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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5266
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pubmed:dateCreated |
1996-7-23
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pubmed:databankReference |
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pubmed:abstractText |
SHP is an orphan member of the nuclear hormone receptor superfamily that contains the dimerization and ligand-binding domain found in other family members but lacks the conserved DNA binding domain. In the yeast two-hybrid system, SHP interacted with several conventional and orphan members of the receptor superfamily, including retinoid receptors, the thyroid hormone receptor, and the orphan receptor MB67. SHP also interacted directly with these receptors in vitro. In mammalian cells, SHP specifically inhibited transactivation by the superfamily members with which it interacted. These results suggest that SHP functions as a negative regulator of receptor-dependent signaling pathways.
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pubmed:grant |
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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/DAX-1 Orphan Nuclear Receptor,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/NR0B1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Nr0b1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytoplasmic and Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Retinoic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Thyroid Hormone,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Retinoid X Receptors,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/retinoic acid receptor beta
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
31
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pubmed:volume |
272
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1336-9
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8650544-Amino Acid Sequence,
pubmed-meshheading:8650544-Animals,
pubmed-meshheading:8650544-DAX-1 Orphan Nuclear Receptor,
pubmed-meshheading:8650544-DNA,
pubmed-meshheading:8650544-DNA-Binding Proteins,
pubmed-meshheading:8650544-Humans,
pubmed-meshheading:8650544-Mice,
pubmed-meshheading:8650544-Molecular Sequence Data,
pubmed-meshheading:8650544-Receptors, Cytoplasmic and Nuclear,
pubmed-meshheading:8650544-Receptors, Retinoic Acid,
pubmed-meshheading:8650544-Receptors, Thyroid Hormone,
pubmed-meshheading:8650544-Recombinant Fusion Proteins,
pubmed-meshheading:8650544-Repressor Proteins,
pubmed-meshheading:8650544-Retinoid X Receptors,
pubmed-meshheading:8650544-Signal Transduction,
pubmed-meshheading:8650544-Transcription Factors,
pubmed-meshheading:8650544-Transcriptional Activation,
pubmed-meshheading:8650544-Tumor Cells, Cultured
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pubmed:year |
1996
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pubmed:articleTitle |
An orphan nuclear hormone receptor that lacks a DNA binding domain and heterodimerizes with other receptors.
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pubmed:affiliation |
Department of Molecular Biology, Massachusetts General Hospital, Boston, 02114, 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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