ER protein quality control and proteasome-mediated protein degradation.
about
The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulumNrf2 and Nrf1 signaling and ER stress crosstalk: implication for proteasomal degradation and autophagyA complex between peptide:N-glycanase and two proteasome-linked proteins suggests a mechanism for the degradation of misfolded glycoproteinsFunction of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chainsRNF185 is a novel E3 ligase of endoplasmic reticulum-associated degradation (ERAD) that targets cystic fibrosis transmembrane conductance regulator (CFTR)TNF-alpha induced c-IAP1/TRAF2 complex translocation to a Ubc6-containing compartment and TRAF2 ubiquitinationThe human DnaJ homologue (Hdj)-1/heat-shock protein (Hsp) 40 co-chaperone is required for the in vivo stabilization of the cystic fibrosis transmembrane conductance regulator by Hsp70The retrotranslocation protein Derlin-1 binds peptide:N-glycanase to the endoplasmic reticulumIdentification of proteins that interact with mammalian peptide:N-glycanase and implicate this hydrolase in the proteasome-dependent pathway for protein degradationPNG1, a yeast gene encoding a highly conserved peptide:N-glycanaseThe cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome systemMisfolding diverts CFTR from recycling to degradation: quality control at early endosomesMisfolded proteins are sorted by a sequential checkpoint mechanism of ER quality controlSelective up-regulation of NMDA-NR1 receptor expression in myenteric plexus after TNBS induced colitis in rats.Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation.Pbn1p: an essential endoplasmic reticulum membrane protein required for protein processing in the endoplasmic reticulum of budding yeast.Determinants of RING-E2 fidelity for Hrd1p, a membrane-anchored ubiquitin ligase.An HRD/DER-independent ER quality control mechanism involves Rsp5p-dependent ubiquitination and ER-Golgi transportTraffic-independent function of the Sar1p/COPII machinery in proteasomal sorting of the cystic fibrosis transmembrane conductance regulatorMnl1p, an alpha -mannosidase-like protein in yeast Saccharomyces cerevisiae, is required for endoplasmic reticulum-associated degradation of glycoproteins.Degradation of misfolded protein in the cytoplasm is mediated by the ubiquitin ligase Ubr1.Distinct retrieval and retention mechanisms are required for the quality control of endoplasmic reticulum protein folding.HRD4/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins.AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation.Nascent lipidated apolipoprotein B is transported to the Golgi as an incompletely folded intermediate as probed by its association with network of endoplasmic reticulum molecular chaperones, GRP94, ERp72, BiP, calreticulin, and cyclophilin BUbiquitination is essential for human cytomegalovirus US11-mediated dislocation of MHC class I molecules from the endoplasmic reticulum to the cytosolProteasomes and ubiquitin are involved in the turnover of the wild-type prion proteinThe NR1 subunit of the N-methyl-D-aspartate receptor can be efficiently expressed alone in the cell surface of mammalian cells and is required for the transport of the NR2A subunitActinfilin is a Cul3 substrate adaptor, linking GluR6 kainate receptor subunits to the ubiquitin-proteasome pathwayFbs2 is a new member of the E3 ubiquitin ligase family that recognizes sugar chainsIdentification and Characterization of Endoplasmic Reticulum-Associated Degradation Proteins Differentially Affected by Endoplasmic Reticulum StressRegulation of cell surface expression of functional pacemaker channels by a motif in the B-helix of the cyclic nucleotide-binding domain.Retrotranslocation of the chaperone calreticulin from the endoplasmic reticulum lumen to the cytosol.The amyotrophic lateral sclerosis 8 protein, VAP, is required for ER protein quality controlA genome-wide screen identifies Yos9p as essential for ER-associated degradation of glycoproteins.The ubiquitin-proteasome system in myocardial ischaemia and preconditioning.Modularity of the Hrd1 ERAD complex underlies its diverse client range.Aggresomes and Russell bodies. Symptoms of cellular indigestion?Evasion of endoplasmic reticulum surveillance makes Wsc1p an obligate substrate of Golgi quality controlTrypanosoma brucei: trypanosome-specific endoplasmic reticulum proteins involved in variant surface glycoprotein expression.
P2860
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P2860
ER protein quality control and proteasome-mediated protein degradation.
description
1999 nî lūn-bûn
@nan
1999 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
ER protein quality control and proteasome-mediated protein degradation.
@ast
ER protein quality control and proteasome-mediated protein degradation.
@en
type
label
ER protein quality control and proteasome-mediated protein degradation.
@ast
ER protein quality control and proteasome-mediated protein degradation.
@en
prefLabel
ER protein quality control and proteasome-mediated protein degradation.
@ast
ER protein quality control and proteasome-mediated protein degradation.
@en
P356
P1476
ER protein quality control and proteasome-mediated protein degradation.
@en
P2093
Brodsky JL
P304
P356
10.1006/SCDB.1999.0321
P577
1999-10-01T00:00:00Z