trap mass spectrometry. Amino Acids 40, 765-779. https://doi.org/10.1007/s00726-010-0645-9.

Snow, C.M., Senior, A., Gerace, L., 1987. Monoclonal antibodies identify a group of nuclear pore complex glycoproteins. J. Cell Biol. 104, 1143-1156. https://doi.org/10.1083/jcb.104.5.1143.

Song, H., Ma, J., Jian, Z., et al., 2019. Global profiling of O-GlcNAcylated and/or phosphorylated proteins in hepatoblastoma. Signal Transduct. Target. Ther. 4, 1-9. https://doi.org/10.1038/s41392-019-0067-4.

Sprung, R., Nandi, A., Chen, Y., et al., 2005. Tagging-via-Substrate strategy for probing O-GlcNAc modified proteins. J. Proteome Res. 4, 950-957. https://doi.org/10.1021/pr05003j.

Stock, C.C., Reilly, H.C., Buckley, S.M., et al., 1954. Azaserine, a new tumour-inhibitory substance; studies with Crocker mouse sarcoma 180. Nature 73, 71-72. https://doi.org/10.1038/173071a0.

Syka, J.E.P., Coon, J.J., Schroeder, M.J., et al., 2004. Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry. Proc. Natl. Acad. Sci. USA 101, 9528-9533. https://doi.org/10.1073/pnas.0402700101.

Szychowski, J., Mahdavi, A., Hodas, J.J.L., et al., 2010. Cleavable biotin probes for labeling of biomolecules via the azide - alkyne cycloaddition. J. Am. Chem. Soc. 132, 18351-18360. https://doi.org/10.1021/ja1083909.

Tan, H.Y., Eskandari, R., Shen, D., et al., 2018. Direct one-step fluorescent labeling of O-GlcNAc-modified proteins in live cells using metabolic intermediates. J. Am. Chem. Soc. 140, 15300-15308. https://doi.org/10.1021/jacs.8b08260.

Tanaka, Y., Kohler, J.J., 2008. Photoactivatable crosslinking sugars for capturing glycoprotein interactions. J. Am. Chem. Soc. 130, 3278-3279. https://doi.org/10.1021/ja1079772.

Tashima, Y., Stanley, P., 2014. Antibodies that detect O-Linked β-d-N-Acetylglucosamine on the extracellular domain of cell surface glycoproteins. J. Biol. Chem. 289, 11132-11142. https://doi.org/10.1074/jbc.M113492512.

Tegl, G., Hanson, J., Chen, H., et al., 2019. Facile formation of β-thioGlcNAc linkages to thiol-containing sugars, peptides, and proteins using a mutant GH20 hexosaminidase. Angew. Chem. Int Ed. Engl. 58, 1632-1637. https://doi.org/10.1002/anie.201809928.

Teo, C.F., Ingale, S., Wolfert, M.A., et al., 2010. Glycopeptide-specific monoclonal antibodies suggest new roles for O-GlcNAc. Nat. Chem. Biol. 6, 338-343. https://doi.org/10.1038/nchembio.338.

Thompson, J.W., Griffin, M.E., Hsieh-Wilson, L.C., 2018. Methods for the detection, study, and dynamic profiling of O-GlcNAc glycosylation. Methods in Enzymology. Elsevier, pp. 101-135.

Torres, C.R., Hart, G.W., 1984. Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc. J. Biol. Chem. 259, 3308-3317.

Tran, D.T., Ten Hagen, K.G., 2013. Mucin-type O-Glycosylation during development. J. Biol. Chem. 288, 6921-6929. https://doi.org/10.1074/jbc.R112418558.

Trapannone, R., Rafie, K., van Aalten, D.M.F., 2016. O-GlcNAc transferase inhibitors: current tools and future challenges. Biochem Soc. Trans. 44, 88-93. https://doi.org/10.1042/BST2015089.

Turner, J.R., Tartakoff, A.M., Greenspan, N.S., 1990. Cytologic assessment of nuclear and cytoplasmic O-linked N-acetylglucosamine distribution by using anti-streptococcal monoclonal antibodies. Proc. Natl. Acad. Sci. USA 87, 5608-5612. https://doi.org/10.1073/pnas.87.15.5608.

Ueda, H., Kojima, K., Saitoh, T., Ogawa, H., 1999. Interaction of a lectin from Psathyrella velutina mushroom with N-acetyleneuraminic acid. FEBS Lett. 448, 75-80. https://doi.org/10.1016/s0014-5793(99)00334-8.

Vocadlo, D.J., Hang, H.C., Kim, E.-J., et al., 2003. A chemical approach for identifying O-GlcNAc-modified proteins in cells. Proc. Natl. Acad. Sci. 100, 9116-9121. https://doi.org/10.1073/pnas.1632821100.

Vosseller, K., Trinidad, J.C., Chalkley, R.J., et al., 2006. O-Linked N-Acetylglucosamine Proteomics of Postsynaptic Density Preparations Using Lectin Weak Affinity Chromatography and Mass Spectrometry. Molecular & Cellular Proteomics 5, 923-934. https://doi.org/10.1074/mcp.T500040-MCP200.

Walter LA (2013) A High-Throughput Screening Campaign To Discover Novel Inhibitors Of Human L-glutamine: D-fructose-6-phosphate Amidotransferase 1. 201.

Walter, L.A., Lin, Y.H., Halbrook, C.J., et al., 2020. Inhibiting the hexosamine biosynthetic pathway lowers o-glcnacylation levels and sensitizes cancer to environmental stress. Biochemistry 59, 3169-3179. https://doi.org/10.1021/acs.biochem.9b00560.

Wang, H., Guo, J., Wang, N., et al., 2019. Ac4GlcNAcF3, an OGT-tolerated but OGA-resistant regulator for O-GlcNAcylation. Bioorg. Med. Chem. Lett. 29, 802-805. https://doi.org/10.1016/j.bmcl.2019.01.021.

Wang, J., Torii, M., Liu, H., et al., 2011. dbOGAP - an integrated bioinformatics resource for protein O-GlcNAcylation. BMC Bioinforma. 12, 91. https://doi.org/10.1186/1471-2105-12-91.

Wang, X., Li, W., Marcus, J., et al., 2020. MK-8719, a novel and selective O-GlcNAcase inhibitor that reduces the formation of pathological tau and ameliorates neurodegeneration in a mouse model of tauopathy. J. Pharm. Exp. Ther. 374, 252-263. https://doi.org/10.1124/jpet.120.266122.

Wang, Z., Udeshi, N.D., O'Malley, M., et al., 2010. Enrichment and Site Mapping of O-Linked N-Acetylglucosamine by a Combination of Chemical/Enzymatic Tagging,

Photochemical Cleavage, and Electron Transfer Dissociation Mass Spectrometry. Mol Cell Proteomics 9, 153-160. https://doi.org/10.1074/mcp.M900268-MCP200.

Wang, Z., Pandey, A., Hart, G.W., 2007. Dynamic Interplay between O-Linked N-Acetylglucosaminylation and glycogen synthase kinase-3-dependent phosphorylation. Mol. Cell. Proteom. 6, 1365-1379. https://doi.org/10.1074/mcp.M600453-MCP200.

Wang, Z., Park, K., Comer, F., et al., 2009. Site-Specific GlcNAcylation of human erythrocyte proteins: potential biomarker(s) for diabetes. Diabetes 58, 309-317. https://doi.org/10.2337/db08-0994.

Wang, Z., Udeshi, N.D., Slawson, C., et al., 2010. Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates cytokinesis. Sci. Signal 3, ra2. https://doi.org/10.1126/scisignal.20000526.

Watson, L.J., Facundo, H.T., Ngoh, G.A., et al., 2010. O-linked β-N-acetylglucosamine transferase is indispensable in the failing heart. PNAS 107, 17797-17802. https://doi.org/10.1073/pnas.1001907107.

Weiss, M., Loi, E.M., Sterle, M., et al., 2021. New quinolinone O-GlcNAc transferase inhibitors based on fragment growth. Front. Chem. 9, 205. https://doi.org/10.3389/fchem.2021.666122.

Wells, L., Vosseller, K., Cole, R.N., et al., 2002. Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications. Mol. Cell Proteom. 1, 791-804. https://doi.org/10.1074/mcp.M200048-MCP200.

Whelan, S.A., Hart, G.W., 2006. Identification of O-GlcNAc sites on proteins. Methods Enzym. 415, 113-133. https://doi.org/10.1016/S0076-6879(06)15008-9.

Wright, C.S., 1987. Refinement of the crystal structure of wheat germ agglutinin isolectin 2 at 1.8Åresolution. J. Mol. Biol. 194, 501-529. https://doi.org/10.1016/0022-2836(87)90678-4.

Wright, C.S., 1992. Crystal structure of a wheat germ agglutinin/glycophorin-sialoglycopeptide receptor complex. Structural basis for cooperative lectin-cell binding. J. Biol. Chem. 267, 14345-14352.

Wu, Z.L., Robey, M.T., Tatge, T., et al., 2014. Detecting O-GlcNAc using in vitro sulfation. Glycobiology 24, 740-747. https://doi.org/10.1093/glycob/cwu037.

Wu, Z.L., Tatge, T.J., Grill, A.E., Zou, Y., 2018. Detecting and Imaging O-GlcNAc Sites Using Glycosyltransferases: A Systematic Approach to Study O-GlcNAc. Cell Chem. Biol. 25 (1428-1435), e3 https://doi.org/10.1016/j.chembiol.2018.07.007.

Wu, Z.L., Luo, A., Grill, A., et al., 2020. Fluorescent detection of O-GlcNAc via tandem glycan labeling. Bioconjugate Chem. 31, 2098-2102. https://doi.org/10.1021/acs.bioconjugate.0c00454.

Wulff-Fuentes, E., Berendt, R.R., Massman, L., et al., 2021. The human O-GlcNAcome database and meta-analysis. Sci. Data 8, 25. https://doi.org/10.1038/s41597-021-00810-4.

Xu, S., Sun, F., Wu, R., 2020. A chemoenzymatic method based on easily accessible enzymes for profiling protein O-GlcNAcylation. Anal. Chem. 92, 9807-9814. https://doi.org/10.1021/acs.analchem.0c01284.

Xu, S., Zheng, J., Xiao, H., Wu, R., 2022. Simultaneously identifying and distinguishing glycoproteins with O-GlcNAc and O-GalNAc (the Tn Antigen) in human cancer cells. Anal. Chem. https://doi.org/10.1021/acs.analchem.1c05438.

Yang, X., Qian, K., 2017. Protein O-GlcNAcylation: emerging mechanisms and functions. Nat. Rev. Mol. Cell Biol. 18, 452-465. https://doi.org/10.1038/nrm.2017.22.

Ying, H., Kimmelman, A.C., Lyssiotis, C.A., et al., 2012. Oncogenic Kras maintains pancreatic tumors through regulation of anabolic glucose metabolism. Cell 149, 656-670. https://doi.org/10.1016/j.cell.2012.01.058.

Yu, S.-H., Boyce, M., Wands, A.M., et al., 2012. Metabolic labeling enables selective photocrosslinking of O-GlcNAc-modified proteins to their binding partners. PNAS 109, 4834-4839. https://doi.org/10.1073/pnas.1114356109.

Yuzwa, S.A., Macauley, M.S., Heinonen, J.E., et al., 2008. A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo. Nat. Chem. Biol. 4, 483-490. https://doi.org/10.1038/nchembio.96.

Zachara, N., Akimoto, Y., Hart, G.W., 2017. The O-GlcNAc modification. Cold Spring Harbor Laboratory Press.

Zachara, N.E., Cheung, W.D., Hart, G.W., 2004. Nucleocytoplasmic glycosylation, O-GlcNAc: identification and site mapping. Methods Mol. Biol. 284, 175-194. https://doi.org/10.1385/1-59259-816-1:175.

Zachara, N.E., Vosseller, K., Hart, G.W., 2011a. Detection and analysis of proteins modified by O-Linked N-Acetylglucosamine. Curr. Protoc. Protein Sci. 8. https://doi.org/10.1002/0471140864.p1208s66. CHAPTER:Unit12.

Zachara, N.E., Vosseller, K., Hart, G.W., 2011b. Detection and analysis of proteins modified by O-Linked N-Acetylglucosamine. Curr. Protoc. Mol. Biol. Chapter 17, 6. https://doi.org/10.1002/0471142727.fm1706s95.

Zaro, B.W., Yang, Y.-Y., Hang, H.C., Pratt, M.R., 2011. Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1. Proc. Natl. Acad. Sci. USA 108, 8146-8151. https://doi.org/10.1073/pnas.1102458108.

Zhang, H., Tomašić, T., Shi, J., et al., 2018. Inhibition of O-GlcNAc transferase (OGT) by peptidic hybrids. Med. Chem. Commun. 9, 883-887. https://doi.org/10.1039/C8MD00115D.

Zhu, Q., Yi, W., 2021. Chemistry-assisted proteomic profiling of O-GlcNAcylation. Front. Chem. 9, 702260 https://doi.org/10.3389/fchem.2021.702260.
trap mass spectrometry. Amino Acids 40, 765-779. https://doi.org/10.1007/s00726-010-0645-9.

Snow, C.M., Senior, A., Gerace, L., 1987. Monoclonal antibodies identify a group of nuclear pore complex glycoproteins. J. Cell Biol. 104, 1143-1156. https://doi.org/10.1083/jcb.104.5.1143.

Song, H., Ma, J., Jian, Z., et al., 2019. Global profiling of O-GlcNAcylated and/or phosphorylated proteins in hepatoblastoma. Signal Transduct. Target. Ther. 4, 1-9. https://doi.org/10.1038/s41392-019-0067-4.

Sprung, R., Nandi, A., Chen, Y., et al., 2005. Tagging-via-Substrate strategy for probing O-GlcNAc modified proteins. J. Proteome Res. 4, 950-957. https://doi.org/10.1021/pr05003j.

Stock, C.C., Reilly, H.C., Buckley, S.M., et al., 1954. Azaserine, a new tumour-inhibitory substance; studies with Crocker mouse sarcoma 180. Nature 73, 71-72. https://doi.org/10.1038/173071a0.

Syka, J.E.P., Coon, J.J., Schroeder, M.J., et al., 2004. Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry. Proc. Natl. Acad. Sci. USA 101, 9528-9533. https://doi.org/10.1073/pnas.0402700101.

Szychowski, J., Mahdavi, A., Hodas, J.J.L., et al., 2010. Cleavable biotin probes for labeling of biomolecules via the azide - alkyne cycloaddition. J. Am. Chem. Soc. 132, 18351-18360. https://doi.org/10.1021/ja1083909.

Tan, H.Y., Eskandari, R., Shen, D., et al., 2018. Direct one-step fluorescent labeling of O-GlcNAc-modified proteins in live cells using metabolic intermediates. J. Am. Chem. Soc. 140, 15300-15308. https://doi.org/10.1021/jacs.8b08260.

Tanaka, Y., Kohler, J.J., 2008. Photoactivatable crosslinking sugars for capturing glycoprotein interactions. J. Am. Chem. Soc. 130, 3278-3279. https://doi.org/10.1021/ja1079772.

Tashima, Y., Stanley, P., 2014. Antibodies that detect O-Linked β-d-N-Acetylglucosamine on the extracellular domain of cell surface glycoproteins. J. Biol. Chem. 289, 11132-11142. https://doi.org/10.1074/jbc.M113492512.

Tegl, G., Hanson, J., Chen, H., et al., 2019. Facile formation of β-thioGlcNAc linkages to thiol-containing sugars, peptides, and proteins using a mutant GH20 hexosaminidase. Angew. Chem. Int Ed. Engl. 58, 1632-1637. https://doi.org/10.1002/anie.201809928.

Teo, C.F., Ingale, S., Wolfert, M.A., et al., 2010. Glycopeptide-specific monoclonal antibodies suggest new roles for O-GlcNAc. Nat. Chem. Biol. 6, 338-343. https://doi.org/10.1038/nchembio.338.

Thompson, J.W., Griffin, M.E., Hsieh-Wilson, L.C., 2018. Methods for the detection, study, and dynamic profiling of O-GlcNAc glycosylation. Methods in Enzymology. Elsevier, pp. 101-135.

Torres, C.R., Hart, G.W., 1984. Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc. J. Biol. Chem. 259, 3308-3317.

Tran, D.T., Ten Hagen, K.G., 2013. Mucin-type O-Glycosylation during development. J. Biol. Chem. 288, 6921-6929. https://doi.org/10.1074/jbc.R112418558.

Trapannone, R., Rafie, K., van Aalten, D.M.F., 2016. O-GlcNAc transferase inhibitors: current tools and future challenges. Biochem Soc. Trans. 44, 88-93. https://doi.org/10.1042/BST2015089.

Turner, J.R., Tartakoff, A.M., Greenspan, N.S., 1990. Cytologic assessment of nuclear and cytoplasmic O-linked N-acetylglucosamine distribution by using anti-streptococcal monoclonal antibodies. Proc. Natl. Acad. Sci. USA 87, 5608-5612. https://doi.org/10.1073/pnas.87.15.5608.

Ueda, H., Kojima, K., Saitoh, T., Ogawa, H., 1999. Interaction of a lectin from Psathyrella velutina mushroom with N-acetyleneuraminic acid. FEBS Lett. 448, 75-80. https://doi.org/10.1016/s0014-5793(99)00334-8.

Vocadlo, D.J., Hang, H.C., Kim, E.-J., et al., 2003. A chemical approach for identifying O-GlcNAc-modified proteins in cells. Proc. Natl. Acad. Sci. 100, 9116-9121. https://doi.org/10.1073/pnas.1632821100.

Vosseller, K., Trinidad, J.C., Chalkley, R.J., et al., 2006. O-Linked N-Acetylglucosamine Proteomics of Postsynaptic Density Preparations Using Lectin Weak Affinity Chromatography and Mass Spectrometry. Molecular & Cellular Proteomics 5, 923-934. https://doi.org/10.1074/mcp.T500040-MCP200.

Walter LA (2013) A High-Throughput Screening Campaign To Discover Novel Inhibitors Of Human L-glutamine: D-fructose-6-phosphate Amidotransferase 1. 201.

Walter, L.A., Lin, Y.H., Halbrook, C.J., et al., 2020. Inhibiting the hexosamine biosynthetic pathway lowers o-glcnacylation levels and sensitizes cancer to environmental stress. Biochemistry 59, 3169-3179. https://doi.org/10.1021/acs.biochem.9b00560.

Wang, H., Guo, J., Wang, N., et al., 2019. Ac4GlcNAcF3, an OGT-tolerated but OGA-resistant regulator for O-GlcNAcylation. Bioorg. Med. Chem. Lett. 29, 802-805. https://doi.org/10.1016/j.bmcl.2019.01.021.

Wang, J., Torii, M., Liu, H., et al., 2011. dbOGAP - an integrated bioinformatics resource for protein O-GlcNAcylation. BMC Bioinforma. 12, 91. https://doi.org/10.1186/1471-2105-12-91.

Wang, X., Li, W., Marcus, J., et al., 2020. MK-8719, a novel and selective O-GlcNAcase inhibitor that reduces the formation of pathological tau and ameliorates neurodegeneration in a mouse model of tauopathy. J. Pharm. Exp. Ther. 374, 252-263. https://doi.org/10.1124/jpet.120.266122.

Wang, Z., Udeshi, N.D., O'Malley, M., et al., 2010. Enrichment and Site Mapping of O-Linked N-Acetylglucosamine by a Combination of Chemical/Enzymatic Tagging,

Photochemical Cleavage, and Electron Transfer Dissociation Mass Spectrometry. Mol Cell Proteomics 9, 153-160. https://doi.org/10.1074/mcp.M900268-MCP200.

Wang, Z., Pandey, A., Hart, G.W., 2007. Dynamic Interplay between O-Linked N-Acetylglucosaminylation and glycogen synthase kinase-3-dependent phosphorylation. Mol. Cell. Proteom. 6, 1365-1379. https://doi.org/10.1074/mcp.M600453-MCP200.

Wang, Z., Park, K., Comer, F., et al., 2009. Site-Specific GlcNAcylation of human erythrocyte proteins: potential biomarker(s) for diabetes. Diabetes 58, 309-317. https://doi.org/10.2337/db08-0994.

Wang, Z., Udeshi, N.D., Slawson, C., et al., 2010. Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates cytokinesis. Sci. Signal 3, ra2. https://doi.org/10.1126/scisignal.20000526.

Watson, L.J., Facundo, H.T., Ngoh, G.A., et al., 2010. O-linked β-N-acetylglucosamine transferase is indispensable in the failing heart. PNAS 107, 17797-17802. https://doi.org/10.1073/pnas.1001907107.

Weiss, M., Loi, E.M., Sterle, M., et al., 2021. New quinolinone O-GlcNAc transferase inhibitors based on fragment growth. Front. Chem. 9, 205. https://doi.org/10.3389/fchem.2021.666122.

Wells, L., Vosseller, K., Cole, R.N., et al., 2002. Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications. Mol. Cell Proteom. 1, 791-804. https://doi.org/10.1074/mcp.M200048-MCP200.

Whelan, S.A., Hart, G.W., 2006. Identification of O-GlcNAc sites on proteins. Methods Enzym. 415, 113-133. https://doi.org/10.1016/S0076-6879(06)15008-9.

Wright, C.S., 1987. Refinement of the crystal structure of wheat germ agglutinin isolectin 2 at 1.8Åresolution. J. Mol. Biol. 194, 501-529. https://doi.org/10.1016/0022-2836(87)90678-4.

Wright, C.S., 1992. Crystal structure of a wheat germ agglutinin/glycophorin-sialoglycopeptide receptor complex. Structural basis for cooperative lectin-cell binding. J. Biol. Chem. 267, 14345-14352.

Wu, Z.L., Robey, M.T., Tatge, T., et al., 2014. Detecting O-GlcNAc using in vitro sulfation. Glycobiology 24, 740-747. https://doi.org/10.1093/glycob/cwu037.

Wu, Z.L., Tatge, T.J., Grill, A.E., Zou, Y., 2018. Detecting and Imaging O-GlcNAc Sites Using Glycosyltransferases: A Systematic Approach to Study O-GlcNAc. Cell Chem. Biol. 25 (1428-1435), e3 https://doi.org/10.1016/j.chembiol.2018.07.007.

Wu, Z.L., Luo, A., Grill, A., et al., 2020. Fluorescent detection of O-GlcNAc via tandem glycan labeling. Bioconjugate Chem. 31, 2098-2102. https://doi.org/10.1021/acs.bioconjugate.0c00454.

Wulff-Fuentes, E., Berendt, R.R., Massman, L., et al., 2021. The human O-GlcNAcome database and meta-analysis. Sci. Data 8, 25. https://doi.org/10.1038/s41597-021-00810-4.

Xu, S., Sun, F., Wu, R., 2020. A chemoenzymatic method based on easily accessible enzymes for profiling protein O-GlcNAcylation. Anal. Chem. 92, 9807-9814. https://doi.org/10.1021/acs.analchem.0c01284.

Xu, S., Zheng, J., Xiao, H., Wu, R., 2022. Simultaneously identifying and distinguishing glycoproteins with O-GlcNAc and O-GalNAc (the Tn Antigen) in human cancer cells. Anal. Chem. https://doi.org/10.1021/acs.analchem.1c05438.

Yang, X., Qian, K., 2017. Protein O-GlcNAcylation: emerging mechanisms and functions. Nat. Rev. Mol. Cell Biol. 18, 452-465. https://doi.org/10.1038/nrm.2017.22.

Ying, H., Kimmelman, A.C., Lyssiotis, C.A., et al., 2012. Oncogenic Kras maintains pancreatic tumors through regulation of anabolic glucose metabolism. Cell 149, 656-670. https://doi.org/10.1016/j.cell.2012.01.058.

Yu, S.-H., Boyce, M., Wands, A.M., et al., 2012. Metabolic labeling enables selective photocrosslinking of O-GlcNAc-modified proteins to their binding partners. PNAS 109, 4834-4839. https://doi.org/10.1073/pnas.1114356109.

Yuzwa, S.A., Macauley, M.S., Heinonen, J.E., et al., 2008. A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo. Nat. Chem. Biol. 4, 483-490. https://doi.org/10.1038/nchembio.96.

Zachara, N., Akimoto, Y., Hart, G.W., 2017. The O-GlcNAc modification. Cold Spring Harbor Laboratory Press.

Zachara, N.E., Cheung, W.D., Hart, G.W., 2004. Nucleocytoplasmic glycosylation, O-GlcNAc: identification and site mapping. Methods Mol. Biol. 284, 175-194. https://doi.org/10.1385/1-59259-816-1:175.

Zachara, N.E., Vosseller, K., Hart, G.W., 2011a. Detection and analysis of proteins modified by O-Linked N-Acetylglucosamine. Curr. Protoc. Protein Sci. 8. https://doi.org/10.1002/0471140864.p1208s66. CHAPTER:Unit12.

Zachara, N.E., Vosseller, K., Hart, G.W., 2011b. Detection and analysis of proteins modified by O-Linked N-Acetylglucosamine. Curr. Protoc. Mol. Biol. Chapter 17, 6. https://doi.org/10.1002/0471142727.fm1706s95.

Zaro, B.W., Yang, Y.-Y., Hang, H.C., Pratt, M.R., 2011. Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1. Proc. Natl. Acad. Sci. USA 108, 8146-8151. https://doi.org/10.1073/pnas.1102458108.

Zhang, H., Tomašić, T., Shi, J., et al., 2018. Inhibition of O-GlcNAc transferase (OGT) by peptidic hybrids. Med. Chem. Commun. 9, 883-887. https://doi.org/10.1039/C8MD00115D.

Zhu, Q., Yi, W., 2021. Chemistry-assisted proteomic profiling of O-GlcNAcylation. Front. Chem. 9, 702260 https://doi.org/10.3389/fchem.2021.702260.