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rdf:type |
|
|
lifeskim:mentions |
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pubmed:issue |
26
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pubmed:dateCreated |
2002-1-10
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pubmed:abstractText |
Seventy-two hundred potential inhibitors of the histone deacetylase (HDAC) enzyme family, based on a 1,3-dioxane diversity structure, were synthesized on polystyrene macrobeads. The compounds were arrayed for biological assays in a "one bead-one stock solution" format. Metal-chelating functional groups were used to direct the 1,3-dioxanes to HDAC enzymes, which are zinc hydrolases. Representative structures from this library were tested for inhibitory activity and the 1,3-dioxane structure was shown to be compatible with HDAC inhibition. [structure: see text]
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
|
|
pubmed:citationSubset |
IM
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|
pubmed:chemical |
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|
pubmed:status |
MEDLINE
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pubmed:month |
Dec
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|
pubmed:issn |
1523-7060
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pubmed:author |
|
|
pubmed:issnType |
Print
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pubmed:day |
27
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pubmed:volume |
3
|
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pubmed:owner |
NLM
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|
pubmed:authorsComplete |
Y
|
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pubmed:pagination |
4239-42
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
|
|
pubmed:year |
2001
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|
pubmed:articleTitle |
Synthesis of 7200 small molecules based on a substructural analysis of the histone deacetylase inhibitors trichostatin and trapoxin.
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|
pubmed:affiliation |
Howard Hughes Medical Institute (HHMI), Institute of Chemistry and Cell Biology (ICCB), Department of Chemistry & Chemical Biology, Harvard University, Cambridge, MA 02138, USA.
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|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
|
