Calcium regulation of thin filament movement in an in vitro motility assay.
about
Human actin mutations associated with hypertrophic and dilated cardiomyopathies demonstrate distinct thin filament regulatory properties in vitroPhosphorylation or glutamic acid substitution at protein kinase C sites on cardiac troponin I differentially depress myofilament tension and shortening velocityStrong binding of myosin increases shortening velocity of rabbit skinned skeletal muscle fibres at low levels of Ca(2+)Regulation of force and unloaded sliding speed in single thin filaments: effects of regulatory proteins and calciumCardiac myosin missense mutations cause dilated cardiomyopathy in mouse models and depress molecular motor function.Effect of viscosity on mechanics of single, skinned fibers from rabbit psoas muscle.Viscosity and solute dependence of F-actin translocation by rabbit skeletal heavy meromyosin.Single-myosin crossbridge interactions with actin filaments regulated by troponin-tropomyosin.Dominant negative mutant actins identified in flightless Drosophila can be classified into three classes.Functional differences between the N-terminal domains of mouse and human myosin binding protein-C.Calcium regulation of skeletal muscle thin filament motility in vitro.Calmidazolium alters Ca2+ regulation of tension redevelopment rate in skinned skeletal muscleEffects of SH1 and SH2 modifications on myosin: similarities and differences.Influence of ADP on cross-bridge-dependent activation of myofibrillar thin filaments.Thin filament regulation and ionic interactions between the N-terminal region in actin and troponin.Regulatory proteins alter nucleotide binding to acto-myosin of sliding filaments in motility assaysCa2+ regulation of rabbit skeletal muscle thin filament sliding: role of cross-bridge number.Activation of the calcium-regulated thin filament by myosin strong bindingEffect of Ca2+ binding properties of troponin C on rate of skeletal muscle force redevelopment.Future challenges in single-molecule fluorescence and laser trap approaches to studies of molecular motors.Effects of troponin T cardiomyopathy mutations on the calcium sensitivity of the regulated thin filament and the actomyosin cross-bridge kinetics of human β-cardiac myosin.Interaction between troponin and myosin enhances contractile activity of myosin in cardiac muscle.Facilitated cross-bridge interactions with thin filaments by familial hypertrophic cardiomyopathy mutations in α-tropomyosin.Micromechanical thermal assays of Ca2+-regulated thin-filament function and modulation by hypertrophic cardiomyopathy mutants of human cardiac troponinCorrelation of molecular and functional effects of mutations in cardiac troponin T linked to familial hypertrophic cardiomyopathy: an integrative in silico/in vitro approachA correlative analysis of actin filament assembly, structure, and dynamics.Tropomyosin directly modulates actomyosin mechanical performance at the level of a single actin filamentAllosteric effects of cardiac troponin TNT1 mutations on actomyosin binding: a novel pathogenic mechanism for hypertrophic cardiomyopathy.Role of cardiac troponin I carboxy terminal mobile domain and linker sequence in regulating cardiac contraction.The functional significance of the last 5 residues of the C-terminus of cardiac troponin I.Effects of oral adenosine-5'-triphosphate supplementation on athletic performance, skeletal muscle hypertrophy and recovery in resistance-trained men.Nuclear tropomyosin and troponin in striated muscle: new roles in a new locale?Cooperativity of myosin interaction with thin filaments is enhanced by stabilizing substitutions in tropomyosin.Sample solution constraints on motor-driven diagnostic nanodevices.Thin filament cooperativity as a major determinant of shortening velocity in skeletal muscle fibers.Role of residues 311/312 in actin-tropomyosin interaction. In vitro motility study using yeast actin mutant e311a/r312a.Ca++-sensitizing mutations in troponin, P(i), and 2-deoxyATP alter the depressive effect of acidosis on regulated thin-filament velocity.Troponin I and troponin T interact with troponin C to produce different Ca2+-dependent effects on actin-tropomyosin filament motility.Stabilization of the Central Part of Tropomyosin Molecule Alters the Ca2+-sensitivity of Actin-Myosin Interaction.A simple method for measuring the relative force exerted by myosin on actin filaments in the in vitro motility assay: evidence that tropomyosin and troponin increase force in single thin filaments.
P2860
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P2860
Calcium regulation of thin filament movement in an in vitro motility assay.
description
1996 nî lūn-bûn
@nan
1996 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Calcium regulation of thin filament movement in an in vitro motility assay.
@ast
Calcium regulation of thin filament movement in an in vitro motility assay.
@en
Calcium regulation of thin filament movement in an in vitro motility assay.
@nl
type
label
Calcium regulation of thin filament movement in an in vitro motility assay.
@ast
Calcium regulation of thin filament movement in an in vitro motility assay.
@en
Calcium regulation of thin filament movement in an in vitro motility assay.
@nl
prefLabel
Calcium regulation of thin filament movement in an in vitro motility assay.
@ast
Calcium regulation of thin filament movement in an in vitro motility assay.
@en
Calcium regulation of thin filament movement in an in vitro motility assay.
@nl
P2093
P2860
P1433
P1476
Calcium regulation of thin filament movement in an in vitro motility assay.
@en
P2093
P2860
P304
P356
10.1016/S0006-3495(96)79753-9
P407
P577
1996-04-01T00:00:00Z