Cooperative binding of myosin subfragment-1 to the actin-troponin-tropomyosin complex.
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Coronin 1C harbours a second actin-binding site that confers co-operative binding to F-actinRegulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filamentCardiac thin filament regulationStructural dynamics of troponin I during Ca2+-activation of cardiac thin filaments: a multi-site Förster resonance energy transfer studyAltered cardiac troponin T in vitro function in the presence of a mutation implicated in familial hypertrophic cardiomyopathyRegulation of force development studied by photolysis of caged ADP in rabbit skinned psoas fibers.Functional consequence of mutation in rat cardiac troponin T is affected differently by myosin heavy chain isoformsTroponin T modulates sarcomere length-dependent recruitment of cross-bridges in cardiac muscle.Effects of a cardiomyopathy-causing troponin t mutation on thin filament function and structure.Force spectroscopy reveals multiple "closed states" of the muscle thin filament.Phosphorylation of tropomyosin extends cooperative binding of myosin beyond a single regulatory unitNonlinear force-length relationship in the ADP-induced contraction of skeletal myofibrils.Regulation of actin-myosin interaction by conserved periodic sites of tropomyosin.Striated muscle regulation of isometric tension by multiple equilibria.Single-myosin crossbridge interactions with actin filaments regulated by troponin-tropomyosin.Close proximity of myosin loop 3 to troponin determined by triangulation of resonance energy transfer distance measurements.Characterizations of cross-bridges in the presence of saturating concentrations of MgAMP-PNP in rabbit permeabilized psoas muscle.Kinetics of thin filament activation probed by fluorescence of N-((2-(iodoacetoxy)ethyl)-N-methyl)amino-7-nitrobenz-2-oxa-1,3-diazole-labeled troponin I incorporated into skinned fibers of rabbit psoas muscle: implications for regulation of muscle cEffect of Ca2+ on weak cross-bridge interaction with actin in the presence of adenosine 5'-[gamma-thio]triphosphate).A cellular automaton model for the regulatory behavior of muscle thin filaments.Cross-bridge scheme and force per cross-bridge state in skinned rabbit psoas muscle fibers.Calcium alone does not fully activate the thin filament for S1 binding to rigor myofibrils.The effect of partial extraction of troponin C on the elementary steps of the cross-bridge cycle in rabbit psoas muscle fibersInitiation of the power stroke in muscle: insights from the phosphate analog AlF4Effect of ionic strength on skinned rabbit psoas fibers in the presence of magnesium pyrophosphateThe effect of the lattice spacing change on cross-bridge kinetics in chemically skinned rabbit psoas muscle fibers. II. Elementary steps affected by the spacing change.Inhibition of actomyosin ATPase activity by troponin-tropomyosin without blocking the binding of myosin to actin.Two step mechanism of phosphate release and the mechanism of force generation in chemically skinned fibers of rabbit psoas muscleEffects of a non-divalent cation binding mutant of myosin regulatory light chain on tension generation in skinned skeletal muscle fibersParallel inhibition of active force and relaxed fiber stiffness by caldesmon fragments at physiological ionic strength and temperature conditions: additional evidence that weak cross-bridge binding to actin is an essential intermediate for force genTroponin-tropomyosin: an allosteric switch or a steric blocker?Spontaneous oscillatory contraction without regulatory proteins in actin filament-reconstituted fibers.The effect of thin filament activation on the attachment of weak binding cross-bridges: A two-dimensional x-ray diffraction study on single muscle fibers.Thin filament activation probed by fluorescence of N-((2-(iodoacetoxy)ethyl)-N-methyl)amino-7-nitrobenz-2-oxa-1,3-diazole-labeled troponin I incorporated into skinned fibers of rabbit psoas muscle.Cooperative regulation of myosin-actin interactions by a continuous flexible chain I: actin-tropomyosin systems.Ca2+ and ionic strength dependencies of S1-ADP binding to actin-tropomyosin-troponin: regulatory implications.Theoretical models for cooperative steady-state ATPase activity of myosin subfragment-1 on regulated actin.Effects of the state of the succinimido-ring on the fluorescence and structural properties of pyrene maleimide-labeled alpha alpha-tropomyosin.Ca2+-sensitive cross-bridge dissociation in the presence of magnesium pyrophosphate in skinned rabbit psoas fibersKinetics of actin-myosin binding. I. An exactly soluble one-variable model.
P2860
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P2860
Cooperative binding of myosin subfragment-1 to the actin-troponin-tropomyosin complex.
description
1980 nî lūn-bûn
@nan
1980年の論文
@ja
1980年学术文章
@wuu
1980年学术文章
@zh-cn
1980年学术文章
@zh-hans
1980年学术文章
@zh-my
1980年学术文章
@zh-sg
1980年學術文章
@yue
1980年學術文章
@zh
1980年學術文章
@zh-hant
name
Cooperative binding of myosin subfragment-1 to the actin-troponin-tropomyosin complex.
@ast
Cooperative binding of myosin subfragment-1 to the actin-troponin-tropomyosin complex.
@en
type
label
Cooperative binding of myosin subfragment-1 to the actin-troponin-tropomyosin complex.
@ast
Cooperative binding of myosin subfragment-1 to the actin-troponin-tropomyosin complex.
@en
prefLabel
Cooperative binding of myosin subfragment-1 to the actin-troponin-tropomyosin complex.
@ast
Cooperative binding of myosin subfragment-1 to the actin-troponin-tropomyosin complex.
@en
P2860
P356
P1476
Cooperative binding of myosin subfragment-1 to the actin-troponin-tropomyosin complex.
@en
P2093
Eisenberg E
P2860
P304
P356
10.1073/PNAS.77.5.2616
P407
P577
1980-05-01T00:00:00Z