Less than a decade ago, it was shown that bromodomains, acetyl lysine 'reader'modules
found in proteins with varied functions, were highly tractable small-molecule targets. This is …

Binding free energy calculations based on molecular simulations provide predicted affinities
for biomolecular complexes. These calculations begin with a detailed description of a …

BRD4, the most extensively studied member of the BET family, is an epigenetic regulator
that localizes to DNA via binding to acetylated histones and controls the expression of …

CBP/p300, functioning as histone acetyltransferases and transcriptional co-factors,
represents an attractive target for various diseases, including malignant tumor. The …

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 …

Components of the chromatin remodelling switch/sucrose nonfermentable (SWI/SNF)
complex are recurrently mutated in tumors, suggesting that altering the activity of the …

Acetylation of histone lysine residues is one of the most well-studied post-translational
modifications of chromatin, selectively recognized by bromodomain “reader” modules …

Bromodomains are epigenetic readers that are recruited to acetyllysine residues in histone
tails. Recent studies have identified non-acetyl acyllysine modifications, raising the …

Bromodomain and extraterminal (BET) domain proteins have emerged as promising
therapeutic targets in glioblastoma and many other cancers. Small molecule inhibitors of …

Members of the bromodomain and extra terminal (BET) family of proteins are essential for
the recognition of acetylated lysine (KAc) residues in histones and have emerged as …