pubmed-article:18538572 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:18538572 | lifeskim:mentions | umls-concept:C0996647 | lld:lifeskim |
pubmed-article:18538572 | lifeskim:mentions | umls-concept:C1157980 | lld:lifeskim |
pubmed-article:18538572 | pubmed:issue | 7 | lld:pubmed |
pubmed-article:18538572 | pubmed:dateCreated | 2008-7-8 | lld:pubmed |
pubmed-article:18538572 | pubmed:abstractText | Proteins that improperly mature in the endoplasmic reticulum (ER) are dislocated to the cytoplasm for proteasome-mediated destruction. A recent study provides insight into the incompletely understood processes for selection and targeting of aberrant proteins for ER-associated protein degradation. The identification of the ER chaperones GRP94 and BiP as binding partners for the mannose-binding proteins OS-9 and XTP3-B, indicates that these protein complexes bind to aberrant proteins and direct them to the Hrd1 dislocation and ubiquitylation complex in the ER membrane. | lld:pubmed |
pubmed-article:18538572 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18538572 | pubmed:language | eng | lld:pubmed |
pubmed-article:18538572 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18538572 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:18538572 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18538572 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18538572 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18538572 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18538572 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18538572 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:18538572 | pubmed:month | Jul | lld:pubmed |
pubmed-article:18538572 | pubmed:issn | 0968-0004 | lld:pubmed |
pubmed-article:18538572 | pubmed:author | pubmed-author:HebertDaniel... | lld:pubmed |
pubmed-article:18538572 | pubmed:author | pubmed-author:TamuraTakuT | lld:pubmed |
pubmed-article:18538572 | pubmed:author | pubmed-author:CormierJames... | lld:pubmed |
pubmed-article:18538572 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:18538572 | pubmed:volume | 33 | lld:pubmed |
pubmed-article:18538572 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:18538572 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:18538572 | pubmed:pagination | 298-300 | lld:pubmed |
pubmed-article:18538572 | pubmed:dateRevised | 2010-9-16 | lld:pubmed |
pubmed-article:18538572 | pubmed:meshHeading | pubmed-meshheading:18538572... | lld:pubmed |
pubmed-article:18538572 | pubmed:meshHeading | pubmed-meshheading:18538572... | lld:pubmed |
pubmed-article:18538572 | pubmed:meshHeading | pubmed-meshheading:18538572... | lld:pubmed |
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pubmed-article:18538572 | pubmed:meshHeading | pubmed-meshheading:18538572... | lld:pubmed |
pubmed-article:18538572 | pubmed:meshHeading | pubmed-meshheading:18538572... | lld:pubmed |
pubmed-article:18538572 | pubmed:meshHeading | pubmed-meshheading:18538572... | lld:pubmed |
pubmed-article:18538572 | pubmed:meshHeading | pubmed-meshheading:18538572... | lld:pubmed |
pubmed-article:18538572 | pubmed:meshHeading | pubmed-meshheading:18538572... | lld:pubmed |
pubmed-article:18538572 | pubmed:year | 2008 | lld:pubmed |
pubmed-article:18538572 | pubmed:articleTitle | Sweet bays of ERAD. | lld:pubmed |
pubmed-article:18538572 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, University of Massachusetts, 710N. Pleasant Street, Amherst, MA 01003, USA. | lld:pubmed |
pubmed-article:18538572 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:18538572 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
entrez-gene:27248 | entrezgene:pubmed | pubmed-article:18538572 | lld:entrezgene |
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