@article{
 title = {Development of chemical probes for the bromodomains of BRD7 and BRD9},
 type = {article},
 year = {2016},
 pages = {73-80},
 volume = {19},
 websites = {http://www.ncbi.nlm.nih.gov/pubmed/27769361},
 month = {3},
 city = {England},
 id = {077fbf48-1e1e-3ea8-9b59-df6a9526e0fe},
 created = {2016-12-01T10:12:02.000Z},
 file_attached = {false},
 profile_id = {64f7fb50-d000-335d-a02d-06c5f340a97a},
 last_modified = {2018-09-03T10:20:46.443Z},
 read = {false},
 starred = {true},
 authored = {true},
 confirmed = {true},
 hidden = {false},
 citation_key = {Clark2016},
 source_type = {JOUR},
 private_publication = {false},
 abstract = {The bromodomain family of proteins are ‘readers’ of acetylated lysines of histones, a key mark in the epigenetic code of gene regulation. Without high quality chemical probes with which to study these proteins, their biological function, and potential use in therapeutics, remains unknown. Recently, a number of chemical ligands were reported for the previously unprobed bromodomain proteins BRD7 and BRD9. Herein the development and characterisation of probes against these proteins is detailed, including the preliminary biological activity of BRD7 and BRD9 assessed using these probes. Future studies utilising these chemically-diverse compounds in parallel will allow for a confident assessment of the role of BRD7/9, and give multiple entry points into any subsequent pharmaceutical programs.},
 bibtype = {article},
 author = {Clark, Peter G.K. and Dixon, Darren J. and Brennan, Paul E.},
 doi = {10.1016/j.ddtec.2016.05.002},
 journal = {Drug Discovery Today: Technologies}
}

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