Isoform specificity of the Na/K-ATPase association and regulation by phospholemman. - Wikidata - awgldk - TriplyDB

Isoform specificity of the Na/K-ATPase association and regulation by phospholemman.

Isoform specificity of the Na/K-ATPase association and regulation by phospholemman.

http://www.wikidata.org/entity/Q37446797

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p62/sequestosome-1 associates with and sustains the expression of retroviral restriction factor TRIM5alpha.Specialized Functional Diversity and Interactions of the Na,K-ATPase Regulation of the cardiac sodium pump Downregulation of miR-151-5p contributes to increased susceptibility to arrhythmogenesis during myocardial infarction with estrogen deprivation Regulation of Cardiac Remodeling by Cardiac Na(+)/K(+)-ATPase Isoforms Na+/Ca2+ exchange and Na+/K+-ATPase in the heart Chronic nicotine modifies skeletal muscle Na,K-ATPase activity through its interaction with the nicotinic acetylcholine receptor and phospholemman A separate pool of cardiac phospholemman that does not regulate or associate with the sodium pump: multimers of phospholemman in ventricular muscle Role of phospholemman phosphorylation sites in mediating kinase-dependent regulation of the Na+-K+-ATPase.Phospholemman and beta-adrenergic stimulation in the heart.The human phospholamban Arg14-deletion mutant localizes to plasma membrane and interacts with the Na/K-ATPase Sodium and proton effects on inward proton transport through Na/K pumps.Activation of cAMP-dependent signaling induces oxidative modification of the cardiac Na+-K+ pump and inhibits its activity.Relative affinity of calcium pump isoforms for phospholamban quantified by fluorescence resonance energy transfer Phospholemman: a novel cardiac stress protein.FXYD proteins stabilize Na,K-ATPase: amplification of specific phosphatidylserine-protein interactions.Phosphomimetic mutations enhance oligomerization of phospholemman and modulate its interaction with the Na/K-ATPase.The inhibitory effect of phospholemman on the sodium pump requires its palmitoylation.Na(+)/K)+)-ATPase α2-isoform preferentially modulates Ca2(+) transients and sarcoplasmic reticulum Ca2(+) release in cardiac myocytes Importance of the Voltage Dependence of Cardiac Na/K ATPase Isozymes.Phospholemman is not required for the acute stimulation of Na⁺-K⁺-ATPase α₂-activity during skeletal muscle fatigue.Na⁺/K⁺-ATPase E960 and phospholemman F28 are critical for their functional interaction Distinct α2 Na,K-ATPase membrane pools are differently involved in early skeletal muscle remodeling during disuse.Development of a high-affinity peptide that prevents phospholemman (PLM) inhibition of the sodium/calcium exchanger 1 (NCX1).Na/K-ATPase--an integral player in the adrenergic fight-or-flight response.L30A Mutation of Phospholemman Mimics Effects of Cardiac Glycosides in Isolated Cardiomyocytes Induced overexpression of phospholemman S68E mutant improves cardiac contractility and mortality after ischemia-reperfusion.Regulation of the cardiac Na(+) pump by palmitoylation of its catalytic and regulatory subunits.Na,K-ATPase regulation in skeletal muscle.Molecular Mechanisms and Kinetic Effects of FXYD1 and Phosphomimetic Mutants on Purified Human Na,K-ATPase Excitation-contraction coupling properties in women with work-related myalgia: a preliminary study.Selective Assembly of Na,K-ATPase α2β2 Heterodimers in the Heart: DISTINCT FUNCTIONAL PROPERTIES AND ISOFORM-SELECTIVE INHIBITORS.Surface charges of the membrane crucially affect regulation of Na,K-ATPase by phospholemman (FXYD1).How does pressure overload cause cardiac hypertrophy and dysfunction? High-ouabain affinity cardiac Na+ pumps are crucial.Pivotal role of α2 Na+ pumps and their high affinity ouabain binding site in cardiovascular health and disease.Cellular properties of extensor carpi radialis brevis and trapezius muscles in healthy males and females.

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P2860

Isoform specificity of the Na/K-ATPase association and regulation by phospholemman.

http://www.wikidata.org/entity/Q37446797

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

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scientific article published on 28 July 2009

@en

vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

@cs

name

Isoform specificity of the Na/K-ATPase association and regulation by phospholemman.

@en

Isoform specificity of the Na/K-ATPase association and regulation by phospholemman.

@nl

type

label

Isoform specificity of the Na/K-ATPase association and regulation by phospholemman.

@en

Isoform specificity of the Na/K-ATPase association and regulation by phospholemman.

@nl

prefLabel

Isoform specificity of the Na/K-ATPase association and regulation by phospholemman.

@en

Isoform specificity of the Na/K-ATPase association and regulation by phospholemman.

@nl

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JBC.M109.047357

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Journal of Biological Chemistry

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Isoform specificity of the Na/K-ATPase association and regulation by phospholemman.

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P2093

Donald M Bers

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Fei Han

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

Jerry B Lingrel

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Julie Bossuyt

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Sanda Despa

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Seth L Robia

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Zhanjia Hou

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P2860

Crystal structure of the sodium–potassium pump

Characterization of the human and rat phospholemman (PLM) cDNAs and localization of the human PLM gene to chromosome 19q13.1

Structure of the Na,K-ATPase regulatory protein FXYD1 in micelles

Cytoplasmic tail of phospholemman interacts with the intracellular loop of the cardiac Na+/Ca2+ exchanger

The FXYD gene family of small ion transport regulators or channels: cDNA sequence, protein signature sequence, and expression

Ischemia-induced phosphorylation of phospholemman directly activates rat cardiac Na/K-ATPase

The alpha 1 isoform of Na,K-ATPase regulates cardiac contractility and functionally interacts and co-localizes with the Na/Ca exchanger in heart

The Na+/K+-ATPase alpha2-isoform regulates cardiac contractility in rat cardiomyocytes

Structural interactions between FXYD proteins and Na+,K+-ATPase: alpha/beta/FXYD subunit stoichiometry and cross-linking

Phospholemman phosphorylation mediates the protein kinase C-dependent effects on Na+/K+ pump function in cardiac myocytes

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26749-26757

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scholarly article

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10.1074/JBC.M109.047357

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39

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2009-07-28T00:00:00Z

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19638348

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2785363

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