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| pubmed-article:17085591 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:17085591 | lifeskim:mentions | umls-concept:C0086222 | lld:lifeskim |
| pubmed-article:17085591 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
| pubmed-article:17085591 | lifeskim:mentions | umls-concept:C0037633 | lld:lifeskim |
| pubmed-article:17085591 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:17085591 | lifeskim:mentions | umls-concept:C1382100 | lld:lifeskim |
| pubmed-article:17085591 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:17085591 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:17085591 | lifeskim:mentions | umls-concept:C1705733 | lld:lifeskim |
| pubmed-article:17085591 | pubmed:issue | 46 | lld:pubmed |
| pubmed-article:17085591 | pubmed:dateCreated | 2006-11-19 | lld:pubmed |
| pubmed-article:17085591 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17085591 | pubmed:abstractText | Transcription enhancer factor 1 is essential for cardiac, skeletal, and smooth muscle development and uses its N-terminal TEA domain (TEAD) to bind M-CAT elements. Here, we present the first structure of TEAD and show that it is a three-helix bundle with a homeodomain fold. Structural data reveal how TEAD binds DNA. Using structure-function correlations, we find that the L1 loop is essential for cooperative loading of TEAD molecules on to tandemly duplicated M-CAT sites. Furthermore, using a microarray chip-based assay, we establish that known binding sites of the full-length protein are only a subset of DNA elements recognized by TEAD. Our results provide a model for understanding the regulation of genome-wide gene expression during development by TEA/ATTS family of transcription factors. | lld:pubmed |
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| pubmed-article:17085591 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17085591 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17085591 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17085591 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17085591 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17085591 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17085591 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17085591 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:17085591 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:17085591 | pubmed:author | pubmed-author:HalderGeorgG | lld:pubmed |
| pubmed-article:17085591 | pubmed:author | pubmed-author:GaoXiaolianX | lld:pubmed |
| pubmed-article:17085591 | pubmed:author | pubmed-author:Veeraraghavan... | lld:pubmed |
| pubmed-article:17085591 | pubmed:author | pubmed-author:AnbanandamAso... | lld:pubmed |
| pubmed-article:17085591 | pubmed:author | pubmed-author:AlbaradoDiana... | lld:pubmed |
| pubmed-article:17085591 | pubmed:author | pubmed-author:NguyenCatheri... | lld:pubmed |
| pubmed-article:17085591 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17085591 | pubmed:day | 14 | lld:pubmed |
| pubmed-article:17085591 | pubmed:volume | 103 | lld:pubmed |
| pubmed-article:17085591 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17085591 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17085591 | pubmed:pagination | 17225-30 | lld:pubmed |
| pubmed-article:17085591 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:17085591 | pubmed:meshHeading | pubmed-meshheading:17085591... | lld:pubmed |
| pubmed-article:17085591 | pubmed:meshHeading | pubmed-meshheading:17085591... | lld:pubmed |
| pubmed-article:17085591 | pubmed:meshHeading | pubmed-meshheading:17085591... | lld:pubmed |
