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 …

Histone acetylation marks are written by histone acetyltransferases (HATs) and read by
bromodomains (BrDs), and less commonly by other protein modules. These proteins …

The papillomavirus E2 proteins are pivotal to the viral life cycle and have well characterized
functions in transcriptional regulation, initiation of DNA replication and partitioning the viral …

The acetylation of histone lysine is central to providing the dynamic regulation of chromatin-
based gene transcription. The bromodomain (BRD), which is the conserved structural …

Human Papillomavirus (HPV) is the most common cause of cervical cancer. Cervical cancer
being the second most common cancer after lung cancer, affecting women of different age …

Therapeutic targeting of the processes that regulate histone modification is a growing area
of scientific exploration. Although most interest has concentrated on the various families of …

Histone–lysine acetylation is a vital chromatin post-translational modification involved in the
epigenetic regulation of gene transcription. Bromodomains bind acetylated lysines, acting as …

Human papillomavirus (HPV) infection is a central and necessary, although not sufficient,
cause of cervical cancer. Besides HPV, the additional multiple risk factors related with the …

Nuclear receptor binding SET domain proteins (NSDs) catalyze the mono-or dimethylation
of histone 3 lysine 36 (H3K36me1 and H3K36me2), using S-adenosyl-l-methionine (SAM) …

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 …