R403Q and L908V mutant beta-cardiac myosin from patients with familial hypertrophic cardiomyopathy exhibit enhanced mechanical performance at the single molecule level.
about
Understanding cardiomyopathy phenotypes based on the functional impact of mutations in the myosin motorEnsemble force changes that result from human cardiac myosin mutations and a small-molecule effectorVascular disease-causing mutation R258C in ACTA2 disrupts actin dynamics and interaction with myosinMolecular mechanics of mouse cardiac myosin isoformsThe molecular phenotype of human cardiac myosin associated with hypertrophic obstructive cardiomyopathyChanges in the chemical and dynamic properties of cardiac troponin T cause discrete cardiomyopathies in transgenic mice.Cardiac myosin missense mutations cause dilated cardiomyopathy in mouse models and depress molecular motor function.Insights into human beta-cardiac myosin function from single molecule and single cell studies.Sexually dimorphic myofilament function and cardiac troponin I phosphospecies distribution in hypertrophic cardiomyopathy miceUsing optics to measure biological forces and mechanics.The biochemical kinetics underlying actin movement generated by one and many skeletal muscle myosin moleculesThe unique properties of tonic smooth muscle emerge from intrinsic as well as intermolecular behaviors of Myosin molecules.The converter domain modulates kinetic properties of Drosophila myosin.Single-myosin crossbridge interactions with actin filaments regulated by troponin-tropomyosin.Functional studies of individual myosin molecules.Hypertrophic and dilated cardiomyopathy mutations differentially affect the molecular force generation of mouse alpha-cardiac myosin in the laser trap assay.The R403Q myosin mutation implicated in familial hypertrophic cardiomyopathy causes disorder at the actomyosin interfaceRescue of familial cardiomyopathies by modifications at the level of sarcomere and Ca2+ fluxes.β-Myosin heavy chain variant Val606Met causes very mild hypertrophic cardiomyopathy in mice, but exacerbates HCM phenotypes in mice carrying other HCM mutationsBiological, biochemical, and kinetic effects of mutations of the cardiomyopathy loop of Dictyostelium myosin II: importance of ALA400Molecular genetics and pathogenesis of 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.Unconventional processive mechanics of non-muscle myosin IIB.The extent of cardiac myosin binding protein-C phosphorylation modulates actomyosin function in a graded mannerNarrative review: harnessing molecular genetics for the diagnosis and management of hypertrophic cardiomyopathy.Suppression of muscle hypercontraction by mutations in the myosin heavy chain gene of Drosophila melanogaster.Positive inotropic effects of low dATP/ATP ratios on mechanics and kinetics of porcine cardiac muscleGenetics of inherited cardiomyopathy.Cell-intrinsic functional effects of the α-cardiac myosin Arg-403-Gln mutation in familial hypertrophic cardiomyopathy.Phosphorylation and calcium antagonistically tune myosin-binding protein C's structure and function.Functional effects of the hypertrophic cardiomyopathy R403Q mutation are different in an alpha- or beta-myosin heavy chain backboneHead-head and head-tail interaction: a general mechanism for switching off myosin II activity in cellsTransgenic mouse α- and β-cardiac myosins containing the R403Q mutation show isoform-dependent transient kinetic differencesGenetic basis of hypertrophic cardiomyopathy: from bench to the clinics.Liver Kinase B1 complex acts as a novel modifier of myofilament function and localizes to the Z-disk in cardiac myocytesSex dimorphisms of crossbridge cycling kinetics in transgenic hypertrophic cardiomyopathy miceRegulatory light chain mutations associated with cardiomyopathy affect myosin mechanics and kineticsMyosin-binding protein C displaces tropomyosin to activate cardiac thin filaments and governs their speed by an independent mechanism.To understand muscle you must take it apart.Increased myofilament Ca2+-sensitivity and arrhythmia susceptibility.
P2860
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P2860
R403Q and L908V mutant beta-cardiac myosin from patients with familial hypertrophic cardiomyopathy exhibit enhanced mechanical performance at the single molecule level.
description
2000 nî lūn-bûn
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2000 թուականի Յունուարին հրատարակուած գիտական յօդուած
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2000 թվականի հունվարին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
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2000年論文
@zh-hant
2000年論文
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2000年論文
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2000年論文
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2000年论文
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name
R403Q and L908V mutant beta-ca ...... at the single molecule level.
@ast
R403Q and L908V mutant beta-ca ...... at the single molecule level.
@en
type
label
R403Q and L908V mutant beta-ca ...... at the single molecule level.
@ast
R403Q and L908V mutant beta-ca ...... at the single molecule level.
@en
prefLabel
R403Q and L908V mutant beta-ca ...... at the single molecule level.
@ast
R403Q and L908V mutant beta-ca ...... at the single molecule level.
@en
P2093
P356
P1476
R403Q and L908V mutant beta-ca ...... at the single molecule level.
@en
P2093
Fananapazir L
Haeberle JR
Palmiter KA
Warshaw DM
P2888
P304
P356
10.1023/A:1005678905119
P577
2000-01-01T00:00:00Z
P6179
1032911269