O-GlcNAcylation regulates phosphorylation of tau: A mechanism involved in Alzheimer's disease

Hearing loss and cognitive decline in older adults

Lin, F. R., Yaffe, K., Xia, J., Xue, Q.-L., Harris, T. B., Purchase-Helzner, E., Satterfield, S., Ayonayon, H. N., Ferrucci, L., Simonsick, E. M., et al. (2013) · JAMA Internal Medicine · doi:10.1001/jamainternmed.2013.1868 · Cited by 4,017

Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease

Arriagada, P. V., Growdon, J. H., Hedley-Whyte, E. T., & Hyman, B. T. (1992) · Neurology · doi:10.1212/wnl.42.3.631 · Cited by 2,668

Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease

Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D., & Crowther, R. A. (1989) · Neuron · doi:10.1016/0896-6273(89)90210-9 · Cited by 2,492

Neurodegenerative Tauopathies

Lee, V. M.-Y., Goedert, M., & Trojanowski, J. Q. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1121 · Cited by 2,480

Diabetes mellitus and the risk of dementia: The Rotterdam Study

Ott, A., Stolk, R. P., van Harskamp, F., Pols, H. A. P., Hofman, A., & Breteler, M. M. B. (1999) · Neurology · doi:10.1212/wnl.53.9.1937 · Cited by 2,175

Tau protein isoforms, phosphorylation and role in neurodegenerative disorders11These authors contributed equally to this work.

Buée, L., Bussière, T., Buée‐Scherrer, V., Delacourte, A., & Hof, P. R. (2000) · Brain Research Reviews · doi:10.1016/s0165-0173(00)00019-9 · Cited by 2,142

Microtubule-associated protein tau. A component of Alzheimer paired helical filaments.

Grundke, I., Iqbal, K., Quinlan, M., Tung, Y. C., Zaidi, M. S., & Wisniewski, H. M. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38495-8 · Cited by 1,780

A68: a Major Subunit of Paired Helical Filaments and Derivatized Forms of Normal Tau

Lee, V. M.-Y., Balin, B. J., Otvos, L., & Trojanowski, J. Q. (1991) · Science · doi:10.1126/science.1899488 · Cited by 1,418

Tau proteins of alzheimer paired helical filaments: Abnormal phosphorylation of all six brain isoforms

Goedert, M., Spillantini, M. G., Cairns, N. J., & Crowther, R. A. (1992) · Neuron · doi:10.1016/0896-6273(92)90117-v · Cited by 1,122

Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease.

Köpke, E., Tung, Y. C., Shaikh, S., Alonso, A. C., Iqbal, K., & Grundke-Iqbal, I. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80536-5 · Cited by 779

Aβ-affected pathogenic induction of S-nitrosylation of OGT and identification of Cys-NO linkage triplet

Ryu, I.-H., Lee, K., & Do, S.-I. (2016) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2016.02.003 · Cited by 28

A Chemoenzymatic Histology Method for O‐GlcNAc Detection

Aguilar, A. L., Hou, X., Wen, L., Wang, P. G., & Wu, P. (2017) · ChemBioChem · doi:10.1002/cbic.201700515 · Cited by 27

Calpain I Activation Causes GLUT3 Proteolysis and Downregulation of O-GlcNAcylation in Alzheimer’s Disease Brain

Gu, J., Jin, N., Ma, D., Chu, D., Iqbal, K., Gong, C., & Liu, F. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-171047 · Cited by 27

Contribution of extracellular O-GlcNAc to the stability of folded epidermal growth factor-like domains and Notch1 trafficking

Ogawa, M., Tashima, Y., Sakaguchi, Y., Takeuchi, H., & Okajima, T. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.03.066 · Cited by 27

Therapeutic potential of rescuing protein O-GlcNAcylation in tau-related pathologies

Domenico, F. D., Lanzillotta, C., & Tramutola, A. (2018) · Expert Review of Neurotherapeutics · doi:10.1080/14737175.2019.1540932 · Cited by 27

Post-Translational Modifications in Alzheimer's Disease and the Potential for New Biomarkers

Russell, C. L., Končarević, S., & Ward, M. A. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-132312 · Cited by 26

Understanding Alzheimer's disease by global quantification of protein phosphorylation and sialylated N-linked glycosylation profiles: A chance for new biomarkers in neuroproteomics?

Lassen, P. S., Thygesen, C., Larsen, M. R., & Kempf, S. J. (2017) · Journal of Proteomics · doi:10.1016/j.jprot.2017.04.003 · Cited by 26

Deciphering Alzheimer’s Disease Pathogenic Pathway: Role of Chronic Brain Hypoperfusion on p-Tau and mTOR

de la Torre, J. C. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-201165 · Cited by 28

SIRT1 deficiency increases O-GlcNAcylation of tau, mediating synaptic tauopathy

Yin, X., Li, Y., Fan, X., Huang, F., Qiu, Y., Zhao, C., Zhou, Z., Gu, Q., Xia, L., Bao, J., et al. (2022) · Molecular Psychiatry · doi:10.1038/s41380-022-01689-2 · Cited by 28

Protein glycosylation and glycoinformatics for novel biomarker discovery in neurodegenerative diseases

Costa, J., Hayes, C. A., & Lisacek, F. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101991 · Cited by 25

Altered protein glycosylation predicts Alzheimer's disease and modulates its pathology in disease model Drosophila

Frenkel‐Pinter, M., Stempler, S., Tal-Mazaki, S., Losev, Y., Singh-Anand, A., Alvarez, D. E., Lezmy, J., Gazit, E., Ruppin, E., & Segal, D. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2017.04.020 · Cited by 27

PET quantification of brain O-GlcNAcase with [18F]LSN3316612 in healthy human volunteers

Lee, J., Liow, J., Paul, S., Morse, C. L., Haskali, M. B., Manly, L. S., Shcherbinin, S., Ruble, J. C., Kant, N., Collins, E. C., et al. (2020) · EJNMMI Research · doi:10.1186/s13550-020-0616-4 · Cited by 26

2-Acetamino-1,2-dideoxynojirimycin—lysine hybrids as hexosaminidase inhibitors

Steiner, A. J., Schitter, G., Stütz, A., Wrodnigg, T. M., Tarling, C. A., Withers, S. G., Mahuran, D. J., & Tropak, M. B. (2009) · Tetrahedron Asymmetry · doi:10.1016/j.tetasy.2009.02.015 · Cited by 26

The mitochondrial O-linked N-acetylglucosamine transferase (mOGT) in the diabetic patient could be the initial trigger to develop Alzheimer disease

Lozano, L., Lara‐Lemus, R., Zenteno, E., & Alvarado‐Vásquez, N. (2014) · Experimental Gerontology · doi:10.1016/j.exger.2014.08.008 · Cited by 28

Therapeutic and diagnostic challenges for frontotemporal dementia

Dâ€TMAlton, S., & Lewis, J. M. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00204 · Cited by 26

Pharmacological Inhibition of O-GlcNAc Transferase Promotes mTOR-Dependent Autophagy in Rat Cortical Neurons

Rahman, M. A., Cho, Y., Hwang, H., & Rhim, H. (2020) · Brain Sciences · doi:10.3390/brainsci10120958 · Cited by 25

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Lin, L., Jhao, Y.-T., Chiu, C., Sun, L.-H., Chou, T.-K., Shiue, C., Cheng, C., & Ma, K. (2022) · Pharmaceuticals · doi:10.3390/ph15020109 · Cited by 27

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Cervilla-Martínez, J. F., Gotor, J. J. R., Wypijewski, K. J., Fontán‐Lozano, Á., Wang, T., Santamaría, E., Fuller, W., & Mejı́as, R. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232214018 · Cited by 25

An O-GlcNAc transferase pathogenic variant linked to intellectual disability affects pluripotent stem cell self-renewal

Omelková, M., Fenger, C., Murray, M., Hammer, T. B., Pravatà, V. M., Bartual, S. G., Czajewski, I., Bayat, A., Ferenbach, A. T., Stavridis, M. P., et al. (2023) · Disease Models & Mechanisms · doi:10.1242/dmm.049132 · Cited by 25

Tau Phosphorylation and Aggregation as a Therapeutic Target in Tauopathies

Badiola, N., Suárez‐Calvet, M., & Lleó, A. (2010) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152710793237403 · Cited by 26

Hexosamine biosynthetic pathway and O-GlcNAc cycling of glucose metabolism in brain function and disease

Kim, D. Y., Park, J., & Han, I. (2023) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00191.2023 · Cited by 26

Efficient stereoselective synthesis of 2-acetamido-1,2-dideoxyallonojirimycin (DAJNAc) and sp2-iminosugar conjugates: Novel hexosaminidase inhibitors with discrimination capabilities between the mature and precursor forms of the enzyme

de la Fuente, A., Rísquez‐Cuadro, R., Verdaguer, X., Fernández, J. M. G., Nanba, E., Higaki, K., Mellet, C. O., & Riéra, A. (2015) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2015.10.038 · Cited by 24

Roles of O-GlcNAcylation on amyloid-β precursor protein processing, tau phosphorylation, and hippocampal synapses dysfunction in Alzheimer’s disease

Zheng, B.-W., Li, Y., Dai, X., Jiang, Z.-F., & Huang, H. (2016) · Neurological Research · doi:10.1080/01616412.2015.1133485 · Cited by 24

Effect of O-Linked Glycosylation on the Equilibrium Structural Ensemble of Intrinsically Disordered Polypeptides

Zerze, G. H., & Mittal, J. (2015) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5b10022 · Cited by 23

Dangerous Liaisons: Tau Interaction with Muscarinic Receptors

Wysocka, A., Pałasz, E., Steczkowska, M., & Niewiadomska, G. (2020) · Current Alzheimer Research · doi:10.2174/1567205017666200424134311 · Cited by 24

Activatable luminescent probes for imaging brain diseases

Li, Z., Wang, C., Zhang, M., Li, S., Mao, Z., & Liu, Z. (2021) · Nano Today · doi:10.1016/j.nantod.2021.101239 · Cited by 23

Heparan Sulfate Proteoglycans in Tauopathy

Zhu, Y., Gandy, L. A., Zhang, F., Liu, J., Wang, C., Blair, L. J., Linhardt, R. J., & Wang, L. (2022) · Biomolecules · doi:10.3390/biom12121792 · Cited by 27

Chronic rapid eye movement sleep deprivation aggravates the pathogenesis of Alzheimer’s disease by decreasing brain O-GlcNAc cycling in mice

Kim, D. Y., Kim, S.-M., & Han, I. (2024) · Journal of Neuroinflammation · doi:10.1186/s12974-024-03179-4 · Cited by 24

Versatile O -GlcNAc Transferase Assay for High-Throughput Identification of Enzyme Variants, Substrates, and Inhibitors

Kim, E. J., Abramowitz, L. K., Bond, M. R., Love, D. C., Kang, D. W., Luecke, H. F., Kang, D.-O., Ahn, J., & Hanover, J. A. (2014) · Bioconjugate Chemistry · doi:10.1021/bc5001774 · Cited by 23

O-GlcNAc modification of radial glial vimentin filaments in the developing chick brain

FARACH, A. M., & Galileo, D. S. (2008) · Journal of Neurocytology · doi:10.1007/s11068-008-9036-5 · Cited by 23

Loss of CRMP2 O-GlcNAcylation leads to reduced novel object recognition performance in mice

Muha, V., Williamson, R., Hills, R., McNeilly, A. D., McWilliams, T. G., Alonso, J., Schimpl, M., Leney, A. C., Heck, A. J. R., Sutherland, C. D., et al. (2019) · Open Biology · doi:10.1098/rsob.190192 · Cited by 23

Diazaspirononane Nonsaccharide Inhibitors of O-GlcNAcase (OGA) for the Treatment of Neurodegenerative Disorders

Martínez‐Viturro, C. M., Trabanco, A. A., Royes, J., Fernández, E., Tresadern, G., Vega, J. A., del Cerro, A., Delgado, F., Molina, A. G., Tovar, F., et al. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01479 · Cited by 23

Exogenous Ketones and Lactate as a Potential Therapeutic Intervention for Brain Injury and Neurodegenerative Conditions

Omori, N. E., Woo, G. H., & Mansor, L. S. (2022) · Frontiers in Human Neuroscience · doi:10.3389/fnhum.2022.846183 · Cited by 22

Clinical relevance of biomarkers, new therapeutic approaches, and role of post-translational modifications in the pathogenesis of Alzheimer’s disease

Mumtaz, I., Ayaz, M. O., Khan, M. S., Manzoor, U., Ganayee, M. A., Bhat, A. Q., Dar, G. H., Alghamdi, B. S. A., Hashem, A. M., Dar, M. J., et al. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.977411 · Cited by 23

Low glucose induced Alzheimer's disease‐like biochemical changes in human induced pluripotent stem cell‐derived neurons is due to dysregulated O‐GlcNAcylation

Huang, C., Rust, N. C., Wu, H., Yin, A., Zeltner, N., Yin, H., & Hart, G. W. (2023) · Alzheimer s & Dementia · doi:10.1002/alz.13058 · Cited by 21

Diabesity and Brain Energy Metabolism: The Case of Alzheimer’s Disease

Cardoso, S., Seiça, R. M. F., & Moreira, P. I. (2017) · Advances in neurobiology · doi:10.1007/978-3-319-63260-5_5 · Cited by 24

Preclinical, phase I, and phase II investigational clinical trials for treatment of progressive supranuclear palsy

Shoeibi, A., Olfati, N., & Litvan, I. (2018) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2018.1460356 · Cited by 23

Deciphering the Functions of O-GlcNAc Glycosylation in the Brain: The Role of Site-Specific Quantitative O-GlcNAcomics

Thompson, J. W., Sorum, A. W., & Hsieh‐Wilson, L. C. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00516 · Cited by 22

Molecular Connection Between Diabetes and Dementia

Chen, Y., Yu, Q., & Gong, C. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-3540-2_6 · Cited by 24

Redox imbalance and metabolic defects in the context of Alzheimer disease

Domenico, F. D., Lanzillotta, C., & Marzia Perluigi, A. (2024) · FEBS Letters · doi:10.1002/1873-3468.14840 · Cited by 22

Regulation of AβPP Glycosylation Modification and Roles of Glycosylation on AβPP Cleavage in Alzheimer’s Disease

Tao, P.-F., & Huang, H. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00574 · Cited by 21

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Garrett, L. R., & Niccoli, T. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.812222 · Cited by 20

Peripheral Pathways to Neurovascular Unit Dysfunction, Cognitive Impairment, and Alzheimer’s Disease

Nelson, A. R. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.858429 · Cited by 24

Intellectual disability-associated disruption of O-GlcNAc cycling impairs habituation learning in Drosophila

Fencková, M., Muha, V., Mariappa, D., Catinozzi, M., Czajewski, I., Blok, L. E. R., Ferenbach, A. T., Storkebaum, E., Schenck, A., & van Aalten, D. M. F. (2022) · PLoS Genetics · doi:10.1371/journal.pgen.1010159 · Cited by 24

N ‐glycosylation induced changes in tau protein dynamics reveal its role in tau misfolding and aggregation: A microsecond long molecular dynamics study

Mathew, A. T., Baidya, A. T. K., Das, B., Devi, B., & Kumar, R. (2022) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26417 · Cited by 23

Regulation of Glycogen Synthase Kinase-3β by Phosphorylation and O-β-Linked N-Acetylglucosaminylation: Implications on Tau Protein Phosphorylation

Hajjar, L. E., Page, A., Bridot, C., Cantrelle, F., Landrieu, I., & Smet‐Nocca, C. (2024) · Biochemistry · doi:10.1021/acs.biochem.4c00095 · Cited by 24

Magnetic mesoporous carbon composites incorporating hydrophilic metallic nanoparticles for enrichment of phosphopeptides prior to their determination by MALDI-TOF mass spectrometry

Zhang, L., Gan, Y., Sun, H., Yu, B., Jin, X., Zhang, W., Zhang, W., & Zhang, L. (2016) · Microchimica Acta · doi:10.1007/s00604-016-2046-6 · Cited by 20

Increased O-GlcNAcylation rapidly decreases GABAAR currents in hippocampus but depresses neuronal output

Stewart, L. T., Abiraman, K., Chatham, J. C., & McMahon, L. L. (2020) · Scientific Reports · doi:10.1038/s41598-020-63188-0 · Cited by 21

Domain focused and residue focused phosphorylation effect on tau protein: A molecular dynamics simulation study

Khan, M. I., Hasan, F., Mahmud, K. A. H. A., & Adnan, A. (2020) · Journal of the mechanical behavior of biomedical materials/Journal of mechanical behavior of biomedical materials · doi:10.1016/j.jmbbm.2020.104149 · Cited by 20

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Du, P., Zhang, X., Lian, X., Hölscher, C., & Xue, G. (2024) · Journal of Alzheimer s Disease · doi:10.3233/jad-230955 · Cited by 20

Synapsin-1 and tau reciprocal O-GlcNAcylation and phosphorylation sites in mouse brain synaptosomes

Kang, M. J., Kim, C., Jeong, H., Cho, B.-K., Ryou, A. L., Hwang, D., Mook‐Jung, I., & Yi, E. C. (2013) · Experimental & Molecular Medicine · doi:10.1038/emm.2013.56 · Cited by 21

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Panza, F., Imbimbo, B. P., Lozupone, M., Greco, A., Seripa, D., Logroscino, G., Daniele, A., & Colosimo, C. (2019) · Expert Review of Neurotherapeutics · doi:10.1080/14737175.2019.1606715 · Cited by 20

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Nam, G., Lin, Y., Lim, M. H., & Lee, Y. (2020) · Chem · doi:10.1016/j.chempr.2020.09.012 · Cited by 20

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Zhang, J., Chi, H., Wang, T., Zhang, S., Shen, T., Leng, B., Sun, H., Li, Z., & Li, F. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-210216 · Cited by 20

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Ning, X., Tao, T., Shen, J., Ji, Y., Xie, L., Wang, H., Liu, N., Xu, X., Sun, C. C., Zhang, D., et al. (2016) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-016-0391-y · Cited by 21

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Zhu, L., Wei, X., Cong, J., Zou, J., Wan, L., & Xu, S. (2022) · Nature Communications · doi:10.1038/s41467-022-35234-0 · Cited by 20

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Gharat, R., Dixit, G., Khambete, M., & Prabhu, A. (2023) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2023.176230 · Cited by 18

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Vang, S., Helton, E. S., Guo, Y., Burpee, B., Rose, E., Easter, M., Bollenbecker, S., Hirsch, M. J., Matthews, E. L., Jones, L., et al. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1387197 · Cited by 18

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Alencar, N., de Sousa, P. R. M., Silva, J. R. A., Lameira, J., Alves, C. N., Martı́, S., & Moliner, V. (2012) · Journal of Chemical Information and Modeling · doi:10.1021/ci2006005 · Cited by 19

Recent Advances in Mass Spectrometry-Based Glycoproteomics

Frost, D. C., & Li, L. (2014) · Advances in protein chemistry and structural biology · doi:10.1016/b978-0-12-800453-1.00003-8 · Cited by 19

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Przewodowska, D., Marzec, W. Z., & Madetko‐Alster, N. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.720220 · Cited by 20

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García‐Ayllón, M., Botella-López, A., Cuchillo‐Ibáñez, I., Rábano, A., Andreasen, N., Blennow, K., Ávila, J., & Sáez‐Valero, J. (2016) · Molecular Neurobiology · doi:10.1007/s12035-015-9644-x · Cited by 19

Development of inhibitors as research tools for carbohydrate-processing enzymes

Gloster, T. M. (2012) · Biochemical Society Transactions · doi:10.1042/bst20120201 · Cited by 20

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Li, J., Zhang, Y., Chen, X., Ma, L., Li, P., & Yu, H. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111520 · Cited by 17

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Run, X., Liang, Z., & Gong, C. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100813 · Cited by 18

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Herrera, M. I., Udovin, L., Toro-Urrego, N., Kusnier, C. F., Luaces, J. P., Losada, M. E. O., & Capani, F. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00339 · Cited by 18

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Lashley, T., Tossounian, M., Heaven, N. C., Wallworth, S., Peak‐Chew, S., Bradshaw, A., Cooper, J. A. D., de Silva, R., Srai, S. K., Malanchuk, O., et al. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.739425 · Cited by 19

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Tremblay‐Mercier, J., Tessier, D., Plourde, M., Fortier, M., Lorrain, D., & Cunnane, S. C. (2010) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.110.166504 · Cited by 17

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Alyenbaawi, H., Allison, W. T., & Mok, S. (2020) · Biomolecules · doi:10.3390/biom10111487 · Cited by 20

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Kositzke, A., Fan, D., Wang, A., Li, H., Worth, M., & Jiang, J. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.12.078 · Cited by 17

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Pan, D., Gu, J., Zhang, J., Hu, Y.-E., Liu, F., Iqbal, K., Cekic, N., Vocadlo, D. J., Dai, C., & Gong, C. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-201450 · Cited by 17

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He, Y., Bubb, A. K., Stubbs, K. A., Gloster, T. M., & Davies, G. J. (2010) · Amino Acids · doi:10.1007/s00726-010-0700-6 · Cited by 17

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Wang, J., Chen, Y., Chen, S., Mu, Z., & Chen, J. (2025) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2025.1623321 · Cited by 19

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Cheng, J., Zhao, Z., Chen, L., Li, Y., Du, R., Wu, Y., Zhu, Q., Fan, M., Duan, X., & Wu, H. (2021) · Neuroscience Bulletin · doi:10.1007/s12264-021-00784-8 · Cited by 16

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Williams, W. M., Weinberg, A., & Smith, M. A. (2011) · Journal of Amino Acids · doi:10.4061/2011/461216 · Cited by 16

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Li, Y., Tan, M., Yu, J., & Tan, L. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9507-5 · Cited by 17

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Burt, R. A., Alghusen, I. M., Ephrame, S. J., Villar, M. T., Artigues, A., & Slawson, C. M. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.920727 · Cited by 18

CREB-associated glycosylation and function in human disease

Zhang, N., Liu, S., & Wang, Y. (2022) · Advances in Clinical and Experimental Medicine · doi:10.17219/acem/151026 · Cited by 16

Intracellular and extracellular O-linked N-acetylglucosamine in the nervous system

Ogawa, M., Sawaguchi, S., Kamemura, K., & Okajima, T. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2015.08.009 · Cited by 16

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Rani, L., & Mallajosyula, S. S. (2017) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.7b08790 · Cited by 16

O-GlcNAcylation modulates PKA-CREB signaling in a manner specific to PKA catalytic subunit isoforms

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Nanopore‐Based High‐Resolution Detection of Multiple Post‐Translational Modifications in Protein

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Wei, C., Sun, R., Jiang, Y., Guo, X., Ying, Y., Wen, Y., Yang, H., & Wu, Y. (2021) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2021.130410 · Cited by 15

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Huynh, D. T., Tsolova, K. N., Watson, A. J., Khal, S. K., Green, J. R., Li, D., Hu, J., Soderblom, E. J., Chi, J., Evans, C. S., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-42227-0 · Cited by 15

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Wang, Y., Du, Y., Huang, H., Cao, Y., Pan, K., Zhou, Y., He, J., Yao, W., Chen, S., & Gao, X. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107133 · Cited by 15

Glucose enrichment impair neurotransmission and induce Aβ oligomerization that cannot be reversed by manipulating O-β-GlcNAcylation in the C. elegans model of Alzheimer's disease

Ahmad, W. (2022) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2022.109100 · Cited by 16

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Silva-Aguiar, R. P., Peruchetti, D. B., Pinheiro, A. A. S., Caruso‐Neves, C., & Dias, W. B. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911260 · Cited by 15

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Hajipour, M. J., Mohammad‐Beigi, H., Nabipour, I., Mahmoudi, N., Azhdarzadeh, M., Derakhshankhah, H., Dawud, D. E., Mohammadinejad, R., & Otzen, D. E. (2020) · Nano Today · doi:10.1016/j.nantod.2020.100983 · Cited by 14

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Liu, F., Shi, J., Tanimukai, H., Gu, J., Gu, J., Grundke-Iqbal, I., Iqbal, K., & Gong, C.-X. (2009) · Brain · doi:10.1093/brain/awp099 · Cited by 439

S3–03–01: O–glycosylation regulates phosphorylation of tau:A novel mechanism leading to neurofibrillarydegeneration in Alzheimer disease

Gong, C., Liu, F., Grundke, I., & Iqbal, K. (2006) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2006.05.174

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Gong, C., Liu, F., Liu, Y., Deng, Y., Grundke, I., & Iqbal, K. (2008) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2008.05.347

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Qian, W. (2003) · PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS

F3‐02‐02: O‐GlcNAcylated tau: A link between impaired glucose metabolism and neurodegeneration in Alzheimer's disease

Gong, C., Liu, F., Grundke, I., & Iqbal, K. (2012) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2012.05.1127