Source:http://linkedlifedata.com/resource/pubmed/id/15276186
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2004-7-27
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pubmed:abstractText |
Nuclear receptors are central to the regulation of development, endocrine signalling and metabolism. The transcriptional activity of many receptors is controlled through the binding of small, fat-soluble molecules to the ligand-binding domain. In most cases, ligand binding turns the receptors into potent activators of transcription. This switch involves the exchange of co-regulator proteins that mediate transcriptional regulation. Structural and biochemical studies have together revealed the mechanism of action of this ligand-induced molecular switch, in which changes in the dynamic behaviour of the receptor play a key role. This remarkable dynamic mechanism has facilitated the evolution of a family of nuclear receptors with highly diverse ligand recognition and signalling properties.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0968-0004
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
29
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
317-24
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15276186-Animals,
pubmed-meshheading:15276186-Gene Expression Regulation,
pubmed-meshheading:15276186-Humans,
pubmed-meshheading:15276186-Ligands,
pubmed-meshheading:15276186-Molecular Structure,
pubmed-meshheading:15276186-Protein Conformation,
pubmed-meshheading:15276186-Receptors, Cytoplasmic and Nuclear,
pubmed-meshheading:15276186-Signal Transduction,
pubmed-meshheading:15276186-Transcription, Genetic
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pubmed:year |
2004
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pubmed:articleTitle |
Mechanism of the nuclear receptor molecular switch.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, Research Center for Molecular Medicine, University of Debrecen, Medical and Health Science Center, Nagyerdei Körút 98, Debrecen H-4012, Hungary. lnagy@indi.biochem.dote.hu
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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