Ontology highlight
ABSTRACT:
SUBMITTER: Bolshan Y
PROVIDER: S-EPMC4027439 | biostudies-literature | 2013 Mar
REPOSITORIES: biostudies-literature
Bolshan Yuri Y Getlik Matthäus M Kuznetsova Ekaterina E Wasney Gregory A GA Hajian Taraneh T Poda Gennadiy G Nguyen Kong T KT Wu Hong H Dombrovski Ludmila L Dong Aiping A Senisterra Guillermo G Schapira Matthieu M Arrowsmith Cheryl H CH Brown Peter J PJ Al-Awar Rima R Vedadi Masoud M Smil David D
ACS medicinal chemistry letters 20130204 3
The WD40-repeat protein WDR5 plays a critical role in maintaining the integrity of MLL complexes and fully activating their methyltransferase function. MLL complexes, the trithorax-like family of SET1 methyltransferases, catalyze trimethylation of lysine 4 on histone 3, and they have been widely implicated in various cancers. Antagonism of WDR5 and MLL subunit interaction by small molecules has recently been presented as a practical way to inhibit activity of the MLL1 complex, and N-(2-(4-methyl ...[more]