{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,22]],"date-time":"2026-04-22T23:23:36Z","timestamp":1776900216364,"version":"3.51.2"},"reference-count":234,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2025,11,26]],"date-time":"2025-11-26T00:00:00Z","timestamp":1764115200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2025,11,26]],"date-time":"2025-11-26T00:00:00Z","timestamp":1764115200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Mol Neurobiol"],"published-print":{"date-parts":[[2026,1]]},"DOI":"10.1007\/s12035-025-05357-8","type":"journal-article","created":{"date-parts":[[2025,11,26]],"date-time":"2025-11-26T08:10:52Z","timestamp":1764144652000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Targeting O-GlcNAcylation: Novel Therapeutic Strategies for Neurological Disease"],"prefix":"10.1007","volume":"63","author":[{"given":"Jingyi","family":"Sui","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lei","family":"Zheng","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Baiwen","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yaxin","family":"Shang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Wei","family":"Zou","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2025,11,26]]},"reference":[{"key":"5357_CR1","doi-asserted-by":"publisher","first-page":"4411","DOI":"10.1021\/bi200346n","volume":"50","author":"A Larkin","year":"2011","unstructured":"Larkin A, Imperiali B (2011) The expanding horizons of asparagine-linked glycosylation. Biochemistry 50:4411\u20134426","journal-title":"Biochemistry"},{"key":"5357_CR2","doi-asserted-by":"publisher","first-page":"3308","DOI":"10.1016\/S0021-9258(17)43295-9","volume":"259","author":"CR Torres","year":"1984","unstructured":"Torres CR, Hart GW (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\u20133317","journal-title":"J Biol Chem"},{"key":"5357_CR3","doi-asserted-by":"publisher","first-page":"14750","DOI":"10.1074\/jbc.RA120.014476","volume":"295","author":"X Sun","year":"2020","unstructured":"Sun X, Tie HC, Chen B et al (2020) Glycans function as a Golgi export signal to promote the constitutive exocytic trafficking. J Biol Chem 295:14750\u201314762","journal-title":"J Biol Chem"},{"key":"5357_CR4","doi-asserted-by":"publisher","DOI":"10.1186\/s40001-024-01773-z","volume":"29","author":"Q Xue","year":"2024","unstructured":"Xue Q, Ji S, Xu H et al (2024) O-GlcNAcylation: a pro-survival response to acute stress in the cardiovascular and central nervous systems. Eur J Med Res 29:174. https:\/\/doi.org\/10.1186\/s40001-024-01773-z","journal-title":"Eur J Med Res"},{"key":"5357_CR5","doi-asserted-by":"publisher","DOI":"10.1038\/s41597-021-00810-4","volume":"8","author":"E Wulff-Fuentes","year":"2021","unstructured":"Wulff-Fuentes E, Berendt RR, 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","journal-title":"Sci Data"},{"issue":"78","key":"5357_CR6","first-page":"88","volume":"243","author":"S Wang","year":"2017","unstructured":"Wang S, Yang F, Petyuk VA et al (2017) Quantitative proteomics identifies altered O-GlcNAcylation of structural, synaptic and memory-associated proteins in Alzheimer\u2019s disease. J Pathol 243(78):88","journal-title":"J Pathol"},{"key":"5357_CR7","doi-asserted-by":"publisher","first-page":"2416","DOI":"10.1002\/cbic.201700515","volume":"18","author":"AL Aguilar","year":"2017","unstructured":"Aguilar AL, Hou X, Wen L et al (2017) A chemoenzymatic histology method for O-GlcNAc detection. Chembiochem 18:2416\u20132421. https:\/\/doi.org\/10.1002\/cbic.201700515","journal-title":"Chembiochem"},{"key":"5357_CR8","doi-asserted-by":"publisher","first-page":"883","DOI":"10.1016\/j.neuron.2015.03.035","volume":"86","author":"PJ Magistretti","year":"2015","unstructured":"Magistretti PJ, Allaman I (2015) A cellular perspective on brain energy metabolism and functional imaging. Neuron 86:883\u2013901. https:\/\/doi.org\/10.1016\/j.neuron.2015.03.035","journal-title":"Neuron"},{"issue":"3462","key":"5357_CR9","first-page":"3478","volume":"45","author":"N Alnaqbi","year":"2023","unstructured":"Alnaqbi N, Mohammad MG, Hamoudi R et al (2023) Molecular heterogeneity of the brain endothelium. Curr Issues Mol Biol 45(3462):3478","journal-title":"Curr Issues Mol Biol"},{"key":"5357_CR10","doi-asserted-by":"publisher","first-page":"E1127","DOI":"10.1152\/ajpendo.00187.2003","volume":"285","author":"SJ Vannucci","year":"2003","unstructured":"Vannucci SJ, Simpson IA (2003) Developmental switch in brain nutrient transporter expression in the rat. Am J Physiol Endocrinol Metab 285:E1127\u2013E1134","journal-title":"Am J Physiol Endocrinol Metab"},{"key":"5357_CR11","doi-asserted-by":"publisher","first-page":"1766","DOI":"10.1038\/sj.jcbfm.9600521","volume":"27","author":"IA Simpson","year":"2007","unstructured":"Simpson IA, Carruthers A, Vannucci SJ (2007) Supply and demand in cerebral energy metabolism: the role of nutrient transporters. J Cereb Blood Flow Metab 27:1766\u20131791. https:\/\/doi.org\/10.1038\/sj.jcbfm.9600521","journal-title":"J Cereb Blood Flow Metab"},{"key":"5357_CR12","doi-asserted-by":"publisher","DOI":"10.1016\/j.crmeth.2023.100518","volume":"3","author":"M Sunden","year":"2023","unstructured":"Sunden M, Upadhyay D, Banerjee R et al (2023) Enzymatic assay for UDP-GlcNAc and its application in the parallel assessment of substrate availability and protein O-GlcNAcylation. Cell Rep Methods 3:100518. https:\/\/doi.org\/10.1016\/j.crmeth.2023.100518","journal-title":"Cell Rep Methods"},{"key":"5357_CR13","doi-asserted-by":"publisher","first-page":"13","DOI":"10.1016\/j.bbagen.2004.03.016","volume":"1673","author":"NE Zachara","year":"2004","unstructured":"Zachara NE, Hart GW (2004) O-GlcNAc a sensor of cellular state: the role of nucleocytoplasmic glycosylation in modulating cellular function in response to nutrition and stress. Biochim Biophys Acta 1673:13\u201328. https:\/\/doi.org\/10.1016\/j.bbagen.2004.03.016","journal-title":"Biochim Biophys Acta"},{"key":"5357_CR14","doi-asserted-by":"publisher","first-page":"5343","DOI":"10.1038\/s41467-023-41028-9","volume":"14","author":"QQ He","year":"2023","unstructured":"He QQ, Huang Y, Nie L et al (2023) MAVS integrates glucose metabolism and RIG-I-like receptor signaling. Nat Commun 14:5343","journal-title":"Nat Commun"},{"key":"5357_CR15","doi-asserted-by":"publisher","first-page":"2419","DOI":"10.2337\/diabetes.50.11.2419","volume":"50","author":"JE Dehaven","year":"2001","unstructured":"Dehaven JE, Robinson KA, Nelson BA et al (2001) A novel variant of glutamine: fructose-6-phosphate amidotransferase-1 (GFAT1) mRNA is selectively expressed in striated muscle. Diabetes 50:2419\u20132424. https:\/\/doi.org\/10.2337\/diabetes.50.11.2419","journal-title":"Diabetes"},{"issue":"39786","key":"5357_CR16","first-page":"39793","volume":"286","author":"WS Lee","year":"2011","unstructured":"Lee WS, Kang C, Drayna D et al (2011) Analysis of mannose 6-phosphate uncovering enzyme mutations associated with persistent stuttering. J Biol Chem 286(39786):39793","journal-title":"J Biol Chem"},{"key":"5357_CR17","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.69223","author":"V Kroef","year":"2022","unstructured":"Kroef V, Ruegenberg S, Horn M et al (2022) GFPT2\/GFAT2 and AMDHD2 act in tandem to control the hexosamine pathway. Elife. https:\/\/doi.org\/10.7554\/eLife.69223","journal-title":"Elife"},{"key":"5357_CR18","doi-asserted-by":"publisher","first-page":"710","DOI":"10.1093\/glycob\/cww019","volume":"26","author":"S Oikari","year":"2016","unstructured":"Oikari S, Makkonen K, Deen AJ et al (2016) Hexosamine biosynthesis in keratinocytes: roles of GFAT and GNPDA enzymes in the maintenance of UDP-GlcNAc content and hyaluronan synthesis. Glycobiology 26:710\u2013722","journal-title":"Glycobiology"},{"key":"5357_CR19","doi-asserted-by":"publisher","first-page":"222","DOI":"10.1007\/s000180300017","volume":"60","author":"L Wells","year":"2003","unstructured":"Wells L, Vosseller K, Hart GW (2003) A role for N-acetylglucosamine as a nutrient sensor and mediator of insulin resistance. Cell Mol Life Sci 60:222\u2013228","journal-title":"Cell Mol Life Sci"},{"key":"5357_CR20","doi-asserted-by":"publisher","first-page":"2143","DOI":"10.1016\/j.devcel.2024.05.008","volume":"59","author":"SB Yu","year":"2024","unstructured":"Yu SB, Wang H, Sanchez RG et al (2024) Neuronal activity-driven O-GlcNAcylation promotes mitochondrial plasticity. Dev Cell 59:2143-2157.e9. https:\/\/doi.org\/10.1016\/j.devcel.2024.05.008","journal-title":"Dev Cell"},{"key":"5357_CR21","doi-asserted-by":"publisher","first-page":"9308","DOI":"10.1074\/jbc.272.14.9308","volume":"272","author":"LK Kreppel","year":"1997","unstructured":"Kreppel LK, Blomberg MA, Hart GW (1997) Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats. J Biol Chem 272:9308\u20139315. https:\/\/doi.org\/10.1074\/jbc.272.14.9308","journal-title":"J Biol Chem"},{"key":"5357_CR22","doi-asserted-by":"publisher","first-page":"9838","DOI":"10.1074\/jbc.M010420200","volume":"276","author":"Y Gao","year":"2001","unstructured":"Gao Y, Wells L, Comer FI et al (2001) Dynamic O-glycosylation of nuclear and cytosolic proteins: cloning and characterization of a neutral, cytosolic beta-N-acetylglucosaminidase from human brain. J Biol Chem 276:9838\u20139845. https:\/\/doi.org\/10.1074\/jbc.M010420200","journal-title":"J Biol Chem"},{"key":"5357_CR23","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2401729121","volume":"121","author":"SC Potter","year":"2024","unstructured":"Potter SC, Gibbs BE, Hammel FA et al (2024) Dissecting OGT\u2019s TPR domain to identify determinants of cellular function. Proc Natl Acad Sci U S A 121:e2401729121","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"9316","key":"5357_CR24","first-page":"9324","volume":"272","author":"WA Lubas","year":"1997","unstructured":"Lubas WA, Frank DW, Krause M et al (1997) O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats. J Biol Chem 272(9316):9324","journal-title":"J Biol Chem"},{"issue":"24608","key":"5357_CR25","first-page":"24616","volume":"278","author":"SP Iyer","year":"2003","unstructured":"Iyer SP, Hart GW (2003) Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity. J Biol Chem 278(24608):24616","journal-title":"J Biol Chem"},{"issue":"6650","key":"5357_CR26","doi-asserted-by":"publisher","first-page":"6650","DOI":"10.1074\/jbc.M110.191627","volume":"286","author":"LD Carrillo","year":"2011","unstructured":"Carrillo LD, Froemming JA, Mahal LK (2011) Targeted in vivo O-GlcNAc sensors reveal discrete compartment-specific dynamics during signal transduction. J Biol Chem 286(6650):6650\u20136658","journal-title":"J Biol Chem"},{"key":"5357_CR27","doi-asserted-by":"publisher","first-page":"32015","DOI":"10.1074\/jbc.274.45.32015","volume":"274","author":"LK Kreppel","year":"1999","unstructured":"Kreppel LK, Hart GW (1999) Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats. J Biol Chem 274:32015\u201332022. https:\/\/doi.org\/10.1074\/jbc.274.45.32015","journal-title":"J Biol Chem"},{"key":"5357_CR28","doi-asserted-by":"publisher","first-page":"287","DOI":"10.1016\/s0003-9861(02)00578-7","volume":"409","author":"JA Hanover","year":"2003","unstructured":"Hanover JA, Yu S, Lubas WB et al (2003) Mitochondrial and nucleocytoplasmic isoforms of O-linked GlcNAc transferase encoded by a single mammalian gene. Arch Biochem Biophys 409:287\u2013297. https:\/\/doi.org\/10.1016\/s0003-9861(02)00578-7","journal-title":"Arch Biochem Biophys"},{"key":"5357_CR29","doi-asserted-by":"publisher","first-page":"17669","DOI":"10.1073\/pnas.1205748109","volume":"109","author":"P Wang","year":"2012","unstructured":"Wang P, Lazarus BD, Forsythe ME et al (2012) O-GlcNAc cycling mutants modulate proteotoxicity in Caenorhabditis elegans models of human neurodegenerative diseases. Proc Natl Acad Sci U S A 109:17669\u201317674. https:\/\/doi.org\/10.1073\/pnas.1205748109","journal-title":"Proc Natl Acad Sci U S A"},{"key":"5357_CR30","doi-asserted-by":"publisher","DOI":"10.1098\/rsob.170078","author":"K Rafie","year":"2017","unstructured":"Rafie K, Raimi O, Ferenbach AT et al (2017) Recognition of a glycosylation substrate by the O-GlcNAc transferase TPR repeats. Open Biol. https:\/\/doi.org\/10.1098\/rsob.170078","journal-title":"Open Biol"},{"key":"5357_CR31","doi-asserted-by":"publisher","first-page":"321","DOI":"10.1016\/j.cell.2011.01.025","volume":"144","author":"JA Hanover","year":"2011","unstructured":"Hanover JA (2011) A versatile sugar transferase makes the cut. Cell 144:321\u2013323. https:\/\/doi.org\/10.1016\/j.cell.2011.01.025","journal-title":"Cell"},{"key":"5357_CR32","doi-asserted-by":"publisher","first-page":"17754","DOI":"10.1074\/jbc.RA118.004185","volume":"293","author":"V Kapuria","year":"2018","unstructured":"Kapuria V, R\u00f6hrig UF, Waridel P et al (2018) The conserved threonine-rich region of the HCF-1(PRO) repeat activates promiscuous OGT:UDP-GlcNAc glycosylation and proteolysis activities. J Biol Chem 293:17754\u201317768","journal-title":"J Biol Chem"},{"key":"5357_CR33","doi-asserted-by":"publisher","first-page":"13009","DOI":"10.1074\/jbc.M801222200","volume":"283","author":"WD Cheung","year":"2008","unstructured":"Cheung WD, Hart GW (2008) AMP-activated protein kinase and p38 MAPK activate O-GlcNAcylation of neuronal proteins during glucose deprivation. J Biol Chem 283:13009\u201313020","journal-title":"J Biol Chem"},{"key":"5357_CR34","doi-asserted-by":"publisher","first-page":"10592","DOI":"10.1074\/jbc.M113.523068","volume":"289","author":"JW Bullen","year":"2014","unstructured":"Bullen JW, Balsbaugh JL, Chanda D et al (2014) Cross-talk between two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK). J Biol Chem 289:10592\u201310606. https:\/\/doi.org\/10.1074\/jbc.M113.523068","journal-title":"J Biol Chem"},{"key":"5357_CR35","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0260072","volume":"16","author":"N Suthakaran","year":"2021","unstructured":"Suthakaran N, Wiggins J, Giles A et al (2021) O-GlcNAc transferase OGT-1 and the ubiquitin ligase EEL-1 modulate seizure susceptibility in C. elegans. PLoS One 16:e0260072","journal-title":"PLoS One"},{"key":"5357_CR36","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2218332120","volume":"120","author":"X Li","year":"2023","unstructured":"Li X, Yue X, Sepulveda H et al (2023) OGT controls mammalian cell viability by regulating the proteasome\/mTOR\/ mitochondrial axis. Proc Natl Acad Sci U S A 120:e2218332120","journal-title":"Proc Natl Acad Sci U S A"},{"key":"5357_CR37","doi-asserted-by":"publisher","first-page":"1080","DOI":"10.1046\/j.1471-4159.2001.00655.x","volume":"79","author":"RN Cole","year":"2001","unstructured":"Cole RN, Hart GW (2001) Cytosolic o-glycosylation is abundant in nerve terminals. J Neurochem 79:1080\u20131089. https:\/\/doi.org\/10.1046\/j.1471-4159.2001.00655.x","journal-title":"J Neurochem"},{"key":"5357_CR38","doi-asserted-by":"publisher","first-page":"1271","DOI":"10.1046\/j.1471-4159.2003.01939.x","volume":"86","author":"R Okuyama","year":"2003","unstructured":"Okuyama R, Marshall S (2003) UDP-N-acetylglucosaminyl transferase (OGT) in brain tissue: temperature sensitivity and subcellular distribution of cytosolic and nuclear enzyme. J Neurochem 86:1271\u20131280","journal-title":"J Neurochem"},{"key":"5357_CR39","doi-asserted-by":"publisher","DOI":"10.3390\/cells9081792","author":"R Tazhitdinova","year":"2020","unstructured":"Tazhitdinova R, Timoshenko AV (2020) The emerging role of galectins and O-GlcNAc homeostasis in processes of cellular differentiation. Cells. https:\/\/doi.org\/10.3390\/cells9081792","journal-title":"Cells"},{"key":"5357_CR40","doi-asserted-by":"publisher","first-page":"12","DOI":"10.1016\/j.cbpa.2019.04.023","volume":"235","author":"O Abernathy","year":"2019","unstructured":"Abernathy O, Kostner D, Buer P et al (2019) Expression of messenger RNA encoding two cellular metabolic regulators, AMP-activated protein kinase (AMPK) and O-GlcNAc transferase (OGT), in channel catfish: their tissue distribution and relationship with changes in food intake. Comp Biochem Physiol A Mol Integr Physiol 235:12\u201321. https:\/\/doi.org\/10.1016\/j.cbpa.2019.04.023","journal-title":"Comp Biochem Physiol A Mol Integr Physiol"},{"key":"5357_CR41","doi-asserted-by":"publisher","DOI":"10.1016\/j.jbc.2024.107599","author":"JM Mayfield","year":"2024","unstructured":"Mayfield JM, Hitefield NL, Czajewski I et al (2024) O-GlcNAc transferase congenital disorder of glycosylation (OGT-CDG): potential mechanistic targets revealed by evaluating the OGT interactome. J Biol Chem. https:\/\/doi.org\/10.1016\/j.jbc.2024.107599","journal-title":"J Biol Chem"},{"issue":"1919","key":"5357_CR42","first-page":"1930","volume":"124","author":"M Wu","year":"2023","unstructured":"Wu M, Jiang H, Li Q et al (2023) OGT-1 regulates synaptic assembly through the insulin signaling pathway. J Cell Biochem 124(1919):1930","journal-title":"J Cell Biochem"},{"issue":"1684","key":"5357_CR43","first-page":"1689","volume":"114","author":"O Lagerl\u00f6f","year":"2017","unstructured":"Lagerl\u00f6f O, Hart GW, Huganir RL (2017) O-GlcNAc transferase regulates excitatory synapse maturity. Proc Natl Acad Sci U S A 114(1684):1689","journal-title":"Proc Natl Acad Sci U S A"},{"key":"5357_CR44","doi-asserted-by":"publisher","first-page":"253","DOI":"10.1038\/nchembio.770","volume":"8","author":"JE Rexach","year":"2012","unstructured":"Rexach JE, Clark PM, Mason DE et al (2012) Dynamic O-GlcNAc modification regulates CREB-mediated gene expression and memory formation. Nat Chem Biol 8:253\u2013261","journal-title":"Nat Chem Biol"},{"key":"5357_CR45","doi-asserted-by":"publisher","first-page":"3667","DOI":"10.1007\/s00018-017-2542-9","volume":"74","author":"X Ma","year":"2017","unstructured":"Ma X, Li H, He Y et al (2017) The emerging link between O-GlcNAcylation and neurological disorders. Cell Mol Life Sci 74:3667\u20133686. https:\/\/doi.org\/10.1007\/s00018-017-2542-9","journal-title":"Cell Mol Life Sci"},{"key":"5357_CR46","doi-asserted-by":"publisher","DOI":"10.1186\/s13550-020-0616-4","volume":"10","author":"JH Lee","year":"2020","unstructured":"Lee JH, Liow JS, Paul S et al (2020) PET quantification of brain O-GlcNAcase with [(18)F]LSN3316612 in healthy human volunteers. EJNMMI Res 10:20","journal-title":"EJNMMI Res"},{"issue":"129","key":"5357_CR47","first-page":"134","volume":"60","author":"S Paul","year":"2019","unstructured":"Paul S, Haskali MB, Liow JS et al (2019) Evaluation of a PET radioligand to image O-GlcNAcase in brain and periphery of rhesus monkey and knock-out mouse. J Nucl Med 60(129):134","journal-title":"J Nucl Med"},{"issue":"2851","key":"5357_CR48","first-page":"2860","volume":"124","author":"CN Keembiyehetty","year":"2011","unstructured":"Keembiyehetty CN, Krzeslak A, Love DC et al (2011) A lipid-droplet-targeted O-GlcNAcase isoform is a key regulator of the proteasome. J Cell Sci 124(2851):2860","journal-title":"J Cell Sci"},{"key":"5357_CR49","doi-asserted-by":"publisher","first-page":"179","DOI":"10.1016\/s0014-5793(02)03322-7","volume":"529","author":"J Schultz","year":"2002","unstructured":"Schultz J, Pils B (2002) Prediction of structure and functional residues for O-GlcNAcase, a divergent homologue of acetyltransferases. FEBS Lett 529:179\u2013182. https:\/\/doi.org\/10.1016\/s0014-5793(02)03322-7","journal-title":"FEBS Lett"},{"issue":"53665","key":"5357_CR50","first-page":"53673","volume":"279","author":"C Toleman","year":"2004","unstructured":"Toleman C, Paterson AJ, Whisenhunt TR et al (2004) Characterization of the histone acetyltransferase (HAT) domain of a bifunctional protein with activable O-GlcNAcase and HAT activities. J Biol Chem 279(53665):53673","journal-title":"J Biol Chem"},{"issue":"12918","key":"5357_CR51","first-page":"13019","volume":"124","author":"SS Cheng","year":"2024","unstructured":"Cheng SS, Mody AC, Woo CM (2024) Opportunities for therapeutic modulation of O-GlcNAc. Chem Rev 124(12918):13019","journal-title":"Chem Rev"},{"key":"5357_CR52","doi-asserted-by":"publisher","first-page":"6952","DOI":"10.1038\/s41467-023-42427-8","volume":"14","author":"P Lu","year":"2023","unstructured":"Lu P, Liu Y, He M et al (2023) Cryo-EM structure of human O-GlcNAcylation enzyme pair OGT-OGA complex. Nat Commun 14:6952","journal-title":"Nat Commun"},{"key":"5357_CR53","doi-asserted-by":"publisher","first-page":"23557","DOI":"10.1074\/jbc.M804116200","volume":"283","author":"C Butkinaree","year":"2008","unstructured":"Butkinaree C, Cheung WD, Park S et al (2008) Characterization of beta-N-acetylglucosaminidase cleavage by caspase-3 during apoptosis. J Biol Chem 283:23557\u201323566. https:\/\/doi.org\/10.1074\/jbc.M804116200","journal-title":"J Biol Chem"},{"key":"5357_CR54","doi-asserted-by":"publisher","first-page":"666","DOI":"10.1038\/s41467-017-00865-1","volume":"8","author":"B Li","year":"2017","unstructured":"Li B, Li H, Hu CW et al (2017) Structural insights into the substrate binding adaptability and specificity of human O-GlcNAcase. Nat Commun 8:666","journal-title":"Nat Commun"},{"key":"5357_CR55","doi-asserted-by":"publisher","DOI":"10.3390\/cancers14123013","author":"E Kim","year":"2022","unstructured":"Kim E, Kang JG, Jho EH et al (2022) O-GlcNAcylation: an emerging protein modification regulating the hippo pathway. Cancers (Basel). https:\/\/doi.org\/10.3390\/cancers14123013","journal-title":"Cancers (Basel)"},{"key":"5357_CR56","doi-asserted-by":"publisher","first-page":"7","DOI":"10.1111\/jnc.14242","volume":"144","author":"I Akan","year":"2018","unstructured":"Akan I, Olivier-Van Stichelen S, Bond MR et al (2018) Nutrient-driven O-GlcNAc in proteostasis and neurodegeneration. J Neurochem 144:7\u201334. https:\/\/doi.org\/10.1111\/jnc.14242","journal-title":"J Neurochem"},{"issue":"6076","key":"5357_CR57","first-page":"6085","volume":"292","author":"S Olivier-Van Stichelen","year":"2017","unstructured":"Olivier-Van Stichelen S, Wang P, Comly M et al (2017) Nutrient-driven O-linked N-acetylglucosamine (O-GlcNAc) cycling impacts neurodevelopmental timing and metabolism. J Biol Chem 292(6076):6085","journal-title":"J Biol Chem"},{"key":"5357_CR58","doi-asserted-by":"publisher","first-page":"1755","DOI":"10.1074\/jbc.m109656200","volume":"277","author":"L Wells","year":"2002","unstructured":"Wells L, Gao Y, Mahoney JA et al (2002) Dynamic O-glycosylation of nuclear and cytosolic proteins: further characterization of the nucleocytoplasmic beta-N-acetylglucosaminidase, O-GlcNAcase. J Biol Chem 277:1755\u20131761. https:\/\/doi.org\/10.1074\/jbc.m109656200","journal-title":"J Biol Chem"},{"key":"5357_CR59","doi-asserted-by":"publisher","first-page":"2376","DOI":"10.1126\/science.1058714","volume":"291","author":"L Wells","year":"2001","unstructured":"Wells L, Vosseller K, Hart GW (2001) Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAc. Science 291:2376\u20132378. https:\/\/doi.org\/10.1126\/science.1058714","journal-title":"Science"},{"key":"5357_CR60","doi-asserted-by":"publisher","first-page":"631","DOI":"10.1016\/j.sbi.2003.08.003","volume":"13","author":"C Slawson","year":"2003","unstructured":"Slawson C, Hart GW (2003) Dynamic interplay between O-GlcNAc and O-phosphate: the sweet side of protein regulation. Curr Opin Struct Biol 13:631\u2013636. https:\/\/doi.org\/10.1016\/j.sbi.2003.08.003","journal-title":"Curr Opin Struct Biol"},{"key":"5357_CR61","doi-asserted-by":"publisher","first-page":"E7255","DOI":"10.1073\/pnas.1620529114","volume":"114","author":"AC Leney","year":"2017","unstructured":"Leney AC, El Atmioui D, Wu W et al (2017) Elucidating crosstalk mechanisms between phosphorylation and O-GlcNAcylation. Proc Natl Acad Sci U S A 114:E7255\u2013E7261","journal-title":"Proc Natl Acad Sci U S A"},{"key":"5357_CR62","doi-asserted-by":"publisher","first-page":"240","DOI":"10.1111\/jnc.14474","volume":"147","author":"J Fourneau","year":"2018","unstructured":"Fourneau J, Canu MH, Cieniewski-Bernard C et al (2018) Synaptic protein changes after a chronic period of sensorimotor perturbation in adult rats: a potential role of phosphorylation\/O-GlcNAcylation interplay. J Neurochem 147:240\u2013255. https:\/\/doi.org\/10.1111\/jnc.14474","journal-title":"J Neurochem"},{"key":"5357_CR63","doi-asserted-by":"publisher","DOI":"10.3389\/fendo.2018.00595","volume":"9","author":"G Bourr\u00e9","year":"2018","unstructured":"Bourr\u00e9 G, Cantrelle FX, Kamah A et al (2018) Direct crosstalk between O-GlcNAcylation and phosphorylation of tau protein investigated by NMR spectroscopy. Front Endocrinol (Lausanne) 9:595","journal-title":"Front Endocrinol (Lausanne)"},{"key":"5357_CR64","doi-asserted-by":"publisher","first-page":"1513","DOI":"10.1021\/acs.biochem.4c00095","volume":"63","author":"L El Hajjar","year":"2024","unstructured":"El Hajjar L, Page A, Bridot C et al (2024) Regulation of glycogen synthase kinase-3\u03b2 by phosphorylation and O-\u03b2-linked N-acetylglucosaminylation: implications on tau protein phosphorylation. Biochemistry 63:1513\u20131533. https:\/\/doi.org\/10.1021\/acs.biochem.4c00095","journal-title":"Biochemistry"},{"issue":"1411","key":"5357_CR65","first-page":"1425.e8","volume":"85","author":"X He","year":"2025","unstructured":"He X, Chen D, Liu G et al (2025) PI3K\u03b2 functions as a protein kinase to promote cellular protein O-GlcNAcylation and acetyl-CoA production for tumor growth. Mol Cell 85(1411):1425.e8","journal-title":"Mol Cell"},{"issue":"71","key":"5357_CR66","first-page":"77","volume":"15","author":"MN Sardoiwala","year":"2024","unstructured":"Sardoiwala MN, Boddu M, Biswal L et al (2024) FTY720 nanoformulation induces O-GlcNacylation of synuclein to alleviate synucleinopathy. ACS Chem Neurosci 15(71):77","journal-title":"ACS Chem Neurosci"},{"key":"5357_CR67","doi-asserted-by":"publisher","DOI":"10.1096\/fj.202400907RR","volume":"38","author":"J Cai","year":"2024","unstructured":"Cai J, Deng Y, Min Z et al (2024) Deciphering the dynamics: exploring the impact of mechanical forces on histone acetylation. FASEB J 38:e23849","journal-title":"FASEB J"},{"key":"5357_CR68","doi-asserted-by":"publisher","first-page":"51","DOI":"10.1186\/s13072-017-0157-x","volume":"10","author":"K Hayakawa","year":"2017","unstructured":"Hayakawa K, Hirosawa M, Tani R et al (2017) H2A O-GlcNAcylation at serine 40 functions genomic protection in association with acetylated H2AZ or \u03b3H2AX. Epigenetics Chromatin 10:51","journal-title":"Epigenetics Chromatin"},{"key":"5357_CR69","doi-asserted-by":"publisher","DOI":"10.1016\/j.jbc.2022.102115","volume":"298","author":"B Xu","year":"2022","unstructured":"Xu B, Zhang C, Jiang A et al (2022) Histone methyltransferase Dot1L recruits O-GlcNAc transferase to target chromatin sites to regulate histone O-GlcNAcylation. J Biol Chem 298:102115. https:\/\/doi.org\/10.1016\/j.jbc.2022.102115","journal-title":"J Biol Chem"},{"key":"5357_CR70","doi-asserted-by":"publisher","first-page":"19251","DOI":"10.1038\/s41598-022-21883-0","volume":"12","author":"J Merx","year":"2022","unstructured":"Merx J, Hintzen JCJ, Proietti G et al (2022) Investigation of in vitro histone H3 glycosylation using H3 tail peptides. Sci Rep 12:19251","journal-title":"Sci Rep"},{"key":"5357_CR71","doi-asserted-by":"publisher","DOI":"10.3390\/ijms21010173","author":"L Zhao","year":"2019","unstructured":"Zhao L, Li M, Wei T et al (2019) O-GlcNAc-modification of NSL3 at Thr755 site maintains the holoenzyme activity of MOF\/NSL histone acetyltransfease complex. Int J Mol Sci. https:\/\/doi.org\/10.3390\/ijms21010173","journal-title":"Int J Mol Sci"},{"key":"5357_CR72","doi-asserted-by":"publisher","first-page":"482","DOI":"10.1093\/glycob\/cwy040","volume":"28","author":"H Shan","year":"2018","unstructured":"Shan H, Sun J, Shi M et al (2018) Generation and characterization of a site-specific antibody for SIRT1 O-GlcNAcylated at serine 549. Glycobiology 28:482\u2013487. https:\/\/doi.org\/10.1093\/glycob\/cwy040","journal-title":"Glycobiology"},{"key":"5357_CR73","doi-asserted-by":"publisher","first-page":"9150","DOI":"10.1074\/jbc.M116.766568","volume":"292","author":"Z Ma","year":"2017","unstructured":"Ma Z, Chalkley RJ, Vosseller K (2017) Hyper-O-GlcNAcylation activates nuclear factor \u03ba-light-chain-enhancer of activated B cells (NF-\u03baB) signaling through interplay with phosphorylation and acetylation. J Biol Chem 292:9150\u20139163. https:\/\/doi.org\/10.1074\/jbc.M116.766568","journal-title":"J Biol Chem"},{"key":"5357_CR74","doi-asserted-by":"publisher","DOI":"10.1002\/alz.70243","volume":"21","author":"H Liu","year":"2025","unstructured":"Liu H, Bui Q, Hassenstab J et al (2025) Ubiquitin-proteasome system in the different stages of dominantly inherited Alzheimer\u2019s disease. Alzheimers Dement 21:e70243","journal-title":"Alzheimers Dement"},{"issue":"1149","key":"5357_CR75","first-page":"1159","volume":"43","author":"Z Feng","year":"2024","unstructured":"Feng Z, Yin J, Zhang Z et al (2024) O-GlcNAcylation of E3 ubiquitin ligase SKP2 promotes hepatocellular carcinoma proliferation. Oncogene 43(1149):1159","journal-title":"Oncogene"},{"key":"5357_CR76","doi-asserted-by":"publisher","unstructured":"Parween\u00a0S, Alawathugoda\u00a0 TT,\u00a0 Prabakaran\u00a0DA  et al (2022) Nutrient sensitive protein O-GlcNAcylation modulates the transcriptome through epigenetic mechanisms during embryonic neurogenesis. Life Sci Alliance https:\/\/doi.org\/10.26508\/lsa.202201385","DOI":"10.26508\/lsa.202201385"},{"key":"5357_CR77","doi-asserted-by":"publisher","DOI":"10.1016\/j.celrep.2021.108905","volume":"34","author":"J Chen","year":"2021","unstructured":"Chen J, Dong X, Cheng X et al (2021) Ogt controls neural stem\/progenitor cell pool and adult neurogenesis through modulating Notch signaling. Cell Rep 34:108905. https:\/\/doi.org\/10.1016\/j.celrep.2021.108905","journal-title":"Cell Rep"},{"key":"5357_CR78","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2320867121","volume":"121","author":"CW Hu","year":"2024","unstructured":"Hu CW, Wang A, Fan D et al (2024) OGA mutant aberrantly hydrolyzes O-GlcNAc modification from PDLIM7 to modulate p53 and cytoskeleton in promoting cancer cell malignancy. Proc Natl Acad Sci U S A 121:e2320867121. https:\/\/doi.org\/10.1073\/pnas.2320867121","journal-title":"Proc Natl Acad Sci U S A"},{"key":"5357_CR79","doi-asserted-by":"publisher","DOI":"10.1016\/j.jbc.2024.107150","volume":"300","author":"J Zhao","year":"2024","unstructured":"Zhao J, Hua J, Zhan Y et al (2024) O-GlcNAcylation stimulates the deubiquitination activity of USP16 and regulates cell cycle progression. J Biol Chem 300:107150. https:\/\/doi.org\/10.1016\/j.jbc.2024.107150","journal-title":"J Biol Chem"},{"key":"5357_CR80","doi-asserted-by":"publisher","first-page":"1530","DOI":"10.1038\/s42003-024-07251-w","volume":"7","author":"Y Li","year":"2024","unstructured":"Li Y, Niu L, Zheng D et al (2024) KDM2B regulates stroke injury by modulating OGT-mediated 0-GlcNAcylation of SLC7A11. Commun Biol 7:1530","journal-title":"Commun Biol"},{"key":"5357_CR81","doi-asserted-by":"publisher","DOI":"10.1016\/j.jbc.2024.107448","volume":"300","author":"L Meng","year":"2024","unstructured":"Meng L, Dong R, Mi W et al (2024) The ubiquitin E3 ligase APC\/C(Cdc20) mediates mitotic degradation of OGT. J Biol Chem 300:107448. https:\/\/doi.org\/10.1016\/j.jbc.2024.107448","journal-title":"J Biol Chem"},{"issue":"173","key":"5357_CR82","first-page":"189","volume":"11","author":"MB Luskin","year":"1993","unstructured":"Luskin MB (1993) Restricted proliferation and migration of postnatally generated neurons derived from the forebrain subventricular zone. Neuron 11(173):189","journal-title":"Neuron"},{"key":"5357_CR83","doi-asserted-by":"publisher","first-page":"2074","DOI":"10.1073\/pnas.90.5.2074","volume":"90","author":"C Lois","year":"1993","unstructured":"Lois C, Alvarez-Buylla A (1993) Proliferating subventricular zone cells in the adult mammalian forebrain can differentiate into neurons and glia. Proc Natl Acad Sci U S A 90:2074\u20132077","journal-title":"Proc Natl Acad Sci U S A"},{"key":"5357_CR84","volume":"2015","author":"J Zhang","year":"2015","unstructured":"Zhang J, Jiao J (2015) Molecular biomarkers for embryonic and adult neural stem cell and neurogenesis. Biomed Res Int 2015:727542","journal-title":"Biomed Res Int"},{"key":"5357_CR85","doi-asserted-by":"publisher","first-page":"2030","DOI":"10.1021\/acschembio.7b00232","volume":"12","author":"LM Andres","year":"2017","unstructured":"Andres LM, Blong IW, Evans AC et al (2017) Chemical modulation of protein O-GlcNAcylation via OGT inhibition promotes human neural cell differentiation. ACS Chem Biol 12:2030\u20132039","journal-title":"ACS Chem Biol"},{"key":"5357_CR86","doi-asserted-by":"publisher","first-page":"57","DOI":"10.1093\/hmg\/ddab223","volume":"31","author":"H Shen","year":"2021","unstructured":"Shen H, Zhao X, Chen J et al (2021) O-GlcNAc transferase Ogt regulates embryonic neuronal development through modulating Wnt\/\u03b2-catenin signaling. Hum Mol Genet 31:57\u201368","journal-title":"Hum Mol Genet"},{"key":"5357_CR87","doi-asserted-by":"publisher","DOI":"10.3389\/fmolb.2022.920727","volume":"9","author":"RA Burt","year":"2022","unstructured":"Burt RA, Alghusen IM, John Ephrame S et al (2022) Mapping the O-GlcNAc modified proteome: applications for health and disease. Front Mol Biosci 9:920727","journal-title":"Front Mol Biosci"},{"key":"5357_CR88","doi-asserted-by":"publisher","first-page":"22214","DOI":"10.1073\/pnas.2007439117","volume":"117","author":"CW White","year":"2020","unstructured":"White CW, Fan X, Maynard JC et al (2020) Age-related loss of neural stem cell O-GlcNAc promotes a glial fate switch through STAT3 activation. Proc Natl Acad Sci U S A 117:22214\u201322224. https:\/\/doi.org\/10.1073\/pnas.2007439117","journal-title":"Proc Natl Acad Sci U S A"},{"key":"5357_CR89","doi-asserted-by":"publisher","first-page":"215","DOI":"10.1074\/mcp.O112.018366","volume":"11","author":"JC Trinidad","year":"2012","unstructured":"Trinidad JC, Barkan DT, Gulledge BF et al (2012) Global identification and characterization of both O-GlcNAcylation and phosphorylation at the murine synapse. Mol Cell Proteomics 11:215\u2013229","journal-title":"Mol Cell Proteomics"},{"key":"5357_CR90","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.90376","author":"I Czajewski","year":"2024","unstructured":"Czajewski I, Swain B, Xu J et al (2024) Rescuable sleep and synaptogenesis phenotypes in a Drosophila model of O-GlcNAc transferase intellectual disability. Elife. https:\/\/doi.org\/10.7554\/eLife.90376","journal-title":"Elife"},{"key":"5357_CR91","doi-asserted-by":"publisher","first-page":"418","DOI":"10.1046\/j.1471-4159.1999.0730418.x","volume":"73","author":"RN Cole","year":"1999","unstructured":"Cole RN, Hart GW (1999) Glycosylation sites flank phosphorylation sites on synapsin I: O-linked N-acetylglucosamine residues are localized within domains mediating synapsin I interactions. J Neurochem 73:418\u2013428. https:\/\/doi.org\/10.1046\/j.1471-4159.1999.0730418.x","journal-title":"J Neurochem"},{"key":"5357_CR92","doi-asserted-by":"publisher","first-page":"3602","DOI":"10.1074\/jbc.M113.512814","volume":"289","author":"Y Skorobogatko","year":"2014","unstructured":"Skorobogatko Y, Landicho A, Chalkley RJ et al (2014) O-linked \u03b2-N-acetylglucosamine (O-GlcNAc) site thr-87 regulates synapsin I localization to synapses and size of the reserve pool of synaptic vesicles. J Biol Chem 289:3602\u20133612","journal-title":"J Biol Chem"},{"key":"5357_CR93","doi-asserted-by":"publisher","first-page":"7430","DOI":"10.1038\/s41467-024-51678-y","volume":"15","author":"A Zare","year":"2024","unstructured":"Zare A, Salehi S, Bader J et al (2024) Hnrnp R promotes O-GlcNAcylation of eIF4G and facilitates axonal protein synthesis. Nat Commun 15:7430","journal-title":"Nat Commun"},{"key":"5357_CR94","doi-asserted-by":"publisher","first-page":"45","DOI":"10.1016\/j.mito.2022.04.007","volume":"65","author":"Q Xue","year":"2022","unstructured":"Xue Q, Yan R, Ji S et al (2022) Regulation of mitochondrial network homeostasis by O-GlcNAcylation. Mitochondrion 65:45\u201355","journal-title":"Mitochondrion"},{"key":"5357_CR95","doi-asserted-by":"publisher","first-page":"44921","DOI":"10.1038\/srep44921","volume":"7","author":"YR Yang","year":"2017","unstructured":"Yang YR, Song S, Hwang H et al (2017) Memory and synaptic plasticity are impaired by dysregulated hippocampal O-GlcNAcylation. Sci Rep 7:44921","journal-title":"Sci Rep"},{"key":"5357_CR96","doi-asserted-by":"publisher","DOI":"10.1038\/s41598-020-63188-0","volume":"10","author":"T Stewart","year":"2020","unstructured":"Stewart T, Abiraman K, Chatham JC et al (2020) Increased O-GlcNAcylation rapidly decreases GABA(A)R currents in hippocampus but depresses neuronal output. Sci Rep 10:7494","journal-title":"Sci Rep"},{"key":"5357_CR97","doi-asserted-by":"publisher","first-page":"7287","DOI":"10.1038\/s41598-019-43017-9","volume":"9","author":"H Hwang","year":"2019","unstructured":"Hwang H, Rhim H (2019) Acutely elevated O-GlcNAcylation suppresses hippocampal activity by modulating both intrinsic and synaptic excitability factors. Sci Rep 9:7287","journal-title":"Sci Rep"},{"key":"5357_CR98","doi-asserted-by":"publisher","first-page":"10686","DOI":"10.1038\/s41598-017-10635-0","volume":"7","author":"JH Gu","year":"2017","unstructured":"Gu JH, Shi J, Dai CL et al (2017) O-GlcNAcylation reduces ischemia-reperfusion-induced brain injury. Sci Rep 7:10686","journal-title":"Sci Rep"},{"key":"5357_CR99","doi-asserted-by":"publisher","DOI":"10.1016\/j.expneurol.2021.113646","volume":"339","author":"Z Wang","year":"2021","unstructured":"Wang Z, Li X, Spasojevic I et al (2021) Increasing O-GlcNAcylation is neuroprotective in young and aged brains after ischemic stroke. Exp Neurol 339:113646. https:\/\/doi.org\/10.1016\/j.expneurol.2021.113646","journal-title":"Exp Neurol"},{"key":"5357_CR100","doi-asserted-by":"publisher","first-page":"393","DOI":"10.1177\/0271678x15608393","volume":"36","author":"S Liu","year":"2016","unstructured":"Liu S, Sheng H, Yu Z et al (2016) O-linked \u03b2-N-acetylglucosamine modification of proteins is activated in post-ischemic brains of young but not aged mice: implications for impaired functional recovery from ischemic stress. J Cereb Blood Flow Metab 36:393\u2013398. https:\/\/doi.org\/10.1177\/0271678x15608393","journal-title":"J Cereb Blood Flow Metab"},{"key":"5357_CR101","doi-asserted-by":"publisher","first-page":"1646","DOI":"10.1161\/STROKEAHA.117.016579","volume":"48","author":"M Jiang","year":"2017","unstructured":"Jiang M, Yu S, Yu Z et al (2017) XBP1 (X-box-binding protein-1)-dependent O-GlcNAcylation is neuroprotective in ischemic stroke in young mice and its impairment in aged mice is rescued by Thiamet-G. Stroke 48:1646\u20131654","journal-title":"Stroke"},{"key":"5357_CR102","doi-asserted-by":"publisher","first-page":"1349","DOI":"10.1097\/wnr.0000000000001734","volume":"32","author":"Y He","year":"2021","unstructured":"He Y, Liu H, Liu Y et al (2021) O-GlcNAcase inhibitor has protective effects in intracerebral hemorrhage by suppressing the inflammatory response. Neuroreport 32:1349\u20131356. https:\/\/doi.org\/10.1097\/wnr.0000000000001734","journal-title":"Neuroreport"},{"key":"5357_CR103","doi-asserted-by":"publisher","unstructured":"Wu K, Chen L,\u00a0 Qiu  Z et al (2023) Protective effect and mechanism of Xbp1s regulating HBP\/O-GlcNAcylation through GFAT1 on brain injury after SAH. Biomedicines https:\/\/doi.org\/10.3390\/biomedicines11051259","DOI":"10.3390\/biomedicines11051259"},{"key":"5357_CR104","doi-asserted-by":"publisher","unstructured":"Hwang SY, Shin JH, Hwang JS et al (1892) 2010 Glucosamine exerts a neuroprotective effect via suppression of inflammation in rat brain ischemia\/reperfusion injury. Glia 58:1881. https:\/\/doi.org\/10.1002\/glia.21058","DOI":"10.1002\/glia.21058"},{"key":"5357_CR105","doi-asserted-by":"publisher","DOI":"10.1007\/s11011-024-01420-w","volume":"40","author":"M Wang","year":"2024","unstructured":"Wang M, Zhu W, Guo Y et al (2024) Astragalus polysaccharide treatment relieves cerebral ischemia-reperfusion injury by promoting M2 polarization of microglia by enhancing O-GlcNAcylation. Metab Brain Dis 40:16. https:\/\/doi.org\/10.1007\/s11011-024-01420-w","journal-title":"Metab Brain Dis"},{"key":"5357_CR106","doi-asserted-by":"publisher","first-page":"2938","DOI":"10.1177\/0271678X16679671","volume":"37","author":"Y He","year":"2017","unstructured":"He Y, Ma X, Li D et al (2017) Thiamet G mediates neuroprotection in experimental stroke by modulating microglia\/macrophage polarization and inhibiting NF-\u03baB p65 signaling. J Cereb Blood Flow Metab 37:2938\u20132951","journal-title":"J Cereb Blood Flow Metab"},{"key":"5357_CR107","doi-asserted-by":"publisher","first-page":"299","DOI":"10.1007\/s12017-021-08688-6","volume":"24","author":"J Zhao","year":"2022","unstructured":"Zhao J, Dong L, Huo T et al (2022) O-GlcNAc transferase (OGT) protects cerebral neurons from death during ischemia\/reperfusion (I\/R) injury by modulating Drp1 in mice. Neuromolecular Med 24:299\u2013310","journal-title":"Neuromolecular Med"},{"key":"5357_CR108","doi-asserted-by":"publisher","first-page":"14500","DOI":"10.1038\/srep14500","volume":"5","author":"J Shi","year":"2015","unstructured":"Shi J, Gu JH, Dai CL et al (2015) O-GlcNAcylation regulates ischemia-induced neuronal apoptosis through AKT signaling. Sci Rep 5:14500","journal-title":"Sci Rep"},{"key":"5357_CR109","doi-asserted-by":"publisher","first-page":"1465","DOI":"10.1007\/s10571-017-0477-1","volume":"37","author":"R Chen","year":"2017","unstructured":"Chen R, Gong P, Tao T et al (2017) O-GlcNAc glycosylation of nNOS promotes neuronal apoptosis following glutamate excitotoxicity cell. Mol Neurobiol 37:1465\u20131475. https:\/\/doi.org\/10.1007\/s10571-017-0477-1","journal-title":"Mol Neurobiol"},{"key":"5357_CR110","doi-asserted-by":"publisher","first-page":"1404","DOI":"10.1016\/j.cmet.2021.05.003","volume":"33","author":"RC Sun","year":"2021","unstructured":"Sun RC, Young LEA, Bruntz RC et al (2021) Brain glycogen serves as a critical glucosamine cache required for protein glycosylation. Cell Metab 33:1404-1417.e9. https:\/\/doi.org\/10.1016\/j.cmet.2021.05.003","journal-title":"Cell Metab"},{"key":"5357_CR111","doi-asserted-by":"publisher","DOI":"10.1016\/j.redox.2024.103234","volume":"74","author":"H Guo","year":"2024","unstructured":"Guo H, Li Y, Wang S et al (2024) Dysfunction of astrocytic glycophagy exacerbates reperfusion injury in ischemic stroke. Redox Biol 74:103234","journal-title":"Redox Biol"},{"key":"5357_CR112","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2025813118","author":"C Larochelle","year":"2021","unstructured":"Larochelle C, Wasser B, Jamann H et al (2021) Pro-inflammatory T helper 17 directly harms oligodendrocytes in neuroinflammation. Proc Natl Acad Sci U S A. https:\/\/doi.org\/10.1073\/pnas.2025813118","journal-title":"Proc Natl Acad Sci U S A"},{"key":"5357_CR113","doi-asserted-by":"publisher","first-page":"2626","DOI":"10.4049\/jimmunol.1601727","volume":"198","author":"R Liu","year":"2017","unstructured":"Liu R, Ma X, Chen L et al (2017) MicroRNA-15b suppresses Th17 differentiation and is associated with pathogenesis of multiple sclerosis by targeting o-GlcNAc transferase. J Immunol 198:2626\u20132639","journal-title":"J Immunol"},{"issue":"36","key":"5357_CR114","first-page":"45","volume":"9","author":"DR Tomlinson","year":"2008","unstructured":"Tomlinson DR, Gardiner NJ (2008) Glucose neurotoxicity. Nat Rev Neurosci 9(36):45","journal-title":"Nat Rev Neurosci"},{"key":"5357_CR115","doi-asserted-by":"publisher","first-page":"2125","DOI":"10.1523\/jneurosci.3384-16.2017","volume":"37","author":"C Su","year":"2017","unstructured":"Su C, Schwarz TL (2017) O-GlcNAc transferase is essential for sensory neuron survival and maintenance. J Neurosci 37:2125\u20132136. https:\/\/doi.org\/10.1523\/jneurosci.3384-16.2017","journal-title":"J Neurosci"},{"key":"5357_CR116","doi-asserted-by":"publisher","first-page":"9633","DOI":"10.1523\/JNEUROSCI.1235-16.2016","volume":"36","author":"S Kim","year":"2016","unstructured":"Kim S, Maynard JC, Sasaki Y et al (2016) Schwann cell O-GlcNAc glycosylation is required for myelin maintenance and axon integrity. J Neurosci 36:9633\u20139646. https:\/\/doi.org\/10.1523\/JNEUROSCI.1235-16.2016","journal-title":"J Neurosci"},{"key":"5357_CR117","doi-asserted-by":"publisher","first-page":"8019","DOI":"10.1073\/pnas.1805538115","volume":"115","author":"S Kim","year":"2018","unstructured":"Kim S, Maynard JC, Strickland A et al (2018) Schwann cell O-GlcNAcylation promotes peripheral nerve remyelination via attenuation of the AP-1 transcription factor JUN. Proc Natl Acad Sci U S A 115:8019\u20138024. https:\/\/doi.org\/10.1073\/pnas.1805538115","journal-title":"Proc Natl Acad Sci U S A"},{"key":"5357_CR118","doi-asserted-by":"publisher","first-page":"1332","DOI":"10.1038\/s41593-018-0235-9","volume":"21","author":"C Soto","year":"2018","unstructured":"Soto C, Pritzkow S (2018) Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat Neurosci 21:1332\u20131340. https:\/\/doi.org\/10.1038\/s41593-018-0235-9","journal-title":"Nat Neurosci"},{"key":"5357_CR119","doi-asserted-by":"publisher","DOI":"10.1186\/1750-1326-9-42","volume":"9","author":"SA Yuzwa","year":"2014","unstructured":"Yuzwa SA, Shan X, Jones BA et al (2014) Pharmacological inhibition of O-GlcNAcase (OGA) prevents cognitive decline and amyloid plaque formation in bigenic tau\/APP mutant mice. Mol Neurodegener 9:42","journal-title":"Mol Neurodegener"},{"key":"5357_CR120","doi-asserted-by":"publisher","first-page":"393","DOI":"10.1038\/nchembio.797","volume":"8","author":"SA Yuzwa","year":"2012","unstructured":"Yuzwa SA, Shan X, Macauley MS et al (2012) Increasing O-GlcNAc slows neurodegeneration and stabilizes tau against aggregation. Nat Chem Biol 8:393\u2013399","journal-title":"Nat Chem Biol"},{"key":"5357_CR121","doi-asserted-by":"publisher","first-page":"10804","DOI":"10.1073\/pnas.0400348101","volume":"101","author":"F Liu","year":"2004","unstructured":"Liu F, Iqbal K, Grundke-Iqbal I et al (2004) O-GlcNAcylation regulates phosphorylation of tau: a mechanism involved in Alzheimer\u2019s disease. Proc Natl Acad Sci U S A 101:10804\u201310809. https:\/\/doi.org\/10.1073\/pnas.0400348101","journal-title":"Proc Natl Acad Sci U S A"},{"key":"5357_CR122","doi-asserted-by":"publisher","first-page":"424","DOI":"10.1006\/bbrc.1995.2149","volume":"213","author":"LS Griffith","year":"1995","unstructured":"Griffith LS, Schmitz B (1995) O-linked N-acetylglucosamine is upregulated in Alzheimer brains. Biochem Biophys Res Commun 213:424\u2013431. https:\/\/doi.org\/10.1006\/bbrc.1995.2149","journal-title":"Biochem Biophys Res Commun"},{"key":"5357_CR123","doi-asserted-by":"publisher","first-page":"359","DOI":"10.1016\/j.febslet.2007.12.035","volume":"582","author":"Y Liu","year":"2008","unstructured":"Liu Y, Liu F, Iqbal K et al (2008) Decreased glucose transporters correlate to abnormal hyperphosphorylation of tau in Alzheimer disease. FEBS Lett 582:359\u2013364. https:\/\/doi.org\/10.1016\/j.febslet.2007.12.035","journal-title":"FEBS Lett"},{"key":"5357_CR124","doi-asserted-by":"publisher","first-page":"1737","DOI":"10.3233\/jad-171047","volume":"62","author":"J Gu","year":"2018","unstructured":"Gu J, Jin N, Ma D et al (2018) Calpain I activation causes GLUT3 proteolysis and downregulation of O-GlcNAcylation in Alzheimer\u2019s disease brain. J Alzheimers Dis 62:1737\u20131746. https:\/\/doi.org\/10.3233\/jad-171047","journal-title":"J Alzheimers Dis"},{"key":"5357_CR125","doi-asserted-by":"publisher","first-page":"1820","DOI":"10.1093\/brain\/awp099","volume":"132","author":"F Liu","year":"2009","unstructured":"Liu F, Shi J, Tanimukai H et al (2009) Reduced O-GlcNAcylation links lower brain glucose metabolism and tau pathology in Alzheimer\u2019s disease. Brain 132:1820\u20131832","journal-title":"Brain"},{"key":"5357_CR126","doi-asserted-by":"publisher","DOI":"10.1186\/s13024-017-0181-0","volume":"12","author":"NB Hastings","year":"2017","unstructured":"Hastings NB, Wang X, Song L et al (2017) Inhibition of O-GlcNAcase leads to elevation of O-GlcNAc tau and reduction of tauopathy and cerebrospinal fluid tau in rTg4510 mice. Mol Neurodegener 12:39","journal-title":"Mol Neurodegener"},{"key":"5357_CR127","doi-asserted-by":"crossref","unstructured":"Rani L, Mittal J, Mallajosyula SS\u00a0 (2020) Effect of phosphorylation and O-GlcNAcylation on proline-rich domains of tau. J Phys Chem B 124:1909","DOI":"10.1021\/acs.jpcb.9b11720"},{"key":"5357_CR128","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0035277","author":"Y Yu","year":"2012","unstructured":"Yu Y, Zhang L, Li X et al (2012) Differential effects of an O-GlcNAcase inhibitor on tau phosphorylation. PLoS ONE. https:\/\/doi.org\/10.1371\/journal.pone.0035277","journal-title":"PLoS ONE"},{"key":"5357_CR129","doi-asserted-by":"publisher","first-page":"186","DOI":"10.1016\/j.phrs.2016.01.006","volume":"105","author":"E Gatta","year":"2016","unstructured":"Gatta E, Lefebvre T, Gaetani S et al (2016) Evidence for an imbalance between tau O-GlcNAcylation and phosphorylation in the hippocampus of a mouse model of Alzheimer\u2019s disease. Pharmacol Res 105:186\u2013197. https:\/\/doi.org\/10.1016\/j.phrs.2016.01.006","journal-title":"Pharmacol Res"},{"key":"5357_CR130","doi-asserted-by":"publisher","first-page":"76","DOI":"10.1016\/j.brainresbull.2020.01.006","volume":"156","author":"R Huang","year":"2020","unstructured":"Huang R, Tian S, Zhang H et al (2020) Chronic hyperglycemia induces tau hyperphosphorylation by downregulating OGT-involved O-GlcNAcylation in vivo and in vitro. Brain Res Bull 156:76\u201385. https:\/\/doi.org\/10.1016\/j.brainresbull.2020.01.006","journal-title":"Brain Res Bull"},{"key":"5357_CR131","doi-asserted-by":"publisher","first-page":"18","DOI":"10.1016\/j.npep.2017.04.001","volume":"63","author":"L Lozano","year":"2017","unstructured":"Lozano L, Guevara J, Lefebvre T et al (2017) Effect of amyloid-\u0392 (25\u201335) in hyperglycemic and hyperinsulinemic rats, effects on phosphorylation and O-GlcNAcylation of tau protein. Neuropeptides 63:18\u201327. https:\/\/doi.org\/10.1016\/j.npep.2017.04.001","journal-title":"Neuropeptides"},{"key":"5357_CR132","doi-asserted-by":"publisher","first-page":"661368","DOI":"10.3389\/fnmol.2021.661368","volume":"14","author":"FX Cantrelle","year":"2021","unstructured":"Cantrelle FX, Loyens A, Trivelli X et al (2021) Phosphorylation and O-GlcNAcylation of the PHF-1 epitope of tau protein induce local conformational changes of the C-terminus and modulate tau self-assembly into fibrillar aggregates. Front Mol Neurosci 14:661368","journal-title":"Front Mol Neurosci"},{"key":"5357_CR133","doi-asserted-by":"publisher","first-page":"455","DOI":"10.1111\/acel.12449","volume":"15","author":"S Xie","year":"2016","unstructured":"Xie S, Jin N, Gu J et al (2016) O-GlcNAcylation of protein kinase A catalytic subunits enhances its activity: a mechanism linked to learning and memory deficits in Alzheimer\u2019s disease. Aging Cell 15:455\u2013464","journal-title":"Aging Cell"},{"key":"5357_CR134","doi-asserted-by":"publisher","DOI":"10.1177\/0271678X211027381","volume":"41","author":"J Park","year":"2021","unstructured":"Park J, Jung S, Kim SM et al (2021) Repeated hypoxia exposure induces cognitive dysfunction, brain inflammation, and amyloid\u03b2\/p-tau accumulation through reduced brain O-GlcNAcylation in zebrafish. J Cereb Blood Flow Metab 41:3111","journal-title":"J Cereb Blood Flow Metab"},{"key":"5357_CR135","doi-asserted-by":"publisher","first-page":"15120","DOI":"10.1073\/pnas.1606899113","volume":"113","author":"AC Wang","year":"2016","unstructured":"Wang AC, Jensen EH, Rexach JE et al (2016) Loss of O-GlcNAc glycosylation in forebrain excitatory neurons induces neurodegeneration. Proc Natl Acad Sci U S A 113:15120\u201315125","journal-title":"Proc Natl Acad Sci U S A"},{"key":"5357_CR136","doi-asserted-by":"publisher","first-page":"1366","DOI":"10.1021\/acschemneuro.8b00015","volume":"9","author":"Y Zhu","year":"2018","unstructured":"Zhu Y, Shan X, Safarpour F et al (2018) Pharmacological inhibition of O-GlcNAcase enhances autophagy in brain through an mTOR-independent pathway ACS. Chem Neurosci 9:1366\u20131379","journal-title":"Chem Neurosci"},{"issue":"273","key":"5357_CR137","first-page":"286","volume":"81","author":"D Pan","year":"2021","unstructured":"Pan D, Gu JH, Zhang J et al (2021) Thiamme2-G, a novel O-GlcNAcase inhibitor, reduces tau hyperphosphorylation and rescues cognitive impairment in mice. J Alzheimers Dis 81(273):286","journal-title":"J Alzheimers Dis"},{"key":"5357_CR138","doi-asserted-by":"publisher","first-page":"e1601576","DOI":"10.1126\/sciadv.1601576","volume":"3","author":"M Frenkel-Pinter","year":"2017","unstructured":"Frenkel-Pinter M, Shmueli MD, Raz C et al (2017) Interplay between protein glycosylation pathways in Alzheimer\u2019s disease. Sci Adv 3:e1601576. https:\/\/doi.org\/10.1126\/sciadv.1601576","journal-title":"Sci Adv"},{"key":"5357_CR139","doi-asserted-by":"publisher","first-page":"1015","DOI":"10.1111\/j.1471-4159.2005.03243.x","volume":"94","author":"RW Collin","year":"2005","unstructured":"Collin RW, Van Den Hurk WH, Martens GJ (2005) Biosynthesis and differential processing of two pools of amyloid-beta precursor protein in a physiologically inducible neuroendocrine cell. J Neurochem 94:1015\u20131024. https:\/\/doi.org\/10.1111\/j.1471-4159.2005.03243.x","journal-title":"J Neurochem"},{"issue":"1","key":"5357_CR140","doi-asserted-by":"publisher","first-page":"17","DOI":"10.3233\/JAD-201027","volume":"81","author":"A Miranda","year":"2021","unstructured":"Miranda A, Montiel E, Ulrich H et al (2021) Selective secretase targeting for Alzheimer\u2019s disease therapy. J Alzheimers Dis 81(1):17","journal-title":"J Alzheimers Dis"},{"key":"5357_CR141","doi-asserted-by":"publisher","first-page":"109886","DOI":"10.1016\/j.cbi.2022.109886","volume":"357","author":"N Zhang","year":"2022","unstructured":"Zhang N, Jiang H, Zhang K et al (2022) OGT as potential novel target: structure, function and inhibitors. Chem Biol Interact 357:109886","journal-title":"Chem Biol Interact"},{"key":"5357_CR142","doi-asserted-by":"publisher","first-page":"2115","DOI":"10.1021\/acschemneuro.8b00574","volume":"10","author":"PF Tao","year":"2019","unstructured":"Tao PF, Huang HC (2019) Regulation of A\u03b2PP glycosylation modification and roles of glycosylation on A\u03b2PP cleavage in Alzheimer\u2019s disease ACS. Chem Neurosci 10:2115\u20132124","journal-title":"Chem Neurosci"},{"key":"5357_CR143","doi-asserted-by":"publisher","first-page":"1195","DOI":"10.3233\/jad-190060","volume":"69","author":"OH Kwon","year":"2019","unstructured":"Kwon OH, Cho YY, Kim TW et al (2019) O-GlcNAcylation of amyloid-\u03b2 protein precursor by insulin signaling reduces amyloid-\u03b2 production. J Alzheimers Dis 69:1195\u20131211. https:\/\/doi.org\/10.3233\/jad-190060","journal-title":"J Alzheimers Dis"},{"key":"5357_CR144","doi-asserted-by":"publisher","first-page":"130","DOI":"10.1016\/j.neurobiolaging.2017.10.009","volume":"62","author":"T Jean-Louis","year":"2018","unstructured":"Jean-Louis T, Rockwell P, Figueiredo-Pereira ME (2018) Prostaglandin J2 promotes O-GlcNAcylation raising APP processing by \u03b1- and \u03b2-secretases: relevance to Alzheimer\u2019s disease. Neurobiol Aging 62:130\u2013145. https:\/\/doi.org\/10.1016\/j.neurobiolaging.2017.10.009","journal-title":"Neurobiol Aging"},{"key":"5357_CR145","doi-asserted-by":"publisher","first-page":"261","DOI":"10.3233\/jad-140096","volume":"44","author":"YS Chun","year":"2015","unstructured":"Chun YS, Park Y, Oh HG et al (2015) O-GlcNAcylation promotes non-amyloidogenic processing of amyloid-\u03b2 protein precursor via inhibition of endocytosis from the plasma membrane. J Alzheimers Dis 44:261\u2013275. https:\/\/doi.org\/10.3233\/jad-140096","journal-title":"J Alzheimers Dis"},{"key":"5357_CR146","doi-asserted-by":"publisher","DOI":"10.1126\/sciadv.abd3207","author":"J Park","year":"2021","unstructured":"Park J, Ha HJ, Chung ES et al (2021) O-GlcNAcylation ameliorates the pathological manifestations of Alzheimer\u2019s disease by inhibiting necroptosis. Sci Adv. https:\/\/doi.org\/10.1126\/sciadv.abd3207","journal-title":"Sci Adv"},{"key":"5357_CR147","doi-asserted-by":"publisher","first-page":"146","DOI":"10.1186\/s12974-023-02824-8","volume":"20","author":"X Dong","year":"2023","unstructured":"Dong X, Shu L, Zhang J et al (2023) Ogt-mediated O-GlcNAcylation inhibits astrocytes activation through modulating NF-\u03baB signaling pathway. J Neuroinflammation 20:146","journal-title":"J Neuroinflammation"},{"key":"5357_CR148","doi-asserted-by":"publisher","DOI":"10.1016\/j.jbc.2024.105677","author":"J Zhang","year":"2024","unstructured":"Zhang J, Wang Y (2024) Emerging roles of O-GlcNAcylation in protein trafficking and secretion. J Biol Chem. https:\/\/doi.org\/10.1016\/j.jbc.2024.105677","journal-title":"J Biol Chem"},{"key":"5357_CR149","doi-asserted-by":"publisher","first-page":"171","DOI":"10.1007\/s12017-019-08584-0","volume":"22","author":"J Park","year":"2020","unstructured":"Park J, Lai MKP, Arumugam TV et al (2020) O-GlcNAcylation as a therapeutic target for Alzheimer\u2019s disease. Neuromolecular Med 22:171\u2013193","journal-title":"Neuromolecular Med"},{"key":"5357_CR150","doi-asserted-by":"publisher","first-page":"441","DOI":"10.1038\/s41557-021-00648-8","volume":"13","author":"AT Balana","year":"2021","unstructured":"Balana AT, Levine PM, Craven TW et al (2021) O-GlcNAc modification of small heat shock proteins enhances their anti-amyloid chaperone activity. Nat Chem 13:441\u2013450","journal-title":"Nat Chem"},{"key":"5357_CR151","doi-asserted-by":"publisher","DOI":"10.1111\/acel.12872","author":"H Choi","year":"2019","unstructured":"Choi H, Kim C, Song H et al (2019) Amyloid \u03b2-induced elevation of O-GlcNAcylated c-Fos promotes neuronal cell death. Aging Cell. https:\/\/doi.org\/10.1111\/acel.12872","journal-title":"Aging Cell"},{"key":"5357_CR152","doi-asserted-by":"publisher","first-page":"6","DOI":"10.1186\/s13041-020-00727-w","volume":"14","author":"SJ Park","year":"2021","unstructured":"Park SJ, Bae JE, Jo DS et al (2021) Increased O-GlcNAcylation of Drp1 by amyloid-beta promotes mitochondrial fission and dysfunction in neuronal cells. Mol Brain 14:6","journal-title":"Mol Brain"},{"key":"5357_CR153","doi-asserted-by":"publisher","DOI":"10.1016\/j.nbd.2024.106702","volume":"202","author":"W Zhou","year":"2024","unstructured":"Zhou W, Daniels S, Singh V et al (2024) \u03b1-Synuclein aggregation decreases cortico-amygdala connectivity and impairs social behavior in mice. Neurobiol Dis 202:106702. https:\/\/doi.org\/10.1016\/j.nbd.2024.106702","journal-title":"Neurobiol Dis"},{"key":"5357_CR154","doi-asserted-by":"publisher","first-page":"646","DOI":"10.1038\/s41589-024-01551-2","volume":"20","author":"AT Balana","year":"2024","unstructured":"Balana AT, Mahul-Mellier AL, Nguyen BA et al (2024) O-GlcNAc forces an \u03b1-synuclein amyloid strain with notably diminished seeding and pathology. Nat Chem Biol 20:646\u2013655. https:\/\/doi.org\/10.1038\/s41589-024-01551-2","journal-title":"Nat Chem Biol"},{"key":"5357_CR155","doi-asserted-by":"publisher","first-page":"3044","DOI":"10.1021\/acschemneuro.4c00301","volume":"15","author":"K Gamage","year":"2024","unstructured":"Gamage K, Wang B, Hard ER et al (2024) O-GlcNAc modification of \u03b1-synuclein can alter monomer dynamics to control aggregation kinetics. ACS Chem Neurosci 15:3044\u20133052","journal-title":"ACS Chem Neurosci"},{"key":"5357_CR156","doi-asserted-by":"publisher","first-page":"4977","DOI":"10.1016\/j.bmc.2017.04.038","volume":"25","author":"PM Levine","year":"2017","unstructured":"Levine PM, De Leon CA, Galesic A et al (2017) O-GlcNAc modification inhibits the calpain-mediated cleavage of \u03b1-synuclein. Bioorg Med Chem 25:4977\u20134982","journal-title":"Bioorg Med Chem"},{"key":"5357_CR157","doi-asserted-by":"crossref","unstructured":"Hu J, Xia W, Zeng\u00a0S  et al (2024) Phosphorylation and O-GlcNAcylation at the same \u03b1-synuclein site generate distinct fibril structures. Nat Commun 15:2677","DOI":"10.1038\/s41467-024-46898-1"},{"key":"5357_CR158","first-page":"1020","volume":"12","author":"YE Lewis","year":"2017","unstructured":"Lewis YE, Galesic A, Levine PM et al (2017) O-GlcNAcylation of \u03b1-synuclein at serine 87 reduces aggregation without affecting membrane binding ACS. Chem Biol 12:1020\u20131027","journal-title":"Chem Biol"},{"key":"5357_CR159","doi-asserted-by":"publisher","first-page":"90","DOI":"10.1016\/j.neulet.2017.06.034","volume":"655","author":"J Zhang","year":"2017","unstructured":"Zhang J, Lei H, Chen Y et al (2017) Enzymatic O-GlcNAcylation of \u03b1-synuclein reduces aggregation and increases SDS-resistant soluble oligomers. Neurosci Lett 655:90\u201394. https:\/\/doi.org\/10.1016\/j.neulet.2017.06.034","journal-title":"Neurosci Lett"},{"key":"5357_CR160","doi-asserted-by":"publisher","DOI":"10.3389\/fnagi.2021.690293","volume":"13","author":"NO Manzanza","year":"2021","unstructured":"Manzanza NO, Sedlackova L, Kalaria RN (2021) Alpha-synuclein post-translational modifications: implications for pathogenesis of Lewy body disorders. Front Aging Neurosci 13:690293","journal-title":"Front Aging Neurosci"},{"key":"5357_CR161","doi-asserted-by":"publisher","DOI":"10.1016\/j.bioorg.2019.103389","volume":"94","author":"P Ryan","year":"2020","unstructured":"Ryan P, Xu MM, Davey AK et al (2020) O-GlcNAcylation of truncated NAC segment alters peptide-dependent effects on \u03b1-synuclein aggregation. Bioorg Chem 94:103389. https:\/\/doi.org\/10.1016\/j.bioorg.2019.103389","journal-title":"Bioorg Chem"},{"key":"5357_CR162","doi-asserted-by":"publisher","first-page":"1511","DOI":"10.1073\/pnas.1808845116","volume":"116","author":"PM Levine","year":"2019","unstructured":"Levine PM, Galesic A, Balana AT et al (2019) \u03b1-Synuclein O-GlcNAcylation alters aggregation and toxicity, revealing certain residues as potential inhibitors of Parkinson\u2019s disease. Proc Natl Acad Sci U S A 116:1511\u20131519","journal-title":"Proc Natl Acad Sci U S A"},{"key":"5357_CR163","doi-asserted-by":"publisher","first-page":"1399","DOI":"10.1093\/brain\/awx056","volume":"140","author":"H Vicente Miranda","year":"2017","unstructured":"Vicente Miranda H, Szego \u00c9M, Oliveira LMA et al (2017) Glycation potentiates \u03b1-synuclein-associated neurodegeneration in synucleinopathies. Brain 140:1399\u20131419. https:\/\/doi.org\/10.1093\/brain\/awx056","journal-title":"Brain"},{"key":"5357_CR164","doi-asserted-by":"publisher","first-page":"32","DOI":"10.1186\/s13041-017-0311-1","volume":"10","author":"WY Wani","year":"2017","unstructured":"Wani WY, Ouyang X, Benavides GA et al (2017) O-GlcNAc regulation of autophagy and \u03b1-synuclein homeostasis; implications for Parkinson\u2019s disease. Mol Brain 10:32","journal-title":"Mol Brain"},{"key":"5357_CR165","doi-asserted-by":"publisher","first-page":"452","DOI":"10.1111\/febs.15349","volume":"288","author":"O Tavassoly","year":"2021","unstructured":"Tavassoly O, Yue J, Vocadlo DJ (2021) Pharmacological inhibition and knockdown of O-GlcNAcase reduces cellular internalization of \u03b1-synuclein preformed fibrils. FEBS J 288:452\u2013470. https:\/\/doi.org\/10.1111\/febs.15349","journal-title":"FEBS J"},{"key":"5357_CR166","doi-asserted-by":"publisher","DOI":"10.1016\/j.neuint.2022.105461","volume":"162","author":"P Sivakumar","year":"2023","unstructured":"Sivakumar P, Nagashanmugam KB, Priyatharshni S et al (2023) Review on the interactions between dopamine metabolites and \u03b1-Synuclein in causing Parkinson\u2019s disease. Neurochem Int 162:105461","journal-title":"Neurochem Int"},{"key":"5357_CR167","doi-asserted-by":"publisher","first-page":"3699","DOI":"10.1093\/brain\/awaa320","volume":"143","author":"BE Lee","year":"2020","unstructured":"Lee BE, Kim HY, Kim HJ et al (2020) O-GlcNAcylation regulates dopamine neuron function, survival and degeneration in Parkinson disease. Brain 143:3699\u20133716","journal-title":"Brain"},{"key":"5357_CR168","doi-asserted-by":"publisher","DOI":"10.3390\/brainsci10120958","author":"MA Rahman","year":"2020","unstructured":"Rahman MA, Cho Y, Hwang H et al (2020) Pharmacological inhibition of O-GlcNAc transferase promotes mTOR-dependent autophagy in rat cortical neurons. Brain Sci. https:\/\/doi.org\/10.3390\/brainsci10120958","journal-title":"Brain Sci"},{"key":"5357_CR169","doi-asserted-by":"publisher","DOI":"10.3390\/cells7060059","author":"BL Tang","year":"2018","unstructured":"Tang BL (2018) Unconventional secretion and intercellular transfer of mutant huntingtin. Cells. https:\/\/doi.org\/10.3390\/cells7060059","journal-title":"Cells"},{"key":"5357_CR170","doi-asserted-by":"publisher","DOI":"10.1016\/j.jbc.2022.102219","volume":"298","author":"E Ahat","year":"2022","unstructured":"Ahat E, Bui S, Zhang J et al (2022) GRASP55 regulates the unconventional secretion and aggregation of mutant huntingtin. J Biol Chem 298:102219. https:\/\/doi.org\/10.1016\/j.jbc.2022.102219","journal-title":"J Biol Chem"},{"key":"5357_CR171","doi-asserted-by":"publisher","first-page":"245","DOI":"10.1016\/j.devcel.2018.03.023","volume":"45","author":"X Zhang","year":"2018","unstructured":"Zhang X, Wang L, Lak B et al (2018) GRASP55 senses glucose deprivation through O-GlcNAcylation to promote autophagosome-lysosome fusion. Dev Cell 45:245-261.e6","journal-title":"Dev Cell"},{"key":"5357_CR172","doi-asserted-by":"publisher","first-page":"93","DOI":"10.1016\/j.neuron.2017.03.023","volume":"94","author":"JC Grima","year":"2017","unstructured":"Grima JC, Daigle JG, Arbez N et al (2017) Mutant huntingtin disrupts the nuclear pore complex. Neuron 94:93-107.e6. https:\/\/doi.org\/10.1016\/j.neuron.2017.03.023","journal-title":"Neuron"},{"key":"5357_CR173","doi-asserted-by":"publisher","first-page":"1537","DOI":"10.1016\/j.str.2016.07.007","volume":"24","author":"AE Conicella","year":"2016","unstructured":"Conicella AE, Zerze GH, Mittal J et al (2016) ALS mutations disrupt phase separation mediated by \u03b1-helical structure in the TDP-43 low-complexity C-terminal domain. Structure 24:1537\u20131549","journal-title":"Structure"},{"key":"5357_CR174","doi-asserted-by":"publisher","DOI":"10.15252\/embj.2021108443","volume":"41","author":"LA Gruijs Da Silva","year":"2022","unstructured":"Gruijs Da Silva LA, Simonetti F, Hutten S et al (2022) Disease-linked TDP-43 hyperphosphorylation suppresses TDP-43 condensation and aggregation. EMBO J 41:e108443","journal-title":"EMBO J"},{"key":"5357_CR175","doi-asserted-by":"publisher","first-page":"82","DOI":"10.1186\/s10020-025-01134-4","volume":"31","author":"Y Hao","year":"2025","unstructured":"Hao Y, Li Z, Du X et al (2025) Characterization and chemoproteomic profiling of protein O-GlcNAcylation in SOD1-G93A mouse model. Mol Med 31:82","journal-title":"Mol Med"},{"key":"5357_CR176","doi-asserted-by":"publisher","DOI":"10.15252\/embr.202051649","volume":"22","author":"MJ Zhao","year":"2021","unstructured":"Zhao MJ, Yao X, Wei P et al (2021) O-GlcNAcylation of TDP-43 suppresses proteinopathies and promotes TDP-43\u2019s mRNA splicing activity. EMBO Rep 22:e51649. https:\/\/doi.org\/10.15252\/embr.202051649","journal-title":"EMBO Rep"},{"key":"5357_CR177","doi-asserted-by":"publisher","first-page":"2134","DOI":"10.1016\/j.celrep.2019.10.053","volume":"29","author":"YL Hsieh","year":"2019","unstructured":"Hsieh YL, Su FY, Tsai LK et al (2019) NPGPx-mediated adaptation to oxidative stress protects motor neurons from degeneration in aging by directly modulating O-GlcNAcase. Cell Rep 29:2134-2143.e7. https:\/\/doi.org\/10.1016\/j.celrep.2019.10.053","journal-title":"Cell Rep"},{"key":"5357_CR178","doi-asserted-by":"publisher","first-page":"138","DOI":"10.1096\/fj.07-8309com","volume":"22","author":"Y Deng","year":"2008","unstructured":"Deng Y, Li B, Liu F et al (2008) Regulation between O-GlcNAcylation and phosphorylation of neurofilament-M and their dysregulation in Alzheimer disease. FASEB J 22:138\u2013145","journal-title":"FASEB J"},{"key":"5357_CR179","doi-asserted-by":"publisher","first-page":"2928","DOI":"10.1093\/brain\/awac498","volume":"146","author":"MD Wheelock","year":"2023","unstructured":"Wheelock MD, Strain JF, Mansfield P et al (2023) Brain network decoupling with increased serum neurofilament and reduced cognitive function in Alzheimer\u2019s disease. Brain 146:2928\u20132943","journal-title":"Brain"},{"key":"5357_CR180","doi-asserted-by":"publisher","unstructured":"Uzunk\u00f6pr\u00fc C, Y\u00fcceyar N, Yilmaz SG, et al (2021) Retinal nerve fiber layer thickness correlates with serum and cerebrospinal fluid neurofilament levels and is associated with current disability in multiple sclerosis. Noro Psikiyatr Ars 58:34\u201340. https:\/\/doi.org\/10.29399\/npa.27355","DOI":"10.29399\/npa.27355"},{"key":"5357_CR181","doi-asserted-by":"publisher","first-page":"4562","DOI":"10.1093\/brain\/awad234","volume":"146","author":"S Keddie","year":"2023","unstructured":"Keddie S, Smyth D, Keh RYS et al (2023) Peripherin is a biomarker of axonal damage in peripheral nervous system disease. Brain 146:4562\u20134573","journal-title":"Brain"},{"key":"5357_CR182","doi-asserted-by":"publisher","first-page":"1682","DOI":"10.1177\/1352458519882279","volume":"26","author":"G Bsteh","year":"2020","unstructured":"Bsteh G, Berek K, Hegen H et al (2020) Serum neurofilament levels correlate with retinal nerve fiber layer thinning in multiple sclerosis. Mult Scler 26:1682\u20131690. https:\/\/doi.org\/10.1177\/1352458519882279","journal-title":"Mult Scler"},{"key":"5357_CR183","doi-asserted-by":"publisher","first-page":"97","DOI":"10.1016\/j.neulet.2018.11.001","volume":"698","author":"P Peng","year":"2019","unstructured":"Peng P, Wang J, Ding N et al (2019) Alteration of O-GlcNAcylation affects assembly and axonal transport of neurofilament via phosphorylation. Neurosci Lett 698:97\u2013104. https:\/\/doi.org\/10.1016\/j.neulet.2018.11.001","journal-title":"Neurosci Lett"},{"key":"5357_CR184","doi-asserted-by":"publisher","first-page":"6558","DOI":"10.1038\/s41467-023-42227-0","volume":"14","author":"DT Huynh","year":"2023","unstructured":"Huynh DT, Tsolova KN, Watson AJ et al (2023) O-GlcNAcylation regulates neurofilament-light assembly and function and is perturbed by Charcot-Marie-Tooth disease mutations. Nat Commun 14:6558. https:\/\/doi.org\/10.1038\/s41467-023-42227-0","journal-title":"Nat Commun"},{"key":"5357_CR185","doi-asserted-by":"publisher","DOI":"10.1111\/jne.12659","volume":"31","author":"I Kolbe","year":"2019","unstructured":"Kolbe I, Brehm N, Oster H (2019) Interplay of central and peripheral circadian clocks in energy metabolism regulation. J Neuroendocrinol 31:e12659","journal-title":"J Neuroendocrinol"},{"key":"5357_CR186","doi-asserted-by":"publisher","first-page":"245","DOI":"10.1002\/iub.2587","volume":"74","author":"Q Cheng","year":"2022","unstructured":"Cheng Q, Fan X, Liu Y et al (2022) miR-455-5p regulates circadian rhythms by accelerating the degradation of Clock mRNA. IUBMB Life 74:245\u2013258","journal-title":"IUBMB Life"},{"key":"5357_CR187","doi-asserted-by":"publisher","first-page":"220215","DOI":"10.1098\/rsob.220215","volume":"12","author":"X Liu","year":"2022","unstructured":"Liu X, Chiu JC (2022) Nutrient-sensitive protein O-GlcNAcylation shapes daily biological rhythms. Open Biol 12:220215","journal-title":"Open Biol"},{"key":"5357_CR188","doi-asserted-by":"publisher","first-page":"e1007953","DOI":"10.1371\/journal.pgen.1007953","volume":"15","author":"YH Li","year":"2019","unstructured":"Li YH, Liu X, Vanselow JT et al (2019) O-GlcNAcylation of PERIOD regulates its interaction with CLOCK and timing of circadian transcriptional repression. PLoS Genet 15:e1007953. https:\/\/doi.org\/10.1371\/journal.pgen.1007953","journal-title":"PLoS Genet"},{"key":"5357_CR189","doi-asserted-by":"publisher","DOI":"10.1111\/jpi.13001","volume":"76","author":"J Park","year":"2024","unstructured":"Park J, Kim DY, Oh ES et al (2024) Light-dependent circadian rhythm governs O-GlcNAc cycling to influence cognitive function in adult zebrafish. J Pineal Res 76:e13001","journal-title":"J Pineal Res"},{"key":"5357_CR190","doi-asserted-by":"publisher","first-page":"2504","DOI":"10.1007\/s13311-021-01094-7","volume":"18","author":"SM Kim","year":"2021","unstructured":"Kim SM, Zhang S, Park J et al (2021) REM sleep deprivation impairs learning and memory by decreasing brain O-GlcNAc cycling in mouse. Neurotherapeutics 18:2504","journal-title":"Neurotherapeutics"},{"key":"5357_CR191","doi-asserted-by":"publisher","first-page":"C978","DOI":"10.1152\/ajpcell.00691.2023","volume":"326","author":"TT Tran","year":"2024","unstructured":"Tran TT, Park J, Kim DY et al (2024) Caffeine-induced protein kinase A activation restores cognitive deficits induced by sleep deprivation by regulating O-GlcNAc cycling in adult zebrafish. Am J Physiol Cell Physiol 326:C978-c989. https:\/\/doi.org\/10.1152\/ajpcell.00691.2023","journal-title":"Am J Physiol Cell Physiol"},{"key":"5357_CR192","doi-asserted-by":"publisher","first-page":"C981","DOI":"10.1152\/ajpcell.00191.2023","volume":"325","author":"DY Kim","year":"2023","unstructured":"Kim DY, Park J, Han IO (2023) Hexosamine biosynthetic pathway and O-GlcNAc cycling of glucose metabolism in brain function and disease. Am J Physiol Cell Physiol 325:C981-c998","journal-title":"Am J Physiol Cell Physiol"},{"key":"5357_CR193","doi-asserted-by":"publisher","DOI":"10.1172\/JCI160016","author":"J Fan","year":"2023","unstructured":"Fan J, Guo F, Mo R et al (2023) O-GlcNAc transferase in astrocytes modulates depression-related stress susceptibility through glutamatergic synaptic transmission. J Clin Invest. https:\/\/doi.org\/10.1172\/JCI160016","journal-title":"J Clin Invest"},{"key":"5357_CR194","doi-asserted-by":"publisher","first-page":"729975","DOI":"10.3389\/fnmol.2021.729975","volume":"14","author":"J Fan","year":"2021","unstructured":"Fan J, Zhong QL, Mo R et al (2021) Proteomic profiling of astrocytic O-GlcNAc transferase-related proteins in the medial prefrontal cortex. Front Mol Neurosci 14:729975","journal-title":"Front Mol Neurosci"},{"key":"5357_CR195","doi-asserted-by":"publisher","first-page":"6924","DOI":"10.1038\/s41598-020-63819-6","volume":"10","author":"Y Cho","year":"2020","unstructured":"Cho Y, Hwang H, Rahman MA et al (2020) Elevated O-GlcNAcylation induces an antidepressant-like phenotype and decreased inhibitory transmission in medial prefrontal cortex. Sci Rep 10:6924","journal-title":"Sci Rep"},{"key":"5357_CR196","doi-asserted-by":"publisher","first-page":"e5917","DOI":"10.7717\/peerj.5917","volume":"6","author":"S Rehman","year":"2018","unstructured":"Rehman S, Obaid A, Naz A et al (2018) Model-based in silico analysis of the PI3K\/Akt pathway: the elucidation of cross-talk between diabetes and breast cancer. PeerJ 6:e5917","journal-title":"PeerJ"},{"key":"5357_CR197","first-page":"422","volume":"110","author":"MD Roos","year":"1998","unstructured":"Roos MD, Xie W, Su K et al (1998) Streptozotocin, an analog of N-acetylglucosamine, blocks the removal of O-GlcNAc from intracellular proteins. Proc Assoc Am Physicians 110:422\u2013432","journal-title":"Proc Assoc Am Physicians"},{"key":"5357_CR198","doi-asserted-by":"publisher","DOI":"10.3390\/molecules25153381","author":"EM Loi","year":"2020","unstructured":"Loi EM, Weiss M, Pajk S et al (2020) Intracellular hydrolysis of small-molecule O-linked N-acetylglucosamine transferase inhibitors differs among cells and is not required for its inhibition. Molecules. https:\/\/doi.org\/10.3390\/molecules25153381","journal-title":"Molecules"},{"key":"5357_CR199","doi-asserted-by":"publisher","DOI":"10.1016\/j.bioorg.2023.106726","volume":"139","author":"X Wu","year":"2023","unstructured":"Wu X, Wang M, Cao Y et al (2023) Discovery of a novel OGT inhibitor through high-throughput screening based on homogeneous time-resolved fluorescence (HTRF). Bioorg Chem 139:106726. https:\/\/doi.org\/10.1016\/j.bioorg.2023.106726","journal-title":"Bioorg Chem"},{"key":"5357_CR200","doi-asserted-by":"publisher","first-page":"1392","DOI":"10.1021\/acschembio.5b00004","volume":"10","author":"RF Ortiz-Meoz","year":"2015","unstructured":"Ortiz-Meoz RF, Jiang J, Lazarus MB et al (2015) A small molecule that inhibits OGT activity in cells. ACS Chem Biol 10:1392\u20131397. https:\/\/doi.org\/10.1021\/acschembio.5b00004","journal-title":"ACS Chem Biol"},{"key":"5357_CR201","doi-asserted-by":"publisher","first-page":"1038","DOI":"10.1016\/j.bbrc.2006.09.155","volume":"350","author":"TN Lee","year":"2006","unstructured":"Lee TN, Alborn WE, Knierman MD et al (2006) Alloxan is an inhibitor of O-GlcNAc-selective N-acetyl-beta-D-glucosaminidase. Biochem Biophys Res Commun 350:1038\u20131043. https:\/\/doi.org\/10.1016\/j.bbrc.2006.09.155","journal-title":"Biochem Biophys Res Commun"},{"key":"5357_CR202","doi-asserted-by":"publisher","first-page":"2183","DOI":"10.7150\/thno.30834","volume":"9","author":"HM Itkonen","year":"2019","unstructured":"Itkonen HM, Urbanucci A, Martin SE et al (2019) High OGT activity is essential for MYC-driven proliferation of prostate cancer cells. Theranostics 9:2183\u20132197","journal-title":"Theranostics"},{"key":"5357_CR203","doi-asserted-by":"publisher","first-page":"31","DOI":"10.1042\/0264-6021:3560031","volume":"356","author":"RJ Konrad","year":"2001","unstructured":"Konrad RJ, Mikolaenko I, Tolar JF et al (2001) The potential mechanism of the diabetogenic action of streptozotocin: inhibition of pancreatic beta-cell O-GlcNAc-selective N-acetyl-beta-D-glucosaminidase. Biochem J 356:31\u201341. https:\/\/doi.org\/10.1042\/0264-6021:3560031","journal-title":"Biochem J"},{"key":"5357_CR204","doi-asserted-by":"publisher","first-page":"25313","DOI":"10.1074\/jbc.M413819200","volume":"280","author":"MS Macauley","year":"2005","unstructured":"Macauley MS, Whitworth GE, Debowski AW et al (2005) O-GlcNAcase uses substrate-assisted catalysis: kinetic analysis and development of highly selective mechanism-inspired inhibitors. J Biol Chem 280:25313\u201325322. https:\/\/doi.org\/10.1074\/jbc.M413819200","journal-title":"J Biol Chem"},{"key":"5357_CR205","doi-asserted-by":"publisher","unstructured":"Shanmugasundaram B, Debowski A W, Dennis R J, et al (2006) Inhibition of O-GlcNAcase by a gluco-configured nagstatin and a PUGNAc-imidazole hybrid inhibitor. Chem Commun (Camb):4372\u20134. https:\/\/doi.org\/10.1039\/b612154c","DOI":"10.1039\/b612154c"},{"key":"5357_CR206","doi-asserted-by":"publisher","first-page":"949","DOI":"10.1016\/j.chembiol.2010.07.005","volume":"17","author":"MS Macauley","year":"2010","unstructured":"Macauley MS, Shan X, Yuzwa SA et al (2010) Elevation of global O-GlcNAc in rodents using a selective O-GlcNAcase inhibitor does not cause insulin resistance or perturb glucohomeostasis. Chem Biol 17:949\u2013958. https:\/\/doi.org\/10.1016\/j.chembiol.2010.07.005","journal-title":"Chem Biol"},{"issue":"8","key":"5357_CR207","doi-asserted-by":"publisher","first-page":"483","DOI":"10.1038\/nchembio.96","volume":"4","author":"SA Yuzwa","year":"2008","unstructured":"Yuzwa SA, Macauley MS, Heinonen JE et al (2008) A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo. Nat Chem Biol 4(8):483\u2013490","journal-title":"Nat Chem Biol"},{"issue":"51","key":"5357_CR208","doi-asserted-by":"publisher","first-page":"16484","DOI":"10.1021\/ja066743n","volume":"128","author":"HC Dorfmueller","year":"2006","unstructured":"Dorfmueller HC, Borodkin VS, Schimpl M et al (2006) GlcNAcstatin: a picomolar, selective O-GlcNAcase inhibitor that modulates intracellular O-glcNAcylation levels. J Am Chem Soc 128(51):16484\u201316485","journal-title":"J Am Chem Soc"},{"issue":"10062","key":"5357_CR209","first-page":"10097","volume":"62","author":"HG Selnick","year":"2019","unstructured":"Selnick HG, Hess JF, Tang C et al (2019) Discovery of MK-8719, a potent O-GlcNAcase inhibitor as a potential treatment for tauopathies. J Med Chem 62(10062):10097","journal-title":"J Med Chem"},{"key":"5357_CR210","doi-asserted-by":"publisher","DOI":"10.3390\/ijms19041160","author":"M Medina","year":"2018","unstructured":"Medina M (2018) An overview on the clinical development of tau-based therapeutics. Int J Mol Sci. https:\/\/doi.org\/10.3390\/ijms19041160","journal-title":"Int J Mol Sci"},{"key":"5357_CR211","doi-asserted-by":"crossref","unstructured":"Kielbasa\u00a0W, Goldsmith\u00a0P, Donnelly\u00a0 KB  et al (2024) Discovery and clinical translation of ceperognastat, an O-GlcNAcase (OGA) inhibitor, for the treatment of Alzheimer\u2019s disease. Alzheimer\u2019s\u00a0 Dementia: Trans Res Clin Intervent 10:e70020","DOI":"10.1002\/trc2.70020"},{"key":"5357_CR212","doi-asserted-by":"publisher","DOI":"10.3390\/ijms22147247","author":"J Riegger","year":"2021","unstructured":"Riegger J, Baumert J, Zaucke F et al (2021) The hexosamine biosynthetic pathway as a therapeutic target after cartilage trauma: modification of chondrocyte survival and metabolism by glucosamine derivatives and PUGNAc in an ex vivo model. Int J Mol Sci. https:\/\/doi.org\/10.3390\/ijms22147247","journal-title":"Int J Mol Sci"},{"key":"5357_CR213","doi-asserted-by":"publisher","DOI":"10.1016\/j.cbi.2024.111308","volume":"405","author":"Y Jia","year":"2025","unstructured":"Jia Y, Song Y, Xue H et al (2025) Sevoflurane postconditioning mitigates neuronal hypoxic-ischemic injury via regulating reactive astrocytic STAT3 protein modification. Chem Biol Interact 405:111308","journal-title":"Chem Biol Interact"},{"key":"5357_CR214","volume":"19","author":"S Zhang","year":"2024","unstructured":"Zhang S, Jiao H (2024) Kaempferol regulates apoptosis and migration of neural stem cells to attenuate cerebral infarction by O-GlcNAcylation of \u03b2-catenin open. Life Sci 19:20220829","journal-title":"Life Sci"},{"key":"5357_CR215","doi-asserted-by":"publisher","unstructured":"Luo Y, Chen P, Yang LP, et al (2023) [Quality control mechanism of mitochondria by 3,4-dihydroxybenzaldehyde through OGT-PINK1 pathway]. Zhongguo Zhong Yao Za Zhi 48:3308\u20133316. https:\/\/doi.org\/10.19540\/j.cnki.cjcmm.20221212.401","DOI":"10.19540\/j.cnki.cjcmm.20221212.401"},{"key":"5357_CR216","doi-asserted-by":"publisher","DOI":"10.3892\/mmr.2022.12896","author":"Y Luo","year":"2023","unstructured":"Luo Y, Chen P, Yang L et al (2023) Metabolomic analysis and pharmacological validation of the cerebral protective effect of 3,4\u2011dihydroxybenzaldehyde on cerebral ischemia\u2011reperfusion injury. Mol Med Rep. https:\/\/doi.org\/10.3892\/mmr.2022.12896","journal-title":"Mol Med Rep"},{"key":"5357_CR217","doi-asserted-by":"publisher","first-page":"60","DOI":"10.1016\/j.neuroscience.2018.09.006","volume":"391","author":"S Yu","year":"2018","unstructured":"Yu S, Xu H, Chi X et al (2018) 2-(4-methoxyphenyl)ethyl-2-acetamido-2-deoxy-\u03b2-d-pyranoside (a salidroside analog) confers neuroprotection with a wide therapeutic window by regulating local glucose metabolism in a rat model of cerebral ischemic injury. Neuroscience 391:60\u201372. https:\/\/doi.org\/10.1016\/j.neuroscience.2018.09.006","journal-title":"Neuroscience"},{"key":"5357_CR218","doi-asserted-by":"publisher","DOI":"10.3390\/molecules26195883","author":"H Xu","year":"2021","unstructured":"Xu H, Du M, Shen Y et al (2021) Enhancement of O-GlcNAcylation on mitochondrial proteins with 2-(4-methoxyphenyl)ethyl-2-acetamido-2-deoxy-\u03b2-d-pyranoside, contributes to the mitochondrial network, cellular bioenergetics and stress response in neuronal cells under ischemic-like conditions. Molecules. https:\/\/doi.org\/10.3390\/molecules26195883","journal-title":"Molecules"},{"key":"5357_CR219","doi-asserted-by":"publisher","first-page":"44","DOI":"10.1016\/j.neuroscience.2016.04.006","volume":"327","author":"S Yu","year":"2016","unstructured":"Yu S, Liu X, Shen Y et al (2016) Therapeutic benefits of combined treatment with tissue plasminogen activator and 2-(4-methoxyphenyl)ethyl-2-acetamido-2-deoxy-\u03b2-d-pyranoside in an animal model of ischemic stroke. Neuroscience 327:44\u201352","journal-title":"Neuroscience"},{"key":"5357_CR220","doi-asserted-by":"crossref","unstructured":"Yu\u00a0S,\u00a0 Wei\u00a0 L,\u00a0 Chi X et al (2018) 2-(4-methoxyphenyl)ethyl-2-acetamido-2-deoxy-\u03b2-D-pyranoside, an analog of salidroside, contributes to neuroprotection in cerebral ischemic injury in vitro and in vivo. NeuroReport 29: 426-431","DOI":"10.1097\/WNR.0000000000000987"},{"key":"5357_CR221","doi-asserted-by":"publisher","first-page":"177","DOI":"10.1007\/s12031-019-01347-3","volume":"69","author":"H Xu","year":"2019","unstructured":"Xu H, Gu H, Yang Y et al (2019) 2-(4-methoxyphenyl)ethyl-2-acetamido-2-deoxy-\u03b2-D-pyranoside exerts a neuroprotective effect through regulation of energy homeostasis and O-GlcNAcylation. J Mol Neurosci 69:177\u2013187","journal-title":"J Mol Neurosci"},{"key":"5357_CR222","doi-asserted-by":"publisher","DOI":"10.1016\/j.jep.2021.114562","volume":"281","author":"JJ Shi","year":"2021","unstructured":"Shi JJ, Liu HF, Hu T et al (2021) Danggui-Shaoyao-San improves cognitive impairment through inhibiting O-GlcNAc-modification of estrogen \u03b1 receptor in female db\/db mice. J Ethnopharmacol 281:114562. https:\/\/doi.org\/10.1016\/j.jep.2021.114562","journal-title":"J Ethnopharmacol"},{"key":"5357_CR223","doi-asserted-by":"publisher","first-page":"836","DOI":"10.1093\/jnen\/nlac055","volume":"81","author":"C She","year":"2022","unstructured":"She C, Zhu J, Liu A et al (2022) Dexmedetomidine inhibits NF-\u03baB-transcriptional activity in neurons undergoing ischemia-reperfusion by regulating O-GlcNAcylation of SNW1. J Neuropathol Exp Neurol 81:836\u2013849","journal-title":"J Neuropathol Exp Neurol"},{"key":"5357_CR224","doi-asserted-by":"publisher","DOI":"10.1016\/j.ejmech.2022.114444","volume":"238","author":"X Li","year":"2022","unstructured":"Li X, Han J, Bujaranipalli S et al (2022) Structure-based discovery and development of novel O-GlcNAcase inhibitors for the treatment of Alzheimer\u2019s disease. Eur J Med Chem 238:114444","journal-title":"Eur J Med Chem"},{"key":"5357_CR225","doi-asserted-by":"publisher","first-page":"1296","DOI":"10.1021\/acschemneuro.2c00057","volume":"13","author":"B Permanne","year":"2022","unstructured":"Permanne B, Sand A, Ousson S et al (2022) O-Glcnacase inhibitor ASN90 is a multimodal drug candidate for tau and \u03b1-synuclein proteinopathies ACS. Chem Neurosci 13:1296\u20131314","journal-title":"Chem Neurosci"},{"key":"5357_CR226","doi-asserted-by":"publisher","first-page":"239","DOI":"10.3233\/JAD-210643","volume":"84","author":"L Xia","year":"2021","unstructured":"Xia L, Pang Y, Li J et al (2021) Dihydroartemisinin induces O-GlcNAcylation and improves cognitive function in a mouse model of tauopathy. J Alzheimers Dis 84:239\u2013248. https:\/\/doi.org\/10.3233\/JAD-210643","journal-title":"J Alzheimers Dis"},{"key":"5357_CR227","doi-asserted-by":"publisher","unstructured":"Kim J, Kang S, Chang KA (2022) Effect of cx-DHED on abnormal glucose transporter expression induced by ad pathologies in the 5xFAD mouse model. Int J Mol Sci 23. https:\/\/doi.org\/10.3390\/ijms231810602","DOI":"10.3390\/ijms231810602"},{"key":"5357_CR228","doi-asserted-by":"publisher","first-page":"947","DOI":"10.1021\/acsmedchemlett.1c00259","volume":"12","author":"W Sabnis","year":"2021","unstructured":"Sabnis W (2021) Benzo[d]thiazol-5-yl compounds as O-GlcNAcase inhibitors for treating Alzheimer\u2019s disease. ACS Med Chem Lett 12:947\u2013948","journal-title":"ACS Med Chem Lett"},{"key":"5357_CR229","doi-asserted-by":"publisher","DOI":"10.1016\/j.bcp.2024.116032","volume":"221","author":"QTN Nguyen","year":"2024","unstructured":"Nguyen QTN, Park J, Kim DY et al (2024) Forskolin rescues hypoxia-induced cognitive dysfunction in zebrafish with potential involvement of O-GlcNAc cycling regulation. Biochem Pharmacol 221:116032","journal-title":"Biochem Pharmacol"},{"issue":"7075","key":"5357_CR230","first-page":"7091","volume":"61","author":"L Zhang","year":"2024","unstructured":"Zhang L, Bai W, Peng Y et al (2024) Role of O-GlcNAcylation in central nervous system development and injuries: a systematic review. Mol Neurobiol 61(7075):7091","journal-title":"Mol Neurobiol"},{"key":"5357_CR231","doi-asserted-by":"publisher","first-page":"107","DOI":"10.1016\/j.bbagen.2009.07.028","volume":"1800","author":"MS Macauley","year":"2010","unstructured":"Macauley MS, Vocadlo DJ (2010) Increasing O-GlcNAc levels: an overview of small-molecule inhibitors of O-GlcNAcase. Biochim Biophys Acta 1800:107\u2013121. https:\/\/doi.org\/10.1016\/j.bbagen.2009.07.028","journal-title":"Biochim Biophys Acta"},{"key":"5357_CR232","doi-asserted-by":"publisher","first-page":"1300","DOI":"10.1002\/anie.200804583","volume":"48","author":"KA Stubbs","year":"2009","unstructured":"Stubbs KA, Macauley MS, Vocadlo DJ (2009) A selective inhibitor Gal-PUGNAc of human lysosomal beta-hexosaminidases modulates levels of the ganglioside GM2 in neuroblastoma cells. Angew Chem Int Ed Engl 48:1300\u20131303","journal-title":"Angew Chem Int Ed Engl"},{"key":"5357_CR233","doi-asserted-by":"publisher","first-page":"531","DOI":"10.1016\/j.nbd.2019.01.001","volume":"124","author":"RG S\u00e1nchez","year":"2019","unstructured":"S\u00e1nchez RG, Parrish RR, Rich M et al (2019) Human and rodent temporal lobe epilepsy is characterized by changes in O-GlcNAc homeostasis that can be reversed to dampen epileptiform activity. Neurobiol Dis 124:531\u2013543. https:\/\/doi.org\/10.1016\/j.nbd.2019.01.001","journal-title":"Neurobiol Dis"},{"key":"5357_CR234","doi-asserted-by":"publisher","first-page":"340","DOI":"10.1007\/s13311-020-00978-4","volume":"18","author":"I Zuliani","year":"2021","unstructured":"Zuliani I, Lanzillotta C, Tramutola A et al (2021) The dysregulation of OGT\/OGA cycle mediates tau and APP neuropathology in down syndrome. Neurotherapeutics 18:340\u2013363. https:\/\/doi.org\/10.1007\/s13311-020-00978-4","journal-title":"Neurotherapeutics"}],"container-title":["Molecular Neurobiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s12035-025-05357-8.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s12035-025-05357-8\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s12035-025-05357-8.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,11,26]],"date-time":"2025-11-26T09:07:43Z","timestamp":1764148063000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s12035-025-05357-8"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,11,26]]},"references-count":234,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2026,1]]}},"alternative-id":["5357"],"URL":"https:\/\/doi.org\/10.1007\/s12035-025-05357-8","relation":{},"ISSN":["0893-7648","1559-1182"],"issn-type":[{"value":"0893-7648","type":"print"},{"value":"1559-1182","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,11,26]]},"assertion":[{"value":"23 June 2025","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"30 September 2025","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"26 November 2025","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"The authors declare no competing interests.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing Interests"}}],"article-number":"176"}}