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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2001-4-18
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pubmed:abstractText |
The TRAP/SMCC/Mediator complex is a mammalian transcriptional regulatory complex that contains over 25 polypeptides and is, in part, phylogenetically conserved. It was originally isolated as a thyroid hormone receptor (TR)-associated protein (TRAP) complex that mediates TR-activated transcription from DNA templates in conjunction with the general transcription machinery, and probably acts in vivo after the action of other receptor-interacting coactivators involved in chromatin remodeling. Subsequently, the TRAP complex was identified as a more broadly used coactivator complex for a wide variety of activators. The TRAP220 subunit mediates ligand-dependent interactions of the complex with TR and other nuclear receptors; and genetic ablation of murine TRAP220 has revealed that it is essential both for optimal TR function and for a variety of early developmental and adult homeostasis events in mice, but not for cell viability per se.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Med1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Med6 protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/Mediator Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Mediator Complex Subunit 1,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Thyroid Hormone,
http://linkedlifedata.com/resource/pubmed/chemical/SRB2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1043-2760
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
127-34
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11306338-Animals,
pubmed-meshheading:11306338-Caenorhabditis elegans,
pubmed-meshheading:11306338-Carrier Proteins,
pubmed-meshheading:11306338-Drosophila Proteins,
pubmed-meshheading:11306338-Drosophila melanogaster,
pubmed-meshheading:11306338-Embryo, Mammalian,
pubmed-meshheading:11306338-Embryo, Nonmammalian,
pubmed-meshheading:11306338-Fungal Proteins,
pubmed-meshheading:11306338-Hypothyroidism,
pubmed-meshheading:11306338-Mediator Complex,
pubmed-meshheading:11306338-Mediator Complex Subunit 1,
pubmed-meshheading:11306338-Mice,
pubmed-meshheading:11306338-Mutation,
pubmed-meshheading:11306338-Receptors, Thyroid Hormone,
pubmed-meshheading:11306338-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:11306338-Trans-Activators,
pubmed-meshheading:11306338-Transcription Factors
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pubmed:year |
2001
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pubmed:articleTitle |
The TRAP/SMCC/Mediator complex and thyroid hormone receptor function.
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pubmed:affiliation |
Laboratory of Biochemistry and Molecular Biology, The Rockefeller University, 1230 York Avenue, New York, NY 10021-6399, USA.
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pubmed:publicationType |
Journal Article,
Review
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