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Potent and selective bivalent inhibitors of BET bromodomains

Michael J Waring,Huawei Chen,Alfred A Rabow,Graeme Walker,Romel Bobby,Scott Boiko, Rob H Bradbury,Rowena Callis,Edwin Clark,Ian Dale,Danette L Daniels,Austin Dulak,Liz Flavell,Geoff Holdgate,Thomas A Jowitt,Alexey Kikhney,Mark McAlister,Jacqui Méndez,Derek Ogg,Joe Patel,Philip Petteruti,Graeme R Robb,Matthew B Robers,Sakina Saif,Natalie Stratton,Dmitri I Svergun,Wenxian Wang,David Whittaker,David M Wilson,Yi Yao

NATURE CHEMICAL BIOLOGY（2016）

Cited 102|Views58
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Abstract
Structural insights demonstrating small-molecule-mediated dimerization of BRD4 bromodomains led to the development of biBET, a compound that potently inhibits BRD4–acetyl-lysine interactions by bivalent binding to tandem bromodomains.
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X-ray crystallography,Chemical biology,Medicinal chemistry,Histone post-translational modifications
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