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• W2263939622 abstract "The O-linked N-acetylglucosamine (O-GlcNAc) post-translational modification (O-GlcNAcylation) is the dynamic and reversible attachment of N-acetylglucosamine to serine and threonine residues of nucleocytoplasmic target proteins. It is abundant in metazoa, involving hundreds of proteins linked to a plethora of biological functions with implications in human diseases. The process is catalysed by two enzymes: O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) that add and remove sugar moieties respectively. OGT knockout is embryonic lethal in a range of animal models, hampering the study of the biological role of O-GlcNAc and the dissection of catalytic compared with non-catalytic roles of OGT. Therefore, selective and potent chemical tools are necessary to inhibit OGT activity in the context of biological systems. The present review focuses on the available OGT inhibitors and summarizes advantages, limitations and future challenges." @default.
• W2263939622 created "2016-06-24" @default.
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• W2263939622 date "2016-02-09" @default.
• W2263939622 modified "2023-10-01" @default.
• W2263939622 title "O-GlcNAc transferase inhibitors: current tools and future challenges" @default.
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• W2263939622 doi "https://doi.org/10.1042/bst20150189" @default.
• W2263939622 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26862193" @default.
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