| pubmed-article:11478808 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11478808 | lifeskim:mentions | umls-concept:C0242299 | lld:lifeskim |
| pubmed-article:11478808 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:11478808 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:11478808 | lifeskim:mentions | umls-concept:C0038304 | lld:lifeskim |
| pubmed-article:11478808 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:11478808 | lifeskim:mentions | umls-concept:C1417830 | lld:lifeskim |
| pubmed-article:11478808 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:11478808 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:11478808 | pubmed:dateCreated | 2001-7-31 | lld:pubmed |
| pubmed-article:11478808 | pubmed:abstractText | The human TR4 orphan receptor (TR4) is a member of the nuclear receptor superfamily. It functions as a transcriptional factor which regulates and controls many important physiological functions. It has been documented that TR4 may bind as a homodimer to a DNA response element containing two direct repeats of the AGGTCA consensus motif. Surprisingly, our data reveal that the expression of the human steroid 21-hydroxylase (21-OHase) gene could be repressed by TR4 via the monomeric AGGTCA motif (-228TR4RE) at its 5' flanking region (nucleotide numbers 1431-1444, 5'-GGAAAAAGGTCAGG-3'). Electrophoretic mobility shift assay showed specific binding with a dissociation constant of 0.4 nM between TR4 and the monomeric -288TR4RE motif. However, TR4 does not form heterodimers with either retinoid X receptor alpha or SHP (short heterodimer partner) orphan receptor. Additionally, both dual-luciferase and chloramphenicol acetyltransferase assays demonstrated that TR4 can function as a repressor via the -228TR4RE of the 21-OHase gene. In conclusion, our data suggest that TR4 may bind to a monomeric DNA response element and play an important role in the suppression of the 21-OHase gene expression. | lld:pubmed |
| pubmed-article:11478808 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11478808 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11478808 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11478808 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11478808 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11478808 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11478808 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11478808 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11478808 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11478808 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11478808 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11478808 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11478808 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11478808 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11478808 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:11478808 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:11478808 | pubmed:author | pubmed-author:ChangCC | lld:pubmed |
| pubmed-article:11478808 | pubmed:author | pubmed-author:LeeY FYF | lld:pubmed |
| pubmed-article:11478808 | pubmed:author | pubmed-author:LeeH JHJ | lld:pubmed |
| pubmed-article:11478808 | pubmed:copyrightInfo | Copyright 2001 Academic Press. | lld:pubmed |
| pubmed-article:11478808 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11478808 | pubmed:day | 3 | lld:pubmed |
| pubmed-article:11478808 | pubmed:volume | 285 | lld:pubmed |
| pubmed-article:11478808 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11478808 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11478808 | pubmed:pagination | 1361-8 | lld:pubmed |
| pubmed-article:11478808 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:11478808 | pubmed:meshHeading | pubmed-meshheading:11478808... | lld:pubmed |
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| pubmed-article:11478808 | pubmed:meshHeading | pubmed-meshheading:11478808... | lld:pubmed |
| pubmed-article:11478808 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11478808 | pubmed:articleTitle | TR4 orphan receptor represses the human steroid 21-hydroxylase gene expression through the monomeric AGGTCA motif. | lld:pubmed |
| pubmed-article:11478808 | pubmed:affiliation | Institute of Biotechnology, National Dong Hwa University, Hualien, Taiwan, 974, Republic of China. hjlee@mail.ndhu.edu.tw | lld:pubmed |
| pubmed-article:11478808 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11478808 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11478808 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11478808 | lld:pubmed |
