Inhibition of JMJD6 by 2‐Oxoglutarate Mimics

Studies on the inhibition of the human 2‐oxoglutarate dependent oxygenase JMJD6, which is a cancer target, by 2‐oxoglutarate mimics / competitors, including human drugs, drug candidates, and metabolites relevant to cancer are described. JMJD6 assays employed NMR to monitor inhibitor binding and use...

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Detalles Bibliográficos
Autores principales: Islam, Md. Sailful, Thinnes, Cyrille C., Holt‐Martyn, James P., Chowdhury, Rasheduzzaman, McDonough, Michael A., Schofield, Christopher J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2021
Materias:
Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9299220/
https://www.ncbi.nlm.nih.gov/pubmed/34581506
http://dx.doi.org/10.1002/cmdc.202100398
Descripción
Sumario:Studies on the inhibition of the human 2‐oxoglutarate dependent oxygenase JMJD6, which is a cancer target, by 2‐oxoglutarate mimics / competitors, including human drugs, drug candidates, and metabolites relevant to cancer are described. JMJD6 assays employed NMR to monitor inhibitor binding and use of mass spectrometry to monitor JMJD6‐catalysed lysine hydroxylation. Notably, some clinically applied prolyl hydroxylase inhibitors also inhibit JMJD6. The results will help enable the development of inhibitors selective for human oxygenases, including JMJD6.

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