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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2000-12-18
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pubmed:abstractText |
Androgen receptor (AR) belongs to the superfamily of nuclear hormone receptors that employ complex molecular mechanisms to guide the development and physiological functions of their target tissues. Our recent work has led to the identification of four novel proteins that recognize AR zinc-finger region (ZFR) both in vivo and in vitro. One is a small nuclear RING-finger protein that possesses separate interaction interfaces for AR and for other transcription activators such as Sp1. The second is a nuclear serine/threonine protein kinase (androgen-receptor-interacting nuclear protein kinase; ANPK); however, the receptor itself does not seem to be a substrate for this kinase. The third one is dubbed androgen-receptor-interacting protein 3 (ARIP3) and is a novel member of the PIAS (protein inhibitor of activated STAT) protein family. The fourth protein, termed ARIP4, is a nuclear ATPase that belongs to the SNF2-like family of chromatin remodelling proteins. All four proteins exhibit a punctate nuclear pattern when expressed in cultured cells. Each protein modulates AR-dependent transactivation in co-transfection experiments; their activating functions are not restricted to AR. Current work is aimed at elucidating the biochemical and functional properties of these AR-interacting proteins and at finding the partner proteins that form complexes with them in vivo.
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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/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Chromatin,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hipk3 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Inhibitors of Activated STAT,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Androgen,
http://linkedlifedata.com/resource/pubmed/chemical/SMARCA1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/SMARCA2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/SMARCA4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Smarca4 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:issn |
0300-5127
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
28
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
401-5
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pubmed:dateRevised |
2011-9-1
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pubmed:meshHeading |
pubmed-meshheading:10961928-Adenosine Triphosphatases,
pubmed-meshheading:10961928-Animals,
pubmed-meshheading:10961928-Carrier Proteins,
pubmed-meshheading:10961928-Cell Nucleus,
pubmed-meshheading:10961928-Chromatin,
pubmed-meshheading:10961928-DNA Helicases,
pubmed-meshheading:10961928-DNA-Binding Proteins,
pubmed-meshheading:10961928-Down-Regulation,
pubmed-meshheading:10961928-Gene Expression Regulation,
pubmed-meshheading:10961928-Humans,
pubmed-meshheading:10961928-Male,
pubmed-meshheading:10961928-Nuclear Proteins,
pubmed-meshheading:10961928-Prostatic Neoplasms,
pubmed-meshheading:10961928-Protein Inhibitors of Activated STAT,
pubmed-meshheading:10961928-Protein-Serine-Threonine Kinases,
pubmed-meshheading:10961928-Proteins,
pubmed-meshheading:10961928-Receptors, Androgen,
pubmed-meshheading:10961928-Transcription, Genetic,
pubmed-meshheading:10961928-Transcription Factors,
pubmed-meshheading:10961928-Transfection,
pubmed-meshheading:10961928-X Chromosome,
pubmed-meshheading:10961928-Zinc Fingers
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pubmed:year |
2000
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pubmed:articleTitle |
Androgen-receptor-interacting nuclear proteins.
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pubmed:affiliation |
Institute of Biomedicine, Department of Physiology and Department of Clinical Chemistry, University of Helsinki, P.O. Box 9 (Siltavuorenpenger 20 J), FIN-00014 Helsinki, Finland. olli.janne@helsinki.fi
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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