| pubmed-article:9253789 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9253789 | lifeskim:mentions | umls-concept:C0025914 | lld:lifeskim |
| pubmed-article:9253789 | lifeskim:mentions | umls-concept:C0026809 | lld:lifeskim |
| pubmed-article:9253789 | lifeskim:mentions | umls-concept:C0034804 | lld:lifeskim |
| pubmed-article:9253789 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:9253789 | lifeskim:mentions | umls-concept:C0162493 | lld:lifeskim |
| pubmed-article:9253789 | lifeskim:mentions | umls-concept:C0596260 | lld:lifeskim |
| pubmed-article:9253789 | lifeskim:mentions | umls-concept:C0392760 | lld:lifeskim |
| pubmed-article:9253789 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:9253789 | pubmed:dateCreated | 1997-10-9 | lld:pubmed |
| pubmed-article:9253789 | pubmed:abstractText | To determine the characteristics of the N-terminal transactivation domain (AF-1) of the mouse estrogen receptor (ER), we constructed a number of deletion mutants. Wild-type and mutant receptors were expressed in yeast cells and assayed for their ability to transactivate an estrogen-responsive reporter plasmid (ERE-CYCl-LacZ) that contained a single estrogen response element of the vitellogenin A2 gene promoter. Deletion of the N-terminal 121 amino acids from the mouse ER resulted in a 50% reduction in transactivation activity compared with the full-length wild-type ER. Deletion of the first 150 amino acids resulted in loss of 90% transactivation activity. An ER deletion mutant lacking residues 121-154 retained full transcriptional activity, suggesting that this region plays a significant transacting role only when the first portion is deleted. A point mutation was introduced in the C-terminal region at Met-521 in order to study the possible interaction between the C-terminal ligand-binding domain and the N-terminal AF-1 region. This mutant ER, M521G, exhibited 150% of the transcriptional activity of the wild-type ER. An M521G mutant lacking the N-terminal 121 amino acids retained full transactivation activity, whereas, M521G lacking 150 amino acids resulted in only 10% of wild-type activity. These results suggest that residues 121-154 might interact with the C terminus to affect transcription. In summary, multiple N-terminal regions in the ER were identified that function in transactivation. Furthermore, a point mutation in the C-terminal portion of the ER may change the conformation of the ER ligand-binding domain, producing a more stable receptor/ligand complex that increases transcriptional activity. These data suggest that the N- and C-terminal portions of the ER interact in a cooperative manner to activate transcription from target genes. | lld:pubmed |
| pubmed-article:9253789 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9253789 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9253789 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9253789 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9253789 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9253789 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9253789 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9253789 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9253789 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:9253789 | pubmed:issn | 0039-128X | lld:pubmed |
| pubmed-article:9253789 | pubmed:author | pubmed-author:KohnoHH | lld:pubmed |
| pubmed-article:9253789 | pubmed:author | pubmed-author:KorachK SKS | lld:pubmed |
| pubmed-article:9253789 | pubmed:author | pubmed-author:CurtinTT | lld:pubmed |
| pubmed-article:9253789 | pubmed:author | pubmed-author:GandiniOO | lld:pubmed |
| pubmed-article:9253789 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9253789 | pubmed:volume | 62 | lld:pubmed |
| pubmed-article:9253789 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9253789 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9253789 | pubmed:pagination | 508-15 | lld:pubmed |
| pubmed-article:9253789 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:9253789 | pubmed:meshHeading | pubmed-meshheading:9253789-... | lld:pubmed |
| pubmed-article:9253789 | pubmed:meshHeading | pubmed-meshheading:9253789-... | lld:pubmed |
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| pubmed-article:9253789 | pubmed:meshHeading | pubmed-meshheading:9253789-... | lld:pubmed |
| pubmed-article:9253789 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9253789 | pubmed:articleTitle | Two transcription activation functions in the amino terminus of the mouse estrogen receptor that are affected by the carboxy terminus. | lld:pubmed |
| pubmed-article:9253789 | pubmed:affiliation | Receptor Biology Section, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, North Carolina 27709, USA. | lld:pubmed |
| pubmed-article:9253789 | pubmed:publicationType | Journal Article | lld:pubmed |
