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- W2080462728 endingPage "1397" @default.
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- W2080462728 abstract "O-GlcNAc transferase (OGT) is an essential mammalian enzyme that regulates numerous cellular processes through the attachment of O-linked N-acetylglucosamine (O-GlcNAc) residues to nuclear and cytoplasmic proteins. Its targets include kinases, phosphatases, transcription factors, histones, and many other intracellular proteins. The biology of O-GlcNAc modification is still not well understood, and cell-permeable inhibitors of OGT are needed both as research tools and for validating OGT as a therapeutic target. Here, we report a small molecule OGT inhibitor, OSMI-1, developed from a high-throughput screening hit. It is cell-permeable and inhibits protein O-GlcNAcylation in several mammalian cell lines without qualitatively altering cell surface N- or O-linked glycans. The development of this molecule validates high-throughput screening approaches for the discovery of glycosyltransferase inhibitors, and further optimization of this scaffold may lead to yet more potent OGT inhibitors useful for studying OGT in animal models." @default.
- W2080462728 created "2016-06-24" @default.
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- W2080462728 date "2015-03-18" @default.
- W2080462728 modified "2023-10-17" @default.
- W2080462728 title "A Small Molecule That Inhibits OGT Activity in Cells" @default.
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- W2080462728 doi "https://doi.org/10.1021/acschembio.5b00004" @default.
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