Ontology highlight
ABSTRACT:
SUBMITTER: Vougiouklakis T
PROVIDER: S-EPMC6112750 | biostudies-literature | 2018 Aug
REPOSITORIES: biostudies-literature
Vougiouklakis Theodore T Saloura Vassiliki V Park Jae-Hyun JH Takamatsu Naofumi N Miyamoto Takashi T Nakamura Yusuke Y Matsuo Yo Y
Oncotarget 20180807 61
Protein methyltransferase SUV39H2 was reported to methylate histone H2AX at lysine 134 and enhance the formation of phosphorylated H2AX (γ-H2AX), which causes chemoresistance of cancer cells. We found that a series of imidazo[1,2-<i>a</i>]pyridine compounds that we synthesized could inhibit SUV39H2 methyltransferase activity. One of the potent compounds, OTS193320, was further analyzed in <i>in vitro</i> studies. The compound decreased global histone H3 lysine 9 tri-methylation levels in breast ...[more]