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ID: ALA3785033

Journal: J Med Chem

Title: Disrupting Acetyl-Lysine Recognition: Progress in the Development of Bromodomain Inhibitors.

Authors: Romero FA, Taylor AM, Crawford TD, Tsui V, Côté A, Magnuson S.

Abstract: Bromodomains, small protein modules that recognize acetylated lysine on histones, play a significant role in the epigenome, where they function as "readers" that ultimately determine the functional outcome of the post-translational modification. Because the initial discovery of selective BET inhibitors have helped define the role of that protein family in oncology and inflammation, BET bromodomains have continued to garner the most attention of any other bromodomain. More recently, non-BET bromodomain inhibitors that are potent and selective have been disclosed for ATAD2, CBP, BRD7/9, BRPF, BRPF/TRIM24, CECR2, SMARCA4, and BAZ2A/B. Such novel inhibitors can be used to probe the physiological function of these non-BET bromodomains and further understanding of their role in certain disease states. Here, we provide an update to the progress in identifying selective bromodomain inhibitors and their use as biological tools, as well as our perspective on the field.

CiteXplore: 26572217

DOI: 10.1021/acs.jmedchem.5b01514