The ubiquitylation machinery of the endoplasmic reticulum.
about
HIV-1 Vpu neutralizes the antiviral factor Tetherin/BST-2 by binding it and directing its beta-TrCP2-dependent degradationA SEL1L mutation links a canine progressive early-onset cerebellar ataxia to the endoplasmic reticulum-associated protein degradation (ERAD) machineryIdentification of the PDI-family member ERp90 as an interaction partner of ERFADSEL1L protein critically determines the stability of the HRD1-SEL1L endoplasmic reticulum-associated degradation (ERAD) complex to optimize the degradation kinetics of ERAD substratesDomain analysis reveals that a deubiquitinating enzyme USP13 performs non-activating catalysis for Lys63-linked polyubiquitinA ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradationThe TRC8 E3 ligase ubiquitinates MHC class I molecules before dislocation from the ERDeubiquitinases sharpen substrate discrimination during membrane protein degradation from the ERThe UBX protein SAKS1 negatively regulates endoplasmic reticulum-associated degradation and p97-dependent degradationUSP13 antagonizes gp78 to maintain functionality of a chaperone in ER-associated degradationEndoplasmic reticulum protein quality control is determined by cooperative interactions between Hsp/c70 protein and the CHIP E3 ligaseRNF185 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 ERADA deubiquitinase negatively regulates retro-translocation of nonubiquitinated substratesMelanoma and the Unfolded Protein ResponseProtein folding and quality control in the ERRecent technical developments in the study of ER-associated degradationEndoplasmic reticulum-mediated protein quality control in ArabidopsisSpliced leader RNA silencing (SLS) - a programmed cell death pathway in Trypanosoma brucei that is induced upon ER stressMechanisms for quality control of misfolded transmembrane proteinsUbiquitin on the move: the ubiquitin modification system plays diverse roles in the regulation of endoplasmic reticulum- and plasma membrane-localized proteinsProtein homeostasis at the plasma membraneThe delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiologyDLK-1, SEK-3 and PMK-3 Are Required for the Life Extension Induced by Mitochondrial Bioenergetic Disruption in C. elegansStructural and Biochemical Basis of Yos9 Protein Dimerization and Possible Contribution to Self-association of 3-Hydroxy-3-methylglutaryl-Coenzyme A Reductase Degradation Ubiquitin-Ligase ComplexA Cdc48p-associated factor modulates endoplasmic reticulum-associated degradation, cell stress, and ubiquitinated protein homeostasisThe yeast ERAD-C ubiquitin ligase Doa10 recognizes an intramembrane degronA Complex of Htm1 and the Oxidoreductase Pdi1 Accelerates Degradation of Misfolded Glycoproteins.Yos9p assists in the degradation of certain nonglycosylated proteins from the endoplasmic reticulumCdc48/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 degradationArms Race between Enveloped Viruses and the Host ERAD MachineryThe cytosolic chaperone Hsc70 promotes traffic to the cell surface of intracellular retained melanocortin-4 receptor mutantsThe ERAD inhibitor Eeyarestatin I is a bifunctional compound with a membrane-binding domain and a p97/VCP inhibitory groupDerlin-1 deficiency is embryonic lethal, Derlin-3 deficiency appears normal, and Herp deficiency is intolerant to glucose load and ischemia in miceThe endoplasmic reticulum-associated Hsp40 DNAJB12 and Hsc70 cooperate to facilitate RMA1 E3-dependent degradation of nascent CFTRDeltaF508Ubiquitin is a versatile scaffold protein for the generation of molecules with de novo binding and advantageous drug-like propertiesNovel ubiquitin-derived high affinity binding proteins with tumor targeting properties.
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The ubiquitylation machinery of the endoplasmic reticulum.
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
P2093
P2860
P356
P1433
P1476
The ubiquitylation machinery of the endoplasmic reticulum.
@en
P2093
Christian Hirsch
Oliver Neuber
Robert Gauss
Sabine C Horn
Thomas Sommer
P2860
P2888
P304
P356
10.1038/NATURE07962
P407
P577
2009-03-01T00:00:00Z
P6179
1019048030