| pubmed-article:18653895 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18653895 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:18653895 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
| pubmed-article:18653895 | lifeskim:mentions | umls-concept:C1539295 | lld:lifeskim |
| pubmed-article:18653895 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
| pubmed-article:18653895 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:18653895 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:18653895 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:18653895 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:18653895 | lifeskim:mentions | umls-concept:C0058482 | lld:lifeskim |
| pubmed-article:18653895 | pubmed:issue | 5888 | lld:pubmed |
| pubmed-article:18653895 | pubmed:dateCreated | 2008-7-25 | lld:pubmed |
| pubmed-article:18653895 | pubmed:abstractText | Membrane and secretory proteins cotranslationally enter and are folded in the endoplasmic reticulum (ER). Misfolded or unassembled proteins are discarded by a process known as ER-associated degradation (ERAD), which involves their retrotranslocation into the cytosol. ERAD substrates frequently contain disulfide bonds that must be cleaved before their retrotranslocation. Here, we found that an ER-resident protein ERdj5 had a reductase activity, cleaved the disulfide bonds of misfolded proteins, and accelerated ERAD through its physical and functional associations with EDEM (ER degradation-enhancing alpha-mannosidase-like protein) and an ER-resident chaperone BiP. Thus, ERdj5 is a member of a supramolecular ERAD complex that recognizes and unfolds misfolded proteins for their efficient retrotranslocation. | lld:pubmed |
| pubmed-article:18653895 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18653895 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18653895 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18653895 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18653895 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18653895 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:18653895 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18653895 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18653895 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18653895 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18653895 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18653895 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18653895 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18653895 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18653895 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:18653895 | pubmed:issn | 1095-9203 | lld:pubmed |
| pubmed-article:18653895 | pubmed:author | pubmed-author:NagataKazuhir... | lld:pubmed |
| pubmed-article:18653895 | pubmed:author | pubmed-author:JansenGregorG | lld:pubmed |
| pubmed-article:18653895 | pubmed:author | pubmed-author:ThomasDavid... | lld:pubmed |
| pubmed-article:18653895 | pubmed:author | pubmed-author:HosekiJunJ | lld:pubmed |
| pubmed-article:18653895 | pubmed:author | pubmed-author:UshiodaRyoR | lld:pubmed |
| pubmed-article:18653895 | pubmed:author | pubmed-author:ArakiKazutaka... | lld:pubmed |
| pubmed-article:18653895 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18653895 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:18653895 | pubmed:volume | 321 | lld:pubmed |
| pubmed-article:18653895 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18653895 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18653895 | pubmed:pagination | 569-72 | lld:pubmed |
| pubmed-article:18653895 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:18653895 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18653895 | pubmed:articleTitle | ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER. | lld:pubmed |
| pubmed-article:18653895 | pubmed:affiliation | Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Kyoto 606-8397, Japan. | lld:pubmed |
| pubmed-article:18653895 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18653895 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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