Exploration of the topological requirements of ERAD identifies Yos9p as a lectin sensor of misfolded glycoproteins in the ER lumen.
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Endoplasmic reticulum (ER) mannosidase I is compartmentalized and required for N-glycan trimming to Man5-6GlcNAc2 in glycoprotein ER-associated degradationA ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradationSGTA recognizes a noncanonical ubiquitin-like domain in the Bag6-Ubl4A-Trc35 complex to promote endoplasmic reticulum-associated degradationThe MRH protein Erlectin is a member of the endoplasmic reticulum synexpression group and functions in N-glycan recognitionOS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERADHuman OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycansHuman XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiPERdj4 and ERdj5 are required for endoplasmic reticulum-associated protein degradation of misfolded surfactant protein CA dual task for the Xbp1-responsive OS-9 variants in the mammalian endoplasmic reticulum: inhibiting secretion of misfolded protein conformers and enhancing their disposalDiversity of degradation signals in the ubiquitin-proteasome systemInhibition of p97-dependent protein degradation by Eeyarestatin IOne step at a time: endoplasmic reticulum-associated degradationUbiquitination of serine, threonine, or lysine residues on the cytoplasmic tail can induce ERAD of MHC-I by viral E3 ligase mK3Recent technical developments in the study of ER-associated degradationSelective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradationGRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulumStructural and Biochemical Basis of Yos9 Protein Dimerization and Possible Contribution to Self-association of 3-Hydroxy-3-methylglutaryl-Coenzyme A Reductase Degradation Ubiquitin-Ligase ComplexRecognition of an ERAD-L substrate analyzed by site-specific in vivo photocrosslinking.A Cdc48p-associated factor modulates endoplasmic reticulum-associated degradation, cell stress, and ubiquitinated protein homeostasisDefining the glycan destruction signal for endoplasmic reticulum-associated degradationRoles of protein-disulfide isomerase-mediated disulfide bond formation of yeast Mnl1p in endoplasmic reticulum-associated degradationThe ER-associated degradation component Der1p and its homolog Dfm1p are contained in complexes with distinct cofactors of the ATPase Cdc48pA novel role for Gtb1p in glucose trimming of N-linked glycans.Yos9p assists in the degradation of certain nonglycosylated proteins from the endoplasmic reticulumRetrotranslocation of a misfolded luminal ER protein by the ubiquitin-ligase Hrd1p.Yos9p and Hrd1p mediate ER retention of misfolded proteins for ER-associated degradation.Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulumAssociation of the SEL1L protein transmembrane domain with HRD1 ubiquitin ligase regulates ERAD-LCyclosporine A-sensitive, cyclophilin B-dependent endoplasmic reticulum-associated degradationEDEM2 and OS-9 are required for ER-associated degradation of non-glycosylated sonic hedgehog.Usa1 protein facilitates substrate ubiquitylation through two separate domainsFree oligosaccharides to monitor glycoprotein endoplasmic reticulum-associated degradation in Saccharomyces cerevisiaeUsa1p is required for optimal function and regulation of the Hrd1p endoplasmic reticulum-associated degradation ubiquitin ligase.Modularity of the Hrd1 ERAD complex underlies its diverse client range.The endoplasmic reticulum-associated degradation of the epithelial sodium channel requires a unique complement of molecular chaperones.OS-9 facilitates turnover of nonnative GRP94 marked by hyperglycosylation.Misfolded proteins induce aggregation of the lectin Yos9.Imbalance of heterologous protein folding and disulfide bond formation rates yields runaway oxidative stress.Proteomic analysis of solid pseudopapillary tumor of the pancreas reveals dysfunction of the endoplasmic reticulum protein processing pathwayThe Unfolded Protein Response, Degradation from Endoplasmic Reticulum and Cancer
P2860
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P2860
Exploration of the topological requirements of ERAD identifies Yos9p as a lectin sensor of misfolded glycoproteins in the ER lumen.
description
2005 nî lūn-bûn
@nan
2005 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Exploration of the topological ...... glycoproteins in the ER lumen.
@ast
Exploration of the topological ...... glycoproteins in the ER lumen.
@en
Exploration of the topological ...... glycoproteins in the ER lumen.
@nl
type
label
Exploration of the topological ...... glycoproteins in the ER lumen.
@ast
Exploration of the topological ...... glycoproteins in the ER lumen.
@en
Exploration of the topological ...... glycoproteins in the ER lumen.
@nl
altLabel
Exploration of the topological ...... glycoproteins in the ER lumen
@en
prefLabel
Exploration of the topological ...... glycoproteins in the ER lumen.
@ast
Exploration of the topological ...... glycoproteins in the ER lumen.
@en
Exploration of the topological ...... glycoproteins in the ER lumen.
@nl
P2093
P1433
P1476
Exploration of the topological ...... glycoproteins in the ER lumen.
@en
P2093
Arunashree Bhamidipati
Erin M Quan
Vladimir Denic
P304
P356
10.1016/J.MOLCEL.2005.07.027
P407
P577
2005-09-16T00:00:00Z