| pubmed-article:17310145 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17310145 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:17310145 | lifeskim:mentions | umls-concept:C0023689 | lld:lifeskim |
| pubmed-article:17310145 | lifeskim:mentions | umls-concept:C0041538 | lld:lifeskim |
| pubmed-article:17310145 | lifeskim:mentions | umls-concept:C0084133 | lld:lifeskim |
| pubmed-article:17310145 | lifeskim:mentions | umls-concept:C0040671 | lld:lifeskim |
| pubmed-article:17310145 | lifeskim:mentions | umls-concept:C1524075 | lld:lifeskim |
| pubmed-article:17310145 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:17310145 | pubmed:issue | 7133 | lld:pubmed |
| pubmed-article:17310145 | pubmed:dateCreated | 2007-3-15 | lld:pubmed |
| pubmed-article:17310145 | pubmed:abstractText | In eukaryotic cells, many short-lived proteins are conjugated with Lys 48-linked ubiquitin chains and degraded by the proteasome. Ubiquitination requires an activating enzyme (E1), a conjugating enzyme (E2) and a ligase (E3). Most ubiquitin ligases use either a HECT (homologous to E6-associated protein C terminus) or a RING (really interesting new gene) domain to catalyse polyubiquitination, but the mechanism of E3 catalysis is poorly defined. Here we dissect this process using mouse Ube2g2 (E2; identical at the amino acid level to human Ube2g2) and human gp78 (E3), an endoplasmic reticulum (ER)-associated conjugating system essential for the degradation of misfolded ER proteins. We demonstrate by expressing recombinant proteins in Escherichia coli that Ube2g2/gp78-mediated polyubiquitination involves preassembly of Lys 48-linked ubiquitin chains at the catalytic cysteine of Ube2g2. The growth of Ube2g2-anchored ubiquitin chains seems to be mediated by an aminolysis-based transfer reaction between two Ube2g2 molecules that each carries a ubiquitin moiety in its active site. Intriguingly, polyubiquitination of a substrate can be achieved by transferring preassembled ubiquitin chains from Ube2g2 to a lysine residue in a substrate. | lld:pubmed |
| pubmed-article:17310145 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17310145 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17310145 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17310145 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17310145 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17310145 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17310145 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17310145 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17310145 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17310145 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17310145 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17310145 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17310145 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:17310145 | pubmed:issn | 1476-4687 | lld:pubmed |
| pubmed-article:17310145 | pubmed:author | pubmed-author:FuY PYP | lld:pubmed |
| pubmed-article:17310145 | pubmed:author | pubmed-author:YeYihongY | lld:pubmed |
| pubmed-article:17310145 | pubmed:author | pubmed-author:BrungerAxel... | lld:pubmed |
| pubmed-article:17310145 | pubmed:author | pubmed-author:TuDaqiD | lld:pubmed |
| pubmed-article:17310145 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:17310145 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:17310145 | pubmed:volume | 446 | lld:pubmed |
| pubmed-article:17310145 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17310145 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17310145 | pubmed:pagination | 333-7 | lld:pubmed |
| pubmed-article:17310145 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
| pubmed-article:17310145 | pubmed:meshHeading | pubmed-meshheading:17310145... | lld:pubmed |
| pubmed-article:17310145 | pubmed:meshHeading | pubmed-meshheading:17310145... | lld:pubmed |
| pubmed-article:17310145 | pubmed:meshHeading | pubmed-meshheading:17310145... | lld:pubmed |
| pubmed-article:17310145 | pubmed:meshHeading | pubmed-meshheading:17310145... | lld:pubmed |
| pubmed-article:17310145 | pubmed:meshHeading | pubmed-meshheading:17310145... | lld:pubmed |
| pubmed-article:17310145 | pubmed:meshHeading | pubmed-meshheading:17310145... | lld:pubmed |
| pubmed-article:17310145 | pubmed:meshHeading | pubmed-meshheading:17310145... | lld:pubmed |
| pubmed-article:17310145 | pubmed:meshHeading | pubmed-meshheading:17310145... | lld:pubmed |
| pubmed-article:17310145 | pubmed:meshHeading | pubmed-meshheading:17310145... | lld:pubmed |
| pubmed-article:17310145 | pubmed:meshHeading | pubmed-meshheading:17310145... | lld:pubmed |
| pubmed-article:17310145 | pubmed:meshHeading | pubmed-meshheading:17310145... | lld:pubmed |
| pubmed-article:17310145 | pubmed:meshHeading | pubmed-meshheading:17310145... | lld:pubmed |
| pubmed-article:17310145 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17310145 | pubmed:articleTitle | A ubiquitin ligase transfers preformed polyubiquitin chains from a conjugating enzyme to a substrate. | lld:pubmed |
| pubmed-article:17310145 | pubmed:affiliation | Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA. | lld:pubmed |
| pubmed-article:17310145 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17310145 | pubmed:publicationType | Research Support, N.I.H., Intramural | lld:pubmed |
| entrez-gene:7316 | entrezgene:pubmed | pubmed-article:17310145 | lld:entrezgene |
| entrez-gene:267 | entrezgene:pubmed | pubmed-article:17310145 | lld:entrezgene |
| entrez-gene:7327 | entrezgene:pubmed | pubmed-article:17310145 | lld:entrezgene |
| entrez-gene:9709 | entrezgene:pubmed | pubmed-article:17310145 | lld:entrezgene |
| entrez-gene:22213 | entrezgene:pubmed | pubmed-article:17310145 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:17310145 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:17310145 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:17310145 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:17310145 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:17310145 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17310145 | lld:pubmed |
