| pubmed-article:7565783 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7565783 | lifeskim:mentions | umls-concept:C0021756 | lld:lifeskim |
| pubmed-article:7565783 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:7565783 | lifeskim:mentions | umls-concept:C0034790 | lld:lifeskim |
| pubmed-article:7565783 | lifeskim:mentions | umls-concept:C1704632 | lld:lifeskim |
| pubmed-article:7565783 | lifeskim:mentions | umls-concept:C0871261 | lld:lifeskim |
| pubmed-article:7565783 | lifeskim:mentions | umls-concept:C0086860 | lld:lifeskim |
| pubmed-article:7565783 | lifeskim:mentions | umls-concept:C2911692 | lld:lifeskim |
| pubmed-article:7565783 | lifeskim:mentions | umls-concept:C1706817 | lld:lifeskim |
| pubmed-article:7565783 | lifeskim:mentions | umls-concept:C1948023 | lld:lifeskim |
| pubmed-article:7565783 | lifeskim:mentions | umls-concept:C0086597 | lld:lifeskim |
| pubmed-article:7565783 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:7565783 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:7565783 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:7565783 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:7565783 | pubmed:dateCreated | 1995-11-21 | lld:pubmed |
| pubmed-article:7565783 | pubmed:abstractText | The transcription factors NFAT and AP-1 have been shown to be essential for inducible interleukin-2 (IL-2) expression in activated T cells. NFAT has been previously reported to bind to two sites in the IL-2 promoter: in association with AP-1 at the distal antigen response element at -280 and at -135. On the basis of DNase I footprinting with recombinant NFAT and AP-1 proteins, gel shift assays, and transfection experiments, we have identified three additional NFAT sites in the IL-2 promoter. Strikingly, all five NFAT sites are essential for the full induction of promoter activity in response to T-cell receptor stimulation. Four of the five NFAT sites are part of composite elements able to bind AP-1 in association with NFAT. These sites display a diverse range of cooperativity and interdependency on NFAT and AP-1 proteins for binding. One of the NFAT sites directly overlaps the CD28-responsive element. We present evidence that CD28 inducibility is conferred by the AP-1 component in NFAT-AP-1 composite elements. These findings provide further insight into the mechanisms involved in the regulation of the IL-2 promoter. | lld:pubmed |
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| pubmed-article:7565783 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7565783 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7565783 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7565783 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7565783 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7565783 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:7565783 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:7565783 | pubmed:author | pubmed-author:GlimcherL HLH | lld:pubmed |
| pubmed-article:7565783 | pubmed:author | pubmed-author:SunY LYL | lld:pubmed |
| pubmed-article:7565783 | pubmed:author | pubmed-author:RooneyJ WJW | lld:pubmed |
| pubmed-article:7565783 | pubmed:author | pubmed-author:HoeyTT | lld:pubmed |
