@article{
 title = {Progress in the Development and Application of Small Molecule Inhibitors of Bromodomain–Acetyl-lysine Interactions},
 type = {article},
 year = {2012},
 pages = {9393-9413},
 volume = {55},
 websites = {http://pubs.acs.org/doi/10.1021/jm300915b},
 publisher = {American Chemical Society},
 id = {47bf5fc5-5933-3417-aba9-7bacb63eba37},
 created = {2015-10-01T17:17:59.000Z},
 file_attached = {true},
 profile_id = {64f7fb50-d000-335d-a02d-06c5f340a97a},
 last_modified = {2018-09-03T10:20:46.364Z},
 read = {false},
 starred = {false},
 authored = {true},
 confirmed = {true},
 hidden = {false},
 citation_key = {Hewings2012b},
 source_type = {Journal Article},
 private_publication = {false},
 abstract = {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...},
 bibtype = {article},
 author = {Hewings, David S. and Rooney, Timothy P. C. and Jennings, Laura E. and Hay, Duncan A. and Schofield, Christopher J. and Brennan, Paul E. and Knapp, Stefan and Conway, Stuart J.},
 doi = {10.1021/jm300915b},
 journal = {Journal of Medicinal Chemistry},
 number = {22}
}

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