Ubiquitination participates in the lysosomal degradation of Na,K-ATPase in steady-state conditions - Wikidata - awgldk - TriplyDB

Ubiquitination participates in the lysosomal degradation of Na,K-ATPase in steady-state conditions

Ubiquitination participates in the lysosomal degradation of Na,K-ATPase in steady-state conditions

http://www.wikidata.org/entity/Q37443221

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Insulin regulates alveolar epithelial function by inducing Na+/K+-ATPase translocation to the plasma membrane in a process mediated by the action of Akt Sodium-potassium ATPase emerges as a player in hippocampal phenotypes of Angelman syndrome mice.Role of kinesin light chain-2 of kinesin-1 in the traffic of Na,K-ATPase-containing vesicles in alveolar epithelial cells.Calcium release-activated calcium (CRAC) channels mediate the β(2)-adrenergic regulation of Na,K-ATPase.Regulation of alpha1 Na/K-ATPase expression by cholesterol Protein expression profile of rat type two alveolar epithelial cells during hyperoxic stress and recovery.Salt-inducible kinase 1 is present in lung alveolar epithelial cells and regulates active sodium transport Ubiquitination and proteolysis in acute lung injury Macrophage-epithelial paracrine crosstalk inhibits lung edema clearance during influenza infection.Functional genomic assessment of phosgene-induced acute lung injury in mice.Ouabain-induced internalization and lysosomal degradation of the Na+/K+-ATPase.

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Ubiquitination participates in the lysosomal degradation of Na,K-ATPase in steady-state conditions

http://www.wikidata.org/entity/Q37443221

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 13 March 2009

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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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RCMB.2008-0365OC

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American Journal of Respiratory Cell and Molecular Biology

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Ubiquitination participates in ...... ase in steady-state conditions

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P2093

Christine Vohwinkel

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Emilia Lecuona

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Haiying Sun

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Jacob I Sznajder

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P2860

Brefeldin A: deciphering an enigmatic inhibitor of secretion

The rab7 GTPase resides on a vesicular compartment connected to lysosomes

Structural basis for species-specific differences in the phosphorylation of Na,K-ATPase by protein kinase C

Cadmium-mediated oxidative stress in kidney proximal tubule cells induces degradation of Na+/K(+)-ATPase through proteasomal and endo-/lysosomal proteolytic pathways

The acute respiratory distress syndrome

rab5 controls early endosome fusion in vitro

Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins

AMP-activated protein kinase regulates CO2-induced alveolar epithelial dysfunction in rats and human cells by promoting Na,K-ATPase endocytosis

High CO2 levels impair alveolar epithelial function independently of pH.

Dopamine-induced exocytosis of Na,K-ATPase is dependent on activation of protein kinase C-epsilon and -delta.

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671-679

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scholarly article

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10.1165/RCMB.2008-0365OC

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6

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41

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Aaron Ciechanover

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2009-03-13T00:00:00Z

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19286978

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protein ubiquitination

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2784405

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