Direct observation of phosphate inhibiting the force-generating capacity of a miniensemble of Myosin molecules. - Wikidata - awgldk - TriplyDB

Direct observation of phosphate inhibiting the force-generating capacity of a miniensemble of Myosin molecules.

Direct observation of phosphate inhibiting the force-generating capacity of a miniensemble of Myosin molecules.

http://www.wikidata.org/entity/Q35051582

about

Direct measurements of the coordination of lever arm swing and the catalytic cycle in myosin V Sequence-dependent nanometer-scale conformational dynamics of individual RecBCD-DNA complexes Can inorganic phosphate explain sag during unfused tetanic contractions of skeletal muscle?Mechanisms of in vivo muscle fatigue in humans: investigating age-related fatigue resistance with a computational model.Phosphate and ADP differently inhibit coordinated smooth muscle myosin groups.The molecular basis of thin filament activation: from single molecule to muscle Inherent force-dependent properties of β-cardiac myosin contribute to the force-velocity relationship of cardiac muscle.Muscle activation described with a differential equation model for large ensembles of locally coupled molecular motors.Modulators of actin-myosin dissociation: basis for muscle type functional differences during fatigue.Do Actomyosin Single-Molecule Mechanics Data Predict Mechanics of Contracting Muscle?

P2860

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P2860

Direct observation of phosphate inhibiting the force-generating capacity of a miniensemble of Myosin molecules.

http://www.wikidata.org/entity/Q35051582

description

2013 nî lūn-bûn

@nan

2013 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年论文

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name

Direct observation of phosphat ...... iensemble of Myosin molecules.

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Direct observation of phosphat ...... iensemble of Myosin molecules.

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type

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Direct observation of phosphat ...... iensemble of Myosin molecules.

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Direct observation of phosphat ...... iensemble of Myosin molecules.

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Direct observation of phosphat ...... iensemble of Myosin molecules.

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Direct observation of phosphat ...... iensemble of Myosin molecules.

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P356

J.BPJ.2013.09.046

P1433

Biophysical Journal

P1476

Direct observation of phosphat ...... iensemble of Myosin molecules.

@en

P2093

Edward P Debold

http://www.w3.org/2001/XMLSchema#string

Matthew A Turner

http://www.w3.org/2001/XMLSchema#string

Mike Woodward

http://www.w3.org/2001/XMLSchema#string

Sam Walcott

http://www.w3.org/2001/XMLSchema#string

P2860

X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4-

Three-dimensional structure of myosin subfragment-1: a molecular motor

Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: visualization of the pre-power stroke state

Mechanism of adenosine triphosphate hydrolysis by actomyosin

Models for the specific adhesion of cells to cells

Load and Pi control flux through the branched kinetic cycle of myosin V.

A mutant heterodimeric myosin with one inactive head generates maximal displacement.

Slip sliding away: load-dependence of velocity generated by skeletal muscle myosin molecules in the laser trap.

The biochemical kinetics underlying actin movement generated by one and many skeletal muscle myosin molecules

Versatile optical traps with feedback control.

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scholarly article

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10.1016/J.BPJ.2013.09.046

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2013-11-01T00:00:00Z

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