The oxidoreductase ERp57 efficiently reduces partially folded in preference to fully folded MHC class I molecules
about
ERp57 is essential for efficient folding of glycoproteins sharing common structural domainsN-linked sugar-regulated protein folding and quality control in the ERWhat is the role of alternate splicing in antigen presentation by major histocompatibility complex class I molecules?ERp57 is a multifunctional thiol-disulfide oxidoreductaseEffects of UVB-induced oxidative stress on protein expression and specific protein oxidation in normal human epithelial keratinocytes: a proteomic approachProtein disulfide isomerase homolog PDILT is required for quality control of sperm membrane protein ADAM3 and male fertility [corrected].pERp1 is significantly up-regulated during plasma cell differentiation and contributes to the oxidative folding of immunoglobulinDifferential cooperative enzymatic activities of protein disulfide isomerase family in protein folding.Genes and proteins differentially expressed during in vitro malignant transformation of bovine pancreatic duct cells.The platelet-surface thiol isomerase enzyme ERp57 modulates platelet function.Mixed-disulfide folding intermediates between thyroglobulin and endoplasmic reticulum resident oxidoreductases ERp57 and protein disulfide isomerase.Protein disulfide isomerase chaperone ERP-57 decreases plasma membrane expression of the human GnRH receptorVersatility of the endoplasmic reticulum protein folding factory.Ca2+-dependent redox modulation of SERCA 2b by ERp57.The redox activity of ERp57 is not essential for its functions in MHC class I peptide loading.Pathogen evasion strategies for the major histocompatibility complex class I assembly pathway.ERp57 does not require interactions with calnexin and calreticulin to promote assembly of class I histocompatibility molecules, and it enhances peptide loading independently of its redox activityThe quality control of MHC class I peptide loading.Polymorphisms in the F Pocket of HLA-B27 Subtypes Strongly Affect Assembly, Chaperone Interactions, and Heavy-Chain Misfolding.Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins.Formation of a major histocompatibility complex class I tapasin disulfide indicates a change in spatial organization of the peptide-loading complex during assembly.Major histocompatibility complex class I-ERp57-tapasin interactions within the peptide-loading complex.Heat Shock Protein member A2 forms a stable complex with angiotensin converting enzyme and protein disulfide isomerase A6 in human spermatozoa.Functions of ERp57 in the folding and assembly of major histocompatibility complex class I molecules.Competition for access to the rat major histocompatibility complex class I peptide-loading complex reveals optimization of peptide cargo in the absence of transporter associated with antigen processing (TAP) association.Formation of HLA-B27 homodimers and their relationship to assembly kinetics.Novel anti-thrombotic agent for modulation of protein disulfide isomerase family member ERp57 for prophylactic therapy.Glutathione is required to regulate the formation of native disulfide bonds within proteins entering the secretory pathway.Mutational analysis of the oxidoreductase ERp57 reveals the importance of the two central residues in the redox motif.Discovery of a Novel ERp57 Inhibitor as Antiplatelet Agent from Danshen (Salvia miltiorrhiza).
P2860
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P2860
The oxidoreductase ERp57 efficiently reduces partially folded in preference to fully folded MHC class I molecules
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2002 nî lūn-bûn
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2002 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հունիսին հրատարակված գիտական հոդված
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2002年の論文
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2002年論文
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2002年論文
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2002年論文
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2002年論文
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2002年論文
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2002年论文
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The oxidoreductase ERp57 effic ...... y folded MHC class I molecules
@ast
The oxidoreductase ERp57 effic ...... y folded MHC class I molecules
@en
The oxidoreductase ERp57 effic ...... y folded MHC class I molecules
@nl
type
label
The oxidoreductase ERp57 effic ...... y folded MHC class I molecules
@ast
The oxidoreductase ERp57 effic ...... y folded MHC class I molecules
@en
The oxidoreductase ERp57 effic ...... y folded MHC class I molecules
@nl
prefLabel
The oxidoreductase ERp57 effic ...... y folded MHC class I molecules
@ast
The oxidoreductase ERp57 effic ...... y folded MHC class I molecules
@en
The oxidoreductase ERp57 effic ...... y folded MHC class I molecules
@nl
P2093
P2860
P50
P356
P1433
P1476
The oxidoreductase ERp57 effic ...... y folded MHC class I molecules
@en
P2093
Andrew Osborne
Magnus Alphey
Stuart Ford
P2860
P304
P356
10.1093/EMBOJ/21.11.2655
P407
P577
2002-06-01T00:00:00Z