| pubmed-article:15456267 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15456267 | lifeskim:mentions | umls-concept:C0019643 | lld:lifeskim |
| pubmed-article:15456267 | lifeskim:mentions | umls-concept:C0449560 | lld:lifeskim |
| pubmed-article:15456267 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:15456267 | pubmed:issue | 21 | lld:pubmed |
| pubmed-article:15456267 | pubmed:dateCreated | 2004-9-30 | lld:pubmed |
| pubmed-article:15456267 | pubmed:abstractText | To probe the steric requirements for deacylation, we synthesized lysine-derived small molecule substrates and examined structure-reactivity relationships with various histone deacetylases. Rat liver, human HeLa, and human recombinant class I and II histone deacetylases (HDACs) as well as human recombinant NAD(+)-dependent SIRT1 (class III enzyme) were used in these studies. A benzyloxycarbonyl substituent on the alpha-amino group yielded the highest conversion rates. Replacing the epsilon-acetyl group with larger lipophilic acyl substituents led to a pronounced decrease in conversion by class I and II enzymes; the class III enzyme displayed a greater tolerance. Incubations with recombinant FLAG-tagged human HDACs 1, 3, and 6 showed a distinct subtype selectivity among small molecule substrates. The subtype selectivity of HDAC inhibitors could be predicted with these substrates and an easily obtainable mixture of HDAC subtypes. | lld:pubmed |
| pubmed-article:15456267 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15456267 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15456267 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15456267 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15456267 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15456267 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15456267 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15456267 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15456267 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15456267 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:15456267 | pubmed:issn | 0022-2623 | lld:pubmed |
| pubmed-article:15456267 | pubmed:author | pubmed-author:YoshidaMinoru... | lld:pubmed |
| pubmed-article:15456267 | pubmed:author | pubmed-author:DequiedtFranc... | lld:pubmed |
| pubmed-article:15456267 | pubmed:author | pubmed-author:VerdinEricE | lld:pubmed |
| pubmed-article:15456267 | pubmed:author | pubmed-author:JungManfredM | lld:pubmed |
| pubmed-article:15456267 | pubmed:author | pubmed-author:HeltwegBirgit... | lld:pubmed |
| pubmed-article:15456267 | pubmed:author | pubmed-author:NishinoNorika... | lld:pubmed |
| pubmed-article:15456267 | pubmed:author | pubmed-author:MarshallBrett... | lld:pubmed |
| pubmed-article:15456267 | pubmed:author | pubmed-author:BrauchCarsten... | lld:pubmed |
| pubmed-article:15456267 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15456267 | pubmed:day | 7 | lld:pubmed |
| pubmed-article:15456267 | pubmed:volume | 47 | lld:pubmed |
| pubmed-article:15456267 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15456267 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15456267 | pubmed:pagination | 5235-43 | lld:pubmed |
| pubmed-article:15456267 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:15456267 | pubmed:meshHeading | pubmed-meshheading:15456267... | lld:pubmed |
| pubmed-article:15456267 | pubmed:meshHeading | pubmed-meshheading:15456267... | lld:pubmed |
| pubmed-article:15456267 | pubmed:meshHeading | pubmed-meshheading:15456267... | lld:pubmed |
| pubmed-article:15456267 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15456267 | pubmed:articleTitle | Subtype selective substrates for histone deacetylases. | lld:pubmed |
| pubmed-article:15456267 | pubmed:affiliation | Department of Pharmaceutical and Medicinal Chemistry, Westfälische Wilhelms-Universität Münster, Hittorfstrasse 58-62, 48149 Münster, Germany. | lld:pubmed |
| pubmed-article:15456267 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15456267 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:15456267 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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