12559765

Source:http://linkedlifedata.com/resource/pubmed/id/12559765

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Subject	Predicate	Object	Context
pubmed-article:12559765	rdf:type	pubmed:Citation	lld:pubmed
pubmed-article:12559765	lifeskim:mentions	umls-concept:C0086418	lld:lifeskim
pubmed-article:12559765	lifeskim:mentions	umls-concept:C0682969	lld:lifeskim
pubmed-article:12559765	lifeskim:mentions	umls-concept:C0017710	lld:lifeskim
pubmed-article:12559765	lifeskim:mentions	umls-concept:C0034809	lld:lifeskim
pubmed-article:12559765	lifeskim:mentions	umls-concept:C0010423	lld:lifeskim
pubmed-article:12559765	lifeskim:mentions	umls-concept:C0597358	lld:lifeskim
pubmed-article:12559765	lifeskim:mentions	umls-concept:C1261552	lld:lifeskim
pubmed-article:12559765	pubmed:issue	2	lld:pubmed
pubmed-article:12559765	pubmed:dateCreated	2003-1-31	lld:pubmed
pubmed-article:12559765	pubmed:abstractText	The crystal structure of the glucocorticoid receptor (GR) ligand binding domain in a ternary complex with dexamethasone and a TIF2 coactivator peptide has been determined recently. The structure reveals several distinct features not found in other nuclear receptors, such as a novel dimerization interface and a second charge clamp that might be important in determining coactivator binding selectivity. The GR ligand binding domain also has a steroid binding pocket that is distinct from other nuclear receptors and might explain its selectivity for glucocorticoids and its diversity of responses.	lld:pubmed
pubmed-article:12559765	pubmed:language	eng	lld:pubmed
pubmed-article:12559765	pubmed:journal	http://linkedlifedata.com/r...	lld:pubmed
pubmed-article:12559765	pubmed:citationSubset	IM	lld:pubmed
pubmed-article:12559765	pubmed:chemical	http://linkedlifedata.com/r...	lld:pubmed
pubmed-article:12559765	pubmed:chemical	http://linkedlifedata.com/r...	lld:pubmed
pubmed-article:12559765	pubmed:status	MEDLINE	lld:pubmed
pubmed-article:12559765	pubmed:month	Feb	lld:pubmed
pubmed-article:12559765	pubmed:issn	0165-6147	lld:pubmed
pubmed-article:12559765	pubmed:author	pubmed-author:CidlowskiJohn...	lld:pubmed
pubmed-article:12559765	pubmed:author	pubmed-author:NecelaBrian...	lld:pubmed
pubmed-article:12559765	pubmed:issnType	Print	lld:pubmed
pubmed-article:12559765	pubmed:volume	24	lld:pubmed
pubmed-article:12559765	pubmed:owner	NLM	lld:pubmed
pubmed-article:12559765	pubmed:authorsComplete	Y	lld:pubmed
pubmed-article:12559765	pubmed:pagination	58-61	lld:pubmed
pubmed-article:12559765	pubmed:dateRevised	2005-11-16	lld:pubmed
pubmed-article:12559765	pubmed:meshHeading	pubmed-meshheading:12559765...	lld:pubmed
pubmed-article:12559765	pubmed:meshHeading	pubmed-meshheading:12559765...	lld:pubmed
pubmed-article:12559765	pubmed:meshHeading	pubmed-meshheading:12559765...	lld:pubmed
pubmed-article:12559765	pubmed:meshHeading	pubmed-meshheading:12559765...	lld:pubmed
pubmed-article:12559765	pubmed:meshHeading	pubmed-meshheading:12559765...	lld:pubmed
pubmed-article:12559765	pubmed:meshHeading	pubmed-meshheading:12559765...	lld:pubmed
pubmed-article:12559765	pubmed:year	2003	lld:pubmed
pubmed-article:12559765	pubmed:articleTitle	Crystallization of the human glucocorticoid receptor ligand binding domain: a step towards selective glucocorticoids.	lld:pubmed
pubmed-article:12559765	pubmed:affiliation	Laboratory of Signal Transduction, Building 101, MD F3-07, Department of Health and Human Services, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC 27709, USA.	lld:pubmed
pubmed-article:12559765	pubmed:publicationType	Journal Article	lld:pubmed
pubmed-article:12559765	pubmed:publicationType	Review	lld:pubmed