Optimisation of a triazolopyridine based histone demethylase inhibitor yields a potent and selective KDM2A (FBXL11) inhibitor.
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ABSTRACT:
SUBMITTER: England KS
PROVIDER: S-EPMC4678576 | biostudies-literature | 2014 Dec
REPOSITORIES: biostudies-literature
Publications
Optimisation of a triazolopyridine based histone demethylase inhibitor yields a potent and selective KDM2A (FBXL11) inhibitor.
England Katherine S KS Tumber Anthony A Krojer Tobias T Scozzafava Giuseppe G Ng Stanley S SS Daniel Michelle M Szykowska Aleksandra A Che KaHing K von Delft Frank F Burgess-Brown Nicola A NA Kawamura Akane A Schofield Christopher J CJ Brennan Paul E PE
MedChemComm 20141201 12
A potent inhibitor of the JmjC histone lysine demethylase KDM2A (compound <b>35</b>, pIC<sub>50</sub> 7.2) with excellent selectivity over representatives from other KDM subfamilies has been developed; the discovery that a triazolopyridine compound binds to the active site of JmjC KDMs was followed by optimisation of the triazole substituent for KDM2A inhibition and selectivity. ...[more]
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