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Updated: Feb 11, 2026

Assays for Validating Histone Acetyltransferase Inhibitors
Published on: August 6, 2020
Lysine acetyltransferase inhibitors: structure-activity relationships and potential therapeutic implications
Francesco Fiorentino1, Antonello Mai2,3, Dante Rotili2
1Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK.
Abstract:
Lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. The dysregulation of this enzyme activity is implicated in many human pathologies such as cancer, neurological and inflammatory disorders. Many lysine acetyltransferase inhibitors (KATi) have been developed so far, but there is still the need for new, more potent, metabolically stable and selective KATi as chemical tools for studying KAT biology and/or as potential therapeutic agents. This review will examine the features of KAT enzymes and related diseases, with particular emphasis on KATi (bisubstrate analogs, natural compounds and synthetic derivatives), analyzing their mechanism of action, structure-activity relationships, pharmacokinetic/pharmacodynamic properties and potential future applications.
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