The DOI matches its Crossref record; 56 of the 56 references it cites were found in a registry or an index.
A Small Molecule That Inhibits OGT Activity in Cells
Open accessAbstract
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.
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Citations
Cites
Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins
Hart, G. W., Housley, M. P., & Slawson, C. (2007) · Nature · doi:10.1038/nature05815 · Cited by 1,418
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Phosphofructokinase 1 Glycosylation Regulates Cell Growth and Metabolism
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The Hexosamine Signaling Pathway: Deciphering the "O-GlcNAc Code"
Love, D. C., & Hanover, J. A. (2005) · Science's STKE · doi:10.1126/stke.3122005re13 · Cited by 461
Structure of human O-GlcNAc transferase and its complex with a peptide substrate
Lazarus, M. B., Nam, Y., Jiang, J., Sliz, P., & Walker, S. (2011) · Nature · doi:10.1038/nature09638 · Cited by 458
Self-citationO-GlcNAc signalling: implications for cancer cell biology
Slawson, C., & Hart, G. W. (2011) · Nature Reviews Cancer · doi:10.1038/nrc3114 · Cited by 458
Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine.
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Ferrer, C. M., Lynch, T. P., Sodi, V. L., Falcone, J. N., Schwab, L. P., Peacock, D. L., Vocadlo, D. J., Seagroves, T. N., & Reginato, M. J. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.04.026 · Cited by 442
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linking metabolism to epigenetics through O-GlcNAcylation
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Cited by
Fueling the fire: emerging role of the hexosamine biosynthetic pathway in cancer
Akella, N. M., Ciraku, L., & Reginato, M. J. (2019) · BMC Biology · doi:10.1186/s12915-019-0671-3 · Cited by 373
O-GlcNAc regulates gene expression by controlling detained intron splicing
Tan, Z.-W., Fei, G., Paulo, J. A., Bellaousov, S., Martin, S. E. S., Duveau, D. Y., Thomas, C. J., Gygi, S. P., Boutz, P. L., & Walker, S. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa263 · Cited by 119
Self-citationAizezi, Y., Zhao, H., Zhang, Z., Bi, Y., Yang, Q., Guo, G., Zhang, H., Guo, H., Jiang, K., & Wang, Z.-Y. (2024) · The Plant Cell · doi:10.1093/plcell/koad299 · Cited by 16
Metadata
- Authors
- Ortiz-Meoz, R. F., Jiang, J., Lazarus, M. B., Orman, M., Janetzko, J., Fan, C., Duveau, D. Y., Tan, Z.-W., Thomas, C. J., & Walker, S.
- Venue
- ACS Chemical Biology
- Publisher
- American Chemical Society (ACS)
- Published
- 2015-03-18
- Volume
- 10
- Issue
- 6
- Pages
- 1392-1397
- ISSN
- 1554-8929 (ISSN-L)
- 1554-8937
- OpenAlex
- W2080462728
- Cited by
- 294
- References
- 56
- FWCI
- 7.59
- Type
- journal article
- Language
- en
- Open access
- green
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