The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity.
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Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulumTwo cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formationMutations in domain a' of protein disulfide isomerase affect the folding pathway of bovine pancreatic ribonuclease AThe Catalytic Activity of Protein-disulfide Isomerase Requires a Conformationally Flexible MoleculeRoles of protein-disulfide isomerase-mediated disulfide bond formation of yeast Mnl1p in endoplasmic reticulum-associated degradationFunctional characterization of transcriptional regulatory elements in the upstream region of the yeast GLK1 geneGenes that control the fidelity of endoplasmic reticulum to Golgi transport identified as suppressors of vesicle budding mutations.A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation.EndoPDI, a novel protein-disulfide isomerase-like protein that is preferentially expressed in endothelial cells acts as a stress survival factorElevated expression of PDI family proteins during differentiation of mouse F9 teratocarcinoma cellspERp1 is significantly up-regulated during plasma cell differentiation and contributes to the oxidative folding of immunoglobulinThe oxidoreductase ERp57 efficiently reduces partially folded in preference to fully folded MHC class I moleculesIdentification and characterization of two distinct ligand binding regions of cubilinThiol-independent interaction of protein disulphide isomerase with type X collagen during intra-cellular folding and assemblyThe protein disulphide-isomerase family: unravelling a string of folds.Disulfide bond formation in prokaryotes: history, diversity and designCell-surface protein disulfide isomerase catalyzes transnitrosation and regulates intracellular transfer of nitric oxide.Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbABoth the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A2.Saccharomyces cerevisiae HOC1, a suppressor of pkc1, encodes a putative glycosyltransferase.Formation and transfer of disulphide bonds in living cells.Chaperone-like activity of protein disulfide-isomerase in the refolding of rhodanese.PDILT, a divergent testis-specific protein disulfide isomerase with a non-classical SXXC motif that engages in disulfide-dependent interactions in the endoplasmic reticulum.Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin.An unconventional role for cytoplasmic disulfide bonds in vaccinia virus proteins.Estrogen receptor accessory proteins: effects on receptor-DNA interactions.Mechanisms of neuroprotection by protein disulphide isomerase in amyotrophic lateral sclerosis.Protein disulfide isomerases contribute differentially to the endoplasmic reticulum-associated degradation of apolipoprotein B and other substratesPapD chaperone function in pilus biogenesis depends on oxidant and chaperone-like activities of DsbAVersatility of the endoplasmic reticulum protein folding factory.Export of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase.Discovery of an orally active small-molecule irreversible inhibitor of protein disulfide isomerase for ovarian cancer treatment.Both chaperone and isomerase functions of protein disulfide isomerase are essential for acceleration of the oxidative refolding and reactivation of dimeric alkaline protease inhibitorOverproduction or absence of the periplasmic protease DegP severely compromises bacterial growth in the absence of the dithiol: disulfide oxidoreductase DsbAProteomic methods unravel the protein quality control in Escherichia coli.Thioredoxin superfamily and its effects on cardiac physiology and pathology.Heat-shock and redox-dependent functional switching of an h-type Arabidopsis thioredoxin from a disulfide reductase to a molecular chaperone.Extracellular Thiol Isomerases and Their Role in Thrombus FormationERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexinParadoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade.
P2860
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P2860
The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
@zh
1993年论文
@zh-cn
name
The essential function of yeas ...... ide in its isomerase activity.
@en
type
label
The essential function of yeas ...... ide in its isomerase activity.
@en
prefLabel
The essential function of yeas ...... ide in its isomerase activity.
@en
P1433
P1476
The essential function of yeas ...... ide in its isomerase activity.
@en
P2093
LaMantia ML
Lennarz WJ
P304
P356
10.1016/0092-8674(93)90469-7
P407
P577
1993-09-01T00:00:00Z