Orientational changes of crossbridges during single turnover of ATP. - Wikidata - awgldk - TriplyDB

Orientational changes of crossbridges during single turnover of ATP.

Orientational changes of crossbridges during single turnover of ATP.

http://www.wikidata.org/entity/Q30909803

about

Fluorescence polarization/anisotropy in diagnostics and imaging Changes in orientation of actin during contraction of muscle Rotation of the lever arm of Myosin in contracting skeletal muscle fiber measured by two-photon anisotropy.Application of surface plasmon coupled emission to study of muscle

P2860

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P2860

Orientational changes of crossbridges during single turnover of ATP.

http://www.wikidata.org/entity/Q30909803

description

2003 nî lūn-bûn

@nan

2003 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2003年の論文

@ja

2003年論文

@yue

2003年論文

@zh-hant

2003年論文

@zh-hk

2003年論文

@zh-mo

2003年論文

@zh-tw

2003年论文

@wuu

name

Orientational changes of crossbridges during single turnover of ATP.

@ast

Orientational changes of crossbridges during single turnover of ATP.

@en

type

label

Orientational changes of crossbridges during single turnover of ATP.

@ast

Orientational changes of crossbridges during single turnover of ATP.

@en

prefLabel

Orientational changes of crossbridges during single turnover of ATP.

@ast

Orientational changes of crossbridges during single turnover of ATP.

@en

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S0006-3495(03)75049-8

P1433

Biophysical Journal

P1476

Orientational changes of crossbridges during single turnover of ATP.

@en

P2093

Akopova I

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

Borejdo J

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

P2860

Atomic structure of scallop myosin subfragment S1 complexed with MgADP: a novel conformation of the myosin head

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

The light chain binding domain of expressed smooth muscle heavy meromyosin acts as a mechanical lever.

Regulatory and essential light chains of myosin rotate equally during contraction of skeletal muscle.

Function of the N terminus of the myosin essential light chain of vertebrate striated muscle.

Steady-state fluorescence polarization studies of the orientation of myosin regulatory light chains in single skeletal muscle fibers using pure isomers of iodoacetamidotetramethylrhodamine.

Carbocyanine dye orientation in red cell membrane studied by microscopic fluorescence polarization.

Some self-consistent two-state sliding filament models of muscle contraction.

Computer simulation of movement-generating cross-bridges.

P304

2450-2459

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scholarly article

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10.1016/S0006-3495(03)75049-8

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4

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84

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2003-04-01T00:00:00Z

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12668452

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1302810

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