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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5229
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pubmed:dateCreated |
1995-10-5
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pubmed:databankReference |
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pubmed:abstractText |
Germline mutations in the von Hippel-Lindau tumor suppressor gene (VHL) predispose individuals to a variety of tumors, including renal carcinoma, hemangioblastoma of the central nervous system, and pheochromocytoma. Here, a cellular transcription factor, Elongin (SIII), is identified as a functional target of the VHL protein. Elongin (SIII) is a heterotrimer consisting of a transcriptionally active subunit (A) and two regulatory subunits (B and C) that activate transcription elongation by RNA polymerase II. The VHL protein was shown to bind tightly and specifically to the Elongin B and C subunits and to inhibit Elongin (SIII) transcriptional activity in vitro. These findings reveal a potentially important transcriptional regulatory network in which the VHL protein may play a key role.
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pubmed:grant |
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pubmed:commentsCorrections |
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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/Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Polymerase II,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/VHL protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Von Hippel-Lindau Tumor Suppressor...,
http://linkedlifedata.com/resource/pubmed/chemical/elongin
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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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 |
8
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pubmed:volume |
269
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pubmed:geneSymbol |
VHL
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1402-6
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:7660122-Amino Acid Sequence,
pubmed-meshheading:7660122-Animals,
pubmed-meshheading:7660122-Cell Line,
pubmed-meshheading:7660122-Cloning, Molecular,
pubmed-meshheading:7660122-Gene Expression Regulation,
pubmed-meshheading:7660122-Genes, Tumor Suppressor,
pubmed-meshheading:7660122-HeLa Cells,
pubmed-meshheading:7660122-Humans,
pubmed-meshheading:7660122-Ligases,
pubmed-meshheading:7660122-Molecular Sequence Data,
pubmed-meshheading:7660122-Mutation,
pubmed-meshheading:7660122-Nuclear Proteins,
pubmed-meshheading:7660122-RNA Polymerase II,
pubmed-meshheading:7660122-Recombinant Proteins,
pubmed-meshheading:7660122-Transcription, Genetic,
pubmed-meshheading:7660122-Transcription Factors,
pubmed-meshheading:7660122-Tumor Suppressor Proteins,
pubmed-meshheading:7660122-Ubiquitin-Protein Ligases,
pubmed-meshheading:7660122-Von Hippel-Lindau Tumor Suppressor Protein,
pubmed-meshheading:7660122-von Hippel-Lindau Disease
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pubmed:year |
1995
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pubmed:articleTitle |
Inhibition of transcription elongation by the VHL tumor suppressor protein.
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pubmed:affiliation |
Urologic Oncology Section, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, 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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