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• W2016012641 abstract "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." @default.
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• W2016012641 date "2010-06-01" @default.
• W2016012641 modified "2023-09-29" @default.
• W2016012641 title "On the inhibition of histone deacetylase 8" @default.
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• W2016012641 doi "https://doi.org/10.1016/j.bmc.2010.03.080" @default.
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