Disulphide production by Ero1α-PDI relay is rapid and effectively regulated - Wikidata - wikimedia - TriplyDB

Disulphide production by Ero1α-PDI relay is rapid and effectively regulated

Disulphide production by Ero1α-PDI relay is rapid and effectively regulated

http://www.wikidata.org/entity/Q24297912

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Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum Protein disulfide isomerases in neurodegeneration: from disease mechanisms to biomedical applications Protein folding and quality control in the ER Disulfide bond formation in the mammalian endoplasmic reticulum Redox regulation in amyotrophic lateral sclerosis Depletion of cyclophilins B and C leads to dysregulation of endoplasmic reticulum redox homeostasis Disulfide bonds in ER protein folding and homeostasis Endoplasmic reticulum thiol oxidase deficiency leads to ascorbic acid depletion and noncanonical scurvy in mice Lifetime imaging of a fluorescent protein sensor reveals surprising stability of ER thiol redox Cancer-associated oxidoreductase ERO1-α promotes immune escape through up-regulation of PD-L1 in human breast cancer.Different interaction modes for protein-disulfide isomerase (PDI) as an efficient regulator and a specific substrate of endoplasmic reticulum oxidoreductin-1α (Ero1α).Thiol-disulfide exchange between the PDI family of oxidoreductases negates the requirement for an oxidase or reductase for each enzyme Ero1-α and PDIs constitute a hierarchical electron transfer network of endoplasmic reticulum oxidoreductases Genetic ablation of N-linked glycosylation reveals two key folding pathways for R345W fibulin-3, a secreted protein associated with retinal degeneration.Identification of protein disulfide isomerase 1 as a key isomerase for disulfide bond formation in apolipoprotein B100.The sarcoplasmic reticulum luminal thiol oxidase ERO1 regulates cardiomyocyte excitation-coupled calcium release and response to hemodynamic load.A novel reaction of peroxiredoxin 4 towards substrates in oxidative protein folding.Balanced Ero1 activation and inactivation establishes ER redox homeostasis Förster resonance energy transfer-based sensor targeting endoplasmic reticulum reveals highly oxidative environment.Cysteines 208 and 241 in Ero1α are required for maximal catalytic turnover Hyperactivity of the Ero1α oxidase elicits endoplasmic reticulum stress but no broad antioxidant response.Novel Roles of the Non-catalytic Elements of Yeast Protein-disulfide Isomerase in Its Interplay with Endoplasmic Reticulum Oxidoreductin 1 Dynamic regulation of Ero1α and peroxiredoxin 4 localization in the secretory pathway.Oxidative protein-folding systems in plant cells.Lack of an efficient endoplasmic reticulum-localized recycling system protects peroxiredoxin IV from hyperoxidation.Biochemical evidence that regulation of Ero1β activity in human cells does not involve the isoform-specific cysteine 262.The oxidative protein folding machinery in plant cells.ER Dysfunction and Protein Folding Stress in ALS.Proteins improving recombinant antibody production in mammalian cells.Redox regulation of protein damage in plasma.Cytosolic thioredoxin reductase 1 is required for correct disulfide formation in the ER.Interplay between redox and protein homeostasis.Ero1-PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum Overexpression of CHOP alone and in combination with chaperones is effective in improving antibody production in mammalian cells.Real-time monitoring of redox changes in the mammalian endoplasmic reticulum.ALS-linked protein disulfide isomerase variants cause motor dysfunction.Kinetic control by limiting glutaredoxin amounts enables thiol oxidation in the reducing mitochondrial intermembrane space.Engineered pathways for correct disulfide bond oxidation.Vitamin K epoxide reductase contributes to protein disulfide formation and redox homeostasis within the endoplasmic reticulum.Intact protein folding in the glutathione-depleted endoplasmic reticulum implicates alternative protein thiol reductants.

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Disulphide production by Ero1α-PDI relay is rapid and effectively regulated

http://www.wikidata.org/entity/Q24297912

description

2010 nî lūn-bûn

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2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2010 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

Disulphide production by Ero1α-PDI relay is rapid and effectively regulated

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Disulphide production by Ero1α-PDI relay is rapid and effectively regulated

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Disulphide production by Ero1α-PDI relay is rapid and effectively regulated

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Disulphide production by Ero1α-PDI relay is rapid and effectively regulated

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type

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Disulphide production by Ero1α-PDI relay is rapid and effectively regulated

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Disulphide production by Ero1α-PDI relay is rapid and effectively regulated

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Disulphide production by Ero1α-PDI relay is rapid and effectively regulated

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Disulphide production by Ero1α-PDI relay is rapid and effectively regulated

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prefLabel

Disulphide production by Ero1α-PDI relay is rapid and effectively regulated

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Disulphide production by Ero1α-PDI relay is rapid and effectively regulated

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Disulphide production by Ero1α-PDI relay is rapid and effectively regulated

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Disulphide production by Ero1α-PDI relay is rapid and effectively regulated

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The EMBO Journal

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Disulphide production by Ero1α-PDI relay is rapid and effectively regulated

@en

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Ester Zito

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

Jan Riemer

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King-Tung Chin

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

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

Domain architecture of protein-disulfide isomerase facilitates its dual role as an oxidase and an isomerase in Ero1p-mediated disulfide formation.

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

Generating disulfides enzymatically: reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p

Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum.

ERp57 is a multifunctional thiol-disulfide oxidoreductase

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3318-29

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scholarly article

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10.1038/EMBOJ.2010.203

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19

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29

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Christian Appenzeller-Herzog

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2010-10-06T00:00:00Z

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46036764

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20802462

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2957208

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