Lysine acetylation is a key mechanism that regulates chromatin structure; aberrant
acetylation levels have been linked to the development of several diseases. Acetyl-lysine …

Lysine acetylation is a fundamental post-translational modification that plays an important
role in the control of gene transcription in chromatin in an ordered fashion. The …

Concomitant inhibition of multiple cancer-driving kinases is an established strategy to
improve the durability of clinical responses to targeted therapies. The difficulty of discovering …

The bromodomain and extraterminal (BET) domain family of proteins binds to acetylated
lysines on histones and regulates gene transcription. Recently, BET inhibitors (BETi) have …

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 …

The estrogen receptor α (ERα) controls cell proliferation and tumorigenesis by recruiting
various cofactors to estrogen response elements (EREs) to control gene transcription. A …

Over the past several years, there has been rapidly expanding evidence of epigenetic
dysregulation in cancer, in which histone and DNA modification play a critical role in tumor …

Bromodomain protein 4 (BRD4) is a member of the bromodomain and extra-terminal domain
(BET) protein family. It binds to acetylated histone tails via its tandem bromodomains BD1 …

Over 60 bromodomains belonging to proteins with very different functions have been
identified in humans. Several of them interact with acetylated lysine residues, leading to the …

Introduction: The bromodomain (BRD) and extra-C terminal domain (BET) protein family
consists of four members (BRD2, BRD3, BRD4 and BRDT). These “epigenetic readers” bind …