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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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
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author Islam, Md. Sailful
Thinnes, Cyrille C.
Holt‐Martyn, James P.
Chowdhury, Rasheduzzaman
McDonough, Michael A.
Schofield, Christopher J.
author_facet Islam, Md. Sailful
Thinnes, Cyrille C.
Holt‐Martyn, James P.
Chowdhury, Rasheduzzaman
McDonough, Michael A.
Schofield, Christopher J.
author_sort Islam, Md. Sailful
collection PubMed
description 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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spelling pubmed-92992202022-07-21 Inhibition of JMJD6 by 2‐Oxoglutarate Mimics Islam, Md. Sailful Thinnes, Cyrille C. Holt‐Martyn, James P. Chowdhury, Rasheduzzaman McDonough, Michael A. Schofield, Christopher J. ChemMedChem Communications 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. John Wiley and Sons Inc. 2021-11-16 2022-01-05 /pmc/articles/PMC9299220/ /pubmed/34581506 http://dx.doi.org/10.1002/cmdc.202100398 Text en © 2021 The Authors. ChemMedChem published by Wiley-VCH GmbH https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Communications
Islam, Md. Sailful
Thinnes, Cyrille C.
Holt‐Martyn, James P.
Chowdhury, Rasheduzzaman
McDonough, Michael A.
Schofield, Christopher J.
Inhibition of JMJD6 by 2‐Oxoglutarate Mimics
title Inhibition of JMJD6 by 2‐Oxoglutarate Mimics
title_full Inhibition of JMJD6 by 2‐Oxoglutarate Mimics
title_fullStr Inhibition of JMJD6 by 2‐Oxoglutarate Mimics
title_full_unstemmed Inhibition of JMJD6 by 2‐Oxoglutarate Mimics
title_short Inhibition of JMJD6 by 2‐Oxoglutarate Mimics
title_sort inhibition of jmjd6 by 2‐oxoglutarate mimics
topic Communications
url 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
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