The molecular basis of frictional loads in the in vitro motility assay with applications to the study of the loaded mechanochemistry of molecular motors.
about
Ensemble force changes that result from human cardiac myosin mutations and a small-molecule effectorIn vivo myosin step-size from zebrafish skeletal muscleA subdomain interaction at the base of the lever allosterically tunes the mechanochemical mechanism of myosin 5aα-Actinin and fimbrin cooperate with myosin II to organize actomyosin bundles during contractile-ring assembly.Harmonic force spectroscopy measures load-dependent kinetics of individual human β-cardiac myosin moleculesN-Terminus of Cardiac Myosin Essential Light Chain Modulates Myosin Step-Size.Biophysical properties of human β-cardiac myosin with converter mutations that cause hypertrophic cardiomyopathy.Unique single molecule binding of cardiac myosin binding protein-C to actin and phosphorylation-dependent inhibition of actomyosin motility requires 17 amino acids of the motif domain.Cardiomyopathy-linked myosin regulatory light chain mutations disrupt myosin strain-dependent biochemistry.Use of fluorescent techniques to study the in vitro movement of myosinsRecent insights into muscle fatigue at the cross-bridge level.The extent of cardiac myosin binding protein-C phosphorylation modulates actomyosin function in a graded mannerA hearing loss-associated myo1c mutation (R156W) decreases the myosin duty ratio and force sensitivity.Calcium regulation of myosin-I tension sensingMolecular mechanics of cardiac myosin-binding protein C in native thick filaments.Myosin regulatory light chain phosphorylation enhances cardiac β-myosin in vitro motility under load.Molecular consequences of the R453C hypertrophic cardiomyopathy mutation on human β-cardiac myosin motor function.A re-interpretation of the rate of tension redevelopment (k(TR)) in active muscle.Hypertrophic and dilated cardiomyopathy: four decades of basic research on muscle lead to potential therapeutic approaches to these devastating genetic diseases.Biochemistry of smooth muscle myosin light chain kinase.In vitro actin motility velocity varies linearly with the number of myosin impellers.Small molecule-mediated refolding and activation of myosin motor function.Force-generating capacity of human myosin isoforms extracted from single muscle fibre segments.A mixed-kinetic model describes unloaded velocities of smooth, skeletal, and cardiac muscle myosin filaments in vitro.Robust mechanobiological behavior emerges in heterogeneous myosin systems.Single cardiac ventricular myosins are autonomous motors.Calcium increases titin N2A binding to F-actin and regulated thin filaments
P2860
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P2860
The molecular basis of frictional loads in the in vitro motility assay with applications to the study of the loaded mechanochemistry of molecular motors.
description
2010 nî lūn-bûn
@nan
2010 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年学术文章
@wuu
2010年学术文章
@zh-cn
2010年学术文章
@zh-hans
2010年学术文章
@zh-my
2010年学术文章
@zh-sg
2010年學術文章
@yue
name
The molecular basis of frictio ...... chemistry of molecular motors.
@ast
The molecular basis of frictio ...... chemistry of molecular motors.
@en
The molecular basis of frictio ...... chemistry of molecular motors.
@nl
type
label
The molecular basis of frictio ...... chemistry of molecular motors.
@ast
The molecular basis of frictio ...... chemistry of molecular motors.
@en
The molecular basis of frictio ...... chemistry of molecular motors.
@nl
prefLabel
The molecular basis of frictio ...... chemistry of molecular motors.
@ast
The molecular basis of frictio ...... chemistry of molecular motors.
@en
The molecular basis of frictio ...... chemistry of molecular motors.
@nl
P2860
P356
P1433
P1476
The molecular basis of frictio ...... chemistry of molecular motors.
@en
P2860
P304
P356
10.1002/CM.20441
P577
2010-05-01T00:00:00Z