Discovery of epigenetic regulator I-BET762: lead optimization to afford a clinical candidate inhibitor of the BET bromodomains
O Mirguet, R Gosmini, J Toum… - Journal of medicinal …, 2013 - ACS Publications
O Mirguet, R Gosmini, J Toum, CA Clément, M Barnathan, JM Brusq, JE Mordaunt…
Journal of medicinal chemistry, 2013•ACS PublicationsThe bromo and extra C-terminal domain (BET) family of bromodomains are involved in
binding epigenetic marks on histone proteins, more specifically acetylated lysine residues.
This paper describes the discovery and structure–activity relationships (SAR) of potent
benzodiazepine inhibitors that disrupt the function of the BET family of bromodomains
(BRD2, BRD3, and BRD4). This work has yielded a potent, selective compound I-BET762
that is now under evaluation in a phase I/II clinical trial for nuclear protein in testis (NUT) …
binding epigenetic marks on histone proteins, more specifically acetylated lysine residues.
This paper describes the discovery and structure–activity relationships (SAR) of potent
benzodiazepine inhibitors that disrupt the function of the BET family of bromodomains
(BRD2, BRD3, and BRD4). This work has yielded a potent, selective compound I-BET762
that is now under evaluation in a phase I/II clinical trial for nuclear protein in testis (NUT) …
The bromo and extra C-terminal domain (BET) family of bromodomains are involved in binding epigenetic marks on histone proteins, more specifically acetylated lysine residues. This paper describes the discovery and structure–activity relationships (SAR) of potent benzodiazepine inhibitors that disrupt the function of the BET family of bromodomains (BRD2, BRD3, and BRD4). This work has yielded a potent, selective compound I-BET762 that is now under evaluation in a phase I/II clinical trial for nuclear protein in testis (NUT) midline carcinoma and other cancers.
ACS Publications