| pubmed-article:17715390 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17715390 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:17715390 | lifeskim:mentions | umls-concept:C1156199 | lld:lifeskim |
| pubmed-article:17715390 | lifeskim:mentions | umls-concept:C1149367 | lld:lifeskim |
| pubmed-article:17715390 | lifeskim:mentions | umls-concept:C0002270 | lld:lifeskim |
| pubmed-article:17715390 | pubmed:issue | 13 | lld:pubmed |
| pubmed-article:17715390 | pubmed:dateCreated | 2007-12-6 | lld:pubmed |
| pubmed-article:17715390 | pubmed:abstractText | To address the mechanism by which the human globin genes are activated during erythropoiesis, we have used a tiled microarray to analyze the pattern of transcription factor binding and associated histone modifications across the telomeric region of human chromosome 16 in primary erythroid and nonerythroid cells. This 220-kb region includes the alpha globin genes and 9 widely expressed genes flanking the alpha globin locus. This un-biased, comprehensive analysis of transcription factor binding and histone modifications (acetylation and methylation) described here not only identified all known cis-acting regulatory elements in the human alpha globin cluster but also demonstrated that there are no additional erythroid-specific regulatory elements in the 220-kb region tested. In addition, the pattern of histone modification distinguished promoter elements from potential enhancer elements across this region. Finally, comparison of the human and mouse orthologous regions in a unique mouse model, with both regions coexpressed in the same animal, showed significant differences that may explain how these 2 clusters are regulated differently in vivo. | lld:pubmed |
| pubmed-article:17715390 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17715390 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17715390 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17715390 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17715390 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17715390 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:17715390 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17715390 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17715390 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17715390 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17715390 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:17715390 | pubmed:issn | 0006-4971 | lld:pubmed |
| pubmed-article:17715390 | pubmed:author | pubmed-author:DunhamIanI | lld:pubmed |
| pubmed-article:17715390 | pubmed:author | pubmed-author:HiggsDouglas... | lld:pubmed |
| pubmed-article:17715390 | pubmed:author | pubmed-author:De... | lld:pubmed |
| pubmed-article:17715390 | pubmed:author | pubmed-author:AnguitaEduard... | lld:pubmed |
| pubmed-article:17715390 | pubmed:author | pubmed-author:SharpeJacquel... | lld:pubmed |
| pubmed-article:17715390 | pubmed:author | pubmed-author:Sloane-Stanle... | lld:pubmed |
| pubmed-article:17715390 | pubmed:author | pubmed-author:WoodWilliam... | lld:pubmed |
| pubmed-article:17715390 | pubmed:author | pubmed-author:HughesJimJ | lld:pubmed |
| pubmed-article:17715390 | pubmed:author | pubmed-author:GibbonsRichar... | lld:pubmed |
| pubmed-article:17715390 | pubmed:author | pubmed-author:KochChristoph... | lld:pubmed |
| pubmed-article:17715390 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17715390 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:17715390 | pubmed:volume | 110 | lld:pubmed |
| pubmed-article:17715390 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17715390 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17715390 | pubmed:pagination | 4503-10 | lld:pubmed |
| pubmed-article:17715390 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:17715390 | pubmed:meshHeading | pubmed-meshheading:17715390... | lld:pubmed |
| pubmed-article:17715390 | pubmed:meshHeading | pubmed-meshheading:17715390... | lld:pubmed |
| pubmed-article:17715390 | pubmed:meshHeading | pubmed-meshheading:17715390... | lld:pubmed |
| pubmed-article:17715390 | pubmed:meshHeading | pubmed-meshheading:17715390... | lld:pubmed |
| pubmed-article:17715390 | pubmed:meshHeading | pubmed-meshheading:17715390... | lld:pubmed |
| pubmed-article:17715390 | pubmed:meshHeading | pubmed-meshheading:17715390... | lld:pubmed |
| pubmed-article:17715390 | pubmed:meshHeading | pubmed-meshheading:17715390... | lld:pubmed |
| pubmed-article:17715390 | pubmed:meshHeading | pubmed-meshheading:17715390... | lld:pubmed |
| pubmed-article:17715390 | pubmed:meshHeading | pubmed-meshheading:17715390... | lld:pubmed |
| pubmed-article:17715390 | pubmed:meshHeading | pubmed-meshheading:17715390... | lld:pubmed |
| pubmed-article:17715390 | pubmed:meshHeading | pubmed-meshheading:17715390... | lld:pubmed |
| pubmed-article:17715390 | pubmed:meshHeading | pubmed-meshheading:17715390... | lld:pubmed |
| pubmed-article:17715390 | pubmed:meshHeading | pubmed-meshheading:17715390... | lld:pubmed |
| pubmed-article:17715390 | pubmed:meshHeading | pubmed-meshheading:17715390... | lld:pubmed |
| pubmed-article:17715390 | pubmed:meshHeading | pubmed-meshheading:17715390... | lld:pubmed |
| pubmed-article:17715390 | pubmed:meshHeading | pubmed-meshheading:17715390... | lld:pubmed |
| pubmed-article:17715390 | pubmed:meshHeading | pubmed-meshheading:17715390... | lld:pubmed |
| pubmed-article:17715390 | pubmed:meshHeading | pubmed-meshheading:17715390... | lld:pubmed |
| pubmed-article:17715390 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17715390 | pubmed:articleTitle | Tissue-specific histone modification and transcription factor binding in alpha globin gene expression. | lld:pubmed |
| pubmed-article:17715390 | pubmed:affiliation | Medical Research Council, Molecular Haematology Unit, Weatherall Institute of Molecular Medicine, Oxford University, Oxford, UK. | lld:pubmed |
| pubmed-article:17715390 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17715390 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:17715390 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| entrez-gene:3040 | entrezgene:pubmed | pubmed-article:17715390 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:17715390 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17715390 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17715390 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17715390 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17715390 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17715390 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17715390 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17715390 | lld:pubmed |
