@article{
 title = {Identification of a chemical probe for bromo and extra C-terminal bromodomain inhibition through optimization of a fragment-derived hit},
 type = {article},
 year = {2012},
 keywords = {Crystallography,Humans,Models,Molecular,Molecular Probes,Molecular Probes: chemical synthesis,Molecular Probes: pharmacology,Molecular Structure,Nuclear Proteins,Nuclear Proteins: antagonists & inhibitors,Nuclear Proteins: metabolism,Protein Binding,Quinazolinones,Quinazolinones: chemical synthesis,Quinazolinones: pharmacology,Structure-Activity Relationship,Sulfonamides,Sulfonamides: chemical synthesis,Sulfonamides: chemistry,Sulfonamides: pharmacology,Transcription Factors,Transcription Factors: antagonists & inhibitors,X-Ray},
 pages = {9831-9837},
 volume = {55},
 websites = {http://dx.doi.org/10.1021/jm3010515,http://pubs.acs.org/doi/pdfplus/10.1021/jm3010515},
 publisher = {American Chemical Society},
 id = {58d737ec-f012-3915-8255-17a2a94caeb8},
 created = {2015-10-07T14:20:50.000Z},
 file_attached = {true},
 profile_id = {64f7fb50-d000-335d-a02d-06c5f340a97a},
 last_modified = {2018-09-03T10:20:46.191Z},
 read = {false},
 starred = {false},
 authored = {true},
 confirmed = {true},
 hidden = {false},
 citation_key = {Fish2012},
 source_type = {Journal Article},
 private_publication = {false},
 abstract = {The posttranslational modification of chromatin through acetylation at selected histone lysine residues is governed by histone acetyltransferases (HATs) and histone deacetylases (HDACs). The significance of this subset of the epigenetic code is interrogated and interpreted by an acetyllysine-specific protein–protein interaction with bromodomain reader modules. Selective inhibition of the bromo and extra C-terminal domain (BET) family of bromodomains with a small molecule is feasible, and this may represent an opportunity for disease intervention through the recently disclosed antiproliferative and anti-inflammatory properties of such inhibitors. Herein, we describe the discovery and structure–activity relationship (SAR) of a novel, small-molecule chemical probe for BET family inhibition that was identified through the application of structure-based fragment assessment and optimization techniques. This has yielded a potent, selective compound with cell-based activity (PFI-1) that may further add to the und...},
 bibtype = {article},
 author = {Fish, Paul V. and Filippakopoulos, Panagis and Bish, Gerwyn and Brennan, Paul E. and Bunnage, Mark E. and Cook, Andrew S. and Federov, Oleg and Gerstenberger, Brian S. and Jones, Hannah and Knapp, Stefan and Marsden, Brian and Nocka, Karl and Owen, Dafydd R. and Philpott, Martin and Picaud, Sarah and Primiano, Michael J. and Ralph, Michael J. and Sciammetta, Nunzio and Trzupek, John D.},
 doi = {10.1021/jm3010515},
 journal = {Journal of Medicinal Chemistry},
 number = {22}
}

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The significance of this subset of the epigenetic code is interrogated and interpreted by an acetyllysine-specific protein–protein interaction with bromodomain reader modules. Selective inhibition of the bromo and extra C-terminal domain (BET) family of bromodomains with a small molecule is feasible, and this may represent an opportunity for disease intervention through the recently disclosed antiproliferative and anti-inflammatory properties of such inhibitors. Herein, we describe the discovery and structure–activity relationship (SAR) of a novel, small-molecule chemical probe for BET family inhibition that was identified through the application of structure-based fragment assessment and optimization techniques. 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