pubmed-article:9242637 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9242637 | lifeskim:mentions | umls-concept:C0230463 | lld:lifeskim |
pubmed-article:9242637 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
pubmed-article:9242637 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
pubmed-article:9242637 | lifeskim:mentions | umls-concept:C0295022 | lld:lifeskim |
pubmed-article:9242637 | lifeskim:mentions | umls-concept:C1420888 | lld:lifeskim |
pubmed-article:9242637 | lifeskim:mentions | umls-concept:C0005456 | lld:lifeskim |
pubmed-article:9242637 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:9242637 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
pubmed-article:9242637 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
pubmed-article:9242637 | lifeskim:mentions | umls-concept:C0205164 | lld:lifeskim |
pubmed-article:9242637 | pubmed:issue | 32 | lld:pubmed |
pubmed-article:9242637 | pubmed:dateCreated | 1997-9-5 | lld:pubmed |
pubmed-article:9242637 | pubmed:abstractText | The TRAF3 molecule interacts with the cytoplasmic carboxyl terminus (COOH terminus) of the Epstein-Barr virus-encoded oncogene LMP-1. NF-kappaB activation is a downstream signaling event of tumor necrosis factor receptor-associated factor (TRAF) molecules in other signaling systems (CD40 for example) and is an event caused by LMP-1 expression. One region capable of TRAF3 interaction in LMP-1 is the membrane-proximal 45 amino acids (188-242) of the COOH terminus. We show that this region contains the only site for binding of TRAF3 in the 200-amino acid COOH terminus of LMP-1. The site also binds TRAF2 and TRAF5, but not TRAF6. TRAF3 binds to critical residues localized between amino acids 196 and 212 (HHDDSLPHPQQATDDSG), including the PXQX(T/S) motif, that share limited identity to the CD40 receptor TRAF binding site (TAAPVQETL). Mutation of critical residues in the TRAF3 binding site of LMP-1 that prevents binding of TRAF2, TRAF3, and TRAF5 does not affect NF-kappaB-activating potential. Deletion mapping localized the major NF-kappaB activating region of LMP-1 to critical residues in the distal 4 amino acids of the COOH terminus (383-386). Therefore, TRAF3 binding and NF-kappaB activation occur through two separate motifs at opposite ends of the LMP-1 COOH-terminal sequence. | lld:pubmed |
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pubmed-article:9242637 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9242637 | pubmed:language | eng | lld:pubmed |
pubmed-article:9242637 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9242637 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:9242637 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9242637 | pubmed:month | Aug | lld:pubmed |
pubmed-article:9242637 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:9242637 | pubmed:author | pubmed-author:BaltimoreDD | lld:pubmed |
pubmed-article:9242637 | pubmed:author | pubmed-author:ChengGG | lld:pubmed |
pubmed-article:9242637 | pubmed:author | pubmed-author:Thorley-Lawso... | lld:pubmed |
pubmed-article:9242637 | pubmed:author | pubmed-author:BrodeurS RSR | lld:pubmed |
pubmed-article:9242637 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9242637 | pubmed:day | 8 | lld:pubmed |
pubmed-article:9242637 | pubmed:volume | 272 | lld:pubmed |
pubmed-article:9242637 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9242637 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9242637 | pubmed:pagination | 19777-84 | lld:pubmed |
pubmed-article:9242637 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
pubmed-article:9242637 | pubmed:meshHeading | pubmed-meshheading:9242637-... | lld:pubmed |
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pubmed-article:9242637 | pubmed:meshHeading | pubmed-meshheading:9242637-... | lld:pubmed |
pubmed-article:9242637 | pubmed:year | 1997 | lld:pubmed |
pubmed-article:9242637 | pubmed:articleTitle | Localization of the major NF-kappaB-activating site and the sole TRAF3 binding site of LMP-1 defines two distinct signaling motifs. | lld:pubmed |
pubmed-article:9242637 | pubmed:affiliation | Department of Pathology, Tufts University School of Medicine, Boston, Massachusetts 02111, USA. | lld:pubmed |
pubmed-article:9242637 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9242637 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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