| pubmed-article:20472442 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20472442 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:20472442 | lifeskim:mentions | umls-concept:C1421934 | lld:lifeskim |
| pubmed-article:20472442 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:20472442 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:20472442 | pubmed:dateCreated | 2010-5-31 | lld:pubmed |
| pubmed-article:20472442 | pubmed:abstractText | Histone deacetylases are key regulators of gene expression and have recently emerged as important therapeutic targets for cancer and a growing number of non-malignant diseases. Many widely studied inhibitors of HDACs such as SAHA are thought to have low selectivity within or between the human HDAC isoform classes. Using an isoform-selective assay, we have shown that a number of the known inhibitors have in fact a low activity against HDAC8. Based on the wealth of structural information available for human HDAC8, we use a combination of docking and molecular dynamics simulations to determine the structural origin of the experimental results. A close relationship is found between the activity and the high surface malleability of HDAC8. These results provide a rationale for the recently described 'linkerless' HDAC8 selective inhibitors and design criteria for HDAC8 selective inhibitors. | lld:pubmed |
| pubmed-article:20472442 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20472442 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20472442 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20472442 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20472442 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20472442 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20472442 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20472442 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20472442 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20472442 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20472442 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:20472442 | pubmed:issn | 1464-3391 | lld:pubmed |
| pubmed-article:20472442 | pubmed:author | pubmed-author:WiestOlafO | lld:pubmed |
| pubmed-article:20472442 | pubmed:author | pubmed-author:MazitschekRal... | lld:pubmed |
| pubmed-article:20472442 | pubmed:author | pubmed-author:WestNathanN | lld:pubmed |
| pubmed-article:20472442 | pubmed:author | pubmed-author:GreenbergEdwa... | lld:pubmed |
| pubmed-article:20472442 | pubmed:author | pubmed-author:EstiuGuillerm... | lld:pubmed |
| pubmed-article:20472442 | pubmed:author | pubmed-author:BradnerJames... | lld:pubmed |
| pubmed-article:20472442 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20472442 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:20472442 | pubmed:volume | 18 | lld:pubmed |
| pubmed-article:20472442 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20472442 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20472442 | pubmed:pagination | 4103-10 | lld:pubmed |
| pubmed-article:20472442 | pubmed:dateRevised | 2011-4-14 | lld:pubmed |
| pubmed-article:20472442 | pubmed:meshHeading | pubmed-meshheading:20472442... | lld:pubmed |
| pubmed-article:20472442 | pubmed:meshHeading | pubmed-meshheading:20472442... | lld:pubmed |
| pubmed-article:20472442 | pubmed:meshHeading | pubmed-meshheading:20472442... | lld:pubmed |
| pubmed-article:20472442 | pubmed:meshHeading | pubmed-meshheading:20472442... | lld:pubmed |
| pubmed-article:20472442 | pubmed:meshHeading | pubmed-meshheading:20472442... | lld:pubmed |
| pubmed-article:20472442 | pubmed:meshHeading | pubmed-meshheading:20472442... | lld:pubmed |
| pubmed-article:20472442 | pubmed:meshHeading | pubmed-meshheading:20472442... | lld:pubmed |
| pubmed-article:20472442 | pubmed:meshHeading | pubmed-meshheading:20472442... | lld:pubmed |
| pubmed-article:20472442 | pubmed:meshHeading | pubmed-meshheading:20472442... | lld:pubmed |
| pubmed-article:20472442 | pubmed:meshHeading | pubmed-meshheading:20472442... | lld:pubmed |
| pubmed-article:20472442 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20472442 | pubmed:articleTitle | On the inhibition of histone deacetylase 8. | lld:pubmed |
| pubmed-article:20472442 | pubmed:affiliation | Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN 46556-5670, USA. | lld:pubmed |
| pubmed-article:20472442 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20472442 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | http://linkedlifedata.com/r... | pubmed-article:20472442 | lld:chembl |
