| pubmed-article:16928765 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16928765 | lifeskim:mentions | umls-concept:C0079904 | lld:lifeskim |
| pubmed-article:16928765 | lifeskim:mentions | umls-concept:C1427812 | lld:lifeskim |
| pubmed-article:16928765 | lifeskim:mentions | umls-concept:C1519623 | lld:lifeskim |
| pubmed-article:16928765 | lifeskim:mentions | umls-concept:C0596788 | lld:lifeskim |
| pubmed-article:16928765 | lifeskim:mentions | umls-concept:C0086597 | lld:lifeskim |
| pubmed-article:16928765 | lifeskim:mentions | umls-concept:C1515877 | lld:lifeskim |
| pubmed-article:16928765 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:16928765 | lifeskim:mentions | umls-concept:C1334346 | lld:lifeskim |
| pubmed-article:16928765 | pubmed:issue | 21 | lld:pubmed |
| pubmed-article:16928765 | pubmed:dateCreated | 2006-10-16 | lld:pubmed |
| pubmed-article:16928765 | pubmed:abstractText | The Epstein-Barr virus oncoprotein LMP1 has six transmembrane domains (TMs) that enable intermolecular aggregation and constitutive signaling through two C-terminal cytosolic domains. Expression of both TMs 1 and 2 without the C terminus (TM1-2DeltaC) and TMs 3 to 6 fused to the C terminus (TM3-6) results in partial association, which is substantially decreased by TM1 F38WLY41 mutation to A38ALA41. We now investigate whether TM1-2DeltaC can functionally interact with TM3-6. TM1-2DeltaC induced TM3-6 to mediate NF-kappaB activation at 59% of LMP1 levels, and the effect was dependent on TM1-2 F38WLY41. TM1-2DeltaC even induced TM3-4 C terminus-mediated NF-kappaB activation to 44% of LMP1 levels. Surprisingly, this effect was TM1 F38WLY41 independent, indicative of a role for TMs 5 and 6 in TM1 F38WLY41 effects. TM3 W98 was also important for TM1-2DeltaC induction of TM3-6-mediated NF-kappaB activation, for association, and for TM1 F38WLY41 dependence on C-terminal NF-kappaB activation. These data support models in which the TM1 F38WLY41 effects are at least partially dependent on TM3 W98 and a residue(s) in TMs 5 and 6. | lld:pubmed |
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| pubmed-article:16928765 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16928765 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16928765 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16928765 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16928765 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16928765 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:16928765 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:16928765 | pubmed:author | pubmed-author:KieffElliottE | lld:pubmed |
| pubmed-article:16928765 | pubmed:author | pubmed-author:Cahir-McFarla... | lld:pubmed |
| pubmed-article:16928765 | pubmed:author | pubmed-author:YasuiTeruhito... | lld:pubmed |
| pubmed-article:16928765 | pubmed:author | pubmed-author:SoniVishalV | lld:pubmed |
| pubmed-article:16928765 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16928765 | pubmed:volume | 80 | lld:pubmed |
| pubmed-article:16928765 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16928765 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16928765 | pubmed:pagination | 10787-93 | lld:pubmed |
| pubmed-article:16928765 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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