Acetylation of lysine residues is a post-translational modification with broad relevance to cellular signaling and disease biology. Enzymes that ‘write’ (histone acetyltransferases, HATs) and ‘erase’ (histone deacetylases, HDACs) acetylation sites are an area of extensive research in current drug development. The principal readers of ɛ-N-acetyl lysine (Kac) marks are Bromo and extra terminal (BET) proteins (BRD2, BRD3, BRD4 and BRDT), which are in turn transcriptional regulators required for efficient expression of several growth promoting and anti-apoptotic genes as well as for cell cycle progression[1]. Moreover, they have an important role in the targeting of chromatin-modifying enzymes to specific sites. Often they act with other protein-interaction modules to guarantee a high level of targeting specificity for these essential enzymes[2].

[1] PFI-1 - A highly Selective Protein Interaction Inhibitor TargetingBET bromodomains. S. Picaud  et al. Cancer Res. 2013, 73, 3336-3346.
[2] Bromodomains as therapeutic targets. S. Muller, P. Filippakopoulos, S. Knapp. Expert Rev. Mol. Med. 2011, 13, e29.

5 Item(s)

per page
Axon ID Name Description From price
2594 CPI 0610 Selective and metabolically stable inhibitor of BET bromodomains €105.00
1989 JQ-1, (+)-

Potent and selective BET bromodomain inhibitor

2530 OTX 015 Potent inhibitor of BRD2, BRD3, and BRD4 with clear anti-proliferative activity €125.00
1887 PFI-1 BET bromodomain (BRD) inhibitor €75.00
2245 RVX 208 BET bromodomain inhibitor specific for second bromodomains (BD2s) €65.00

5 Item(s)

per page
Please wait...