| pubmed-article:9592157 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9592157 | lifeskim:mentions | umls-concept:C0084821 | lld:lifeskim |
| pubmed-article:9592157 | lifeskim:mentions | umls-concept:C0162493 | lld:lifeskim |
| pubmed-article:9592157 | lifeskim:mentions | umls-concept:C1148673 | lld:lifeskim |
| pubmed-article:9592157 | lifeskim:mentions | umls-concept:C0037791 | lld:lifeskim |
| pubmed-article:9592157 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:9592157 | pubmed:dateCreated | 1998-7-20 | lld:pubmed |
| pubmed-article:9592157 | pubmed:abstractText | Hepatocyte nuclear factor 4 (HNF-4) is an orphan intracellular receptor that appears to be a key factor in the regulation of energy metabolism. In order to gain greater understanding of the binding and activation requirements of HNF-4, we performed genetic analysis of the apoCIII promoter, a promoter that has previously been shown to be highly sensitive to HNF-4-induced transcription. We identified two elements within the apoCIII promoter that bind HNF-4, either of which are sufficient to confer promoter induction in response to HNF-4. These two elements are both direct repeat-like in nature, but they differ significantly in motif sequence and the repeats are separated by either 1 or 2 nt. Therefore, to better define the DNA sequence recognition requirements of HNF-4, we utilized PCR-based binding site selection. HNF-4 selected for direct repeat-like elements with either 1 or 2 nt between the repeats. Surprisingly, the strongest selection was for a core motif that included the nucleotides between the repeats. Mutation of the nucleotide between the repeats resulted in a 6-fold reduction in affinity, indicating that the interaction between HNF-4 and the intervening nucleotide(s) is critical for high affinity binding. | lld:pubmed |
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| pubmed-article:9592157 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:9592157 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9592157 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9592157 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:9592157 | pubmed:issn | 0305-1048 | lld:pubmed |
| pubmed-article:9592157 | pubmed:author | pubmed-author:FraserJ DJD | lld:pubmed |
| pubmed-article:9592157 | pubmed:author | pubmed-author:MartinetLL | lld:pubmed |
| pubmed-article:9592157 | pubmed:author | pubmed-author:BriggsM RMR | lld:pubmed |
| pubmed-article:9592157 | pubmed:author | pubmed-author:StraneyRR | lld:pubmed |
| pubmed-article:9592157 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9592157 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:9592157 | pubmed:volume | 26 | lld:pubmed |
| pubmed-article:9592157 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9592157 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9592157 | pubmed:pagination | 2702-7 | lld:pubmed |
| pubmed-article:9592157 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:9592157 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9592157 | pubmed:articleTitle | DNA binding and transcription activation specificity of hepatocyte nuclear factor 4. | lld:pubmed |
| pubmed-article:9592157 | pubmed:affiliation | Ligand Pharmaceuticals Inc., 10255 Science Center Drive, San Diego, CA 92121, USA. jfraser@ligand.com | lld:pubmed |
| pubmed-article:9592157 | pubmed:publicationType | Journal Article | lld:pubmed |
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