Structural changes in the actin-myosin cross-bridges associated with force generation induced by temperature jump in permeabilized frog muscle fibers
about
Electron tomography of cryofixed, isometrically contracting insect flight muscle reveals novel actin-myosin interactionsPolarized fluorescence depletion reports orientation distribution and rotational dynamics of muscle cross-bridges.Changes in myosin S1 orientation and force induced by a temperature increase.Structural responses to the photolytic release of ATP in frog muscle fibres, observed by time-resolved X-ray diffraction.ATP consumption and efficiency of human single muscle fibers with different myosin isoform compositionEndothermic force generation, temperature-jump experiments and effects of increased [MgADP] in rabbit psoas muscle fibres.Mechanics and models of the myosin motorMyosin heads contribute to the maintenance of filament order in relaxed rabbit muscleStructural characterization of weakly attached cross-bridges in the A*M*ATP state in permeabilized rabbit psoas muscle.Structural features of cross-bridges in isometrically contracting skeletal muscle.Kinetic effects of fiber type on the two subcomponents of the Huxley-Simmons phase 2 in muscle.Evidence for pre- and post-power stroke of cross-bridges of contracting skeletal myofibrils.The spatial distribution of actin and mechanical cycle of myosin are different in right and left ventricles of healthy mouse heartsCoupling between phosphate release and force generation in muscle actomyosin.Effect of a myosin regulatory light chain mutation K104E on actin-myosin interactions.Temperature effect on the chemomechanical regulation of substeps within the power stroke of a single Myosin II.Comparison of orientation and rotational motion of skeletal muscle cross-bridges containing phosphorylated and dephosphorylated myosin regulatory light chain.Direct modeling of X-ray diffraction pattern from contracting skeletal muscle.Phosphorylation of myosin regulatory light chain has minimal effect on kinetics and distribution of orientations of cross bridges of rabbit skeletal muscle.Mesoscopic analysis of motion and conformation of cross-bridges.The endothermic ATP hydrolysis and crossbridge attachment steps drive the increase of force with temperature in isometric and shortening muscle.Myosin cross-bridges do not form precise rigor bonds in hypertrophic heart muscle carrying troponin T mutations.Orientation of the myosin light chain region by single molecule total internal reflection fluorescence polarization microscopy.No Difference in Myosin Kinetics and Spatial Distribution of the Lever Arm in the Left and Right Ventricles of Human HeartsMyosin light chain phosphorylation inhibits muscle fiber shortening velocity in the presence of vanadate.The force-generation process in active muscle is strain sensitive and endothermic: a temperature-perturbation study.The structural basis of the increase in isometric force production with temperature in frog skeletal muscle
P2860
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P2860
Structural changes in the actin-myosin cross-bridges associated with force generation induced by temperature jump in permeabilized frog muscle fibers
description
1999 nî lūn-bûn
@nan
1999 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Structural changes in the acti ...... rmeabilized frog muscle fibers
@ast
Structural changes in the acti ...... rmeabilized frog muscle fibers
@en
Structural changes in the acti ...... rmeabilized frog muscle fibers
@nl
type
label
Structural changes in the acti ...... rmeabilized frog muscle fibers
@ast
Structural changes in the acti ...... rmeabilized frog muscle fibers
@en
Structural changes in the acti ...... rmeabilized frog muscle fibers
@nl
prefLabel
Structural changes in the acti ...... rmeabilized frog muscle fibers
@ast
Structural changes in the acti ...... rmeabilized frog muscle fibers
@en
Structural changes in the acti ...... rmeabilized frog muscle fibers
@nl
P2093
P2860
P1433
P1476
Structural changes in the acti ...... rmeabilized frog muscle fibers
@en
P2093
A K Tsaturyan
M A Ferenczi
S Y Bershitsky
P2860
P304
P356
10.1016/S0006-3495(99)76895-5
P407
P577
1999-07-01T00:00:00Z