Sec61p-independent degradation of the tail-anchored ER membrane protein Ubc6p
about
ATG12 conjugation to ATG3 regulates mitochondrial homeostasis and cell deathA membrane protein required for dislocation of misfolded proteins from the ERMembrane topology of the yeast endoplasmic reticulum-localized ubiquitin ligase Doa10 and comparison with its human ortholog TEB4 (MARCH-VI)The E3 ubiquitin ligase TEB4 mediates degradation of type 2 iodothyronine deiodinaseA conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradationThe Crystal Structures of Yeast Get3 Suggest a Mechanism for Tail-Anchored Protein Membrane InsertionProtein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48.The yeast ERAD-C ubiquitin ligase Doa10 recognizes an intramembrane degronYos9p assists in the degradation of certain nonglycosylated proteins from the endoplasmic reticulumDistinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble luminal protein.Cue1p is an activator of Ubc7p E2 activity in vitro and in vivo.Der1 promotes movement of misfolded proteins through the endoplasmic reticulum membrane.Ubx2 links the Cdc48 complex to ER-associated protein degradation.Inositol 1,4,5-trisphosphate receptor ubiquitination is mediated by mammalian Ubc7, a component of the endoplasmic reticulum-associated degradation pathway, and is inhibited by chelation of intracellular Zn2+Roles of molecular chaperones in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD)ERAD: the long road to destructionMembrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathwaysSequential 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.The tale of tail-anchored proteins: coming from the cytosol and looking for a membrane.The short-lived Matalpha2 transcriptional repressor is protected from degradation in vivo by interactions with its corepressors Tup1 and Ssn6Uncoupling retro-translocation and degradation in the ER-associated degradation of a soluble protein.Human homologs of Ubc6p ubiquitin-conjugating enzyme and phosphorylation of HsUbc6e in response to endoplasmic reticulum stress.Proteasomal degradation of Sfp1 contributes to the repression of ribosome biogenesis during starvation and is mediated by the proteasome activator Blm10.Processing and turnover of the Hedgehog protein in the endoplasmic reticulum.An unusual transmembrane helix in the endoplasmic reticulum ubiquitin ligase Doa10 modulates degradation of its cognate E2 enzyme.For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection.Ubiquitin-dependent protein degradation at the yeast endoplasmic reticulum and nuclear envelope.Proteostasis regulation at the endoplasmic reticulum: a new perturbation site for targeted cancer therapy.Subcellular Fractionation Analysis of the Extraction of Ubiquitinated Polytopic Membrane Substrate during ER-Associated DegradationSEL1L, the homologue of yeast Hrd3p, is involved in protein dislocation from the mammalian ER.Viral modulation of antigen presentation: manipulation of cellular targets in the ER and beyond.The ubiquitin-proteasome system of Saccharomyces cerevisiae.Dislocation and degradation from the ER are regulated by cytosolic stress.Ubiquitin ligases, critical mediators of endoplasmic reticulum-associated degradationThe endoplasmic reticulum-associated degradation pathways of budding yeast.Doa1 targets ubiquitinated substrates for mitochondria-associated degradation.A Conserved C-terminal Element in the Yeast Doa10 and Human MARCH6 Ubiquitin Ligases Required for Selective Substrate Degradation.Preliminary X-ray crystallographic studies of yeast Get3.Protein quality control in the ER: balancing the ubiquitin checkbook.Regulation of Endoplasmic Reticulum-Associated Protein Degradation (ERAD) by Ubiquitin.
P2860
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P2860
Sec61p-independent degradation of the tail-anchored ER membrane protein Ubc6p
description
2001 nî lūn-bûn
@nan
2001 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Sec61p-independent degradation of the tail-anchored ER membrane protein Ubc6p
@ast
Sec61p-independent degradation of the tail-anchored ER membrane protein Ubc6p
@en
Sec61p-independent degradation of the tail-anchored ER membrane protein Ubc6p
@nl
type
label
Sec61p-independent degradation of the tail-anchored ER membrane protein Ubc6p
@ast
Sec61p-independent degradation of the tail-anchored ER membrane protein Ubc6p
@en
Sec61p-independent degradation of the tail-anchored ER membrane protein Ubc6p
@nl
prefLabel
Sec61p-independent degradation of the tail-anchored ER membrane protein Ubc6p
@ast
Sec61p-independent degradation of the tail-anchored ER membrane protein Ubc6p
@en
Sec61p-independent degradation of the tail-anchored ER membrane protein Ubc6p
@nl
P2093
P2860
P3181
P356
P1433
P1476
Sec61p-independent degradation of the tail-anchored ER membrane protein Ubc6p
@en
P2093
P2860
P304
P3181
P356
10.1093/EMBOJ/20.12.3124
P407
P577
2001-06-15T00:00:00Z