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

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

http://www.wikidata.org/entity/Q24292308

about

The human protein disulfide isomerase gene family Sequential steps and checkpoints in the early exocytic compartment during secretory IgM biogenesis The protein disulfide isomerase AGR2 is essential for production of intestinal mucus 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 human protein disulphide isomerase family: substrate interactions and functional properties 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 Crystal structure of human ERp44 shows a dynamic functional modulation by its carboxy-terminal tail NMR structures of the selenoproteins Sep15 and SelM reveal redox activity of a new thioredoxin-like family.Interactions among yeast protein-disulfide isomerase proteins and endoplasmic reticulum chaperone proteins influence their activities.ERp19 and ERp46, new members of the thioredoxin family of endoplasmic reticulum proteins The branched-chain aminotransferase proteins: novel redox chaperones for protein disulfide isomerase--implications in Alzheimer's disease Disulfide bonds in ER protein folding and homeostasis Insulin biosynthetic interaction network component, TMEM24, facilitates insulin reserve pool release Epididymis response partly compensates for spermatozoa oxidative defects in snGPx4 and GPx5 double mutant mice Catalysis of Protein Folding by Protein Disulfide Isomerase and Small-Molecule Mimics Low intensity focused ultrasound (LOFU) modulates unfolded protein response and sensitizes prostate cancer to 17AAG.The trypanosome transcriptome is remodelled during differentiation but displays limited responsiveness within life stages.Acute ablation of PERK results in ER dysfunctions followed by reduced insulin secretion and cell proliferation.Mixed-disulfide folding intermediates between thyroglobulin and endoplasmic reticulum resident oxidoreductases ERp57 and protein disulfide isomerase.Panobinostat synergizes with bortezomib to induce endoplasmic reticulum stress and ubiquitinated protein accumulation in renal cancer cells.Formation and transfer of disulphide bonds in living cells.Functional characterization of ERp18, a new endoplasmic reticulum-located thioredoxin superfamily member.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.PDILT, a divergent testis-specific protein disulfide isomerase with a non-classical SXXC motif that engages in disulfide-dependent interactions in the endoplasmic reticulum.Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Ero1beta.Drosophila vitelline membrane assembly: a critical role for an evolutionarily conserved cysteine in the "VM domain" of sV23.Progressive quality control of secretory proteins in the early secretory compartment by ERp44 A molecular specificity code for the three mammalian KDEL receptors.Proteins of the PDI family: unpredicted non-ER locations and functions.Endoplasmic reticulum resident protein 44 (ERp44) deficiency in mice and zebrafish leads to cardiac developmental and functional defects A dynamic study of protein secretion and aggregation in the secretory pathway.The making of a professional secretory cell: architectural and functional changes in the ER during B lymphocyte plasma cell differentiation.Golgi and related vesicle proteomics: simplify to identify.Novel roles for protein disulphide isomerase in disease states: a double edged sword?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

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P2860

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

http://www.wikidata.org/entity/Q24292308

description

2002 nî lūn-bûn

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2002 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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2002 թվականի փետրվարին 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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name

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

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

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

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

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type

label

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

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

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

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

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prefLabel

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

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

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

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

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P1433

The EMBO Journal

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

@en

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Alexandre Mezghrani

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

Angela Bachi

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Fabio Talamo

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Thomas Simmen

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

P2860

Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors

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

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

Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels

SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling

Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites

Functional differences in yeast protein disulfide isomerases.

Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation

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835-44

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scholarly article

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557225

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10.1093/EMBOJ/21.4.835

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P433

4

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21

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Massimo Alessio

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2002-02-15T00:00:00Z

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11514436

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11847130

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P921

cell redox homeostasis

Endoplasmic reticulum protein 44

endoplasmic reticulum

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125352

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