pubmed-article:11572867 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:11572867 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
pubmed-article:11572867 | lifeskim:mentions | umls-concept:C1428372 | lld:lifeskim |
pubmed-article:11572867 | lifeskim:mentions | umls-concept:C1511662 | lld:lifeskim |
pubmed-article:11572867 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:11572867 | pubmed:issue | 48 | lld:pubmed |
pubmed-article:11572867 | pubmed:dateCreated | 2001-11-23 | lld:pubmed |
pubmed-article:11572867 | pubmed:abstractText | CpG-binding protein is a transcriptional activator that exhibits a unique DNA binding specificity for unmethylated CpG motifs. CpG-binding protein contains a cysteine-rich CXXC domain that is conserved in DNA methyltransferase 1, methyl binding domain protein 1, and human trithorax. In vitro DNA binding assays reveal that CpG-binding protein contains a single DNA binding domain comprised of the CXXC domain and a short carboxyl extension. Specific mutation to alanine of individual conserved cysteine residues within the CXXC domain abolishes DNA binding activity. Denaturation/renaturation experiments in the presence of various metal cations demonstrate that the CXXC domain requires zinc for efficient DNA binding activity. Ligand selection of high affinity binding sites from a pool of degenerate oligonucleotides reveals that CpG-binding protein interacts with a variety of sequences that contains the CpG dinucleotide with a consensus binding site of (A/C)CpG(A/C). Mutation of the CpG motif(s) present within ligand-selected oligonucleotides ablates the interaction with CpG-binding protein, and mutation to thymine of the nucleotides flanking the CpG motifs reduces the affinity of CpG-binding protein. Hence, a CpG motif is necessary and sufficient to comprise a binding site for CpG-binding protein, although the immediate flanking sequence affects binding affinity. | lld:pubmed |
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pubmed-article:11572867 | pubmed:language | eng | lld:pubmed |
pubmed-article:11572867 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11572867 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:11572867 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11572867 | pubmed:month | Nov | lld:pubmed |
pubmed-article:11572867 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:11572867 | pubmed:author | pubmed-author:LeeJ HJH | lld:pubmed |
pubmed-article:11572867 | pubmed:author | pubmed-author:DevV GVG | lld:pubmed |
pubmed-article:11572867 | pubmed:author | pubmed-author:SkalnikD GDG | lld:pubmed |
pubmed-article:11572867 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:11572867 | pubmed:day | 30 | lld:pubmed |
pubmed-article:11572867 | pubmed:volume | 276 | lld:pubmed |
pubmed-article:11572867 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11572867 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11572867 | pubmed:pagination | 44669-76 | lld:pubmed |
pubmed-article:11572867 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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pubmed-article:11572867 | pubmed:year | 2001 | lld:pubmed |
pubmed-article:11572867 | pubmed:articleTitle | Identification and characterization of the DNA binding domain of CpG-binding protein. | lld:pubmed |
pubmed-article:11572867 | pubmed:affiliation | Herman B Wells Center for Pediatric Research, Section of Pediatric Hematology/Oncology and the Department of Pediatrics, Indiana University School of Medicine, Indianapolis, Indiana 46202, USA. | lld:pubmed |
pubmed-article:11572867 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:11572867 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:11572867 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:30827 | entrezgene:pubmed | pubmed-article:11572867 | lld:entrezgene |
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