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Effect of low pH on single skeletal muscle myosin mechanics and kineticsPhosphorylation of cardiac troponin I at protein kinase C site threonine 144 depresses cooperative activation of thin filaments.Mechanism of regulation of native cardiac muscle thin filaments by rigor cardiac myosin-S1 and calciumAltered cross-bridge properties in skeletal muscle dystrophiesDirect observation of phosphate inhibiting the force-generating capacity of a miniensemble of Myosin molecules.Mechanical coupling between myosin molecules causes differences between ensemble and single-molecule measurements.A strain-dependency of Myosin off-rate must be sensitive to frequency to predict the B-process of sinusoidal analysis.Maximal activation of skeletal muscle thin filaments requires both rigor myosin S1 and calcium.
P2860
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P2860
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
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scientific article published on 23 August 2004
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Repriming the actomyosin crossbridge cycle.
@en
Repriming the actomyosin crossbridge cycle.
@nl
type
label
Repriming the actomyosin crossbridge cycle.
@en
Repriming the actomyosin crossbridge cycle.
@nl
prefLabel
Repriming the actomyosin crossbridge cycle.
@en
Repriming the actomyosin crossbridge cycle.
@nl
P2860
P356
P1476
Repriming the actomyosin crossbridge cycle.
@en
P2093
John Sleep
Walter Steffen
P2860
P304
12904-12909
P356
10.1073/PNAS.0400227101
P407
P577
2004-08-23T00:00:00Z