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O-GlcNAc transferase (OGT) is involved in many cellular processes, and selective OGT inhibitors are valuable tools to investigate O-GlcNAcylation functions, and could potentially lead to therapeutics. However, high-throughput OGT assays that are suitable for large-scale HTS and can identify inhibitors targeting both acceptor, donor sites, and allosteric binding-sites are still lacking. Here, we report the development of a high-throughput "FP-Tag" OGT assay with bovine serum albumin (BSA) as a low-cost and superior "FP-Tag". With this assay, 2-methyleurotinone was identified as a low-micromolar OGT inhibitor. This type of assay with BSA as "FP-Tag" would find more applications with other glycosyltransferases.
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Yin et al. (2020) studied this question.
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