Myofibrillar ATPase activity and mechanical performance of skinned fibres from rabbit psoas muscle (Q58088120)

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22 October 2019

title

Myofibrillar ATPase activity and mechanical performance of skinned fibres from rabbit psoas muscle (English)

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22 October 2019

2

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22 October 2019

author name string

E J Potma

series ordinal

1

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22 October 2019

J P Barends

series ordinal

3

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22 October 2019

G Elzinga

series ordinal

4

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22 October 2019

language of work or name

English

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publication date

1 January 1994

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22 October 2019

published in

Journal of Physiology

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22 October 2019

volume

474

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22 October 2019

issue

2

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22 October 2019

page(s)

303-317

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The effect of phosphate and calcium on force generation in glycerinated rabbit skeletal muscle fibers. A steady-state and transient kinetic study

22 October 2019

cites work

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Discrimination of Ca(2+)-ATPase activity of the sarcoplasmic reticulum from actomyosin-type ATPase activity of myofibrils in skinned mammalian skeletal muscle fibres: distinct effects of cyclopiazonic acid on the two ATPase activities.

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The apparent rate constant for the dissociation of force generating myosin crossbridges from actin decreases during Ca2+ activation of skinned muscle fibres

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Effect of Ca2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: implications for regulation of muscle contraction

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Force and stiffness in glycerinated rabbit psoas fibers. Effects of calcium and elevated phosphate

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The cross-bridge cycle in muscle. Mechanical, biochemical, and structural studies on single skinned rabbit psoas fibers to characterize cross-bridge kinetics in muscle for correlation with the actomyosin-ATPase in solution

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ADENOSINE TRIPHOSPHATE: CHANGES IN MUSCLES DOING NEGATIVE WORK

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Coupling of Movement of Cross-Bridges with ATP Splitting Studied in Terms of the Acceleration of the ATPase Activity of Glycerol-Treated Muscle Fibers on Applying Various Types of Repetitive Stretch-Release Cycles1

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Stable maintenance heat rate and contractile properties of different single muscle fibres from Xenopus laevis at 20 degrees C.

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