| pubmed-article:15225747 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15225747 | lifeskim:mentions | umls-concept:C0043457 | lld:lifeskim |
| pubmed-article:15225747 | lifeskim:mentions | umls-concept:C0682969 | lld:lifeskim |
| pubmed-article:15225747 | lifeskim:mentions | umls-concept:C1261322 | lld:lifeskim |
| pubmed-article:15225747 | lifeskim:mentions | umls-concept:C0919430 | lld:lifeskim |
| pubmed-article:15225747 | lifeskim:mentions | umls-concept:C1704241 | lld:lifeskim |
| pubmed-article:15225747 | lifeskim:mentions | umls-concept:C0010423 | lld:lifeskim |
| pubmed-article:15225747 | lifeskim:mentions | umls-concept:C0043301 | lld:lifeskim |
| pubmed-article:15225747 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:15225747 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:15225747 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:15225747 | lifeskim:mentions | umls-concept:C0439611 | lld:lifeskim |
| pubmed-article:15225747 | pubmed:issue | 1-5 | lld:pubmed |
| pubmed-article:15225747 | pubmed:dateCreated | 2004-6-30 | lld:pubmed |
| pubmed-article:15225747 | pubmed:abstractText | The nuclear receptor of Vitamin D can be activated by a large number of agonist molecules with a wide spectrum in their stereochemical framework. Up to now most of our structural information related to the protein-ligand complex formation is based on an engineered ligand binding domain (LBD) of the human receptor. We now have extended our database, using a wild-type LBD from zebrafish that confirms the previously reported results and allows to investigate the binding of ligands that induce significant conformational changes at the protein level. | lld:pubmed |
| pubmed-article:15225747 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15225747 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15225747 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15225747 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15225747 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15225747 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15225747 | pubmed:month | May | lld:pubmed |
| pubmed-article:15225747 | pubmed:issn | 0960-0760 | lld:pubmed |
| pubmed-article:15225747 | pubmed:author | pubmed-author:MorasDinoD | lld:pubmed |
| pubmed-article:15225747 | pubmed:author | pubmed-author:RochelNatacha... | lld:pubmed |
| pubmed-article:15225747 | pubmed:author | pubmed-author:MitschlerAndr... | lld:pubmed |
| pubmed-article:15225747 | pubmed:author | pubmed-author:KouzmenkoAlex... | lld:pubmed |
| pubmed-article:15225747 | pubmed:author | pubmed-author:CiesielskiFab... | lld:pubmed |
| pubmed-article:15225747 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15225747 | pubmed:volume | 89-90 | lld:pubmed |
| pubmed-article:15225747 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15225747 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15225747 | pubmed:pagination | 55-9 | lld:pubmed |
| pubmed-article:15225747 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:15225747 | pubmed:meshHeading | pubmed-meshheading:15225747... | lld:pubmed |
| pubmed-article:15225747 | pubmed:meshHeading | pubmed-meshheading:15225747... | lld:pubmed |
| pubmed-article:15225747 | pubmed:meshHeading | pubmed-meshheading:15225747... | lld:pubmed |
| pubmed-article:15225747 | pubmed:meshHeading | pubmed-meshheading:15225747... | lld:pubmed |
| pubmed-article:15225747 | pubmed:meshHeading | pubmed-meshheading:15225747... | lld:pubmed |
| pubmed-article:15225747 | pubmed:meshHeading | pubmed-meshheading:15225747... | lld:pubmed |
| pubmed-article:15225747 | pubmed:meshHeading | pubmed-meshheading:15225747... | lld:pubmed |
| pubmed-article:15225747 | pubmed:meshHeading | pubmed-meshheading:15225747... | lld:pubmed |
| pubmed-article:15225747 | pubmed:meshHeading | pubmed-meshheading:15225747... | lld:pubmed |
| pubmed-article:15225747 | pubmed:meshHeading | pubmed-meshheading:15225747... | lld:pubmed |
| pubmed-article:15225747 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15225747 | pubmed:articleTitle | Structural investigation of the ligand binding domain of the zebrafish VDR in complexes with 1alpha,25(OH)2D3 and Gemini: purification, crystallization and preliminary X-ray diffraction analysis. | lld:pubmed |
| pubmed-article:15225747 | pubmed:affiliation | Département de Biologie et de Génomique Structurales, IGBMC, CNRS/INSERM/Université Louis Pasteur, Parc d'Innovation BP10142, 67404 Illkirch cedex, France. | lld:pubmed |
| pubmed-article:15225747 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15225747 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:30076 | entrezgene:pubmed | pubmed-article:15225747 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:15225747 | lld:entrezgene |
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