| pubmed-article:11520662 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11520662 | lifeskim:mentions | umls-concept:C0206588 | lld:lifeskim |
| pubmed-article:11520662 | lifeskim:mentions | umls-concept:C0242617 | lld:lifeskim |
| pubmed-article:11520662 | lifeskim:mentions | umls-concept:C1417839 | lld:lifeskim |
| pubmed-article:11520662 | lifeskim:mentions | umls-concept:C0162808 | lld:lifeskim |
| pubmed-article:11520662 | pubmed:issue | 1-2 | lld:pubmed |
| pubmed-article:11520662 | pubmed:dateCreated | 2001-8-24 | lld:pubmed |
| pubmed-article:11520662 | pubmed:abstractText | The Drosophila homeodomain protein Fushi Tarazu (Ftz) and its partner, the orphan receptor Ftz-F1, are members of two distinct families of DNA binding transcriptional regulators. Ftz and Ftz-F1 form a novel partnership in vivo as a Hox/orphan receptor heterodimer. Here we show that the murine Ftz-F1 ortholog SF-1 functionally substitutes for Ftz-F1 in vivo, rescuing the defects of ftz-f1 mutants. This finding identified evolutionarily conserved domains of Ftz-F1 as critical for activity of this receptor in vivo. These domains function, at least in part, by mediating direct protein interactions with Ftz. The Ftz-F1 DNA binding domain interacts strongly with Ftz and dramatically facilitates the binding of Ftz to target DNA. This interaction is augmented by a second interaction between the AF-2 domain of Ftz-F1 and the N-terminus of Ftz via an LRALL sequence in Ftz that is reminiscent of LXXLL motifs in nuclear receptor coactivators. We propose that Ftz-F1 serves as a cofactor for Ftz by facilitating the selection of target sites in the genome that contain Ftz/Ftz-F1 composite binding sites. Ftz, on the other hand, influences Ftz-F1 activity by interacting with its AF-2 domain in a manner that mimics a nuclear receptor coactivator. | lld:pubmed |
| pubmed-article:11520662 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11520662 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11520662 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11520662 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11520662 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11520662 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11520662 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11520662 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11520662 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11520662 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11520662 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11520662 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11520662 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11520662 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11520662 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:11520662 | pubmed:issn | 0925-4773 | lld:pubmed |
| pubmed-article:11520662 | pubmed:author | pubmed-author:ORRR TRT | lld:pubmed |
| pubmed-article:11520662 | pubmed:author | pubmed-author:SageE HEH | lld:pubmed |
| pubmed-article:11520662 | pubmed:author | pubmed-author:PickLL | lld:pubmed |
| pubmed-article:11520662 | pubmed:author | pubmed-author:YussaMM | lld:pubmed |
| pubmed-article:11520662 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11520662 | pubmed:volume | 107 | lld:pubmed |
| pubmed-article:11520662 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11520662 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11520662 | pubmed:pagination | 39-53 | lld:pubmed |
| pubmed-article:11520662 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:11520662 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11520662 | pubmed:articleTitle | The nuclear receptor Ftz-F1 and homeodomain protein Ftz interact through evolutionarily conserved protein domains. | lld:pubmed |
| pubmed-article:11520662 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, Mount Sinai School of Medicine, One Gustave L. Levy Place, New York, NY 10029, USA. | lld:pubmed |
| pubmed-article:11520662 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11520662 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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