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J Med Chem ; 56(19): 7501-15, 2013 Oct 10.
Article in English | MEDLINE | ID: mdl-24015967

ABSTRACT

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.


Subject(s)
Antineoplastic Agents/pharmacology , Benzodiazepines/pharmacology , Nuclear Proteins/antagonists & inhibitors , Transcription Factors/antagonists & inhibitors , Animals , Anti-Inflammatory Agents/chemical synthesis , Anti-Inflammatory Agents/pharmacokinetics , Anti-Inflammatory Agents/pharmacology , Antineoplastic Agents/chemical synthesis , Antineoplastic Agents/pharmacokinetics , Apolipoprotein A-I/biosynthesis , Benzodiazepines/chemical synthesis , Benzodiazepines/pharmacokinetics , Cell Cycle Proteins , Dogs , Epigenesis, Genetic , Humans , Macaca fascicularis , Mice , Models, Molecular , Permeability , Protein Structure, Tertiary , Rats , Stereoisomerism , Structure-Activity Relationship
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