodynamic overload in rabbit hearts expressing V3 myosinMyosin V exhibits a high duty cycle and large unitary displacementInsights into human beta-cardiac myosin function from single molecule and single cell studies.The Qdot-labeled actin super-resolution motility assay measures low-duty cycle muscle myosin step size.N-Terminus of Cardiac Myosin Essential Light Chain Modulates Myosin Step-Size.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 compositionThe converter domain modulates kinetic properties of Drosophila myosin.Effect of low pH on single skeletal muscle myosin mechanics and kineticsAnalytical comparison of natural and pharmaceutical ventricular myosin activatorsTwo independent mechanical events in the interaction cycle of skeletal muscle myosin with actinRecent insights into muscle fatigue at the cross-bridge level.Kinetics of cardiac myosin isoforms in mouse myocardium are affected differently by presence of myosin binding protein-CMolecular determinants of force production in human skeletal muscle fibers: effects of myosin isoform expression and cross-sectional areaRoles for cardiac MyBP-C in maintaining myofilament lattice rigidity and prolonging myosin cross-bridge lifetime.Two-state model of acto-myosin attachment-detachment predicts C-process of sinusoidal analysisIdentification of functional differences between recombinant human α and β cardiac myosin motors.The rates of Ca2+ dissociation and cross-bridge detachment from ventricular myofibrils as reported by a fluorescent cardiac troponin C.Molecular effects of the myosin activator omecamtiv mecarbil on contractile properties of skinned myocardium lacking cardiac myosin binding protein-CCardiac myosin isoforms exhibit differential rates of MgADP release and MgATP binding detected by myocardial viscoelasticity.In vitro and in vivo single myosin step-sizes in striated muscleSize and speed of the working stroke of cardiac myosin in situ.Erratum to: Identification of functional differences between recombinant human α and β cardiac myosin motors.Myocardial short-range force responses increase with age in F344 ratsDetermination of rate constants for turnover of myosin isoforms in rat myocardium: implications for in vivo contractile kinetics.Effects of cardiac myosin isoform variation on myofilament function and crossbridge kinetics in transgenic rabbitsTri-modal regulation of cardiac muscle relaxation; intracellular calcium decline, thin filament deactivation, and cross-bridge cycling kinetics.Modeling the Actin.myosin ATPase Cross-Bridge Cycle for Skeletal and Cardiac Muscle Myosin Isoforms.In vitro actin motility velocity varies linearly with the number of myosin impellers.Myosin MgADP Release Rate Decreases as Sarcomere Length Increases in Skinned Rat Soleus Muscle Fibers.Ventricular myosin modifies in vitro step-size when phosphorylated.A strain-dependency of Myosin off-rate must be sensitive to frequency to predict the B-process of sinusoidal analysis.Actomyosin kinetics of pure fast and slow rat myosin isoforms studied by in vitro motility assay approach.Troponin I serines 43/45 and regulation of cardiac myofilament function.On mice, rabbits, and human heart failure.
P2860
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P2860
Kinetic differences at the single molecule level account for the functional diversity of rabbit cardiac myosin isoforms.
description
1999 nî lūn-bûn
@nan
1999 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Kinetic differences at the sin ...... abbit cardiac myosin isoforms.
@ast
Kinetic differences at the sin ...... abbit cardiac myosin isoforms.
@en
type
label
Kinetic differences at the sin ...... abbit cardiac myosin isoforms.
@ast
Kinetic differences at the sin ...... abbit cardiac myosin isoforms.
@en
prefLabel
Kinetic differences at the sin ...... abbit cardiac myosin isoforms.
@ast
Kinetic differences at the sin ...... abbit cardiac myosin isoforms.
@en
P2093
P2860
P1476
Kinetic differences at the sin ...... abbit cardiac myosin isoforms.
@en
P2093
D E Dupuis
D M Warshaw
K A Palmiter
N R Alpert
P2860
P304
P356
10.1111/J.1469-7793.1999.0669N.X
P407
P478
P577
1999-09-01T00:00:00Z