The double bromodomain protein Brd4 binds to acetylated chromatin during interphase and mitosis

By A. Dey, Farideh Chitsaz, A. Abbasi, Tom Misteli, K. Ozato. Proceedings of the National Academy of Sciences of the United States of America, 2003

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Selective Inhibition of Tumor Oncogenes by Disruption of Super-Enhancers (2013, background): “Inhibition of BRD4 Leads to Displacement of BRD4 Genome Wide BRD4 interacts with chromatin-associated proteins such as transcription factors, the Mediator complex, and acetylated histones (Dawson et al., 2011; Dey et al., 2003; Jang et al., 2005; Jiang et al., 1998; Wu and Chiang, 2007; Wu et al., 2”
Discovery and Characterization of Super-Enhancer Associated Dependencies in Diffuse Large B-Cell Lymphoma (2013, neutral): “In cancer, BET bromodomains promote M to G1 cell cycle progression (Yang et al., 2008) and contribute to mitotic memory (Dey et al., 2003; Zhao et al., 2011).”
Liquid Nuclear Condensates Mechanically Sense and Restructure the Genome. (2018, positive): “Many IDR-rich proteins possess targeting ‘‘reader’’ motifs, such as the bromodomain found in BRD4, which targets this phase separation-prone protein to histones exhibiting acetylated lysine resides (Dey et al., 2003).”
The mechanisms behind the therapeutic activity of BET bromodomain inhibition (2014, background): “Bromodomain-mediated interactions with acetylated chromatin result in the localization of BET proteins to discrete locations along the chromosome, where they recruit other regulatory complexes to influence gene expression (Figure 2) (Dey et al., 2003).”