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Bromodomains (BRDs) are evolutionarily conserved protein-protein interaction modules that are found in a wide range of proteins with diverse catalytic and scaffolding functions and are present in most tissues. BRDs selectively recognize and bind to acetylated Lys residues - particularly in histones - and thereby have important roles in the regulation of gene expression. BRD-containing proteins are frequently dysregulated in cancer, they participate in gene fusions that generate diverse, frequently oncogenic proteins, and many cancer-causing mutations have been mapped to the BRDs themselves. Importantly, BRDs can be targeted by small-molecule inhibitors, which has stimulated many translational research projects that seek to attenuate the aberrant functions of BRD-containing proteins in disease.

Original publication




Journal article


Nat Rev Mol Cell Biol

Publication Date





246 - 262


Acylation, Animals, Chromatin Assembly and Disassembly, Gene Expression Regulation, Histones, Homeostasis, Humans, Lysine, Mutation, Neoplasms, Oncogene Proteins, Fusion, Protein Domains, Protein Processing, Post-Translational, Proteins, Tumor Suppressor Proteins