| pubmed-article:10066435 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10066435 | lifeskim:mentions | umls-concept:C0126732 | lld:lifeskim |
| pubmed-article:10066435 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:10066435 | lifeskim:mentions | umls-concept:C1334877 | lld:lifeskim |
| pubmed-article:10066435 | lifeskim:mentions | umls-concept:C1519751 | lld:lifeskim |
| pubmed-article:10066435 | lifeskim:mentions | umls-concept:C1420081 | lld:lifeskim |
| pubmed-article:10066435 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:10066435 | lifeskim:mentions | umls-concept:C0332256 | lld:lifeskim |
| pubmed-article:10066435 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:10066435 | pubmed:dateCreated | 1999-4-13 | lld:pubmed |
| pubmed-article:10066435 | pubmed:abstractText | Destruction of the transcriptional inhibitor IkappaB by the ubiquitin (Ub) system is required for signal-dependent activation of the multifunctional transcriptional factor NF-kappaB, but details of this ubiquitination are largely unknown. We report here that the IkappaBalpha-ubiquitin ligase (IkappaBalpha-E3) is an SCF-like complex containing Skp1, cullin-1, and two homologous F-box/WD40-repeat proteins, betaTrCP1 and betaTrCP2. Intriguingly, all these components are cooperatively recruited to bind to a phosphorylated IkappaBalpha (pIkappaBalpha) produced by tumor necrosis factor-alpha (TNF-alpha) stimulation. IkappaBalpha-E3 bound to pIkappaBalpha catalyzed in vitro ubiquitination of pIkappaBalpha in the presence of ATP, Ub, and E1-activating and E2-conjugating enzymes. Forced expression of betaTrCP1 and betaTrCP2 resulted in dramatic augmentation of the in vitro polyubiquitination activity of IkappaBalpha-E3. These results indicate that the long-sought IkappaBalpha-E3 is an SCF-like complex consisting of multiple proteins which are coordinately assembled during phosphorylation of IkappaBalpha in response to external signals. | lld:pubmed |
| pubmed-article:10066435 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10066435 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10066435 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10066435 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10066435 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:10066435 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:10066435 | pubmed:author | pubmed-author:SuzukiTT | lld:pubmed |
| pubmed-article:10066435 | pubmed:author | pubmed-author:TanakaKK | lld:pubmed |
| pubmed-article:10066435 | pubmed:author | pubmed-author:SuzukiHH | lld:pubmed |
| pubmed-article:10066435 | pubmed:author | pubmed-author:KobayashiMM | lld:pubmed |
| pubmed-article:10066435 | pubmed:author | pubmed-author:IkenoueTT | lld:pubmed |
| pubmed-article:10066435 | pubmed:author | pubmed-author:TakeuchiMM | lld:pubmed |
| pubmed-article:10066435 | pubmed:author | pubmed-author:ChibaTT | lld:pubmed |
| pubmed-article:10066435 | pubmed:author | pubmed-author:OmataMM | lld:pubmed |
| pubmed-article:10066435 | pubmed:author | pubmed-author:FuruichiKK | lld:pubmed |
| pubmed-article:10066435 | pubmed:author | pubmed-author:IchiyamaAA | lld:pubmed |
| pubmed-article:10066435 | pubmed:copyrightInfo | Copyright 1999 Academic Press. | lld:pubmed |
| pubmed-article:10066435 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10066435 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:10066435 | pubmed:volume | 256 | lld:pubmed |
| pubmed-article:10066435 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10066435 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10066435 | pubmed:pagination | 127-32 | lld:pubmed |
| pubmed-article:10066435 | pubmed:dateRevised | 2007-5-16 | lld:pubmed |
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| pubmed-article:10066435 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10066435 | pubmed:articleTitle | IkappaBalpha ubiquitination is catalyzed by an SCF-like complex containing Skp1, cullin-1, and two F-box/WD40-repeat proteins, betaTrCP1 and betaTrCP2. | lld:pubmed |
| pubmed-article:10066435 | pubmed:affiliation | Institute for Drug Discovery Research, Yamanouchi Pharmaceutical Co., Ltd., 21 Miyukigaoka, Ibaraki, Tsukuba-shi, 305-8585, Japan. | lld:pubmed |
| pubmed-article:10066435 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10066435 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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