ERp57 is a multifunctional thiol-disulfide oxidoreductase - sprookjes - yvandenbroek - TriplyDB

ERp57 is a multifunctional thiol-disulfide oxidoreductase

ERp57 is a multifunctional thiol-disulfide oxidoreductase

http://www.wikidata.org/entity/Q28243986

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Identification of the PDI-family member ERp90 as an interaction partner of ERFAD Disulphide production by Ero1α-PDI relay is rapid and effectively regulated ERp57 is essential for efficient folding of glycoproteins sharing common structural domains Identification and characterization of a novel thioredoxin-related transmembrane protein of the endoplasmic reticulum Modulation of STIM1 and capacitative Ca2+ entry by the endoplasmic reticulum luminal oxidoreductase ERp57 The human protein disulphide isomerase family: substrate interactions and functional properties The Unfolded Protein Response and the Role of Protein Disulfide Isomerase in Neurodegeneration The Catalytic Activity of Protein-disulfide Isomerase Requires a Conformationally Flexible Molecule (4R)- and (4S)-fluoroproline in the conserved cis-prolyl peptide bond of the thioredoxin fold: tertiary structure context dictates ring puckering Domain architecture of protein-disulfide isomerase facilitates its dual role as an oxidase and an isomerase in Ero1p-mediated disulfide formation.A novel group of glutaredoxins in the cis-Golgi critical for oxidative stress resistance.N-Glycan-based ER Molecular Chaperone and Protein Quality Control System: The Calnexin Binding Cycle Protein disulfide isomerase homolog PDILT is required for quality control of sperm membrane protein ADAM3 and male fertility [corrected].Efficient IgM assembly and secretion require the plasma cell induced endoplasmic reticulum protein pERp1 Distribution of PDIA3 transcript and protein in rat testis and sperm cells Knockdown of ERp57 increases BiP/GRP78 induction and protects against hyperoxia and tunicamycin-induced apoptosis.Platelet protein disulfide isomerase is required for thrombus formation but not for hemostasis in mice Conditional independence mapping of DIGE data reveals PDIA3 protein species as key nodes associated with muscle aerobic capacity.Proteomic profiling of hepatic endoplasmic reticulum-associated proteins in an animal model of insulin resistance and metabolic dyslipidemia.Proteomic identification of secreted proteins as surrogate markers for signal transduction inhibitor activity Novel thioredoxin-related transmembrane protein TMX4 has reductase activity.Glucose-regulated protein 58 modulates β-catenin protein stability in a cervical adenocarcinoma cell line The platelet-surface thiol isomerase enzyme ERp57 modulates platelet function.Structure-function analysis of the endoplasmic reticulum oxidoreductase TMX3 reveals interdomain stabilization of the N-terminal redox-active domain.Ero1-α and PDIs constitute a hierarchical electron transfer network of endoplasmic reticulum oxidoreductases Both platelet- and endothelial cell-derived ERp5 support thrombus formation in a laser-induced mouse model of thrombosis.Dimerization of ERp29, a PDI-like protein, is essential for its diverse functions Protein disulfide isomerase chaperone ERP-57 decreases plasma membrane expression of the human GnRH receptor The disulfide isomerase ERp57 mediates platelet aggregation, hemostasis, and thrombosis Comparison of protein expression profiles of different stages of lymph nodes metastasis in breast cancer Approaches toward High-Mannose-Type Glycan Libraries.Flagging and docking: dual roles for N-glycans in protein quality control and cellular proteostasis.Tyrosinase maturation through the mammalian secretory pathway: bringing color to life.Alg13p, the catalytic subunit of the endoplasmic reticulum UDP-GlcNAc glycosyltransferase, is a target for proteasomal degradation.Oxidative folding and N-terminal cyclization of onconase.How sugars convey information on protein conformation in the endoplasmic reticulum 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 activity Generating an unfoldase from thioredoxin-like domains The quality control of MHC class I peptide loading.The peptide-loading complex--antigen translocation and MHC class I loading.

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P2860

ERp57 is a multifunctional thiol-disulfide oxidoreductase

http://www.wikidata.org/entity/Q28243986

description

2004 nî lūn-bûn

@nan

2004 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2004年の論文

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2004年論文

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2004年論文

@zh-hant

2004年論文

@zh-hk

2004年論文

@zh-mo

2004年論文

@zh-tw

2004年论文

@wuu

name

ERp57 is a multifunctional thiol-disulfide oxidoreductase

@ast

ERp57 is a multifunctional thiol-disulfide oxidoreductase

@en

ERp57 is a multifunctional thiol-disulfide oxidoreductase

@nl

type

label

ERp57 is a multifunctional thiol-disulfide oxidoreductase

@ast

ERp57 is a multifunctional thiol-disulfide oxidoreductase

@en

ERp57 is a multifunctional thiol-disulfide oxidoreductase

@nl

prefLabel

ERp57 is a multifunctional thiol-disulfide oxidoreductase

@ast

ERp57 is a multifunctional thiol-disulfide oxidoreductase

@en

ERp57 is a multifunctional thiol-disulfide oxidoreductase

@nl

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Journal of Biological Chemistry

P1476

ERp57 is a multifunctional thiol-disulfide oxidoreductase

@en

P2093

Ari Helenius

http://www.w3.org/2001/XMLSchema#string

Eva-Maria Frickel

http://www.w3.org/2001/XMLSchema#string

Lars Ellgaard

http://www.w3.org/2001/XMLSchema#string

Marlène Bouvier

http://www.w3.org/2001/XMLSchema#string

Patrick Frei

http://www.w3.org/2001/XMLSchema#string

Rudi Glockshuber

http://www.w3.org/2001/XMLSchema#string

Walter F Stafford

http://www.w3.org/2001/XMLSchema#string

P2860

ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum

Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response

Identification of a novel thioredoxin-related transmembrane protein

Manipulation of oxidative protein folding and PDI redox state in mammalian cells

cDNA cloning and baculovirus expression of the human liver endoplasmic reticulum P58: characterization as a protein disulfide isomerase isoform, but not as a protease or a carnitine acyltransferase

ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress

TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain.

NMR structure of the calreticulin P-domain

The Structure of calnexin, an ER chaperone involved in quality control of protein folding

NMR structures of 36 and 73-residue fragments of the calreticulin P-domain

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18277-87

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scholarly article

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881488

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10.1074/JBC.M314089200

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18

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279

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2004-04-30T00:00:00Z

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8778361

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P698

14871896

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