Source:http://linkedlifedata.com/resource/pubmed/id/21334896
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9
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pubmed:dateCreated |
2011-4-25
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pubmed:abstractText |
We have developed an efficient method for synthesizing candidate histone deacetylase (HDAC) inhibitors in 96-well plates, which are used directly in high-throughput screening. We selected building blocks having hydrazide, aldehyde and hydroxamic acid functionalities. The hydrazides were coupled with different aldehydes in DMSO. The resulting products have the previously identified 'cap/linker/biasing element' structure known to favor inhibition of HDACs. These compounds were assayed without further purification. HDAC8-selective inhibitors were discovered from this novel collection of compounds.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1464-3405
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pubmed:author | |
pubmed:copyrightInfo |
Copyright © 2011 Elsevier Ltd. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
21
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2601-5
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pubmed:meshHeading |
pubmed-meshheading:21334896-Biological Assay,
pubmed-meshheading:21334896-Enzyme Activation,
pubmed-meshheading:21334896-Histone Deacetylase Inhibitors,
pubmed-meshheading:21334896-Histone Deacetylases,
pubmed-meshheading:21334896-Humans,
pubmed-meshheading:21334896-Inhibitory Concentration 50,
pubmed-meshheading:21334896-Molecular Structure,
pubmed-meshheading:21334896-Repressor Proteins
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pubmed:year |
2011
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pubmed:articleTitle |
Discovery of histone deacetylase 8 selective inhibitors.
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pubmed:affiliation |
Howard Hughes Medical Institute, Broad Institute of Harvard and MIT, 7 Cambridge Center, Cambridge, MA 02142, USA. wtang@pharmacy.wisc.edu
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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