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Lookup NU author(s): Professor Akane Kawamura
This is the authors' accepted manuscript of an article that has been published in its final definitive form by John Wiley & Sons, Inc., 2018.
For re-use rights please refer to the publisher's terms and conditions.
© 2018 by John Wiley & Sons, Inc. Histone modifications, including lysine methylation marks on histone tails, modulate the accessibility of genes for transcription. Changes in histone tail methylation patterns can cause transcriptional activation or repression. The dynamic regulation of lysine methylation patterns is enabled by two distinct groups of enzymes: histone methyltransferases (KMTs) and demethylases (KDMs). The Jumonji C (JmjC) domain–containing lysine histone demethylases (JmjC-KDMs) alter the methylation levels of histone tails by removing tri-, di-, or mono-methylation marks. Because JmjC-KDMs activities are dysfunctional in cancer and other clinical conditions, they are targets for drug discovery. Efforts are underway to develop high-throughput assays capable of identifying selective, small-molecule inhibitors of KDMs. Detailed in this unit are protocols for mass spectrometry–based and formaldehyde dehydrogenase–coupled enzyme-based assays that can be used to identify inhibitors of JmjC-KDMs.
Author(s): Tarhonskaya H, Tumber A, Kawamura A, Schofield CJ
Publication type: Article
Publication status: Published
Journal: Current Protocols in Pharmacology
Online publication date: 02/04/2018
Acceptance date: 02/04/2018
Date deposited: 14/10/2019
ISSN (print): 1934-8282
ISSN (electronic): 1934-8290
Publisher: John Wiley & Sons, Inc.
PubMed id: 30040204
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