Anton V. Bieliauskas

TL;DR: This tutorial review focuses on the recent progress toward the identification of class- selective and isoform-selective HDAC inhibitors, suggesting that subtle differences in the active sites of the HDAC isoforms can be exploited to dictate selectivity.

TL;DR: A small molecule library with a variety of substituent attached adjacent to the metal binding hydroxamic acid of SAHA led to an 800- to 5000-fold decrease in inhibition compared to SAHA, suggesting that HDAC inhibitors with substituents near the metalbinding moiety will have inhibitory activities in the micromolar rather than nanomolar range.

TL;DR: In this article, a tutorial review focuses on the recent progress toward the identification of class-selective and iso-formselective histone deacetylase (HDAC) inhibitors and the emerging trends suggest that subtle differences in the active sites of the HDAC isoforms can be exploited to dictate selectivity.

TL;DR: Modification of the nonselective inhibitor SAHA generated HDAC6/HDAC8 dual selective inhibitors, which can be useful lead compounds toward developing pharmacological tools and more effective anticancer drugs.

TL;DR: N‐substituted SAHA analogs with substituents on the hydroxamic acid metal binding moiety are synthesized and tested and are consistent with the strategy exploiting the 14‐Å internal cavity of HDAC proteins to create HDAC1/2 selective inhibitors.