Ontology highlight
ABSTRACT:
SUBMITTER: Hewings DS
PROVIDER: S-EPMC3188285 | biostudies-literature | 2011 Oct
REPOSITORIES: biostudies-literature
Hewings David S DS Wang Minghua M Philpott Martin M Fedorov Oleg O Uttarkar Sagar S Filippakopoulos Panagis P Picaud Sarah S Vuppusetty Chaitanya C Marsden Brian B Knapp Stefan S Conway Stuart J SJ Heightman Tom D TD
Journal of medicinal chemistry 20110906 19
Histone-lysine acetylation is a vital chromatin post-translational modification involved in the epigenetic regulation of gene transcription. Bromodomains bind acetylated lysines, acting as readers of the histone-acetylation code. Competitive inhibitors of this interaction have antiproliferative and anti-inflammatory properties. With 57 distinct bromodomains known, the discovery of subtype-selective inhibitors of the histone-bromodomain interaction is of great importance. We have identified the 3 ...[more]