BRD4
“Kaposi's sarcoma-associated herpesvirus latency-associated nuclear antigen interacts with bromodomain protein Brd4 on host mitotic chromosomes”. Journal of Virology 80 (18): 8909–19. (Sep 2006). doi:10.1128/JVI.00502-06. PMC 1563901. PMID 16940503. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1563901/.
“Amino acid substitutions that specifically impair the transcriptional activity of papillomavirus E2 affect binding to the long isoform of Brd4”. Virology 358 (1): 10–7. (Feb 2007). doi:10.1016/j.virol.2006.08.035. PMID 17023018.
“Global, in vivo, and site-specific phosphorylation dynamics in signaling networks”. Cell 127 (3): 635–48. (Nov 2006). doi:10.1016/j.cell.2006.09.026. PMID 17081983.
“Structure of the papillomavirus DNA-tethering complex E2:Brd4 and a peptide that ablates HPV chromosomal association”.
Molecular Cell 24 (6): 877–89. (Dec 2006). doi:10.1016/j.molcel.2006.11.002. PMID 17189190.
“Brd4-independent transcriptional repression function of the papillomavirus e2 proteins”. Journal of Virology 81 (18): 9612–22. (Sep 2007). doi:10.1128/JVI.00447-07. PMC 2045424. PMID 17626100. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2045424/.
“Conserved P-TEFb-interacting domain of BRD4 inhibits HIV transcription”. Proceedings of the National Academy of Sciences of the United States of America 104 (34): 13690–5. (Aug 2007). Bibcode: 2007PNAS..10413690B. doi:10.1073/pnas.0705053104. PMC 1959443. PMID 17690245. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1959443/.