pubmed-article:11042264 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:11042264 | lifeskim:mentions | umls-concept:C0140283 | lld:lifeskim |
pubmed-article:11042264 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
pubmed-article:11042264 | lifeskim:mentions | umls-concept:C0251211 | lld:lifeskim |
pubmed-article:11042264 | lifeskim:mentions | umls-concept:C0040624 | lld:lifeskim |
pubmed-article:11042264 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:11042264 | lifeskim:mentions | umls-concept:C0439851 | lld:lifeskim |
pubmed-article:11042264 | lifeskim:mentions | umls-concept:C1552596 | lld:lifeskim |
pubmed-article:11042264 | lifeskim:mentions | umls-concept:C1880177 | lld:lifeskim |
pubmed-article:11042264 | lifeskim:mentions | umls-concept:C1947931 | lld:lifeskim |
pubmed-article:11042264 | lifeskim:mentions | umls-concept:C0062529 | lld:lifeskim |
pubmed-article:11042264 | pubmed:issue | 2-3 | lld:pubmed |
pubmed-article:11042264 | pubmed:dateCreated | 2000-11-3 | lld:pubmed |
pubmed-article:11042264 | pubmed:abstractText | The X gene product of the human hepatitis B virus (HBx), a major factor responsible for hepatitis and hepatocellular carcinoma, modulates transactivation by a variety of transcription factors. Herein, expression of the phosphoenolpyruvate carboxykinase (PEPCK) gene was found to be regulated transcriptionally by HBx through two distinct promoter regions. The cAMP response element (CRE)-1 site within the proximal promoter region mediated the HBx-induced transactivation of the PEPCK gene through C/EBP alpha and ATF-2. A retinoid X receptor (RXR) response element within the distal promoter region also contributed to the HBx-induced transactivation. Consistent with these results, HBx directly interacted with RXR, and the interaction interfaces were localized to the transactivation domain of HBx and the ligand binding domain of RXR. | lld:pubmed |
pubmed-article:11042264 | pubmed:language | eng | lld:pubmed |
pubmed-article:11042264 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11042264 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:11042264 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11042264 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11042264 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11042264 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11042264 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11042264 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11042264 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11042264 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11042264 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11042264 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11042264 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11042264 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11042264 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11042264 | pubmed:month | Oct | lld:pubmed |
pubmed-article:11042264 | pubmed:issn | 0014-5793 | lld:pubmed |
pubmed-article:11042264 | pubmed:author | pubmed-author:KimH DHD | lld:pubmed |
pubmed-article:11042264 | pubmed:author | pubmed-author:LeeJ WJW | lld:pubmed |
pubmed-article:11042264 | pubmed:author | pubmed-author:LeeM YMY | lld:pubmed |
pubmed-article:11042264 | pubmed:author | pubmed-author:CheongJJ | lld:pubmed |
pubmed-article:11042264 | pubmed:author | pubmed-author:HongS HSH | lld:pubmed |
pubmed-article:11042264 | pubmed:author | pubmed-author:KongH JHJ | lld:pubmed |
pubmed-article:11042264 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:11042264 | pubmed:day | 20 | lld:pubmed |
pubmed-article:11042264 | pubmed:volume | 483 | lld:pubmed |
pubmed-article:11042264 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11042264 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11042264 | pubmed:pagination | 114-8 | lld:pubmed |
pubmed-article:11042264 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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pubmed-article:11042264 | pubmed:year | 2000 | lld:pubmed |
pubmed-article:11042264 | pubmed:articleTitle | Direct binding of hepatitis B virus X protein and retinoid X receptor contributes to phosphoenolpyruvate carboxykinase gene transactivation. | lld:pubmed |
pubmed-article:11042264 | pubmed:affiliation | Center for Ligand and Transcription, Chonnam National University, Kwangju, South Korea. | lld:pubmed |
pubmed-article:11042264 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:11042264 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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