Journal
JOURNAL OF MEDICINAL CHEMISTRY
Volume 55, Issue 22, Pages 9393-9413Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jm300915b
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Funding
- Cancer Research UK
- GlaxoSmithKline
- Pfizer Neusentis
- UCB
- Structural Genomics Consortium [1097737]
- Canadian Institutes for Health Research
- Canada Foundation for Innovation
- Genome Canada
- Pfizer
- Eli Lilly
- Novartis Research Foundation
- Ontario Ministry of Research and Innovation
- Wellcome Trust
- Cancer Research UK [6947] Funding Source: researchfish
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Bromodomains, protein modules that recognize and bind to acetylated lysine, are emerging as important components of cellular machinery. These acetyl-lysine (KAc) reader domains are part of the write-read-erase concept that has been linked with the transfer of epigenetic information. By reading KAc marks on histones, bromodomains mediate protein-protein interactions between a diverse array of partners. There has been intense activity in developing potent and selective small molecule probes that disrupt the interaction between a given bromodomain and KAc. Rapid success has been achieved with the BET family of bromodomains, and a number of potent and selective probes have been reported. These compounds have enabled linking of the BET bromodomains with diseases, including cancer and inflammation, suggesting that bromodomains are druggable targets. Herein, we review the biology of the bromodomains and discuss the SAR for the existing small molecule probes. The biology that has been enabled by these compounds is summarized.
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