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Open AccessReview

Overview of the Assays to Probe O-Linked β-N-Acetylglucosamine Transferase Binding and Activity

1
Department of Chemical Biology & Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, P.O. Box 80082, NL-3508 TB Utrecht, The Netherlands
2
Faculty of Pharmacy, University of Ljubljana, 1000 Ljubljana, Slovenia
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Authors to whom correspondence should be addressed.
Academic Editor: Patrick M. Martin
Molecules 2021, 26(4), 1037; https://doi.org/10.3390/molecules26041037
Received: 21 January 2021 / Revised: 11 February 2021 / Accepted: 12 February 2021 / Published: 16 February 2021
(This article belongs to the Special Issue Advances on Glycoconjugates – Chemistry and Chemical Biology)
O-GlcNAcylation is a posttranslational modification that occurs at serine and threonine residues of protein substrates by the addition of O-linked β-d-N-acetylglucosamine (GlcNAc) moiety. Two enzymes are involved in this modification: O-GlcNac transferase (OGT), which attaches the GlcNAc residue to the protein substrate, and O-GlcNAcase (OGA), which removes it. This biological balance is important for many biological processes, such as protein expression, cell apoptosis, and regulation of enzyme activity. The extent of this modification has sparked interest in the medical community to explore OGA and OGT as therapeutic targets, particularly in degenerative diseases. While some OGA inhibitors are already in phase 1 clinical trials for the treatment of Alzheimer’s disease, OGT inhibitors still have a long way to go. Due to complex expression and instability, the discovery of potent OGT inhibitors is challenging. Over the years, the field has grappled with this problem, and scientists have developed a number of techniques and assays. In this review, we aim to highlight assays and techniques for OGT inhibitor discovery, evaluate their strength for the field, and give us direction for future bioassay methods. View Full-Text
Keywords: OGT; GlcNAcylation; O-GlcNAc Transferase; bioassay; OGT inhibitor OGT; GlcNAcylation; O-GlcNAc Transferase; bioassay; OGT inhibitor
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MDPI and ACS Style

Balsollier, C.; Pieters, R.J.; Anderluh, M. Overview of the Assays to Probe O-Linked β-N-Acetylglucosamine Transferase Binding and Activity. Molecules 2021, 26, 1037. https://doi.org/10.3390/molecules26041037

AMA Style

Balsollier C, Pieters RJ, Anderluh M. Overview of the Assays to Probe O-Linked β-N-Acetylglucosamine Transferase Binding and Activity. Molecules. 2021; 26(4):1037. https://doi.org/10.3390/molecules26041037

Chicago/Turabian Style

Balsollier, Cyril; Pieters, Roland J.; Anderluh, Marko. 2021. "Overview of the Assays to Probe O-Linked β-N-Acetylglucosamine Transferase Binding and Activity" Molecules 26, no. 4: 1037. https://doi.org/10.3390/molecules26041037

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Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

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