Export of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase.
about
A membrane protein complex mediates retro-translocation from the ER lumen into the cytosolRole of ubiquilin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell deathERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stressProtein disulphide isomerase is required for signal peptide peptidase-mediated protein degradationSecretory defect and cytotoxicity: the potential disease mechanisms for the retinitis pigmentosa (RP)-associated interphotoreceptor retinoid-binding protein (IRBP)The CXXCXXC motif determines the folding, structure and stability of human Ero1-LalphaFolding-competent and folding-defective forms of ricin A chain have different fates after retrotranslocation from the endoplasmic reticulumOne step at a time: endoplasmic reticulum-associated degradationPNG1, a yeast gene encoding a highly conserved peptide:N-glycanaseUnfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality controlThe protein translocation channel mediates glycopeptide export across the endoplasmic reticulum membraneCrystal structure and functional analysis of Drosophila Wind, a protein-disulfide isomerase-related proteinRoles of protein-disulfide isomerase-mediated disulfide bond formation of yeast Mnl1p in endoplasmic reticulum-associated degradationSubstrate recognition in ER-associated degradation mediated by Eps1, a member of the protein disulfide isomerase familyA Complex of Htm1 and the Oxidoreductase Pdi1 Accelerates Degradation of Misfolded Glycoproteins.Yos9p and Hrd1p mediate ER retention of misfolded proteins for ER-associated degradation.Functional differences in yeast protein disulfide isomerases.Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulumRoles of molecular chaperones in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD)ER chaperones in mammalian development and human diseasesChaperones ameliorate beta cell dysfunction associated with human islet amyloid polypeptide overexpressionProteomic analysis of MG132-treated germinating pollen reveals expression signatures associated with proteasome inhibitionThe endoplasmic reticulum-associated degradation of the epithelial sodium channel requires a unique complement of molecular chaperones.Role of intramembrane charged residues in the quality control of unassembled T-cell receptor alpha-chains at the endoplasmic reticulumProtein disulfide isomerases exploit synergy between catalytic and specific binding domains.Emerging features of ER resident J-proteins in plants.Glycoprotein folding in the endoplasmic reticulum.Protein Disulfide Isomerase Superfamily in Disease and the Regulation of ApoptosisUncoupling retro-translocation and degradation in the ER-associated degradation of a soluble protein.For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection.Proteasome 19S RP binding to the Sec61 channel plays a key role in ERAD.Dependence of endoplasmic reticulum-associated degradation on the peptide binding domain and concentration of BiP.Protein disulfide isomerases contribute differentially to the endoplasmic reticulum-associated degradation of apolipoprotein B and other substratesBiology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.Beyond transcription--new mechanisms for the regulation of molecular chaperones.Search and destroy: ER quality control and ER-associated protein degradation.PDI reductase acts on Akita mutant proinsulin to initiate retrotranslocation along the Hrd1/Sel1L-p97 axis.Versatility of the endoplasmic reticulum protein folding factory.Hsp70 molecular chaperone facilitates endoplasmic reticulum-associated protein degradation of cystic fibrosis transmembrane conductance regulator in yeast.
P2860
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P2860
Export of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh
1999年學術文章
@zh-hant
name
Export of a cysteine-free misf ...... h protein disulfide isomerase.
@ast
Export of a cysteine-free misf ...... h protein disulfide isomerase.
@en
type
label
Export of a cysteine-free misf ...... h protein disulfide isomerase.
@ast
Export of a cysteine-free misf ...... h protein disulfide isomerase.
@en
prefLabel
Export of a cysteine-free misf ...... h protein disulfide isomerase.
@ast
Export of a cysteine-free misf ...... h protein disulfide isomerase.
@en
P2093
P2860
P356
P1476
Export of a cysteine-free misf ...... h protein disulfide isomerase.
@en
P2093
F J de La Cruz
W J Lennarz
P2860
P304
P356
10.1083/JCB.147.7.1443
P407
P577
1999-12-01T00:00:00Z