Ontology highlight
ABSTRACT:
SUBMITTER: Mobitz H
PROVIDER: S-EPMC5346981 | biostudies-literature | 2017 Mar
REPOSITORIES: biostudies-literature
Möbitz Henrik H Machauer Rainer R Holzer Philipp P Vaupel Andrea A Stauffer Frédéric F Ragot Christian C Caravatti Giorgio G Scheufler Clemens C Fernandez Cesar C Hommel Ulrich U Tiedt Ralph R Beyer Kim S KS Chen Chao C Zhu Hugh H Gaul Christoph C
ACS medicinal chemistry letters 20170214 3
Misdirected catalytic activity of histone methyltransferase Dot1L is believed to be causative for a subset of highly aggressive acute leukemias. Targeting the catalytic domain of Dot1L represents a potential therapeutic approach for these leukemias. In the context of a comprehensive Dot1L hit finding strategy, a knowledge-based virtual screen of the Dot1L SAM binding pocket led to the discovery of <b>2</b>, a non-nucleoside fragment mimicking key interactions of SAM bound to Dot1L. Fragment link ...[more]