pubmed-article:21205830 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:21205830 | lifeskim:mentions | umls-concept:C0014239 | lld:lifeskim |
pubmed-article:21205830 | lifeskim:mentions | umls-concept:C0108187 | lld:lifeskim |
pubmed-article:21205830 | lifeskim:mentions | umls-concept:C0019868 | lld:lifeskim |
pubmed-article:21205830 | lifeskim:mentions | umls-concept:C1313794 | lld:lifeskim |
pubmed-article:21205830 | lifeskim:mentions | umls-concept:C1538252 | lld:lifeskim |
pubmed-article:21205830 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
pubmed-article:21205830 | lifeskim:mentions | umls-concept:C1704735 | lld:lifeskim |
pubmed-article:21205830 | lifeskim:mentions | umls-concept:C1552603 | lld:lifeskim |
pubmed-article:21205830 | lifeskim:mentions | umls-concept:C0220922 | lld:lifeskim |
pubmed-article:21205830 | lifeskim:mentions | umls-concept:C1706202 | lld:lifeskim |
pubmed-article:21205830 | pubmed:issue | 10 | lld:pubmed |
pubmed-article:21205830 | pubmed:dateCreated | 2011-3-10 | lld:pubmed |
pubmed-article:21205830 | pubmed:abstractText | To identify novel regulators of endoplasmic reticulum (ER)-linked protein degradation and ER function, we determined the entire inventory of membrane-spanning RING finger E3 ubiquitin ligases localized to the ER. We identified 24 ER membrane-anchored ubiquitin ligases and found Nixin/ZNRF4 to be central for the regulation of calnexin turnover. Ectopic expression of wild type Nixin induced a dramatic down-regulation of the ER-localized chaperone calnexin that was prevented by inactivation of the Nixin RING domain. Importantly, Nixin physically interacts with calnexin in a glycosylation-independent manner, induces calnexin ubiquitination, and p97-dependent degradation, indicating an ER-associated degradation-like mechanism of calnexin turnover. | lld:pubmed |
pubmed-article:21205830 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21205830 | pubmed:language | eng | lld:pubmed |
pubmed-article:21205830 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21205830 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:21205830 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21205830 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21205830 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:21205830 | pubmed:month | Mar | lld:pubmed |
pubmed-article:21205830 | pubmed:issn | 1083-351X | lld:pubmed |
pubmed-article:21205830 | pubmed:author | pubmed-author:YouleRichard... | lld:pubmed |
pubmed-article:21205830 | pubmed:author | pubmed-author:RyuSeung-Wook... | lld:pubmed |
pubmed-article:21205830 | pubmed:author | pubmed-author:KarbowskiMari... | lld:pubmed |
pubmed-article:21205830 | pubmed:author | pubmed-author:FrankStephanS | lld:pubmed |
pubmed-article:21205830 | pubmed:author | pubmed-author:NeutznerAlber... | lld:pubmed |
pubmed-article:21205830 | pubmed:author | pubmed-author:NeutznerMelan... | lld:pubmed |
pubmed-article:21205830 | pubmed:author | pubmed-author:BenischkeAnne... | lld:pubmed |
pubmed-article:21205830 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:21205830 | pubmed:day | 11 | lld:pubmed |
pubmed-article:21205830 | pubmed:volume | 286 | lld:pubmed |
pubmed-article:21205830 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:21205830 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:21205830 | pubmed:pagination | 8633-43 | lld:pubmed |
pubmed-article:21205830 | pubmed:meshHeading | pubmed-meshheading:21205830... | lld:pubmed |
pubmed-article:21205830 | pubmed:meshHeading | pubmed-meshheading:21205830... | lld:pubmed |
pubmed-article:21205830 | pubmed:meshHeading | pubmed-meshheading:21205830... | lld:pubmed |
pubmed-article:21205830 | pubmed:meshHeading | pubmed-meshheading:21205830... | lld:pubmed |
pubmed-article:21205830 | pubmed:meshHeading | pubmed-meshheading:21205830... | lld:pubmed |
pubmed-article:21205830 | pubmed:meshHeading | pubmed-meshheading:21205830... | lld:pubmed |
pubmed-article:21205830 | pubmed:meshHeading | pubmed-meshheading:21205830... | lld:pubmed |
pubmed-article:21205830 | pubmed:meshHeading | pubmed-meshheading:21205830... | lld:pubmed |
pubmed-article:21205830 | pubmed:year | 2011 | lld:pubmed |
pubmed-article:21205830 | pubmed:articleTitle | A systematic search for endoplasmic reticulum (ER) membrane-associated RING finger proteins identifies Nixin/ZNRF4 as a regulator of calnexin stability and ER homeostasis. | lld:pubmed |
pubmed-article:21205830 | pubmed:affiliation | Biochemistry Section, Surgical Neurological Branch, NINDS, National Institutes of Health, Bethesda, Maryland 20892, USA. albert.neutzner@unibas.ch | lld:pubmed |
pubmed-article:21205830 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:21205830 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
entrez-gene:821 | entrezgene:pubmed | pubmed-article:21205830 | lld:entrezgene |
entrez-gene:7316 | entrezgene:pubmed | pubmed-article:21205830 | lld:entrezgene |
entrez-gene:148066 | entrezgene:pubmed | pubmed-article:21205830 | lld:entrezgene |
http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:21205830 | lld:entrezgene |
http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:21205830 | lld:entrezgene |
http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:21205830 | lld:entrezgene |
http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:21205830 | lld:entrezgene |