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rdf:type |
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lifeskim:mentions |
umls-concept:C0024660,
umls-concept:C0205314,
umls-concept:C0206588,
umls-concept:C0542341,
umls-concept:C0679622,
umls-concept:C1412133,
umls-concept:C1413550,
umls-concept:C1539082,
umls-concept:C1704241,
umls-concept:C1704259,
umls-concept:C1705987,
umls-concept:C1880371,
umls-concept:C2003939
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pubmed:issue |
3
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pubmed:dateCreated |
1999-4-26
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pubmed:databankReference |
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pubmed:abstractText |
The human thyroid hormone receptor-associated protein (TRAP) complex, an earlier described coactivator for nuclear receptors, and an SRB- and MED-containing cofactor complex (SMCC) that mediates activation by Gal4-p53 are shown to be virtually the same with respect to specific polypeptide subunits, coactivator functions, and mechanisms of action (activator interactions). In parallel with ligand-dependent interactions of nuclear receptors with the TRAP220 subunit, p53 and VP16 activation domains interact directly with a newly cloned TRAP80 subunit. These results indicate novel pathways for the function of nuclear receptors and other activators (p53 and VP16) through a common coactivator complex that is likely to target RNA polymerase II. Identification of the TRAP230 subunit as a previously predicted gene product also suggests a coactivator-related transcription defect in certain disease states.
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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/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Herpes Simplex Virus Protein Vmw65,
http://linkedlifedata.com/resource/pubmed/chemical/MED1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/MED14 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/MED6 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Med17 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Mediator Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Mediator Complex Subunit 1,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Polymerase II,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Calcitriol,
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,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Protein p53
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1097-2765
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
361-70
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10198638-Amino Acid Sequence,
pubmed-meshheading:10198638-Blotting, Northern,
pubmed-meshheading:10198638-Blotting, Western,
pubmed-meshheading:10198638-Carrier Proteins,
pubmed-meshheading:10198638-Cloning, Molecular,
pubmed-meshheading:10198638-Fungal Proteins,
pubmed-meshheading:10198638-Gene Expression Regulation,
pubmed-meshheading:10198638-HeLa Cells,
pubmed-meshheading:10198638-Herpes Simplex Virus Protein Vmw65,
pubmed-meshheading:10198638-Humans,
pubmed-meshheading:10198638-Mediator Complex,
pubmed-meshheading:10198638-Mediator Complex Subunit 1,
pubmed-meshheading:10198638-Molecular Sequence Data,
pubmed-meshheading:10198638-Protein Binding,
pubmed-meshheading:10198638-RNA Polymerase II,
pubmed-meshheading:10198638-Receptors, Calcitriol,
pubmed-meshheading:10198638-Receptors, Thyroid Hormone,
pubmed-meshheading:10198638-Response Elements,
pubmed-meshheading:10198638-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:10198638-Trans-Activators,
pubmed-meshheading:10198638-Transcription Factors,
pubmed-meshheading:10198638-Tumor Suppressor Protein p53
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pubmed:year |
1999
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pubmed:articleTitle |
Identity between TRAP and SMCC complexes indicates novel pathways for the function of nuclear receptors and diverse mammalian activators.
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pubmed:affiliation |
Laboratory of Biochemistry and Molecular Biology, Rockefeller University, New York, New York 10021, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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