Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum.
about
ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulumAssociation between the 15-kDa selenoprotein and UDP-glucose:glycoprotein glucosyltransferase in the endoplasmic reticulum of mammalian cellsManipulation of oxidative protein folding and PDI redox state in mammalian cellsA membrane protein complex mediates retro-translocation from the ER lumen into the cytosolDisulphide production by Ero1α-PDI relay is rapid and effectively regulatedRecycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulumIdentification and characterization of a novel thioredoxin-related transmembrane protein of the endoplasmic reticulumTwo pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulumThe CXXCXXC motif determines the folding, structure and stability of human Ero1-LalphaThiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44Yeast flavin-containing monooxygenase generates oxidizing equivalents that control protein folding in the endoplasmic reticulumUnfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1Oxidative protein folding in eukaryotes: mechanisms and consequencesEndoplasmic Reticulum Stress and Associated ROSProgrammed Cell Death Initiation and Execution in Budding YeastProtein disulfide isomerases in neurodegeneration: from disease mechanisms to biomedical applicationsProtein folding and quality control in the EROxidative protein folding: selective pressure for prolamin evolution in riceDisulfide bond formation in the mammalian endoplasmic reticulumIntegration of the unfolded protein and oxidative stress responses through SKN-1/NrfQSOX contains a pseudo-dimer of functional and degenerate sulfhydryl oxidase domainsSteps in reductive activation of the disulfide-generating enzyme Ero1pCrystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDIDomain architecture of protein-disulfide isomerase facilitates its dual role as an oxidase and an isomerase in Ero1p-mediated disulfide formation.Cod1p/Spf1p is a P-type ATPase involved in ER function and Ca2+ homeostasis.A novel group of glutaredoxins in the cis-Golgi critical for oxidative stress resistance.Pbn1p: an essential endoplasmic reticulum membrane protein required for protein processing in the endoplasmic reticulum of budding yeast.The yeast integral membrane protein Apq12 potentially links membrane dynamics to assembly of nuclear pore complexesADD66, a gene involved in the endoplasmic reticulum-associated degradation of alpha-1-antitrypsin-Z in yeast, facilitates proteasome activity and assembly.Yeast ERV2p is the first microsomal FAD-linked sulfhydryl oxidase of the Erv1p/Alrp protein family.The thioredoxin system protects ribosomes against stress-induced aggregationThe contributions of protein disulfide isomerase and its homologues to oxidative protein folding in the yeast endoplasmic reticulum.The Ca2+ homeostasis defects in a pgm2Delta strain of Saccharomyces cerevisiae are caused by excessive vacuolar Ca2+ uptake mediated by the Ca2+-ATPase Pmc1p.Generating disulfides enzymatically: reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1pComprehensive characterization of genes required for protein folding in the endoplasmic reticulumFunctional differences in yeast protein disulfide isomerases.A screen for genes of heme uptake identifies the FLC family required for import of FAD into the endoplasmic reticulum.HRD4/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins.A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation.Depletion of cyclophilins B and C leads to dysregulation of endoplasmic reticulum redox homeostasis
P2860
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P2860
Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum.
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年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Ero1p: a novel and ubiquitous ...... in the endoplasmic reticulum.
@ast
Ero1p: a novel and ubiquitous ...... in the endoplasmic reticulum.
@en
Ero1p: a novel and ubiquitous ...... in the endoplasmic reticulum.
@nl
type
label
Ero1p: a novel and ubiquitous ...... in the endoplasmic reticulum.
@ast
Ero1p: a novel and ubiquitous ...... in the endoplasmic reticulum.
@en
Ero1p: a novel and ubiquitous ...... in the endoplasmic reticulum.
@nl
prefLabel
Ero1p: a novel and ubiquitous ...... in the endoplasmic reticulum.
@ast
Ero1p: a novel and ubiquitous ...... in the endoplasmic reticulum.
@en
Ero1p: a novel and ubiquitous ...... in the endoplasmic reticulum.
@nl
P2093
P1433
P1476
Ero1p: a novel and ubiquitous ...... in the endoplasmic reticulum.
@en
P2093
J S Weissman
K J Travers
M G Pollard
P304
P356
10.1016/S1097-2765(00)80018-0
P407
P577
1998-01-01T00:00:00Z