Structural basis of an ERAD pathway mediated by the ER-resident protein disulfide reductase ERdj5 - Wikidata - awgldk - TriplyDB

Structural basis of an ERAD pathway mediated by the ER-resident protein disulfide reductase ERdj5

Structural basis of an ERAD pathway mediated by the ER-resident protein disulfide reductase ERdj5

http://www.wikidata.org/entity/Q27666741

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Identification of the PDI-family member ERp90 as an interaction partner of ERFAD ERdj5 is the ER reductase that catalyzes the removal of non-native disulfides and correct folding of the LDL receptor An interaction map of endoplasmic reticulum chaperones and foldases Unfolded Protein Response and Macroautophagy in Alzheimer's, Parkinson's and Prion Diseases Protein folding and quality control in the ER Molecular chaperones in targeting misfolded proteins for ubiquitin-dependent degradation Disulfide bond formation in the mammalian endoplasmic reticulum Mechanisms and models of endoplasmic reticulum stress in chondrodysplasia The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology Co- and Post-Translational Protein Folding in the ER A bacterial toxin and a nonenveloped virus hijack ER-to-cytosol membrane translocation pathways to cause disease ERdj4 protein is a soluble endoplasmic reticulum (ER) DnaJ family protein that interacts with ER-associated degradation machinery Redox regulation in the endoplasmic reticulum.ER stress in retinal degeneration in S334ter Rho rats.An additional function of the rough endoplasmic reticulum protein complex prolyl 3-hydroxylase 1·cartilage-associated protein·cyclophilin B: the CXXXC motif reveals disulfide isomerase activity in vitro.Thiol-disulfide exchange between the PDI family of oxidoreductases negates the requirement for an oxidase or reductase for each enzyme Retarded PDI diffusion and a reductive shift in poise of the calcium depleted endoplasmic reticulum Protein disulfide isomerases contribute differentially to the endoplasmic reticulum-associated degradation of apolipoprotein B and other substrates Members of the Hsp70 Family Recognize Distinct Types of Sequences to Execute ER Quality Control.A Novel Interacting Protein SERP1 Regulates the N-Linked Glycosylation and Function of GLP-1 Receptor in the Liver.Cleaning up: ER-associated degradation to the rescue.Thyroglobulin From Molecular and Cellular Biology to Clinical Endocrinology.The ERdj5-Sel1L complex facilitates cholera toxin retrotranslocation ERdj3 regulates BiP occupancy in living cells.The Grp170 nucleotide exchange factor executes a key role during ERAD of cellular misfolded clients.How early studies on secreted and membrane protein quality control gave rise to the ER associated degradation (ERAD) pathway: the early history of ERAD.Redox-assisted regulation of Ca2+ homeostasis in the endoplasmic reticulum by disulfide reductase ERdj5.CD4 and BST-2/tetherin proteins retro-translocate from endoplasmic reticulum to cytosol as partially folded and multimeric molecules.Endoplasmic reticulum-dependent redox reactions control endoplasmic reticulum-associated degradation and pathogen entry.Disulfide bond formation network in the three biological kingdoms, bacteria, fungi and mammals.Protein secretion and the endoplasmic reticulum.The Role of Lectin-Carbohydrate Interactions in the Regulation of ER-Associated Protein Degradation.Cytosolic thioredoxin reductase 1 is required for correct disulfide formation in the ER.ERdj5 Reductase Cooperates with Protein Disulfide Isomerase To Promote Simian Virus 40 Endoplasmic Reticulum Membrane Translocation The co-chaperone and reductase ERdj5 facilitates rod opsin biogenesis and quality control.Quality control of glycoprotein folding and ERAD: the role of N-glycan handling, EDEM1 and OS-9.Ero1-PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum Development of a stable ERroGFP variant suitable for monitoring redox dynamics in the ER.A nucleotide exchange factor promotes endoplasmic reticulum-to-cytosol membrane penetration of the nonenveloped virus simian virus 40.Varicella-zoster virus glycoprotein expression differentially induces the unfolded protein response in infected cells.

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Structural basis of an ERAD pathway mediated by the ER-resident protein disulfide reductase ERdj5

http://www.wikidata.org/entity/Q27666741

description

2011 nî lūn-bûn

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2011 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի փետրվարին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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Structural basis of an ERAD pa ...... tein disulfide reductase ERdj5

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J.MOLCEL.2011.01.021

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Structural basis of an ERAD pa ...... tein disulfide reductase ERdj5

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Jun Hoseki

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Kazuhiro Nagata

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Kazutaka Araki

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Ken-Ichi Maegawa

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Kenji Inaba

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Mamoru Suzuki

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Masatoshi Hagiwara

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Ryo Ushioda

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Yushi Matsumoto

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432-44

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scholarly article

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881486

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10.1016/J.MOLCEL.2011.01.021

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4

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41

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2011-02-18T00:00:00Z

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21329881

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