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

DOI: 10.1039/C4MD00291A DOI Help

Authors: Katherine S. England (Structural Genomics Consortium, University of Oxford) , Anthony Tumber (Structural Genomics Consortium, University of Oxford) , Tobias Krojer (Structural Genomics Consortium, University of Oxford) , Guiseppe Scozzafava (Structural Genomics Consortium, University of Oxford) , Stanley Ng (Structural Genomics Consortium, University of Oxford) , Michelle Daniel (Structural Genomics Consortium, University of Oxford) , Aleksandra Szykowska (Structural Genomics Consortium, University of Oxford) , Kahing Che (Structural Genomics Consortium, University of Oxford) , Frank Von Delft (Structural Genomics Consortium, University of Oxford, Diamond Light Source) , Nicola A. Burgess-brown (Structural Genomics Consortium, University of Oxford) , Akane Kawamura (Structural Genomics Consortium, University of Oxford) , Christopher J. Schofield (Structural Genomics Consortium, University of Oxford) , Paul E. Brennan (Structural Genomics Consortium, University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Medchemcomm , VOL 5 (12) , PAGES 1879 - 1886

State: Published (Approved)
Published: September 2014
Diamond Proposal Number(s): 8421

Open Access Open Access

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.

Subject Areas: Biology and Bio-materials, Chemistry, Medicine


Instruments: I03-Macromolecular Crystallography , I04-1-Macromolecular Crystallography (fixed wavelength)

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c4md00291a.pdf