ArticleBioconjugate chemistry2014
Versatile O-GlcNAc transferase assay for high-throughput identification of enzyme variants, substrates, and inhibitors.
Article in Bioconjugate chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Selective bioorthogonal probe for N-glycan hybrid structures.Nature chemical biology · 2025Article
- The O-GlcNAc Modification of Recombinant Tau Protein and Characterization of the O-GlcNAc Pattern for Functional Study.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Review
- Chronically ElevatedFrontiers in immunology · 2022Article
- Blocked O-GlcNAc cycling alters mitochondrial morphology, function, and mass.Scientific reports · 2021Article
- Overview of the Assays to ProbeMolecules (Basel, Switzerland) · 2021Review
- cat-ELCCA: catalyzing drug discovery through click chemistry.Chemical communications (Cambridge, England) · 2018Article
- O-GlcNAc-ylation in the Nuclear Pore Complex.Cellular and molecular bioengineering · 2016Article
- Activity Based High-Throughput Screening for Novel O-GlcNAc Transferase Substrates Using a Dynamic Peptide Microarray.PloS one · 2016Article
- Chemical tools to explore nutrient-driven O-GlcNAc cycling.Critical reviews in biochemistry and molecular biologyReview
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
The dynamic glycosylation of serine/threonine residues on nucleocytoplasmic proteins with a single N-acetylglucosamine (O-GlcNAcylation) is critical for many important cellular processes. Cellular O-GlcNAc levels are highly regulated by two enzymes: O-GlcNAc transferase (OGT) is responsible for GlcNAc addition and O-GlcNAcase (OGA) is responsible for removal of the sugar. The lack of a rapid and simple method for monitoring OGT activity has impeded the efficient discovery of potent OGT inhibitors. In this study we describe a novel, single-well OGT enzyme assay that utilizes 6 × His-tagged substrates, a chemoselective chemical reaction, and unpurified OGT. The high-throughput Ni-NTA Plate OGT Assay will facilitate discovery of potent OGT-specific inhibitors on versatile substrates and the characterization of new enzyme variants.
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Registered trials
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