| pubmed-article:19910467 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19910467 | lifeskim:mentions | umls-concept:C0521447 | lld:lifeskim |
| pubmed-article:19910467 | lifeskim:mentions | umls-concept:C0030940 | lld:lifeskim |
| pubmed-article:19910467 | lifeskim:mentions | umls-concept:C1456820 | lld:lifeskim |
| pubmed-article:19910467 | lifeskim:mentions | umls-concept:C0297981 | lld:lifeskim |
| pubmed-article:19910467 | lifeskim:mentions | umls-concept:C1335623 | lld:lifeskim |
| pubmed-article:19910467 | lifeskim:mentions | umls-concept:C1157996 | lld:lifeskim |
| pubmed-article:19910467 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:19910467 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
| pubmed-article:19910467 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:19910467 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:19910467 | pubmed:dateCreated | 2010-1-4 | lld:pubmed |
| pubmed-article:19910467 | pubmed:abstractText | Ubiquitination and deubiquitination of receptor-interacting protein 1 (RIP1) play an important role in the positive and negative regulation of the tumor necrosis factor alpha (TNFalpha)-induced nuclear factor kappaB (NF-kappaB) activation. Using a combination of functional genomic and proteomic approaches, we have identified ubiquitin-specific peptidase 21 (USP21) as a deubiquitinase for RIP1. USP21 is constitutively associated with RIP1 and deubiquitinates RIP1 in vitro and in vivo. Notably, knockdown of USP21 in HeLa cells enhances TNFalpha-induced RIP1 ubiquitination, IkappaB kinase beta (IKKbeta), and NF-kappaB phosphorylation, inhibitor of NF-kappaB alpha (IkappaB alpha) phosphorylation and ubiquitination, as well as NF-kappaB-dependent gene expression. Therefore, our results demonstrate that USP21 plays an important role in the down-regulation of TNFalpha-induced NF-kappaB activation through deubiquitinating RIP1. | lld:pubmed |
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| pubmed-article:19910467 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19910467 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19910467 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19910467 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:19910467 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19910467 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:19910467 | pubmed:issn | 1083-351X | lld:pubmed |
| pubmed-article:19910467 | pubmed:author | pubmed-author:VigPP | lld:pubmed |
| pubmed-article:19910467 | pubmed:author | pubmed-author:JinS GSG | lld:pubmed |
| pubmed-article:19910467 | pubmed:author | pubmed-author:ZhangTingT | lld:pubmed |
| pubmed-article:19910467 | pubmed:author | pubmed-author:WangHongmeiH | lld:pubmed |
| pubmed-article:19910467 | pubmed:author | pubmed-author:YangJianhuaJ | lld:pubmed |
| pubmed-article:19910467 | pubmed:author | pubmed-author:CaoGuangwenG | lld:pubmed |
| pubmed-article:19910467 | pubmed:author | pubmed-author:GuXueX | lld:pubmed |
| pubmed-article:19910467 | pubmed:author | pubmed-author:BurlingameSus... | lld:pubmed |
| pubmed-article:19910467 | pubmed:author | pubmed-author:XuGufengG | lld:pubmed |
| pubmed-article:19910467 | pubmed:author | pubmed-author:TanXiaojieX | lld:pubmed |
| pubmed-article:19910467 | pubmed:author | pubmed-author:SunWenjingW | lld:pubmed |
| pubmed-article:19910467 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19910467 | pubmed:day | 8 | lld:pubmed |
| pubmed-article:19910467 | pubmed:volume | 285 | lld:pubmed |
| pubmed-article:19910467 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19910467 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19910467 | pubmed:pagination | 969-78 | lld:pubmed |
| pubmed-article:19910467 | pubmed:dateRevised | 2011-7-20 | lld:pubmed |
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