Modulation of cross-bridge affinity for MgGTP by Ca2+ in skinned fibers of rabbit psoas muscle. - Wikidata - awgldk - TriplyDB

Modulation of cross-bridge affinity for MgGTP by Ca2+ in skinned fibers of rabbit psoas muscle.

Modulation of cross-bridge affinity for MgGTP by Ca2+ in skinned fibers of rabbit psoas muscle.

http://www.wikidata.org/entity/Q33915461

about

Characterizations of cross-bridges in the presence of saturating concentrations of MgAMP-PNP in rabbit permeabilized psoas muscle.The M.ADP.Pi state is required for helical order in the thick filaments of skeletal muscle.

P2860

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P2860

Modulation of cross-bridge affinity for MgGTP by Ca2+ in skinned fibers of rabbit psoas muscle.

http://www.wikidata.org/entity/Q33915461

description

1997 nî lūn-bûn

@nan

1997 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

1997 թվականի մայիսին հրատարակված գիտական հոդված

@hy

1997年の論文

@ja

1997年学术文章

@wuu

1997年学术文章

@zh-cn

1997年学术文章

@zh-hans

1997年学术文章

@zh-my

1997年学术文章

@zh-sg

1997年學術文章

@yue

name

Modulation of cross-bridge aff ...... fibers of rabbit psoas muscle.

@ast

Modulation of cross-bridge aff ...... fibers of rabbit psoas muscle.

@en

type

label

Modulation of cross-bridge aff ...... fibers of rabbit psoas muscle.

@ast

Modulation of cross-bridge aff ...... fibers of rabbit psoas muscle.

@en

prefLabel

Modulation of cross-bridge aff ...... fibers of rabbit psoas muscle.

@ast

Modulation of cross-bridge aff ...... fibers of rabbit psoas muscle.

@en

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P1433

Biophysical Journal

P1476

Modulation of cross-bridge aff ...... fibers of rabbit psoas muscle.

@en

P2093

B Brenner

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J M Chalovich

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L C Yu

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S M Frisbie

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P2860

Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament

Relaxation of muscle fibers with adenosine 5'-[gamma-thio]triphosphate (ATP[gamma S]) and by laser photolysis of caged ATP[gamma S]: evidence for Ca2+-dependent affinity of rapidly detaching zero-force cross-bridges.

Effect of Ca2+ on weak cross-bridge interaction with actin in the presence of adenosine 5'-[gamma-thio]triphosphate).

Adenosine 5'-(gamma-thiotriphosphate): an ATP analog that should be used with caution in muscle contraction studies.

Inhibition of actomyosin ATPase activity by troponin-tropomyosin without blocking the binding of myosin to actin.

Mechanics of glycerinated muscle fibers using nonnucleoside triphosphate substrates.

Analysis of equatorial x-ray diffraction patterns from muscle fibers: factors that affect the intensities.

Parallel 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 gen

Theoretical models for cooperative steady-state ATPase activity of myosin subfragment-1 on regulated actin.

Structures of actomyosin crossbridges in relaxed and rigor muscle fibers.

P304

2255-2261

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P31

scholarly article

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10.1016/S0006-3495(97)78869-6

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5

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1997-05-01T00:00:00Z

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14088169

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9129828

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1184420

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