Der3p/Hrd1p is required for endoplasmic reticulum-associated degradation of misfolded lumenal and integral membrane proteins.
about
RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitinationThe tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulumTEB4 is a C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulumDefining human ERAD networks through an integrative mapping strategySEL1L protein critically determines the stability of the HRD1-SEL1L endoplasmic reticulum-associated degradation (ERAD) complex to optimize the degradation kinetics of ERAD substratesHuman HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulumDownregulation of major histocompatibility complex class I by human ubiquitin ligases related to viral immune evasion proteinsp53RFP, a p53-inducible RING-finger protein, regulates the stability of p21WAF1CYP3A4 ubiquitination by gp78 (the tumor autocrine motility factor receptor, AMFR) and CHIP E3 ligasesSynoviolin promotes IRE1 ubiquitination and degradation in synovial fibroblasts from mice with collagen-induced arthritisRNF185 is a novel E3 ligase of endoplasmic reticulum-associated degradation (ERAD) that targets cystic fibrosis transmembrane conductance regulator (CFTR)Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membraneCytoplasmic destruction of p53 by the endoplasmic reticulum-resident ubiquitin ligase 'Synoviolin'Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane.Ariadne-1: a vital Drosophila gene is required in development and defines a new conserved family of ring-finger proteinsE2-25K mediates US11-triggered retro-translocation of MHC class I heavy chains in a permeabilized cell systemIdentification of proteins that interact with mammalian peptide:N-glycanase and implicate this hydrolase in the proteasome-dependent pathway for protein degradationCdc53/cullin and the essential Hrt1 RING-H2 subunit of SCF define a ubiquitin ligase module that activates the E2 enzyme Cdc34Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality controlRheumatoid arthritis as a hyper-endoplasmic-reticulum-associated degradation diseaseProtein folding and quality control in the ERSelective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradationIntegration of UPRER and oxidative stress signaling in the control of intestinal stem cell proliferationIn vivo action of the HRD ubiquitin ligase complex: mechanisms of endoplasmic reticulum quality control and sterol regulation.Key steps in ERAD of luminal ER proteins reconstituted with purified componentsPreviously unknown role for the ubiquitin ligase Ubr1 in endoplasmic reticulum-associated protein degradation.Recognition of an ERAD-L substrate analyzed by site-specific in vivo photocrosslinking.Sec61p is part of the endoplasmic reticulum-associated degradation machineryProtein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48.A regulatory link between ER-associated protein degradation and the unfolded-protein response.The conserved npl4 protein complex mediates proteasome-dependent membrane-bound transcription factor activation.Determinants of RING-E2 fidelity for Hrd1p, a membrane-anchored ubiquitin ligase.Quality control of inner nuclear membrane proteins by the Asi complex.Membrane topology and function of Der3/Hrd1p as a ubiquitin-protein ligase (E3) involved in endoplasmic reticulum degradation.Analysis of quality control substrates in distinct cellular compartments reveals a unique role for Rpn4p in tolerating misfolded membrane proteins.An HRD/DER-independent ER quality control mechanism involves Rsp5p-dependent ubiquitination and ER-Golgi transportA genomic screen identifies Dsk2p and Rad23p as essential components of ER-associated degradationSubstrate recognition in ER-associated degradation mediated by Eps1, a member of the protein disulfide isomerase familyDfm1 forms distinct complexes with Cdc48 and the ER ubiquitin ligases and is required for ERAD.Degradation of a cytosolic protein requires endoplasmic reticulum-associated degradation machinery.
P2860
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P2860
Der3p/Hrd1p is required for endoplasmic reticulum-associated degradation of misfolded lumenal and integral membrane proteins.
description
1998 nî lūn-bûn
@nan
1998 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
name
Der3p/Hrd1p is required for en ...... nd integral membrane proteins.
@ast
Der3p/Hrd1p is required for en ...... nd integral membrane proteins.
@en
Der3p/Hrd1p is required for en ...... nd integral membrane proteins.
@nl
type
label
Der3p/Hrd1p is required for en ...... nd integral membrane proteins.
@ast
Der3p/Hrd1p is required for en ...... nd integral membrane proteins.
@en
Der3p/Hrd1p is required for en ...... nd integral membrane proteins.
@nl
prefLabel
Der3p/Hrd1p is required for en ...... nd integral membrane proteins.
@ast
Der3p/Hrd1p is required for en ...... nd integral membrane proteins.
@en
Der3p/Hrd1p is required for en ...... nd integral membrane proteins.
@nl
P2093
P2860
P3181
P356
P1476
Der3p/Hrd1p is required for en ...... nd integral membrane proteins.
@en
P2093
P2860
P304
P3181
P356
10.1091/MBC.9.1.209
P407
P577
1998-01-01T00:00:00Z