| pubmed-article:16815975 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16815975 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:16815975 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:16815975 | lifeskim:mentions | umls-concept:C0023689 | lld:lifeskim |
| pubmed-article:16815975 | lifeskim:mentions | umls-concept:C1332749 | lld:lifeskim |
| pubmed-article:16815975 | lifeskim:mentions | umls-concept:C0086597 | lld:lifeskim |
| pubmed-article:16815975 | lifeskim:mentions | umls-concept:C1521840 | lld:lifeskim |
| pubmed-article:16815975 | pubmed:issue | 28 | lld:pubmed |
| pubmed-article:16815975 | pubmed:dateCreated | 2006-7-12 | lld:pubmed |
| pubmed-article:16815975 | pubmed:abstractText | Type I IFNs induce the expression of IFN-stimulated gene 15 (ISG15) and its conjugation to cellular targets. ISGylation is a multistep process involving IFN-inducible Ube1L, UbcH8, and a yet-to-be identified E3 ligase. Here we report the identification of an IFN-induced HECT-type E3 protein ligase, HERC5/Ceb1, which mediates ISGylation. We also defined a number of proteins modified by ISG15 after IFN triggering or HERC5 overexpression. A reduction in endogenous HERC5 by small interfering RNA inhibition blocks the IFN-induced ISG15 conjugation. Conversely, HERC5 coexpression with Ube1L and UbcH8 induces the ISG15 conjugation in vivo independent of IFN stimulation. A targeted substitution of Cys-994 to Ala in the HECT domain of HERC5 completely abrogates its E3 protein ligase activity. Therefore, this study demonstrates that HERC5/Ceb1 is involved in the conjugation of ISG15 to cellular proteins. | lld:pubmed |
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| pubmed-article:16815975 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16815975 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16815975 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16815975 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16815975 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:16815975 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:16815975 | pubmed:author | pubmed-author:PungYuh FenYF | lld:pubmed |
| pubmed-article:16815975 | pubmed:author | pubmed-author:WongJoyce... | lld:pubmed |
| pubmed-article:16815975 | pubmed:author | pubmed-author:SzeNewman... | lld:pubmed |
| pubmed-article:16815975 | pubmed:author | pubmed-author:ChinKeh-Chuan... | lld:pubmed |
| pubmed-article:16815975 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16815975 | pubmed:day | 11 | lld:pubmed |
| pubmed-article:16815975 | pubmed:volume | 103 | lld:pubmed |
| pubmed-article:16815975 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16815975 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16815975 | pubmed:pagination | 10735-40 | lld:pubmed |
| pubmed-article:16815975 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:16815975 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16815975 | pubmed:articleTitle | HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates type I IFN-induced ISGylation of protein targets. | lld:pubmed |
| pubmed-article:16815975 | pubmed:affiliation | Immunology and Virology Laboratory and Proteomics Laboratory, Genome Institute of Singapore, 60 Biopolis Street, #02-01 Genome, Singapore. | lld:pubmed |
| pubmed-article:16815975 | pubmed:publicationType | Journal Article | lld:pubmed |
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