Calcium-binding protein, parvalbumin, is reduced in mutant mammalian muscle with abnormal contractile properties. - Wikidata - wikimedia - TriplyDB

Calcium-binding protein, parvalbumin, is reduced in mutant mammalian muscle with abnormal contractile properties.

Calcium-binding protein, parvalbumin, is reduced in mutant mammalian muscle with abnormal contractile properties.

http://www.wikidata.org/entity/Q37561384

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Control of IP(3)-mediated Ca2+ puffs in Xenopus laevis oocytes by the Ca2+-binding protein parvalbumin Developmental control of the excitability of muscle: transplantation experiments on a myotonic mouse mutant Fatigue-inducing stimulation resolves myotonia in a drug-induced model.Expression of the Ca2+-binding protein, parvalbumin, during embryonic development of the frog, Xenopus laevis Specific isomyosin proportions in hyperexcitable and physiologically denervated mouse muscle.The ClC family of voltage-gated chloride channels: structure and function.Impaired Wheel Running Exercise in CLC-1 Chloride Channel-Deficient Myotonic Mice.Characterization of excitation-contraction coupling components in human extraocular muscles.Isotonic contractile impairment due to genetic CLC-1 chloride channel deficiency in myotonic mouse diaphragm muscle.

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P2860

Calcium-binding protein, parvalbumin, is reduced in mutant mammalian muscle with abnormal contractile properties.

http://www.wikidata.org/entity/Q37561384

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

@tr

scientific article published on August 1984

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Calcium-binding protein, parva ...... normal contractile properties.

@en

Calcium-binding protein, parva ...... normal contractile properties.

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type

label

Calcium-binding protein, parva ...... normal contractile properties.

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Calcium-binding protein, parva ...... normal contractile properties.

@nl

prefLabel

Calcium-binding protein, parva ...... normal contractile properties.

@en

Calcium-binding protein, parva ...... normal contractile properties.

@nl

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PNAS.81.15.4814

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Proceedings of the National Academy of Sciences of the United States of America

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Calcium-binding protein, parva ...... normal contractile properties.

@en

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Heizmann CW

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Jockusch H

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Reininghaus J

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Stuhlfauth I

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P2860

Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications

High resolution two-dimensional electrophoresis of proteins

Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane

The time-course of Ca2+ exchange with calmodulin, troponin, parvalbumin, and myosin in response to transient increases in Ca2+

Correlation of parvalbumin concentration with relaxation speed in mammalian muscles.

An hereditary motor neurone disease with progressive denervation of muscle in the mouse: the mutant 'wobbler'.

Isolation and characterization of parvalbumin from chicken leg-muscle.

Chicken parvalbumin. Comparison with parvalbumin-like protein and three other components (Mr = 8,000 to 13,000).

Structure and evolution of calcium-modulated proteins.

Inherited muscle and nerve diseases in mice: a tabulation with commentary.

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4814-4818

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scholarly article

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10.1073/PNAS.81.15.4814

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15

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81

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1984-08-01T00:00:00Z

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