Jump to main content
Jump to site search

Issue 12, 2014
Previous Article Next Article

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

Author affiliations

Abstract

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.

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

Back to tab navigation

Supplementary files

Article information


Submitted
04 Jul 2014
Accepted
14 Sep 2014
First published
15 Sep 2014

This article is Open Access

Med. Chem. Commun., 2014,5, 1879-1886
Article type
Concise Article

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

K. S. England, A. Tumber, T. Krojer, G. Scozzafava, S. S. Ng, M. Daniel, A. Szykowska, K. Che, F. von Delft, N. A. Burgess-Brown, A. Kawamura, C. J. Schofield and P. E. Brennan, Med. Chem. Commun., 2014, 5, 1879
DOI: 10.1039/C4MD00291A

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. Material from this article can be used in other publications provided that the correct acknowledgement is given with the reproduced material.

Reproduced material should be attributed as follows:

  • For reproduction of material from NJC:
    [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the Centre National de la Recherche Scientifique (CNRS) and the RSC.
  • For reproduction of material from PCCP:
    [Original citation] - Published by the PCCP Owner Societies.
  • For reproduction of material from PPS:
    [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the European Society for Photobiology, the European Photochemistry Association, and RSC.
  • For reproduction of material from all other RSC journals:
    [Original citation] - Published by The Royal Society of Chemistry.

Information about reproducing material from RSC articles with different licences is available on our Permission Requests page.


Search articles by author

Spotlight

Advertisements