Eps1, a novel PDI-related protein involved in ER quality control in yeast
about
Human quiescin-sulfhydryl oxidase, QSOX1: probing internal redox steps by mutagenesisUnfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1Domain architecture of protein-disulfide isomerase facilitates its dual role as an oxidase and an isomerase in Ero1p-mediated disulfide formation.Vacuolar cation/H+ antiporters of Saccharomyces cerevisiaeThe Saccharomyces cerevisiae TIF6 gene encoding translation initiation factor 6 is required for 60S ribosomal subunit biogenesis.Interactions among yeast protein-disulfide isomerase proteins and endoplasmic reticulum chaperone proteins influence their activities.Traffic-independent function of the Sar1p/COPII machinery in proteasomal sorting of the cystic fibrosis transmembrane conductance regulatorMolecular interactions of yeast Neo1p, an essential member of the Drs2 family of aminophospholipid translocases, and its role in membrane trafficking within the endomembrane system.Substrate recognition in ER-associated degradation mediated by Eps1, a member of the protein disulfide isomerase familyThe contributions of protein disulfide isomerase and its homologues to oxidative protein folding in the yeast endoplasmic reticulum.Characterization of the Saccharomyces cerevisiae high affinity copper transporter Ctr3.Functional 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.Regulation of intracellular heme levels by HMX1, a homologue of heme oxygenase, in Saccharomyces cerevisiae.Distinct retrieval and retention mechanisms are required for the quality control of endoplasmic reticulum protein folding.A mutant plasma membrane ATPase, Pma1-10, is defective in stability at the yeast cell surface.Formation and transfer of disulphide bonds in living cells.Sphingoid base synthesis is required for oligomerization and cell surface stability of the yeast plasma membrane ATPase, Pma1.Functional characterization of ERp18, a new endoplasmic reticulum-located thioredoxin superfamily member.The yeast Pma1 proton pump: a model for understanding the biogenesis of plasma membrane proteins.Characterization of two second-site mutations preventing wild type protein aggregation caused by a dominant negative PMA1 mutantFor whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection.Biology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.Search and destroy: ER quality control and ER-associated protein degradation.Versatility of the endoplasmic reticulum protein folding factory.Protein disulfides and protein disulfide oxidoreductases in hyperthermophiles.Substrate-specific mediators of ER associated degradation (ERAD).The evolving role of ubiquitin modification in endoplasmic reticulum-associated degradation.Large-scale identification of putative exported proteins in Candida albicans by genetic selection.Pathogenic mutations inactivate parkin by distinct mechanisms.Identification of an Htm1 (EDEM)-dependent, Mns1-independent Endoplasmic Reticulum-associated Degradation (ERAD) pathway in Saccharomyces cerevisiae: application of a novel assay for glycoprotein ERAD.Systematic Optimization of Protein Secretory Pathways in Saccharomyces cerevisiae to Increase Expression of Hepatitis B Small Antigen.Phylogenetic analyses identify 10 classes of the protein disulfide isomerase family in plants, including single-domain protein disulfide isomerase-related proteins.Cytoplasmic Hsp70 promotes ubiquitination for endoplasmic reticulum-associated degradation of a misfolded mutant of the yeast plasma membrane ATPase, PMA1.Effect of EPS1 gene deletion in Saccharomyces cerevisiae on the secretion of foreign proteins which have disulfide bridges.Overexpression of PMA1 enhances tolerance to various types of stress and constitutively activates the SAPK pathways in Saccharomyces cerevisiae.Post-translational import of the prion protein into the endoplasmic reticulum interferes with cell viability: a critical role for the putative transmembrane domain.The degradation pathway of a model misfolded protein is determined by aggregation propensity.Toolbox: Creating a systematic database of secretory pathway proteins uncovers new cargo for COPI.Quality Control in the Yeast Secretory Pathway
P2860
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P2860
Eps1, a novel PDI-related protein involved in ER quality control in yeast
description
1999 nî lūn-bûn
@nan
1999 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
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
name
Eps1, a novel PDI-related protein involved in ER quality control in yeast
@ast
Eps1, a novel PDI-related protein involved in ER quality control in yeast
@en
Eps1, a novel PDI-related protein involved in ER quality control in yeast.
@nl
type
label
Eps1, a novel PDI-related protein involved in ER quality control in yeast
@ast
Eps1, a novel PDI-related protein involved in ER quality control in yeast
@en
Eps1, a novel PDI-related protein involved in ER quality control in yeast.
@nl
prefLabel
Eps1, a novel PDI-related protein involved in ER quality control in yeast
@ast
Eps1, a novel PDI-related protein involved in ER quality control in yeast
@en
Eps1, a novel PDI-related protein involved in ER quality control in yeast.
@nl
P356
P1433
P1476
Eps1, a novel PDI-related protein involved in ER quality control in yeast
@en
P304
P356
10.1093/EMBOJ/18.21.5972
P407
P577
1999-11-01T00:00:00Z