ePrints

Optimisation of a triazolopyridine based histone demethylase inhibitor yields a potent and selective KDM2A (FBXL11) inhibitor

Lookup NU author(s): Professor Akane KawamuraORCiD

Downloads

• Published version [.pdf]

Licence

This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).

Abstract

© The Royal Society of Chemistry. A potent inhibitor of the JmjC histone lysine demethylase KDM2A (compound 35, pIC50 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. This journal is

Publication metadata

Author(s): England KS, Tumber A, Krojer T, Scozzafava G, Ng SS, Daniel M, Szykowska A, Che K, Von Delft F, Burgess-Brown NA, Kawamura A, Schofield CJ, Brennan PE

Publication type: Article

Publication status: Published

Journal: MedChemComm

Year: 2014

Volume: 5

Issue: 12

Pages: 1879-1886

Print publication date: 01/12/2014

Online publication date: 15/09/2014

Acceptance date: 14/09/2014

Date deposited: 10/10/2019

ISSN (print): 2040-2503

ISSN (electronic): 2040-2511

Publisher: Royal Society of Chemistry

URL: https://doi.org/10.1039/c4md00291a

DOI: 10.1039/c4md00291a

Altmetrics

Funding

Share