The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase.
about
Human quiescin-sulfhydryl oxidase, QSOX1: probing internal redox steps by mutagenesisMapping of residues forming the voltage sensor of the voltage-dependent anion-selective channelVma21p is a yeast membrane protein retained in the endoplasmic reticulum by a di-lysine motif and is required for the assembly of the vacuolar H(+)-ATPase complexDomain architecture of protein-disulfide isomerase facilitates its dual role as an oxidase and an isomerase in Ero1p-mediated disulfide formation.The FKB2 gene of Saccharomyces cerevisiae, encoding the immunosuppressant-binding protein FKBP-13, is regulated in response to accumulation of unfolded proteins in the endoplasmic reticulumInteractions among yeast protein-disulfide isomerase proteins and endoplasmic reticulum chaperone proteins influence their activities.VMA12 encodes a yeast endoplasmic reticulum protein required for vacuolar H+-ATPase assemblySSI1 encodes a novel Hsp70 of the Saccharomyces cerevisiae endoplasmic reticulum.Different subcellular localization of Saccharomyces cerevisiae HMG-CoA reductase isozymes at elevated levels corresponds to distinct endoplasmic reticulum membrane proliferations.A novel Hsp70 of the yeast ER lumen is required for the efficient translocation of a number of protein precursorsDer1, a novel protein specifically required for endoplasmic reticulum degradation in yeastN-Glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase yscY in yeast.Substrate recognition in ER-associated degradation mediated by Eps1, a member of the protein disulfide isomerase familyA homolog of voltage-gated Ca(2+) channels stimulated by depletion of secretory Ca(2+) in yeastVma22p is a novel endoplasmic reticulum-associated protein required for assembly of the yeast vacuolar H(+)-ATPase complexThe contributions of protein disulfide isomerase and its homologues to oxidative protein folding in the yeast endoplasmic reticulum.Functional differences in yeast protein disulfide isomerases.Shr3p mediates specific COPII coatomer-cargo interactions required for the packaging of amino acid permeases into ER-derived transport vesiclesHut1 proteins identified in Saccharomyces cerevisiae and Schizosaccharomyces pombe are functional homologues involved in the protein-folding process at the endoplasmic reticulum.Early steps in assembly of the yeast vacuolar H+-ATPaseMutation of yeast Eug1p CXXS active sites to CXXC results in a dramatic increase in protein disulphide isomerase activityCaBP2 is a rat homolog of ERp72 with proteindisulfide isomerase activityCatalysis of Protein Folding by Protein Disulfide Isomerase and Small-Molecule MimicsProduction of soluble and active transferrin receptor-targeting single-chain antibody using Saccharomyces cerevisiae.The protein disulphide-isomerase family: unravelling a string of folds.Formation and transfer of disulphide bonds in living cells.Characterization of the EYE2 gene required for eyespot assembly in Chlamydomonas reinhardtiiAcid-denatured Green Fluorescent Protein (GFP) as model substrate to study the chaperone activity of protein disulfide isomeraseBalanced Ero1 activation and inactivation establishes ER redox homeostasisBiology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.Nuclear congression and membrane fusion: two distinct events in the yeast karyogamy pathway.Assembly of ER-associated protein degradation in vitro: dependence on cytosol, calnexin, and ATP.Versatility 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.The unfolded protein response regulates multiple aspects of secretory and membrane protein biogenesis and endoplasmic reticulum quality control.The endoplasmic reticulum-associated degradation pathways of budding yeast.Genomic-scale comparison of sequence- and structure-based methods of function prediction: does structure provide additional insight?Emerging roles for the pro-oncogenic anterior gradient-2 in cancer development.Endoplasmic reticulum stress-induced mRNA splicing permits synthesis of transcription factor Hac1p/Ern4p that activates the unfolded protein responseThe CXXC motif: imperatives for the formation of native disulfide bonds in the cell.
P2860
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P2860
The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
The yeast EUG1 gene encodes an ...... o protein disulfide isomerase.
@en
The yeast EUG1 gene encodes an ...... o protein disulfide isomerase.
@nl
type
label
The yeast EUG1 gene encodes an ...... o protein disulfide isomerase.
@en
The yeast EUG1 gene encodes an ...... o protein disulfide isomerase.
@nl
prefLabel
The yeast EUG1 gene encodes an ...... o protein disulfide isomerase.
@en
The yeast EUG1 gene encodes an ...... o protein disulfide isomerase.
@nl
P2860
P356
P1476
The yeast EUG1 gene encodes an ...... o protein disulfide isomerase.
@en
P2093
C Tachibana
T H Stevens
P2860
P304
P356
10.1128/MCB.12.10.4601
P407
P577
1992-10-01T00:00:00Z