| pubmed-article:9520405 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9520405 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
| pubmed-article:9520405 | lifeskim:mentions | umls-concept:C0062773 | lld:lifeskim |
| pubmed-article:9520405 | lifeskim:mentions | umls-concept:C0018270 | lld:lifeskim |
| pubmed-article:9520405 | lifeskim:mentions | umls-concept:C1414639 | lld:lifeskim |
| pubmed-article:9520405 | lifeskim:mentions | umls-concept:C1333931 | lld:lifeskim |
| pubmed-article:9520405 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
| pubmed-article:9520405 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:9520405 | pubmed:dateCreated | 1998-5-1 | lld:pubmed |
| pubmed-article:9520405 | pubmed:abstractText | Posttranslational acetylation of core histone amino termini has long been associated with transcriptionally active chromatin. Recent reports have demonstrated histone acetyltransferase activity in a small group of conserved transcriptional regulators directly linked to gene activation. In addition, the presence of a putative acetyltransferase domain has been discovered in a group of proteins known as the MYST family (for its founding members MOZ, YBF2/SAS3, SAS2, and Tip60). Members of this family are implicated in acute myeloid leukemia (MOZ), transcriptional silencing in yeast (SAS2 and YBF2/SAS3), HIV Tat interaction in humans (Tip60), and dosage compensation in Drosophila (MOF). In this report, we express a yeast ORF with homology to MYST family members and show it possesses histone acetyltransferase activity. Unlike the other MYST family members in Saccharomyces cerevisiae this gene is essential for growth. | lld:pubmed |
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| pubmed-article:9520405 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:9520405 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9520405 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9520405 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:9520405 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:9520405 | pubmed:author | pubmed-author:SmithE RER | lld:pubmed |
| pubmed-article:9520405 | pubmed:author | pubmed-author:LucchesiJ CJC | lld:pubmed |
| pubmed-article:9520405 | pubmed:author | pubmed-author:AllisC DCD | lld:pubmed |
| pubmed-article:9520405 | pubmed:author | pubmed-author:CookR GRG | lld:pubmed |
| pubmed-article:9520405 | pubmed:author | pubmed-author:EisenAA | lld:pubmed |
| pubmed-article:9520405 | pubmed:author | pubmed-author:ZhouJJ | lld:pubmed |
| pubmed-article:9520405 | pubmed:author | pubmed-author:FOXJ LJL | lld:pubmed |
| pubmed-article:9520405 | pubmed:author | pubmed-author:PannutiAA | lld:pubmed |
| pubmed-article:9520405 | pubmed:author | pubmed-author:SattahMM | lld:pubmed |
| pubmed-article:9520405 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9520405 | pubmed:day | 31 | lld:pubmed |
| pubmed-article:9520405 | pubmed:volume | 95 | lld:pubmed |
| pubmed-article:9520405 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9520405 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9520405 | pubmed:pagination | 3561-5 | lld:pubmed |
| pubmed-article:9520405 | pubmed:dateRevised | 2011-10-27 | lld:pubmed |
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| pubmed-article:9520405 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9520405 | pubmed:articleTitle | ESA1 is a histone acetyltransferase that is essential for growth in yeast. | lld:pubmed |
| pubmed-article:9520405 | pubmed:affiliation | Department of Biology, University of Rochester, Rochester, NY 14627, USA. | lld:pubmed |
| pubmed-article:9520405 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9520405 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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