About: ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER

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rdf:type	Item
description	artículu científicu espublizáu en 2008 (ast) vědecký článek publikovaný v roce 2008 (cs) наукова стаття, опублікована в липні 2008 (uk) 2008 թվականի հուլիսին հրատարակված գիտական հոդված (hy) 2008 թուականի Յուլիսին հրատարակուած գիտական յօդուած (hyw) vedecký článok (publikovaný 2008/07/25) (sk) wetenschappelijk artikel (gepubliceerd op 2008/07/25) (nl) مقالة علمية (نشرت في 25-7-2008) (ar) im Juli 2008 veröffentlichter wissenschaftlicher Artikel (de) article publié dans la revue scientifique Science (fr) scientific journal article (en)
publication date	wds:Q28512215-C1FB5A13-45BD-4B53-8FE0-3C3274114CFE
publication date	2008-07-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28512215-402D58CC-BEEA-4BBD-95FE-CB5481B0956D
language of work or name	English
cites work	wds:Q28512215-0D613648-E08A-4F57-AF71-3715B08E32D3 wds:Q28512215-4EE84C05-8B13-4043-99C5-41A921822185 wds:Q28512215-54F94C56-41E6-4D9F-A363-C3BB01865EE5 wds:Q28512215-61A2463F-70A6-40C8-BCA5-545170B7EB5F wds:Q28512215-7F361FA6-D8B8-4E69-B795-911048C764C5 wds:Q28512215-87954287-2B13-4A7E-8CA3-153358A27C5D wds:Q28512215-8C73369E-8668-4DF8-8159-F2D179E23591 wds:Q28512215-A2B01D0C-B453-46F3-A154-B99E46642E90 wds:Q28512215-A802A818-B2C8-482F-97FF-FA9752C79B94 wds:Q28512215-B9A23CC2-6350-4305-9FDF-3A1C95041CFD wds:Q28512215-BAE3AA0D-483D-41F6-81C6-D588674FE8AF wds:Q28512215-C93D3AC9-2646-497D-8382-39F9F5960F29 wds:Q28512215-D3904637-EB6F-4A3D-B299-BA1052DFE8BA wds:Q28512215-DC6DD294-9E5E-4C0C-8FBF-48D4E52E67F3 wds:Q28512215-EB519726-8EB4-482D-96D8-28648F2B3F24 wds:Q28512215-EDB6F1C0-8F1B-4194-8C3C-FEE7EC25017A wds:Q28512215-EFE932E6-029A-4FB6-B826-644A33A7BB32 wds:Q28512215-FBFAA2C2-95A0-4275-8C11-92C2DB0C7940
cites work	Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation Manipulation of oxidative protein folding and PDI redox state in mammalian cells ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for BiP's interactions with unfolded substrates A novel ER alpha-mannosidase-like protein accelerates ER-associated degradation The human protein disulphide isomerase family: substrate interactions and functional properties EDEM accelerates ERAD by preventing aberrant dimer formation of misfolded alpha1-antitrypsin Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin The EDEM and Yos9p families of lectin-like ERAD factors Oxidized redox state of glutathione in the endoplasmic reticulum Dislocation of type I membrane proteins from the ER to the cytosol is sensitive to changes in redox potential ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress Quality control in the endoplasmic reticulum Characterization of the active site cysteine residues of the thioredoxin-like domains of protein disulfide isomerase. The conserved active site proline determines the reducing power of Staphylococcus aureus thioredoxin JPDI, a novel endoplasmic reticulum-resident protein containing both a BiP-interacting J-domain and thioredoxin-like motifs Specific interaction of ERp57 and calnexin determined by NMR spectroscopy and an ER two-hybrid system Uncoupled redox systems in the lumen of the endoplasmic reticulum. Pyridine nucleotides stay reduced in an oxidative environment
author name string	wds:Q28512215-AFFEB7CB-9D25-4E00-8099-B548757E9118 wds:Q28512215-DC141497-179B-4DBE-B01A-5AA769C131E1
OpenCitations bibliographic resource ID	wds:Q28512215-A13FD853-A85C-4E0F-95D0-CCC9AA05F92F
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/881492
author name string	Jun Hoseki Ryo Ushioda
OpenCitations bibliographic resource ID	881492
rdfs:label	ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER (en) ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER (nl) ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER (ast)
skos:prefLabel	ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER (en) ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER (nl) ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER (ast)
name	ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER (en) ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER (nl) ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER (ast)
author	wds:Q28512215-6C9358ED-C549-45A4-A62C-D14FE6B10423 wds:Q28512215-965414F2-9539-4089-9185-E13263BCD830 wds:Q28512215-9D490716-85A4-423B-BC65-38784490AA08 wds:Q28512215-F6181D6C-1EF1-4D3F-8534-B551C754DD80
author	Kazuhiro Nagata Gregor Jansen David Y. Thomas Kazutaka Araki
title	wds:Q28512215-C8614EF0-19E4-467D-8C7D-DA02F0A48EF7
title	ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER (en)
page(s)	wds:Q28512215-C0517D24-1B91-4B59-9443-0E190F57BB81
page(s)	569-572
instance of	wds:Q28512215-E45B26AE-9920-4B44-951B-A7012FA34B1B
instance of	scholarly article
main subject	wds:Q28512215-A68F1833-B491-4C8A-A5B5-8ACC2E3ACE72
main subject	DnaJ heat shock protein family (Hsp40) member C10
PubMed ID	wds:Q28512215-315F0C6A-BD5A-4AD1-B52A-505FDEBDDA2A
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/18653895
PubMed ID	18653895
published in	wds:Q28512215-0A29FC9D-060C-4958-A5FD-242F74894ACC
published in	Science
issue	wds:Q28512215-3BA0873D-95E9-4799-B1A3-C7FDCC2A3E39
volume	wds:Q28512215-A930FBE8-CBD7-4F4B-A513-2F223ADC975B
issue	5888
volume	321
DOI	wds:Q28512215-F46B078A-1C05-4BA1-9C85-F10EDB3EEE1D
DOI	http://dx.doi.org/10.1126/SCIENCE.1159293
DOI	10.1126/SCIENCE.1159293
ResearchGate publication ID	wds:Q28512215-AC6FFFA4-E002-4BA0-8000-039AC20F448D
ResearchGate publication ID	51427301
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28512215
is cites work of	Dysferlin-peptides reallocate mutated dysferlin thereby restoring function

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