Dislocation of HMG-CoA reductase and Insig-1, two polytopic endoplasmic reticulum proteins, en route to proteasomal degradation. - Wikidata - wikimedia - TriplyDB

Dislocation of HMG-CoA reductase and Insig-1, two polytopic endoplasmic reticulum proteins, en route to proteasomal degradation.

Dislocation of HMG-CoA reductase and Insig-1, two polytopic endoplasmic reticulum proteins, en route to proteasomal degradation.

http://www.wikidata.org/entity/Q39848785

about

Dual functions of Insig proteins in cholesterol homeostasis The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology From neurodevelopment to neurodegeneration: the interaction of neurofibromin and valosin-containing protein/p97 in regulation of dendritic spine formation Sequential actions of the AAA-ATPase valosin-containing protein (VCP)/p97 and the proteasome 19 S regulatory particle in sterol-accelerated, endoplasmic reticulum (ER)-associated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase.Sterol-induced dislocation of 3-hydroxy-3-methylglutaryl coenzyme A reductase from endoplasmic reticulum membranes into the cytosol through a subcellular compartment resembling lipid droplets.Control of cholesterol synthesis through regulated ER-associated degradation of HMG CoA reductase Liver cytochrome P450 3A endoplasmic reticulum-associated degradation: a major role for the p97 AAA ATPase in cytochrome P450 3A extraction into the cytosol.The chaperone BAG6 captures dislocated glycoproteins in the cytosol.Protein folding and quality control in the endoplasmic reticulum: Recent lessons from yeast and mammalian cell systems.Valosin-containing protein and neurofibromin interact to regulate dendritic spine density Subcellular Fractionation Analysis of the Extraction of Ubiquitinated Polytopic Membrane Substrate during ER-Associated Degradation Differential regulation of HMG-CoA reductase and Insig-1 by enzymes of the ubiquitin-proteasome system.Sterol-induced dislocation of 3-hydroxy-3-methylglutaryl coenzyme A reductase from membranes of permeabilized cells Metabolically regulated endoplasmic reticulum-associated degradation of 3-hydroxy-3-methylglutaryl-CoA reductase: evidence for requirement of a geranylgeranylated protein.Membrane Protein Quantity Control at the Endoplasmic Reticulum.Rapid degradation of cyclooxygenase-1 and hematopoietic prostaglandin D synthase through ubiquitin-proteasome system in response to intracellular calcium level Transmembrane helix hydrophobicity is an energetic barrier during the retrotranslocation of integral membrane ERAD substrates Haploid Mammalian Genetic Screen Identifies UBXD8 as a Key Determinant of HMGCR Degradation and Cholesterol Biosynthesis.

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P2860

Dislocation of HMG-CoA reductase and Insig-1, two polytopic endoplasmic reticulum proteins, en route to proteasomal degradation.

http://www.wikidata.org/entity/Q39848785

description

2009 nî lūn-bûn

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2009年の論文

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2009年学术文章

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2009年学术文章

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2009年学术文章

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2009年学术文章

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2009年学术文章

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2009年學術文章

@yue

2009年學術文章

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2009年學術文章

@zh-hant

name

Dislocation of HMG-CoA reducta ...... te to proteasomal degradation.

@en

Dislocation of HMG-CoA reducta ...... te to proteasomal degradation.

@nl

type

label

Dislocation of HMG-CoA reducta ...... te to proteasomal degradation.

@en

Dislocation of HMG-CoA reducta ...... te to proteasomal degradation.

@nl

prefLabel

Dislocation of HMG-CoA reducta ...... te to proteasomal degradation.

@en

Dislocation of HMG-CoA reducta ...... te to proteasomal degradation.

@nl

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MBC.E08-09-0953

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Molecular Biology of the Cell

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Dislocation of HMG-CoA reducta ...... te to proteasomal degradation.

@en

P2093

Dror Harats

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

Gil S Leichner

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

Joseph Roitelman

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Rachel Avner

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P2860

Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis

The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum

Crucial step in cholesterol homeostasis: sterols promote binding of SCAP to INSIG-1, a membrane protein that facilitates retention of SREBPs in ER

Sterol-regulated degradation of Insig-1 mediated by the membrane-bound ubiquitin ligase gp78

Insig-2, a second endoplasmic reticulum protein that binds SCAP and blocks export of sterol regulatory element-binding proteins

Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains

Identification of complexes between the COOH-terminal domains of sterol regulatory element-binding proteins (SREBPs) and SREBP cleavage-activating protein

Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase

Ufd1 is a cofactor of gp78 and plays a key role in cholesterol metabolism by regulating the stability of HMG-CoA reductase

Three mutations in sterol-sensing domain of SCAP block interaction with insig and render SREBP cleavage insensitive to sterols.

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3330-3341

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10.1091/MBC.E08-09-0953

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14

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20

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2009-05-20T00:00:00Z

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19458199

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endoplasmic reticulum

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2710830

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