| pubmed-article:13679578 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:13679578 | lifeskim:mentions | umls-concept:C1257890 | lld:lifeskim |
| pubmed-article:13679578 | lifeskim:mentions | umls-concept:C0019647 | lld:lifeskim |
| pubmed-article:13679578 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:13679578 | lifeskim:mentions | umls-concept:C0024337 | lld:lifeskim |
| pubmed-article:13679578 | lifeskim:mentions | umls-concept:C0025723 | lld:lifeskim |
| pubmed-article:13679578 | lifeskim:mentions | umls-concept:C0013138 | lld:lifeskim |
| pubmed-article:13679578 | lifeskim:mentions | umls-concept:C1426004 | lld:lifeskim |
| pubmed-article:13679578 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
| pubmed-article:13679578 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:13679578 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:13679578 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:13679578 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:13679578 | pubmed:issue | 20 | lld:pubmed |
| pubmed-article:13679578 | pubmed:dateCreated | 2003-10-1 | lld:pubmed |
| pubmed-article:13679578 | pubmed:abstractText | Covalent modifications of histone tails modulate gene expression via chromatin organization. As examples, methylation of lysine 9 residues of histone H3 (H3) (H3-K9) is believed to repress transcription by compacting chromatin, whereas methylation of lysine 4 residues of H3 (H3-K4) is believed to activate transcription by relaxing chromatin. The Drosophila trithorax group protein absent, small, or homeotic discs 1 (ASH1) is involved in maintaining active transcription of many genes. Here we report that in extreme ash1 mutants, no H3-K4 methylation is detectable. Within the limits of our assays, this lack of detectable H3-K4 methylation implies that ASH1 is required for essentially all H3-K4 methylation that occurs in vivo. We report further that the 149-aa SET domain of ASH1 is sufficient for H3-K4 methylation in vitro. These findings support a model in which ASH1 is directly involved in maintaining active transcription by conferring a relaxed chromatin structure. | lld:pubmed |
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| pubmed-article:13679578 | pubmed:language | eng | lld:pubmed |
| pubmed-article:13679578 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:13679578 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:13679578 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:13679578 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:13679578 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:13679578 | pubmed:author | pubmed-author:ShearnAllenA | lld:pubmed |
| pubmed-article:13679578 | pubmed:author | pubmed-author:ByrdKristin... | lld:pubmed |
| pubmed-article:13679578 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:13679578 | pubmed:day | 30 | lld:pubmed |
| pubmed-article:13679578 | pubmed:volume | 100 | lld:pubmed |
| pubmed-article:13679578 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:13679578 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:13679578 | pubmed:pagination | 11535-40 | lld:pubmed |
| pubmed-article:13679578 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:13679578 | pubmed:meshHeading | pubmed-meshheading:13679578... | lld:pubmed |
| pubmed-article:13679578 | pubmed:meshHeading | pubmed-meshheading:13679578... | lld:pubmed |
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| pubmed-article:13679578 | pubmed:meshHeading | pubmed-meshheading:13679578... | lld:pubmed |
| pubmed-article:13679578 | pubmed:meshHeading | pubmed-meshheading:13679578... | lld:pubmed |
| pubmed-article:13679578 | pubmed:meshHeading | pubmed-meshheading:13679578... | lld:pubmed |
| pubmed-article:13679578 | pubmed:meshHeading | pubmed-meshheading:13679578... | lld:pubmed |
| pubmed-article:13679578 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:13679578 | pubmed:articleTitle | ASH1, a Drosophila trithorax group protein, is required for methylation of lysine 4 residues on histone H3. | lld:pubmed |
| pubmed-article:13679578 | pubmed:affiliation | Department of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218, USA. | lld:pubmed |
| pubmed-article:13679578 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:13679578 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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