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We note that there are significant discrepancies between what is reported in ref 1b and our results reported here with respect to the biochemical HDAC inhibitory data obtained and supporting mechanism of action. The biochemical data provided herein reflect activity in highly robust, miniaturized homogeneous assays, with Z′ calculations compatible with high-throughput screening. In this assay, we observe high concordance with published kinetic measurements of enzyme inhibition Ki, Thus, the accuracy of our reported HDAC inhibitory data would be expected to be markedly improved. This is important due to our observation of the unusual, perhaps unprecedented potency of 2 for HDAC1 and the direct comparison provided to FK228. The data offered in ref 1b are IC50 data, which have substantial variation between assays and are thus of limited utility and extensibility. We also note that the present synthesis is significantly higher yielding than that reported
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