Tag: BET

GSK778 is a Potent and Selective Inhibitor of BET BD1

The bromodomain is a protein domain of about 110 amino acids, which can recognize acetylated lysine residues. Specifically, the bet (Bromo- and terminal domain) family consists of germ cell-specific (BRDT) and ubiquitously expressed (BRD2, BRD3, Brd4) epigenetic reader proteins. As a “reader” of lysine acetylation, bromodomain is responsible for...

MS645, a Bivalent BET BrD Inhibitor, Inhibits BRD4 Transcriptional Activity

Bromodomains (BrDs) in transcription proteins bind acetyl-lysine in histones and transcription factors to direct gene transcription in biology and disease conditions.  BRD4 contains two characteristic tandem BrDs. Meanwhile, BRD4 is a major drug target owing to its implicated functions in oncogenesis and inflammation. BET protein BRD4 in gene transcription...

CD161 is an Orally Active BET Bromodomain Inhibitor

Bromodomain and extra-terminal (BET) family proteins include BRD2, BRD3, BRD4, and a testis-specific protein BRDT. In this study, researchers identify CD161. CD161 is a potent, orally bioavailable and selective BET bromodomain inhibitor. Especially, CD161 binds to BET proteins with low nanomolar affinities and demonstrates high selectivity over 24 non-BET...

BY27 is a Selective and Orally Active BET BD2 Inhibitor

BET (Bromodomain and extra terminal domain) is a well-known member of the bromodomain family. It contains BRD2, BRD3, BRD4, and BRDT, which have two tandem bromodomains (BD1 and BD2). BD1 and BD2 are recognition motifs for the acetyl-lysine residues of N terminuses of histones as well as other proteins....

BAY1238097 is a Selective Inhibitor of BET Binding to Histones

Several BET inhibitors with strong anti-tumor efficacy have been described in recent years. Most of them are derived from diazepine and azepine scaffolds, besides, more recently quinazolinones and isoxazoles chemotypes have been identified. Additionally, a study from Pascale Lejeune identified and verified a novel BET inhibitor BAY1238097, which shows...