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

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

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

http://www.wikidata.org/entity/Q22254117

about

A conserved endoplasmic reticulum membrane protein complex (EMC) facilitates phospholipid transfer from the ER to mitochondria Manipulation of oxidative protein folding and PDI redox state in mammalian cells ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family Disulphide production by Ero1α-PDI relay is rapid and effectively regulated ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress Identification and characterization of a novel thioredoxin-related transmembrane protein of the endoplasmic reticulum The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha Thiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44 Unfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1 Oxidative protein folding in eukaryotes: mechanisms and consequences Antioxidant responses and cellular adjustments to oxidative stress Protein disulfide isomerases in neurodegeneration: from disease mechanisms to biomedical applications Disulfide bond formation in the mammalian endoplasmic reticulum Crystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDI Structure of Yeast Sulfhydryl Oxidase Erv1 Reveals Electron Transfer of the Disulfide Relay System in the Mitochondrial Intermembrane Space Domain architecture of protein-disulfide isomerase facilitates its dual role as an oxidase and an isomerase in Ero1p-mediated disulfide formation.Oxidative stress, unfolded protein response, and apoptosis in developmental toxicity ERp57 is a multifunctional thiol-disulfide oxidoreductase Disulfide bonds in ER protein folding and homeostasis Endoplasmic reticulum redox state is not perturbed by pharmacological or pathological endoplasmic reticulum stress in live pancreatic β-cells Endoplasmic reticulum thiol oxidase deficiency leads to ascorbic acid depletion and noncanonical scurvy in mice CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum The cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1-Lalpha Lifetime imaging of a fluorescent protein sensor reveals surprising stability of ER thiol redox ERO1-beta, a pancreas-specific disulfide oxidase, promotes insulin biogenesis and glucose homeostasis Potential role of glutathione in evolution of thiol-based redox signaling sites in proteins Catalysis of Protein Folding by Protein Disulfide Isomerase and Small-Molecule Mimics Genome-scale analysis identifies GJB2 and ERO1LB as prognosis markers in patients with pancreatic cancer.Endoplasmic reticulum stress response in an INS-1 pancreatic beta-cell line with inducible expression of a folding-deficient proinsulin.Oxidative protein folding in vitro: a study of the cooperation between quiescin-sulfhydryl oxidase and protein disulfide isomerase A small molecule inhibitor of endoplasmic reticulum oxidation 1 (ERO1) with selectively reversible thiol reactivity.Transcriptional profiling of chondrodysplasia growth plate cartilage reveals adaptive ER-stress networks that allow survival but disrupt hypertrophy The C-terminal domain of yeast Ero1p mediates membrane localization and is essential for function.Glycoprotein folding in the endoplasmic reticulum.Formation and transfer of disulphide bonds in living cells.Oxidative protein folding and the Quiescin-sulfhydryl oxidase family of flavoproteins.Two conserved cysteine triads in human Ero1alpha cooperate for efficient disulfide bond formation in the endoplasmic reticulum.Glutathione limits Ero1-dependent oxidation in the endoplasmic reticulum.Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Ero1beta.Different interaction modes for protein-disulfide isomerase (PDI) as an efficient regulator and a specific substrate of endoplasmic reticulum oxidoreductin-1α (Ero1α).

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P2860

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

http://www.wikidata.org/entity/Q22254117

description

2000 nî lūn-bûn

@nan

2000 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2000 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2000年の論文

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2000年論文

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2000年論文

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2000年論文

@zh-hk

2000年論文

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2000年論文

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2000年论文

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name

Endoplasmic reticulum oxidored ...... the unfolded protein response

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Endoplasmic reticulum oxidored ...... the unfolded protein response

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Endoplasmic reticulum oxidored ...... the unfolded protein response

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type

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Endoplasmic reticulum oxidored ...... the unfolded protein response

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Endoplasmic reticulum oxidored ...... the unfolded protein response

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Endoplasmic reticulum oxidored ...... the unfolded protein response

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Endoplasmic reticulum oxidored ...... the unfolded protein response

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Endoplasmic reticulum oxidored ...... the unfolded protein response

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Endoplasmic reticulum oxidored ...... the unfolded protein response

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Endoplasmic reticulum oxidored ...... the unfolded protein response

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Endoplasmic reticulum oxidoreductase 1 beta

endoplasmic reticulum