Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
about
Retrograde transport pathways utilised by viruses and protein toxinsHuman ubiquitin-protein ligase Nedd4: expression, subcellular localization and selective interaction with ubiquitin-conjugating enzymesTEB4 is a C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulumA high-coverage shRNA screen identifies TMEM129 as an E3 ligase involved in ER-associated protein degradationA membrane protein required for dislocation of misfolded proteins from the ERA membrane protein complex mediates retro-translocation from the ER lumen into the cytosolHuman HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulumDerlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradationThe TRC8 E3 ligase ubiquitinates MHC class I molecules before dislocation from the ERNMR characterization of the interaction between the PUB domain of peptide:N-glycanase and ubiquitin-like domain of HR23Protein disulphide isomerase is required for signal peptide peptidase-mediated protein degradationThe otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ERRecruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membraneHRD1 and UBE2J1 target misfolded MHC class I heavy chains for endoplasmic reticulum-associated degradationPerturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasomeA glycosylated type I membrane protein becomes cytosolic when peptide: N-glycanase is compromised.Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretomeIdentification of proteins that interact with mammalian peptide:N-glycanase and implicate this hydrolase in the proteasome-dependent pathway for protein degradationThe COG and COPI complexes interact to control the abundance of GEARs, a subset of Golgi integral membrane proteinsConsensus on the role of human cytomegalovirus in glioblastomaInhibition of p97-dependent protein degradation by Eeyarestatin IPNG1, a yeast gene encoding a highly conserved peptide:N-glycanaseGene expression during ER stress-induced apoptosis in neurons: induction of the BH3-only protein Bbc3/PUMA and activation of the mitochondrial apoptosis pathwayMurine polyomavirus requires the endoplasmic reticulum protein Derlin-2 to initiate infectionIdentifying the ERAD ubiquitin E3 ligases for viral and cellular targeting of MHC class ICross-Presentation of Cell-Associated Antigens by MHC Class I in Dendritic Cell SubsetsProtein folding and quality control in the ERHuman cytomegalovirus and autoimmune diseaseGRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulumThe delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiologyThe protein translocation channel mediates glycopeptide export across the endoplasmic reticulum membraneAntigen presentation subverted: Structure of the human cytomegalovirus protein US2 bound to the class I molecule HLA-A2Studies on peptide:N-glycanase-p97 interaction suggest that p97 phosphorylation modulates endoplasmic reticulum-associated degradationStructural Mechanism of ER Retrieval of MHC Class I by CowpoxThe Structure of the Cytomegalovirus-Encoded m04 Glycoprotein, a Prototypical Member of the m02 Family of ImmunoevasinsMolecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation.Dissecting the ER-associated degradation of a misfolded polytopic membrane protein.Endoplasmic Reticulum-associated Degradation of Pca1p, a Polytopic Protein, via Interaction with the Proteasome at the MembraneSec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation.Sec61p is part of the endoplasmic reticulum-associated degradation machinery
P2860
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P2860
Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
description
1996 nî lūn-bûn
@nan
1996 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Sec61-mediated transfer of a m ...... the proteasome for destruction
@ast
Sec61-mediated transfer of a m ...... the proteasome for destruction
@en
Sec61-mediated transfer of a m ...... the proteasome for destruction
@en-gb
Sec61-mediated transfer of a m ...... the proteasome for destruction
@nl
type
label
Sec61-mediated transfer of a m ...... the proteasome for destruction
@ast
Sec61-mediated transfer of a m ...... the proteasome for destruction
@en
Sec61-mediated transfer of a m ...... the proteasome for destruction
@en-gb
Sec61-mediated transfer of a m ...... the proteasome for destruction
@nl
prefLabel
Sec61-mediated transfer of a m ...... the proteasome for destruction
@ast
Sec61-mediated transfer of a m ...... the proteasome for destruction
@en
Sec61-mediated transfer of a m ...... the proteasome for destruction
@en-gb
Sec61-mediated transfer of a m ...... the proteasome for destruction
@nl
P2093
P921
P3181
P356
P1433
P1476
Sec61-mediated transfer of a m ...... the proteasome for destruction
@en
P2093
P2888
P3181
P356
10.1038/384432A0
P407
P577
1996-12-05T00:00:00Z
P5875
P6179
1013734677