| pubmed-article:14961076 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14961076 | lifeskim:mentions | umls-concept:C0126732 | lld:lifeskim |
| pubmed-article:14961076 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
| pubmed-article:14961076 | lifeskim:mentions | umls-concept:C0376525 | lld:lifeskim |
| pubmed-article:14961076 | lifeskim:mentions | umls-concept:C0012854 | lld:lifeskim |
| pubmed-article:14961076 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:14961076 | lifeskim:mentions | umls-concept:C1334877 | lld:lifeskim |
| pubmed-article:14961076 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:14961076 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:14961076 | pubmed:dateCreated | 2004-2-12 | lld:pubmed |
| pubmed-article:14961076 | pubmed:abstractText | The avian Rev-T retrovirus encodes the oncoprotein v-Rel, a member of the Rel/nuclear factor (NF)-kappaB transcription factor family. The aggressive oncogenic potential of v-Rel has arisen from multiple mutations within the coding sequence of the avian cellular protein c-Rel. In this study, using quantitative biochemical experiments, we have tested the role of a limited set of alterations between v-Rel and c-Rel located within the Rel homology region (RHR) of the family that might confer functional differences. Our results show that only a set of six mutations within the RHR of v-Rel are responsible for its ability to bind to a broad spectrum of kappaB-DNA that are normally regulated by distinct NF-kappaB dimers. We also observe that both v-Rel homodimer and p50/v-Rel heterodimer bind IkappaBalpha weakly compared to other cellular Rel/NF-kappaB dimers with transcription activation potential. We suggest that the ability of v-Rel homodimer to deregulate subunit-specific gene expression and its ability to evade IkappaB inhibition are crucial to its strong oncogenic potential. | lld:pubmed |
| pubmed-article:14961076 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14961076 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14961076 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:14961076 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14961076 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14961076 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14961076 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14961076 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14961076 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14961076 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14961076 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14961076 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14961076 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:14961076 | pubmed:issn | 0950-9232 | lld:pubmed |
| pubmed-article:14961076 | pubmed:author | pubmed-author:GhoshGourisan... | lld:pubmed |
| pubmed-article:14961076 | pubmed:author | pubmed-author:PhelpsChristo... | lld:pubmed |
| pubmed-article:14961076 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14961076 | pubmed:day | 12 | lld:pubmed |
| pubmed-article:14961076 | pubmed:volume | 23 | lld:pubmed |
| pubmed-article:14961076 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14961076 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14961076 | pubmed:pagination | 1229-38 | lld:pubmed |
| pubmed-article:14961076 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:14961076 | pubmed:meshHeading | pubmed-meshheading:14961076... | lld:pubmed |
| pubmed-article:14961076 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:14961076 | pubmed:articleTitle | Discreet mutations from c-Rel to v-Rel alter kappaB DNA recognition, IkappaBalpha binding, and dimerization: implications for v-Rel oncogenicity. | lld:pubmed |
| pubmed-article:14961076 | pubmed:affiliation | Department of Chemistry and Biochemistry, University of California, San Deigo, USA. | lld:pubmed |
| pubmed-article:14961076 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14961076 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:14961076 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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