The contributions of protein disulfide isomerase and its homologues to oxidative protein folding in the yeast endoplasmic reticulum.
about
Intracellular catalysis of disulfide bond formation by the human sulfhydryl oxidase, QSOX1Human quiescin-sulfhydryl oxidase, QSOX1: probing internal redox steps by mutagenesisEndoplasmic Reticulum Stress and Associated ROSProtein disulfide isomerase and host-pathogen interactionDomain architecture of protein-disulfide isomerase facilitates its dual role as an oxidase and an isomerase in Ero1p-mediated disulfide formation.Protein Oxidative Modifications: Beneficial Roles in Disease and HealthDifferent interaction modes for protein-disulfide isomerase (PDI) as an efficient regulator and a specific substrate of endoplasmic reticulum oxidoreductin-1α (Ero1α).Toxoplasma gondii protein disulfide isomerase (TgPDI) is a novel vaccine candidate against toxoplasmosisThe protein disulfide isomerase 1 of Phytophthora parasitica (PpPDI1) is associated with the haustoria-like structures and contributes to plant infection.Versatility of the endoplasmic reticulum protein folding factory.Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway.Functional relationship between protein disulfide isomerase family members during the oxidative folding of human secretory proteinsProtein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins.Contribution of the HEDJ/ERdj3 cysteine-rich domain to substrate interactions.Cysteine residues in a yeast viral A/B toxin crucially control host cell killing via pH-triggered disulfide rearrangements.PDI improves secretion of redox-inactive beta-glucosidase.Low reduction potential of Ero1alpha regulatory disulphides ensures tight control of substrate oxidation.Catalysis of protein disulfide bond isomerization in a homogeneous substrateThe unfolded protein response is necessary but not sufficient to compensate for defects in disulfide isomerization.Revealing unexpected mechanisms for nucleophilic attack on S-S and Se-Se bridges.Chemistry and Enzymology of Disulfide Cross-Linking in Proteins.Dramatic substituent effects on the mechanisms of nucleophilic attack on Se-S bridges.Effects of signal sequences and folding accessory proteins on extracellular expression of carboxypeptidase Y in recombinant Saccharomyces cerevisiae.
P2860
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P2860
The contributions of protein disulfide isomerase and its homologues to oxidative protein folding in the yeast endoplasmic reticulum.
description
2004 nî lūn-bûn
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2004 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի նոյեմբերին հրատարակված գիտական հոդված
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2004年の論文
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年學術文章
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name
The contributions of protein d ...... e yeast endoplasmic reticulum.
@ast
The contributions of protein d ...... e yeast endoplasmic reticulum.
@en
The contributions of protein d ...... e yeast endoplasmic reticulum.
@nl
type
label
The contributions of protein d ...... e yeast endoplasmic reticulum.
@ast
The contributions of protein d ...... e yeast endoplasmic reticulum.
@en
The contributions of protein d ...... e yeast endoplasmic reticulum.
@nl
prefLabel
The contributions of protein d ...... e yeast endoplasmic reticulum.
@ast
The contributions of protein d ...... e yeast endoplasmic reticulum.
@en
The contributions of protein d ...... e yeast endoplasmic reticulum.
@nl
P2093
P2860
P356
P1476
The contributions of protein d ...... e yeast endoplasmic reticulum.
@en
P2093
Anton Solovyov
Arne Holmgren
Bonney Wilkinson
Hiram F Gilbert
Jakob R Winther
Johanna Lundström-Ljung
Ruoyu Xiao
P2860
P304
P356
10.1074/JBC.M409210200
P407
P577
2004-11-26T00:00:00Z