pubmed-article:17292329 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17292329 | lifeskim:mentions | umls-concept:C1166825 | lld:lifeskim |
pubmed-article:17292329 | lifeskim:mentions | umls-concept:C0079904 | lld:lifeskim |
pubmed-article:17292329 | lifeskim:mentions | umls-concept:C0120465 | lld:lifeskim |
pubmed-article:17292329 | lifeskim:mentions | umls-concept:C0004083 | lld:lifeskim |
pubmed-article:17292329 | lifeskim:mentions | umls-concept:C1515877 | lld:lifeskim |
pubmed-article:17292329 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:17292329 | lifeskim:mentions | umls-concept:C0205485 | lld:lifeskim |
pubmed-article:17292329 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:17292329 | pubmed:dateCreated | 2007-2-23 | lld:pubmed |
pubmed-article:17292329 | pubmed:abstractText | Constitutive activity of NF-kappaB is associated with various human cancers including adult T-cell leukemia (ATL). In this study, we have found Tgat that activates NF-kappaB by screening a cDNA expression library derived from ATL cells. We previously identified Tgat as the oncogene, which consists of the Rho-guanine nucleotide exchange factor (Rho-GEF) domain and the unique C-terminal region, as a consequence of alternative splicing of the Trio transcript. Tgat activated the IKK activity by binding with the IkappaB kinase (IKK) complex. The Tgat mutants lacking the C-terminal region failed to associate with the IKK complex suggesting an essential role of the unique sequence. The mutation causing the loss of GEF activity also abolished the NF-kappaB activation. Moreover, co-expressed p100 was efficiently processed into p52 in the Tgat-expressing cells, suggesting the co-involvement of non-canonical pathway. | lld:pubmed |
pubmed-article:17292329 | pubmed:language | eng | lld:pubmed |
pubmed-article:17292329 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17292329 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:17292329 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17292329 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17292329 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17292329 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17292329 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17292329 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17292329 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17292329 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17292329 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17292329 | pubmed:month | Mar | lld:pubmed |
pubmed-article:17292329 | pubmed:issn | 0006-291X | lld:pubmed |
pubmed-article:17292329 | pubmed:author | pubmed-author:KatamineShige... | lld:pubmed |
pubmed-article:17292329 | pubmed:author | pubmed-author:KohnoTomokoT | lld:pubmed |
pubmed-article:17292329 | pubmed:author | pubmed-author:MatsuyamaTosh... | lld:pubmed |
pubmed-article:17292329 | pubmed:author | pubmed-author:YamadaKenjiK | lld:pubmed |
pubmed-article:17292329 | pubmed:author | pubmed-author:MoriTsuyoshiT | lld:pubmed |
pubmed-article:17292329 | pubmed:author | pubmed-author:NagayasuTakes... | lld:pubmed |
pubmed-article:17292329 | pubmed:author | pubmed-author:MoriuchiRyozo... | lld:pubmed |
pubmed-article:17292329 | pubmed:author | pubmed-author:OkazakiEikoE | lld:pubmed |
pubmed-article:17292329 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:17292329 | pubmed:day | 30 | lld:pubmed |
pubmed-article:17292329 | pubmed:volume | 355 | lld:pubmed |
pubmed-article:17292329 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17292329 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17292329 | pubmed:pagination | 269-74 | lld:pubmed |
pubmed-article:17292329 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
pubmed-article:17292329 | pubmed:meshHeading | pubmed-meshheading:17292329... | lld:pubmed |
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pubmed-article:17292329 | pubmed:meshHeading | pubmed-meshheading:17292329... | lld:pubmed |
pubmed-article:17292329 | pubmed:year | 2007 | lld:pubmed |
pubmed-article:17292329 | pubmed:articleTitle | Tgat, a Rho-specific guanine nucleotide exchange factor, activates NF-kappaB via physical association with IkappaB kinase complexes. | lld:pubmed |
pubmed-article:17292329 | pubmed:affiliation | Department of Molecular Microbiology and Immunology, Nagasaki University Graduate School of Biomedical Sciences, 1-12-4 Sakamoto, Nagasaki 852-8523, Japan. | lld:pubmed |
pubmed-article:17292329 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:17292329 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |