Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Ero1beta. - Wikidata - awgldk - TriplyDB

Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Ero1beta.

Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Ero1beta.

http://www.wikidata.org/entity/Q34433364

about

Disulphide production by Ero1α-PDI relay is rapid and effectively regulated Protein disulfide isomerases in neurodegeneration: from disease mechanisms to biomedical applications Protein folding and quality control in the ER Crystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDI Endoplasmic reticulum redox state is not perturbed by pharmacological or pathological endoplasmic reticulum stress in live pancreatic β-cells ERO1-beta, a pancreas-specific disulfide oxidase, promotes insulin biogenesis and glucose homeostasis 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.Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin.Mutations in the FAD binding domain cause stress-induced misoxidation of the endoplasmic reticulum oxidoreductase Ero1beta.Disulfide transfer between two conserved cysteine pairs imparts selectivity to protein oxidation by Ero1 Activation of endoplasmic reticulum stress response during the development of ischemic heart disease.The interaction of thioredoxin with Txnip. Evidence for formation of a mixed disulfide by disulfide exchange.Secretion of the adipocyte-specific secretory protein adiponectin critically depends on thiol-mediated protein retention.A developmentally regulated chaperone complex for the endoplasmic reticulum of male haploid germ cells Adiponectin secretion is regulated by SIRT1 and the endoplasmic reticulum oxidoreductase Ero1-L alpha.Molecular Characterization of Endoplasmic Reticulum Oxidoreductin 1 from Bombyx mori Hyperactivity of the Ero1α oxidase elicits endoplasmic reticulum stress but no broad antioxidant response.A novel disulphide switch mechanism in Ero1alpha balances ER oxidation in human cells Human pancreas-specific protein disulfide isomerase homolog (PDIp) is an intracellular estrogen-binding protein that modulates estrogen levels and actions in target cells Protein folding includes oligomerization - examples from the endoplasmic reticulum and cytosol.Oxidative protein-folding systems in plant cells.Biochemical evidence that regulation of Ero1β activity in human cells does not involve the isoform-specific cysteine 262.Oxidative protein folding in the endoplasmic reticulum: tight links to the mitochondria-associated membrane (MAM).Disulfide bond formation network in the three biological kingdoms, bacteria, fungi and mammals.Protein secretion and the endoplasmic reticulum.Deregulation of pancreas-specific oxidoreductin ERO1β in the pathogenesis of diabetes mellitus.Identification and characterization of GmPDIL7, a soybean ER membrane-bound protein disulfide isomerase family protein.Ero1-PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum PDIp is a major intracellular oestrogen-storage protein that modulates tissue levels of oestrogen in the pancreas.Highly efficient adenoviral transduction of pancreatic islets using a microfluidic device.Ero1alpha requires oxidizing and normoxic conditions to localize to the mitochondria-associated membrane (MAM).New insights into oxidative folding.Disulfide-dependent protein folding is linked to operation of the vitamin K cycle in the endoplasmic reticulum. A protein disulfide isomerase-VKORC1 redox enzyme complex appears to be responsible for vitamin K1 2,3-epoxide reduction.Low reduction potential of Ero1alpha regulatory disulphides ensures tight control of substrate oxidation.Human ER Oxidoreductin-1α (Ero1α) Undergoes Dual Regulation through Complementary Redox Interactions with Protein-Disulfide Isomerase.Disulfide bond formation activity of soybean quiescin sulfhydryl oxidase.Polyamine Metabolism and Oxidative Protein Folding in the ER as ROS-Producing Systems Neglected in Virology.CCAAT/enhancer binding protein homologous protein knockdown alleviates hypoxia-induced myocardial injury in rat cardiomyocytes exposed to high glucose.

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Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Ero1beta.

http://www.wikidata.org/entity/Q34433364

description

2005 nî lūn-bûn

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2005 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2005 թվականի հուլիսին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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name

Tissue-specific expression and ...... culum oxidoreductase Ero1beta.

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Tissue-specific expression and ...... culum oxidoreductase Ero1beta.

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Tissue-specific expression and ...... culum oxidoreductase Ero1beta.

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type

label

Tissue-specific expression and ...... culum oxidoreductase Ero1beta.

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Tissue-specific expression and ...... culum oxidoreductase Ero1beta.

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Tissue-specific expression and ...... culum oxidoreductase Ero1beta.

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prefLabel

Tissue-specific expression and ...... culum oxidoreductase Ero1beta.

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Tissue-specific expression and ...... culum oxidoreductase Ero1beta.

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Tissue-specific expression and ...... culum oxidoreductase Ero1beta.

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P1433

Journal of Biological Chemistry

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Tissue-specific expression and ...... culum oxidoreductase Ero1beta.

@en

P2093

Adam M Benham

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

Adrian Lapthorn

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

Christine Dunne

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

David Scoones

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

J A Gareth Williams

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

Jacob Gubbens

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

Marcel van Lith

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

Neil J Bulleid

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

Ritu Kataky

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

Sanjika Dias-Gunasekara

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

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

XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor

ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family

Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum

The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha

Unfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1

The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum.

Functional differences in yeast protein disulfide isomerases.

P304

33066-33075

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10.1074/JBC.M505023200

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P433

38

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280

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2005-07-12T00:00:00Z

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16012172

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P921

endoplasmic reticulum