Post-translationally appended acetyllysine marks on histone tails are key regulatory features
of the epigenetic code. Bromodomains are “readers” of this specific lysine acetylation code …

Bromodomains, epigenetic “readers” of lysine acetylation marks, exist in different nuclear
proteins with diverse biological functions in chromatin biology. Malfunctions of …

Bromodomains are protein modules that bind to acetylated lysine residues. Their interaction
with histone proteins suggests that they function as “readers” of histone lysine acetylation, a …

Background Proteins that 'read'the histone code are central elements in epigenetic control
and bromodomains, which bind acetyl-lysine motifs, are increasingly recognized as potential …

The bromodomain (BrD) is a conserved protein modular domain found in many chromatin-
and transcription-associated proteins that has the ability to recognize acetylated lysine …

Bromodomains are protein modules that bind to acetylated lysine residues and hence
facilitate protein–protein interactions. These bromodomain-mediated interactions often play …

There is intense interest in the development of small molecule inhibitors of the acetyl-lysine-
reading bromodomain protein module. These inhibitors represent a way of interfering …

Bromodomains are structurally conserved protein modules present in a large number of
chromatin-associated proteins and in many nuclear histone acetyltransferases. The …

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 …

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 …