The ubiquitylation machinery of the endoplasmic reticulum. - Wikidata - awgldk - TriplyDB

The ubiquitylation machinery of the endoplasmic reticulum.

The ubiquitylation machinery of the endoplasmic reticulum.

http://www.wikidata.org/entity/Q37424805

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HIV-1 Vpu neutralizes the antiviral factor Tetherin/BST-2 by binding it and directing its beta-TrCP2-dependent degradation A SEL1L mutation links a canine progressive early-onset cerebellar ataxia to the endoplasmic reticulum-associated protein degradation (ERAD) machinery Identification of the PDI-family member ERp90 as an interaction partner of ERFAD SEL1L protein critically determines the stability of the HRD1-SEL1L endoplasmic reticulum-associated degradation (ERAD) complex to optimize the degradation kinetics of ERAD substrates Domain analysis reveals that a deubiquitinating enzyme USP13 performs non-activating catalysis for Lys63-linked polyubiquitin A ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradation The TRC8 E3 ligase ubiquitinates MHC class I molecules before dislocation from the ER Deubiquitinases sharpen substrate discrimination during membrane protein degradation from the ER The UBX protein SAKS1 negatively regulates endoplasmic reticulum-associated degradation and p97-dependent degradation USP13 antagonizes gp78 to maintain functionality of a chaperone in ER-associated degradation Endoplasmic reticulum protein quality control is determined by cooperative interactions between Hsp/c70 protein and the CHIP E3 ligase RNF185 is a novel E3 ligase of endoplasmic reticulum-associated degradation (ERAD) that targets cystic fibrosis transmembrane conductance regulator (CFTR)Ubiquilin and p97/VCP bind erasin, forming a complex involved in ERAD A deubiquitinase negatively regulates retro-translocation of nonubiquitinated substrates Melanoma and the Unfolded Protein Response Protein folding and quality control in the ER Recent technical developments in the study of ER-associated degradation Endoplasmic reticulum-mediated protein quality control in Arabidopsis Spliced leader RNA silencing (SLS) - a programmed cell death pathway in Trypanosoma brucei that is induced upon ER stress Mechanisms for quality control of misfolded transmembrane proteins Ubiquitin on the move: the ubiquitin modification system plays diverse roles in the regulation of endoplasmic reticulum- and plasma membrane-localized proteins Protein homeostasis at the plasma membrane The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology DLK-1, SEK-3 and PMK-3 Are Required for the Life Extension Induced by Mitochondrial Bioenergetic Disruption in C. elegans Structural and Biochemical Basis of Yos9 Protein Dimerization and Possible Contribution to Self-association of 3-Hydroxy-3-methylglutaryl-Coenzyme A Reductase Degradation Ubiquitin-Ligase Complex A Cdc48p-associated factor modulates endoplasmic reticulum-associated degradation, cell stress, and ubiquitinated protein homeostasis The yeast ERAD-C ubiquitin ligase Doa10 recognizes an intramembrane degron A Complex of Htm1 and the Oxidoreductase Pdi1 Accelerates Degradation of Misfolded Glycoproteins.Yos9p assists in the degradation of certain nonglycosylated proteins from the endoplasmic reticulum Cdc48/p97 mediates UV-dependent turnover of RNA Pol II.Der1 promotes movement of misfolded proteins through the endoplasmic reticulum membrane.Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-ligase Hrd1p.The yeast ubr1 ubiquitin ligase participates in a prominent pathway that targets cytosolic thermosensitive mutants for degradation Arms Race between Enveloped Viruses and the Host ERAD Machinery The cytosolic chaperone Hsc70 promotes traffic to the cell surface of intracellular retained melanocortin-4 receptor mutants The ERAD inhibitor Eeyarestatin I is a bifunctional compound with a membrane-binding domain and a p97/VCP inhibitory group Derlin-1 deficiency is embryonic lethal, Derlin-3 deficiency appears normal, and Herp deficiency is intolerant to glucose load and ischemia in mice The endoplasmic reticulum-associated Hsp40 DNAJB12 and Hsc70 cooperate to facilitate RMA1 E3-dependent degradation of nascent CFTRDeltaF508 Ubiquitin is a versatile scaffold protein for the generation of molecules with de novo binding and advantageous drug-like properties Novel ubiquitin-derived high affinity binding proteins with tumor targeting properties.

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The ubiquitylation machinery of the endoplasmic reticulum.

http://www.wikidata.org/entity/Q37424805

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on March 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

The ubiquitylation machinery of the endoplasmic reticulum.

@en

The ubiquitylation machinery of the endoplasmic reticulum.

@nl

type

label

The ubiquitylation machinery of the endoplasmic reticulum.

@en

The ubiquitylation machinery of the endoplasmic reticulum.

@nl

prefLabel

The ubiquitylation machinery of the endoplasmic reticulum.

@en

The ubiquitylation machinery of the endoplasmic reticulum.

@nl

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The ubiquitylation machinery of the endoplasmic reticulum.

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Christian Hirsch

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

Oliver Neuber

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

Robert Gauss

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

Sabine C Horn

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

Thomas Sommer

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

P2860

A novel ER alpha-mannosidase-like protein accelerates ER-associated degradation

Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast.

HRD4/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins.

Polyubiquitination is required for US11-dependent movement of MHC class I heavy chain from endoplasmic reticulum into cytosol

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453-460

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scholarly article

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10.1038/NATURE07962

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7237

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458

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2009-03-01T00:00:00Z

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1019048030

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19325625

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P921

endoplasmic reticulum