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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 |
2008-4-4
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pubmed:databankReference |
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pubmed:abstractText |
The histone H3 lysine 4 demethylase RBP2 contains a DNA binding domain, the AT-rich interaction domain (ARID). We solved the structure of ARID by NMR, identified its DNA binding motif (CCGCCC) and characterized the binding contacts. Immunofluorescence and luciferase assays indicated that ARID is required for RBP2 demethylase activity in cells and that DNA recognition is essential to regulate transcription.
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1545-9985
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
15
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
419-21
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:18270511-DNA,
pubmed-meshheading:18270511-Fluorescent Antibody Technique,
pubmed-meshheading:18270511-Humans,
pubmed-meshheading:18270511-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:18270511-Promoter Regions, Genetic,
pubmed-meshheading:18270511-Protein Binding,
pubmed-meshheading:18270511-Protein-Serine-Threonine Kinases,
pubmed-meshheading:18270511-Retinol-Binding Proteins, Cellular,
pubmed-meshheading:18270511-Structure-Activity Relationship
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pubmed:year |
2008
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pubmed:articleTitle |
The ARID domain of the H3K4 demethylase RBP2 binds to a DNA CCGCCC motif.
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pubmed:affiliation |
Department of Chemistry, Ohio State University, 100 West 18th Ave., Columbus, Ohio 43210, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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