Behavior of N-phenylmaleimide-reacted muscle fibers in magnesium-free rigor solution (Q34167303)

31 July 2017

title

Behavior of N-phenylmaleimide-reacted muscle fibers in magnesium-free rigor solution (English)

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31 July 2017

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Xu S

1

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31 July 2017

Yu LC

series ordinal

2

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31 July 2017

Schoenberg M

series ordinal

3

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31 July 2017

language of work or name

English

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publication date

1 March 1998

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31 July 2017

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31 July 2017

volume

74

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31 July 2017

issue

3

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31 July 2017

page(s)

1110-1114

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Graphical evaluation of alkylation of myosin's SH1 and SH2: the N-phenylmaleimide reaction

31 July 2017

cites work

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5 July 2018

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5 July 2018

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5 July 2018

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Characterization of the myosin adenosine triphosphate (M.ATP) crossbridge in rabbit and frog skeletal muscle fibers

5 July 2018

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Catalytic cooperativity induced by sulfhydryl1-labeling of myosin filaments

5 July 2018

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Formation of ATP-insensitive weakly-binding crossbridges in single rabbit psoas fibers by treatment with phenylmaleimide or para-phenylenedimaleimide

5 July 2018

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All myosin heads form bonds with actin in rigor rabbit skeletal muscle

5 July 2018

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The effect of myosin sulphydryl modification on the mechanics of fibre contraction

7 January 2021

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The site and stoichiometry of the N-phenylmaleimide reaction with myosin when weakly-binding crossbridges are formed in skinned rabbit psoas fibers

7 January 2021

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Effect of nucleotide on the binding of N,N'-p-phenylenedimaleimide-modified S-1 to unregulated and regulated actin

7 January 2021

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Flexibility of the myosin heavy chain: direct evidence that the region containing SH1 and SH2 can move 10 A under the influence of nucleotide binding

7 January 2021

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X-ray diffraction studies of cross-bridges weakly bound to actin in relaxed skinned fibers of rabbit psoas muscle

7 January 2021

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Sulfhydryl groups involved in the active site of myosin A adenosine triphosphatase. I. Specific blocking of the SH group responsible for the inhibitory phase in "B phasic response" of the catalytic activity

7 January 2021

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Studies on the role of sulfhydryls in the myosin ATPase. Characterization of the site of modification by the bifunctional sulfhydryl reagent p-N,N'-phenylenedimaleimide

7 January 2021

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12 December 2020

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A structural role for the Ca2+-Mg2+ sites on troponin C in the regulation of muscle contraction. Preparation and properties of troponin C depleted myofibrils

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Evidence for cooperative interactions of myosin heads with thin filament in the force generation of vertebrate skeletal muscle fibers

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Identifiers

DOI

10.1016/S0006-3495(98)77829-4

1 reference

31 July 2017

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31 July 2017

1 reference