{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,8]],"date-time":"2026-10-08T19:16:22Z","timestamp":1791486982486,"version":"4.3.4"},"reference-count":221,"publisher":"MDPI AG","issue":"9","license":[{"start":{"date-parts":[[2025,4,24]],"date-time":"2025-04-24T00:00:00Z","timestamp":1745452800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Florida Department of Health, Ed and Ethel Moore Alzheimer\u2019s Disease Research Program","award":["24A02"],"award-info":[{"award-number":["24A02"]}]},{"name":"Palm Health Foundation","award":["24A02"],"award-info":[{"award-number":["24A02"]}]},{"name":"Stiles-Nicholson Brain Institute","award":["24A02"],"award-info":[{"award-number":["24A02"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>Alzheimer\u2019s disease (AD) is one of the most common neurodegenerative disorders linked to aging. Major hallmarks of AD pathogenesis include amyloid-\u03b2 peptide (A\u03b2) plaques, which are extracellular deposits originating from the processing of the amyloid precursor protein (APP), and neurofibrillary tangles (NFTs), which are intracellular aggregates of tau protein. Recent evidence indicates that disruptions in metal homeostasis and impaired immune recognition of these aggregates trigger neuroinflammation, ultimately driving disease progression. Therefore, a more comprehensive approach is needed to understand the underlying causes of the disease. Patients with AD present abnormal glycan profiles, and most known AD-related molecules are either modified with glycans or involved in glycan regulation. A deeper understanding of how O-glycosylation influences the balance between amyloid-beta peptide production and clearance, as well as microglia\u2019s pro- and anti-inflammatory responses, is crucial for deciphering the early pathogenic events of AD. This review aims to provide a comprehensive summary of the extensive research conducted on the role of mucin-type O-glycosylation in the pathogenesis of AD, discussing its role in disease onset and immune recognition.<\/jats:p>","DOI":"10.3390\/molecules30091895","type":"journal-article","created":{"date-parts":[[2025,4,24]],"date-time":"2025-04-24T08:08:41Z","timestamp":1745482121000},"page":"1895","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["Implications of Mucin-Type O-Glycosylation in Alzheimer\u2019s Disease"],"prefix":"10.3390","volume":"30","author":[{"ORCID":"https:\/\/orcid.org\/0009-0002-9755-5231","authenticated-orcid":false,"given":"Nancy","family":"Vela Navarro","sequence":"first","affiliation":[{"name":"Department of Chemistry and Biochemistry, Florida Atlantic University, 777 Glades Rd., Boca Raton, FL 33431, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6734-4428","authenticated-orcid":false,"given":"Gustavo","family":"De Nadai Mundim","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry, Florida Atlantic University, 777 Glades Rd., Boca Raton, FL 33431, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7657-0400","authenticated-orcid":false,"given":"Mar\u00e9","family":"Cudic","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry, Florida Atlantic University, 777 Glades Rd., Boca Raton, FL 33431, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,4,24]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Silva, M.V.F., de Loures, C.M.G., Alves, L.C.V., de Souza, L.C., Borges, K.B.G., and Carvalho, M.d.G. (2019). Alzheimer\u2019s Disease: Risk Factors and Potentially Protective Measures. J. Biomed. Sci., 26.","DOI":"10.1186\/s12929-019-0524-y"},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"(2024). 2024 Alzheimer\u2019s Disease Facts and Figures. Alzheimer\u2019s Dement., 20, 3708\u20133821.","DOI":"10.1002\/alz.13809"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1002\/alz.12694","article-title":"Global Estimates on the Number of Persons across the Alzheimer\u2019s Disease Continuum","volume":"19","author":"Gustavsson","year":"2023","journal-title":"Alzheimer\u2019s Dement."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"e447","DOI":"10.1016\/S2468-2667(18)30118-X","article-title":"Forecasting the Care Needs of the Older Population in England over the next 20 Years: Estimates from the Population Ageing and Care Simulation (PACSim) Modelling Study","volume":"3","author":"Kingston","year":"2018","journal-title":"Lancet Public Health"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1016\/j.trci.2019.05.008","article-title":"Alzheimer\u2019s Disease Drug Development Pipeline: 2019","volume":"5","author":"Cummings","year":"2019","journal-title":"Alzheimer\u2019s Dement. Transl. Res. Clin. Interv."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1007\/s40259-023-00633-2","article-title":"Anti-Amyloid Monoclonal Antibodies for the Treatment of Alzheimer\u2019s Disease","volume":"38","author":"Cummings","year":"2024","journal-title":"BioDrugs"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"512","DOI":"10.1001\/jama.2023.13239","article-title":"Donanemab in Early Symptomatic Alzheimer Disease","volume":"330","author":"Sims","year":"2023","journal-title":"JAMA"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1038\/s41573-022-00391-w","article-title":"The Amyloid Hypothesis in Alzheimer Disease: New Insights from New Therapeutics","volume":"21","author":"Karran","year":"2022","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1002\/ca.980080612","article-title":"An English Translation of Alzheimer\u2019s 1907 Paper, \u201c\u00dcber Eine Eigenartige Erkankung Der Hirnrinde\u201d","volume":"8","author":"Stelzmann","year":"1995","journal-title":"Clin. Anat."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"196","DOI":"10.59566\/IJBS.2006.2196","article-title":"Alois Alzheimer: A Hundred Years after the Discovery of the Eponymous Disorder","volume":"2","author":"Tagarelli","year":"2006","journal-title":"Int. J. Biomed. Sci."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"885","DOI":"10.1016\/S0006-291X(84)80190-4","article-title":"Alzheimer\u2019s Disease: Initial Report of the Purification and Characterization of a Novel Cerebrovascular Amyloid Protein","volume":"120","author":"Glenner","year":"1984","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"4245","DOI":"10.1073\/pnas.82.12.4245","article-title":"Amyloid Plaque Core Protein in Alzheimer Disease and Down Syndrome","volume":"82","author":"Masters","year":"1985","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1093\/brain\/87.2.307","article-title":"Alzheimer\u2019s Disease-an Electron Microscopical Study","volume":"87","author":"Kidd","year":"1964","journal-title":"Brain"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1038\/197192b0","article-title":"Paired Helical Filaments in Electron Microscopy of Alzheimer\u2019s Disease","volume":"197","author":"Kidd","year":"1963","journal-title":"Nature"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"629","DOI":"10.1097\/00005072-196310000-00005","article-title":"The FIne Structure of Neurofibrillary Tangles in Alzheimer\u2019s Disease","volume":"22","author":"Terry","year":"1963","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"ref_16","first-page":"269","article-title":"Ultrastructural Studies in Alzheimer\u2019s Presenile Dementia","volume":"44","author":"Terry","year":"1964","journal-title":"Am. J. Pathol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"219","DOI":"10.3233\/JAD-2006-9S325","article-title":"Discoveries of Tau, Abnormally Hyperphosphorylated Tau and Others of Neurofibrillary Degeneration: A Personal Historical Perspective","volume":"9","author":"Iqbal","year":"2006","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"307","DOI":"10.3233\/JAD-1999-14-511","article-title":"Tau Protein in Normal and Alzheimer\u2019s Disease Brain","volume":"1","author":"Johnson","year":"1999","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s00401-011-0910-3","article-title":"National Institute on Aging-Alzheimer\u2019s Association Guidelines for the Neuropathologic Assessment of Alzheimer\u2019s Disease: A Practical Approach","volume":"123","author":"Montine","year":"2012","journal-title":"Acta Neuropathol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1186\/s13024-019-0333-5","article-title":"The Neuropathological Diagnosis of Alzheimer\u2019s Disease","volume":"14","author":"Deture","year":"2019","journal-title":"Mol. Neurodegener."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"a006247","DOI":"10.1101\/cshperspect.a006247","article-title":"Biochemistry and Cell Biology of Tau Protein in Neurofibrillary Degeneration","volume":"2","author":"Mandelkow","year":"2012","journal-title":"Cold Spring Harb. Perspect. Med."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1002\/cm.21796","article-title":"The Discovery of Tau Protein","volume":"81","author":"Kirschner","year":"2024","journal-title":"Cytoskeleton"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"1858","DOI":"10.1073\/pnas.72.5.1858","article-title":"A Protein Factor Essential for Microtubule Assembly","volume":"72","author":"Weingarten","year":"1975","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"1615","DOI":"10.1016\/0896-6273(89)90050-0","article-title":"The Microtubule Binding Domain of Tau Protein","volume":"2","author":"Lee","year":"1989","journal-title":"Neuron"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1327","DOI":"10.1083\/jcb.131.5.1327","article-title":"Interaction of Tau with the Neural Plasma Membrane Mediated by Tau\u2019s Amino-Terminal Projection Domain","volume":"131","author":"Brandt","year":"1995","journal-title":"J. Cell Biol."},{"key":"ref_26","doi-asserted-by":"crossref","unstructured":"Alquezar, C., Arya, S., and Kao, A.W. (2021). Tau Post-Translational Modifications: Dynamic Transformers of Tau Function, Degradation, and Aggregation. Front. Neurol., 11.","DOI":"10.3389\/fneur.2020.595532"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1186\/s40478-018-0557-6","article-title":"Phosphorylation of Different Tau Sites during Progression of Alzheimer\u2019s Disease","volume":"6","author":"Neddens","year":"2018","journal-title":"Acta Neuropathol. Commun."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"24374","DOI":"10.1016\/S0021-9258(20)80536-5","article-title":"Microtubule-Associated Protein Tau. Abnormal Phosphorylation of a Non-Paired Helical Filament Pool in Alzheimer Disease","volume":"268","author":"Tung","year":"1993","journal-title":"J. Biol. Chem."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1016\/0022-2836(77)90214-5","article-title":"Physical and Chemical Properties of Purified Tau Factor and the Role of Tau in Microtubule Assembly","volume":"116","author":"Cleveland","year":"1977","journal-title":"J. Mol. Biol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"5301","DOI":"10.1016\/S0021-9258(17)42989-9","article-title":"Phosphorylation Affects the Ability of Tau Protein to Promote Microtubule Assembly","volume":"259","author":"Lindwall","year":"1984","journal-title":"J. Biol. Chem."},{"key":"ref_31","doi-asserted-by":"crossref","unstructured":"Tenreiro, S., Eckermann, K., and Outeiro, T.F. (2014). Protein Phosphorylation in Neurodegeneration: Friend or Foe?. Front. Mol. Neurosci., 7.","DOI":"10.3389\/fnmol.2014.00042"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1126\/science.1566067","article-title":"Alzheimer\u2019s Disease: The Amyloid Cascade Hypothesis","volume":"256","author":"Hardy","year":"1992","journal-title":"Science"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"595","DOI":"10.15252\/emmm.201606210","article-title":"The Amyloid Hypothesis of Alzheimer\u2019s Disease at 25 Years","volume":"8","author":"Selkoe","year":"2016","journal-title":"EMBO Mol. Med."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1172","DOI":"10.1111\/j.1471-4159.2006.04426.x","article-title":"A\u03b2 Oligomers\u2014A Decade of Discovery","volume":"101","author":"Walsh","year":"2007","journal-title":"J. Neurochem."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1111\/jnc.12202","article-title":"Alzheimer\u2019s A\u03b242 and A\u03b240 Peptides Form Interlaced Amyloid Fibrils","volume":"126","author":"Gu","year":"2013","journal-title":"J. Neurochem."},{"key":"ref_36","doi-asserted-by":"crossref","unstructured":"Wang, L., Eom, K., and Kwon, T. (2021). Different Aggregation Pathways and Structures for A\u03b240 and A\u03b242 Peptides. Biomolecules, 11.","DOI":"10.3390\/biom11020198"},{"key":"ref_37","doi-asserted-by":"crossref","unstructured":"Tolar, M., Hey, J., Power, A., and Abushakra, S. (2021). Neurotoxic Soluble Amyloid Oligomers Drive Alzheimer\u2019s Pathogenesis and Represent a Clinically Validated Target for Slowing Disease Progression. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22126355"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"1205","DOI":"10.1038\/aps.2017.28","article-title":"Amyloid Beta: Structure, Biology and Structure-Based Therapeutic Development","volume":"38","author":"Chen","year":"2017","journal-title":"Acta Pharmacol. Sin."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"5481","DOI":"10.1038\/s41380-021-01249-0","article-title":"The Amyloid-\u03b2 Pathway in Alzheimer\u2019s Disease","volume":"26","author":"Hampel","year":"2021","journal-title":"Mol. Psychiatry"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"794","DOI":"10.1038\/nn.4017","article-title":"The Case for Rejecting the Amyloid Cascade Hypothesis","volume":"18","author":"Herrup","year":"2015","journal-title":"Nat. Neurosci."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1097\/00005072-199704000-00001","article-title":"The Pathogenesis of Senile Plaques","volume":"56","author":"Dickson","year":"1997","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"A23","DOI":"10.1038\/399a023","article-title":"Translating Cell Biology into Therapeutic Advances in Alzheimer\u2019s Disease","volume":"399","author":"Selkoe","year":"1999","journal-title":"Nature"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.npep.2015.06.008","article-title":"Amyloid Cascade Hypothesis: Pathogenesis and Therapeutic Strategies in Alzheimer\u2019s Disease","volume":"52","author":"Barage","year":"2015","journal-title":"Neuropeptides"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1038\/s41582-020-00435-y","article-title":"Neuroinflammation and Microglial Activation in Alzheimer Disease: Where Do We Go from Here?","volume":"17","author":"Leng","year":"2021","journal-title":"Nat. Rev. Neurol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"3969","DOI":"10.1093\/brain\/awad159","article-title":"The Amyloid Cascade Hypothesis: An Updated Critical Review","volume":"146","author":"Kepp","year":"2023","journal-title":"Brain"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"590","DOI":"10.1136\/jnnp-2018-319148","article-title":"Inflammatory Markers in Alzheimer\u2019s Disease and Mild Cognitive Impairment: A Meta-Analysis and Systematic Review of 170 Studies","volume":"90","author":"Shen","year":"2019","journal-title":"J. Neurol. Neurosurg. Psychiatry"},{"key":"ref_47","doi-asserted-by":"crossref","unstructured":"Garland, E.F., Hartnell, I.J., and Boche, D. (2022). Microglia and Astrocyte Function and Communication: What Do We Know in Humans?. Front. Neurosci., 16.","DOI":"10.3389\/fnins.2022.824888"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"388","DOI":"10.1016\/S1474-4422(15)70016-5","article-title":"Neuroinflammation in Alzheimer\u2019s Disease","volume":"14","author":"Heneka","year":"2015","journal-title":"Lancet Neurol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1016\/0304-3940(87)90696-3","article-title":"Reactive Microglia in Patients with Senile Dementia of the Alzheimer Type Are Positive for the Histocompatibility Glycoprotein HLA-DR","volume":"79","author":"McGeer","year":"1987","journal-title":"Neurosci. Lett."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1016\/0006-8993(90)91496-4","article-title":"Reactive Microglia Express Class I and Class II Major Histocompatibility Complex Antigens in Alzheimer\u2019s Disease","volume":"523","author":"Tooyama","year":"1990","journal-title":"Brain Res."},{"key":"ref_51","first-page":"2740","article-title":"Microglial Activation Correlates in Vivo with Both Tau and Amyloid in Alzheimer\u2019s Disease","volume":"141","author":"Dani","year":"2018","journal-title":"Brain"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1007\/s10571-017-0504-2","article-title":"Microglia: Housekeeper of the Central Nervous System","volume":"38","author":"Kabba","year":"2018","journal-title":"Cell. Mol. Neurobiol."},{"key":"ref_53","doi-asserted-by":"crossref","unstructured":"Al-Qahtani, A.A., Alhamlan, F.S., and Al-Qahtani, A.A. (2024). Pro-Inflammatory and Anti-Inflammatory Interleukins in Infectious Diseases: A Comprehensive Review. Trop. Med. Infect. Dis., 9.","DOI":"10.3390\/tropicalmed9010013"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/j.imbio.2014.10.002","article-title":"Novel Insights into the Immunomodulatory Role of the Dendritic Cell and Macrophage-Expressed C-Type Lectin MGL","volume":"220","author":"Ilarregui","year":"2015","journal-title":"Immunobiology"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1186\/s12974-019-1522-4","article-title":"Macrophage Galactose-Type Lectin (MGL) Is Induced on M2 Microglia and Participates in the Resolution Phase of Autoimmune Neuroinflammation","volume":"16","author":"Ilarregui","year":"2019","journal-title":"J. Neuroinflamm."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/j.it.2007.10.010","article-title":"Sweet Preferences of MGL: Carbohydrate Specificity and Function","volume":"29","author":"Saeland","year":"2008","journal-title":"Trends Immunol."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1515\/BC.2001.022","article-title":"O-Glycosylation of the Mucin Type","volume":"382","author":"Hanisch","year":"2001","journal-title":"Biol. Chem."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1097\/00005072-199810000-00003","article-title":"Altered Glycosylation Pattern of Proteins in Alzheimer Disease","volume":"57","author":"Guevara","year":"1998","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1016\/j.nurt.2008.05.001","article-title":"Therapeutics for Alzheimer\u2019s Disease Based on the Metal Hypothesis","volume":"5","author":"Bush","year":"2008","journal-title":"Neurotherapeutics"},{"key":"ref_60","doi-asserted-by":"crossref","unstructured":"Babi\u0107 Leko, M., Langer Horvat, L., \u0160pani\u0107 Popova\u010dki, E., Zub\u010di\u0107, K., Hof, P.R., and \u0160imi\u0107, G. (2023). Metals in Alzheimer\u2019s Disease. Biomedicines, 11.","DOI":"10.3390\/biomedicines11041161"},{"key":"ref_61","doi-asserted-by":"crossref","unstructured":"Chen, L.-L., Fan, Y.-G., Zhao, L.-X., Zhang, Q., and Wang, Z.-Y. (2023). The Metal Ion Hypothesis of Alzheimer\u2019s Disease and the Anti-Neuroinflammatory Effect of Metal Chelators. Bioorg. Chem., 131.","DOI":"10.1016\/j.bioorg.2022.106301"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"3059","DOI":"10.1021\/acschembio.1c00932","article-title":"In-Depth Site-Specific O-Glycosylation Analysis of Glycoproteins and Endogenous Peptides in Cerebrospinal Fluid (CSF) from Healthy Individuals, Mild Cognitive Impairment (MCI), and Alzheimer\u2019s Disease (AD) Patients","volume":"17","author":"Chen","year":"2022","journal-title":"ACS Chem. Biol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1186\/s13195-020-00664-9","article-title":"Amyloid Precursor Protein Glycosylation Is Altered in the Brain of Patients with Alzheimer\u2019s Disease","volume":"12","author":"Boix","year":"2020","journal-title":"Alzheimer\u2019s Res. Ther."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"eabc5802","DOI":"10.1126\/sciadv.abc5802","article-title":"Integrative Glycoproteomics Reveals Protein N-Glycosylation Aberrations and Glycoproteomic Network Alterations in Alzheimer\u2019s Disease","volume":"6","author":"Zhang","year":"2020","journal-title":"Sci. Adv."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"100433","DOI":"10.1016\/j.mcpro.2022.100433","article-title":"Glycoproteomics Landscape of Asymptomatic and Symptomatic Human Alzheimer\u2019s Disease Brain","volume":"21","author":"Suttapitugsakul","year":"2022","journal-title":"Mol. Cell. Proteom."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"E509","DOI":"10.1073\/pnas.1512952113","article-title":"Nicastrin Functions to Sterically Hinder \u03b3-Secretase\u2013Substrate Interactions Driven by Substrate Transmembrane Domain","volume":"113","author":"Bolduc","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"4086","DOI":"10.1091\/mbc.e08-05-0459","article-title":"Consequences of Individual N-Glycan Deletions and of Proteasomal Inhibition on Secretion of Active BACE","volume":"19","author":"Vanoni","year":"2008","journal-title":"Mol. Biol. Cell"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"e1601576","DOI":"10.1126\/sciadv.1601576","article-title":"Interplay between Protein Glycosylation Pathways in Alzheimer\u2019s Disease","volume":"3","author":"Shmueli","year":"2017","journal-title":"Sci. Adv."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1021\/acs.biochem.7b00861","article-title":"Post-Translational Modifications of Protein Backbones: Unique Functions, Mechanisms, and Challenges","volume":"57","year":"2018","journal-title":"Biochemistry"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"1868","DOI":"10.1016\/j.molcel.2021.03.015","article-title":"Discovering the Landscape of Protein Modifications","volume":"81","author":"Keenan","year":"2021","journal-title":"Mol. Cell"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1021\/cb3005066","article-title":"Chemically Modified Tandem Repeats in Proteins: Natural Combinatorial Peptide Libraries","volume":"8","author":"Fuchs","year":"2013","journal-title":"ACS Chem. Biol."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1186\/2047-9158-3-23","article-title":"Proteomics of Protein Post-Translational Modifications Implicated in Neurodegeneration","volume":"3","author":"Ren","year":"2014","journal-title":"Transl. Neurodegener."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"101336","DOI":"10.1016\/j.arr.2021.101336","article-title":"Post-Translational Modifications: Regulators of Neurodegenerative Proteinopathies","volume":"68","author":"Gupta","year":"2021","journal-title":"Ageing Res. Rev."},{"key":"ref_74","doi-asserted-by":"crossref","unstructured":"Schaffert, L.-N., and Carter, W.G. (2020). Do Post-Translational Modifications Influence Protein Aggregation in Neurodegenerative Diseases: A Systematic Review. Brain Sci., 10.","DOI":"10.3390\/brainsci10040232"},{"key":"ref_75","doi-asserted-by":"crossref","unstructured":"Li, W., Li, H.-L., Wang, J.-Z., Liu, R., and Wang, X. (2024). Abnormal Protein Post-Translational Modifications Induces Aggregation and Abnormal Deposition of Protein, Mediating Neurodegenerative Diseases. Cell Biosci., 14.","DOI":"10.1186\/s13578-023-01189-y"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1038\/s41467-023-35795-8","article-title":"Control of Protein Stability by Post-Translational Modifications","volume":"14","author":"Lee","year":"2023","journal-title":"Nat. Commun."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1016\/j.brainres.2018.11.024","article-title":"Lysine Methylation: Implications in Neurodegenerative Disease","volume":"1707","author":"Rowe","year":"2019","journal-title":"Brain Res."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1007\/s00401-011-0893-0","article-title":"Dual Modification of Alzheimer\u2019s Disease PHF-Tau Protein by Lysine Methylation and Ubiquitylation: A Mass Spectrometry Approach","volume":"123","author":"Thomas","year":"2012","journal-title":"Acta Neuropathol."},{"key":"ref_79","doi-asserted-by":"crossref","unstructured":"Xiao, X., Liu, X., and Jiao, B. (2020). Epigenetics: Recent Advances and Its Role in the Treatment of Alzheimer\u2019s Disease. Front. Neurol., 11.","DOI":"10.3389\/fneur.2020.538301"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"3617","DOI":"10.1007\/s12035-023-03277-z","article-title":"The Involvement of Post-Translational Modifications in Regulating the Development and Progression of Alzheimer\u2019s Disease","volume":"60","author":"Guan","year":"2023","journal-title":"Mol. Neurobiol."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"834","DOI":"10.1126\/science.1175371","article-title":"Lysine Acetylation Targets Protein Complexes and Co-Regulates Major Cellular Functions","volume":"325","author":"Choudhary","year":"2009","journal-title":"Science"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"111062","DOI":"10.1016\/j.celrep.2022.111062","article-title":"Inhibition of SIRT2 Promotes APP Acetylation and Ameliorates Cognitive Impairment in APP\/PS1 Transgenic Mice","volume":"40","author":"Bai","year":"2022","journal-title":"Cell Rep."},{"key":"ref_83","doi-asserted-by":"crossref","unstructured":"Tracy, T., Claiborn, K.C., and Gan, L. (2019). Regulation of Tau Homeostasis and Toxicity by Acetylation. Tau Biology, Springer.","DOI":"10.1007\/978-981-32-9358-8_4"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"831","DOI":"10.1146\/annurev.bi.44.070175.004151","article-title":"Protein Phosphorylation","volume":"44","author":"Rubin","year":"1975","journal-title":"Annu. Rev. Biochem."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s10930-017-9696-z","article-title":"Phosphorylation: Implications in Cancer","volume":"36","author":"Singh","year":"2017","journal-title":"Protein J."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"e175","DOI":"10.1002\/mco2.175","article-title":"Role of Protein Phosphorylation in Cell Signaling, Disease, and the Intervention Therapy","volume":"3","author":"Pang","year":"2022","journal-title":"MedComm"},{"key":"ref_87","doi-asserted-by":"crossref","unstructured":"Zhang, T., Chen, D., and Lee, T.H. (2019). Phosphorylation Signaling in APP Processing in Alzheimer\u2019s Disease. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21010209"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"3549","DOI":"10.1021\/bi981874p","article-title":"Phosphorylation That Detaches Tau Protein from Microtubules (Ser262, Ser214) Also Protects It against Aggregation into Alzheimer Paired Helical Filaments","volume":"38","author":"Schneider","year":"1999","journal-title":"Biochemistry"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"576","DOI":"10.1016\/j.sbi.2011.08.005","article-title":"Mechanisms and Principles of N-Linked Protein Glycosylation","volume":"21","author":"Schwarz","year":"2011","journal-title":"Curr. Opin. Struct. Biol."},{"key":"ref_90","unstructured":"Stanley, P., Moremen, K.W., Lewis, N.E., Taniguchi, N., and Aebi, M. (2022). N-Glycans. Essentials of Glycobiology, Cold Spring Harbor Laboratory Press. [4th ed.]."},{"key":"ref_91","doi-asserted-by":"crossref","unstructured":"Esmail, S., and Manolson, M.F. (2021). Advances in Understanding N-Glycosylation Structure, Function, and Regulation in Health and Disease. Eur. J. Cell Biol., 100.","DOI":"10.1016\/j.ejcb.2021.151186"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"506","DOI":"10.1093\/glycob\/cwac009","article-title":"Lack of N-Glycosylation Increases Amyloidogenic Processing of the Amyloid Precursor Protein","volume":"32","author":"Lin","year":"2022","journal-title":"Glycobiology"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1016\/S0014-5793(01)02421-8","article-title":"Analysis of N-glycans of Pathological Tau: Possible Occurrence of Aberrant Processing of Tau in Alzheimer\u2019s Disease","volume":"496","author":"Sato","year":"2001","journal-title":"FEBS Lett."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/S0014-5793(02)02228-7","article-title":"Role of Glycosylation in Hyperphosphorylation of Tau in Alzheimer\u2019s Disease","volume":"512","author":"Liu","year":"2002","journal-title":"FEBS Lett."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"2447","DOI":"10.1016\/j.bbagen.2017.04.012","article-title":"N-Glycan and Alzheimer\u2019s Disease","volume":"1861","author":"Kizuka","year":"2017","journal-title":"Biochim. Biophys. Acta\u2014Gen. Subj."},{"key":"ref_96","unstructured":"Haltiwanger, R.S., Wells, L., Freeze, H.H., Jafar-Nejad, H., Okajima, T., and Stanley, P. (2022). Other Classes of Eukaryotic Glycans. Essentials of Glycobiology, Cold Spring Harbor Laboratory Press. [4th ed.]."},{"key":"ref_97","unstructured":"Brockhausen, I., Schachter, H., and Stanley, P. (2009). O-GalNAc Glycans. Essentials of Glycobiology, Cold Spring Harbor Laboratory Press. [2nd ed.]."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"4140","DOI":"10.1093\/bioinformatics\/btz215","article-title":"SPRINT-Gly: Predicting N- and O-Linked Glycosylation Sites of Human and Mouse Proteins by Using Sequence and Predicted Structural Properties","volume":"35","author":"Taherzadeh","year":"2019","journal-title":"Bioinformatics"},{"key":"ref_99","doi-asserted-by":"crossref","unstructured":"Pakhrin, S.C., Chauhan, N., Khan, S., Upadhyaya, J., Beck, M.R., and Blanco, E. (2024). Prediction of Human O-Linked Glycosylation Sites Using Stacked Generalization and Embeddings from Pre-Trained Protein Language Model. Bioinformatics, 40.","DOI":"10.1093\/bioinformatics\/btae643"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"3308","DOI":"10.1016\/S0021-9258(17)43295-9","article-title":"Topography and Polypeptide Distribution of Terminal N-Acetylglucosamine Residues on the Surfaces of Intact Lymphocytes. Evidence for O-Linked GlcNAc","volume":"259","author":"Torres","year":"1984","journal-title":"J. Biol. Chem."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1016\/S0304-4165(02)00477-4","article-title":"Evidence of a Balance between Phosphorylation and O-GlcNAc Glycosylation of Tau Proteins\u2014A Role in Nuclear Localization","volume":"1619","author":"Lefebvre","year":"2003","journal-title":"Biochim. Biophys. Acta\u2014Gen. Subj."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"10804","DOI":"10.1073\/pnas.0400348101","article-title":"O-GlcNAcylation Regulates Phosphorylation of Tau: A Mechanism Involved in Alzheimer\u2019s Disease","volume":"101","author":"Liu","year":"2004","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"1078","DOI":"10.1016\/j.jalz.2016.02.011","article-title":"O-GlcNAcylation: A Regulator of Tau Pathology and Neurodegeneration","volume":"12","author":"Gong","year":"2016","journal-title":"Alzheimer\u2019s Dement."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1002\/jnr.490410214","article-title":"\u0392-Amyloid Precursor Protein Is Modified with O-linked N-acetylglucosamine","volume":"41","author":"Griffith","year":"1995","journal-title":"J. Neurosci. Res."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"882","DOI":"10.1016\/j.bbrc.2010.12.080","article-title":"O-GlcNAcylation Increases Non-Amyloidogenic Processing of the Amyloid-\u03b2 Precursor Protein (APP)","volume":"404","author":"Jacobsen","year":"2011","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1016\/j.bbrc.2017.06.067","article-title":"O-GlcNAcylation of Amyloid-\u03b2 Precursor Protein at Threonine 576 Residue Regulates Trafficking and Processing","volume":"490","author":"Chun","year":"2017","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"6921","DOI":"10.1074\/jbc.R112.418558","article-title":"Mucin-Type O-Glycosylation during Development","volume":"288","author":"Tran","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_108","doi-asserted-by":"crossref","unstructured":"Bagdonaite, I., Pallesen, E.M.H., Nielsen, M.I., Bennett, E.P., and Wandall, H.H. (2021). Mucin-Type O-GalNAc Glycosylation in Health and Disease. The Role of Glycosylation in Health and Disease, Springer.","DOI":"10.1007\/978-3-030-70115-4_2"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"736","DOI":"10.1093\/glycob\/cwr182","article-title":"Control of Mucin-Type O-Glycosylation: A Classification of the Polypeptide GalNAc-Transferase Gene Family","volume":"22","author":"Bennett","year":"2012","journal-title":"Glycobiology"},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"101389","DOI":"10.1016\/j.smim.2020.101389","article-title":"Tumor-Associated O-Glycans of MUC1: Carriers of the Glyco-Code and Targets for Cancer Vaccine Design","volume":"47","author":"Beckwith","year":"2020","journal-title":"Semin. Immunol."},{"key":"ref_111","doi-asserted-by":"crossref","unstructured":"Lohmueller, J.J., Sato, S., Popova, L., Chu, I.M., Tucker, M.A., Barberena, R., Innocenti, G.M., Cudic, M., Ham, J.D., and Cheung, W.C. (2016). Antibodies Elicited by the First Non-Viral Prophylactic Cancer Vaccine Show Tumor-Specificity and Immunotherapeutic Potential. Sci. Rep., 6.","DOI":"10.1038\/srep31740"},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1021\/pr800758g","article-title":"Elucidation of O-Glycosylation Structures of the \u03b2-Amyloid Precursor Protein by Liquid Chromatography\u2212Mass Spectrometry Using Electron Transfer Dissociation and Collision Induced Dissociation","volume":"8","author":"Perdivara","year":"2009","journal-title":"J. Proteome Res."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"11848","DOI":"10.1073\/pnas.1102664108","article-title":"Site-Specific Characterization of Threonine, Serine, and Tyrosine Glycosylations of Amyloid Precursor Protein\/Amyloid \u03b2-Peptides in Human Cerebrospinal Fluid","volume":"108","author":"Halim","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_114","doi-asserted-by":"crossref","unstructured":"Akasaka-Manya, K., and Manya, H. (2020). The Role of APP O-Glycosylation in Alzheimer\u2019s Disease. Biomolecules, 10.","DOI":"10.3390\/biom10111569"},{"key":"ref_115","doi-asserted-by":"crossref","unstructured":"Shi, J., Ku, X., Zou, X., Hou, J., Yan, W., and Zhang, Y. (2021). Comprehensive Analysis of O-Glycosylation of Amyloid Precursor Protein (APP) Using Targeted and Multi-Fragmentation MS Strategy. Biochim. Biophys. Acta\u2014Gen. Subj., 1865.","DOI":"10.1016\/j.bbagen.2021.129954"},{"key":"ref_116","doi-asserted-by":"crossref","unstructured":"Tachida, Y., Iijima, J., Takahashi, K., Suzuki, H., Kizuka, Y., Yamaguchi, Y., Tanaka, K., Nakano, M., Takakura, D., and Kawasaki, N. (2023). O-GalNAc Glycosylation Determines Intracellular Trafficking of APP and A\u03b2 Production. J. Biol. Chem., 299.","DOI":"10.1016\/j.jbc.2023.104905"},{"key":"ref_117","doi-asserted-by":"crossref","unstructured":"Singh, Y., Regmi, D., Ormaza, D., Ayyalasomayajula, R., Vela, N., Mundim, G., Du, D., Minond, D., and Cudic, M. (2022). Mucin-Type O-Glycosylation Proximal to \u03b2-Secretase Cleavage Site Affects APP Processing and Aggregation Fate. Front. Chem., 10.","DOI":"10.3389\/fchem.2022.859822"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"20216","DOI":"10.1021\/jacs.1c08607","article-title":"O-Glycosylation Induces Amyloid-\u03b2 To Form New Fibril Polymorphs Vulnerable for Degradation","volume":"143","author":"Liu","year":"2021","journal-title":"J. Am. Chem. Soc."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1016\/j.molmed.2022.01.004","article-title":"Role and Therapeutic Implications of Protein Glycosylation in Neuroinflammation","volume":"28","author":"Rebelo","year":"2022","journal-title":"Trends Mol. Med."},{"key":"ref_120","doi-asserted-by":"crossref","unstructured":"Gabriele, R.M.C., Abel, E., Fox, N.C., Wray, S., and Arber, C. (2022). Knockdown of Amyloid Precursor Protein: Biological Consequences and Clinical Opportunities. Front. Neurosci., 16.","DOI":"10.3389\/fnins.2022.835645"},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1186\/1756-6606-4-3","article-title":"APP Processing in Alzheimer\u2019s Disease","volume":"4","author":"Zhang","year":"2011","journal-title":"Mol. Brain"},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1111\/j.1471-4159.2011.07519.x","article-title":"Proteolytic Processing of Alzheimer\u2019s \u0392-amyloid Precursor Protein","volume":"120","author":"Zhang","year":"2012","journal-title":"J. Neurochem."},{"key":"ref_123","doi-asserted-by":"crossref","unstructured":"Pfundstein, G., Nikonenko, A.G., and Sytnyk, V. (2022). Amyloid Precursor Protein (APP) and Amyloid \u03b2 (A\u03b2) Interact with Cell Adhesion Molecules: Implications in Alzheimer\u2019s Disease and Normal Physiology. Front. Cell Dev. Biol., 10.","DOI":"10.3389\/fcell.2022.969547"},{"key":"ref_124","doi-asserted-by":"crossref","unstructured":"Coburger, I., Dahms, S.O., Roeser, D., G\u00fchrs, K.-H., Hortschansky, P., and Than, M.E. (2013). Analysis of the Overall Structure of the Multi-Domain Amyloid Precursor Protein (APP). PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0081926"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"308","DOI":"10.1016\/j.phrs.2010.05.002","article-title":"\u03b2-Amyloid Precursor Protein Metabolism: Focus on the Functions and Degradation of Its Intracellular Domain","volume":"62","author":"Buoso","year":"2010","journal-title":"Pharmacol. Res."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"7817","DOI":"10.1523\/JNEUROSCI.1026-07.2007","article-title":"The Secreted \u03b2-Amyloid Precursor Protein Ectodomain APPs\u03b1 Is Sufficient to Rescue the Anatomical, Behavioral, and Electrophysiological Abnormalities of APP-Deficient Mice","volume":"27","author":"Ring","year":"2007","journal-title":"J. Neurosci."},{"key":"ref_127","doi-asserted-by":"crossref","unstructured":"Orobets, K.S., and Karamyshev, A.L. (2023). Amyloid Precursor Protein and Alzheimer\u2019s Disease. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms241914794"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"658","DOI":"10.4103\/1673-5374.247469","article-title":"Mutations of Beta-Amyloid Precursor Protein Alter the Consequence of Alzheimer\u2019s Disease Pathogenesis","volume":"14","author":"Li","year":"2019","journal-title":"Neural Regen. Res."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"783","DOI":"10.1002\/ana.10208","article-title":"Increased Expression of the Amyloid Precursor \u0392-secretase in Alzheimer\u2019s Disease","volume":"51","author":"Holsinger","year":"2002","journal-title":"Ann. Neurol."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"a024539","DOI":"10.1101\/cshperspect.a024539","article-title":"Genetics of \u03b2-Amyloid Precursor Protein in Alzheimer\u2019s Disease","volume":"7","author":"TCW","year":"2017","journal-title":"Cold Spring Harb. Perspect. Med."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1186\/1750-1326-6-27","article-title":"Biology and Pathophysiology of the Amyloid Precursor Protein","volume":"6","author":"Zheng","year":"2011","journal-title":"Mol. Neurodegener."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"3020","DOI":"10.1038\/emboj.2010.167","article-title":"ADAM10 Is the Physiologically Relevant, Constitutive \u03b1-Secretase of the Amyloid Precursor Protein in Primary Neurons","volume":"29","author":"Kuhn","year":"2010","journal-title":"EMBO J."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1126\/science.286.5440.735","article-title":"\u03b2-Secretase Cleavage of Alzheimer\u2019s Amyloid Precursor Protein by the Transmembrane Aspartic Protease BACE","volume":"286","author":"Vassar","year":"1999","journal-title":"Science"},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"1505","DOI":"10.1016\/S1357-2725(03)00133-X","article-title":"Amyloid Precursor Protein (APP) and the Biology of Proteolytic Processing: Relevance to Alzheimer\u2019s Disease","volume":"35","author":"Ling","year":"2003","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"6438","DOI":"10.1523\/JNEUROSCI.3522-13.2014","article-title":"Genetic Analysis Reveals That Amyloid Precursor Protein and Death Receptor 6 Function in the Same Pathway to Control Axonal Pruning Independent of \u03b2-Secretase","volume":"34","author":"Olsen","year":"2014","journal-title":"J. Neurosci."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"215","DOI":"10.3233\/JAD-150046","article-title":"Modeling the Aggregation Propensity and Toxicity of Amyloid-\u03b2 Variants","volume":"47","author":"Tiwari","year":"2015","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"28176","DOI":"10.1074\/jbc.M803159200","article-title":"The Ratio of Monomeric to Aggregated Forms of A\u03b240 and A\u03b242 Is an Important Determinant of Amyloid-\u03b2 Aggregation, Fibrillogenesis, and Toxicity","volume":"283","author":"Jan","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_138","doi-asserted-by":"crossref","unstructured":"Garc\u00eda-Gonz\u00e1lez, L., Pilat, D., Baranger, K., and Rivera, S. (2019). Emerging Alternative Proteinases in APP Metabolism and Alzheimer\u2019s Disease Pathogenesis: A Focus on MT1-MMP and MT5-MMP. Front. Aging Neurosci., 11.","DOI":"10.3389\/fnagi.2019.00244"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"3167","DOI":"10.1007\/s00018-019-03178-2","article-title":"Metalloproteinases and Their Tissue Inhibitors in Alzheimer\u2019s Disease and Other Neurodegenerative Disorders","volume":"76","author":"Rivera","year":"2019","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1007\/s00018-015-1992-1","article-title":"MT5-MMP Is a New pro-Amyloidogenic Proteinase That Promotes Amyloid Pathology and Cognitive Decline in a Transgenic Mouse Model of Alzheimer\u2019s Disease","volume":"73","author":"Baranger","year":"2016","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"2910","DOI":"10.1096\/fj.201801076R","article-title":"Proamyloidogenic Effects of Membrane Type 1 Matrix Metalloproteinase Involve MMP-2 and BACE-1 Activities, and the Modulation of APP Trafficking","volume":"33","author":"Paumier","year":"2019","journal-title":"FASEB J."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1186\/s12974-022-02407-z","article-title":"MT5-MMP Promotes Neuroinflammation, Neuronal Excitability and A\u03b2 Production in Primary Neuron\/Astrocyte Cultures from the 5xFAD Mouse Model of Alzheimer\u2019s Disease","volume":"19","author":"Pilat","year":"2022","journal-title":"J. Neuroinflamm."},{"key":"ref_143","doi-asserted-by":"crossref","unstructured":"Becker-Pauly, C., and Pietrzik, C.U. (2017). The Metalloprotease Meprin \u03b2 Is an Alternative \u03b2-Secretase of APP. Front. Mol. Neurosci., 9.","DOI":"10.3389\/fnmol.2016.00159"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"33304","DOI":"10.1074\/jbc.M112.395608","article-title":"The Metalloprotease Meprin \u03b2 Generates Amino Terminal-Truncated Amyloid \u03b2 Peptide Species","volume":"287","author":"Bien","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"17768","DOI":"10.1074\/jbc.RA119.008310","article-title":"Phosphorylation of the Amyloid Precursor Protein (APP) at Ser-675 Promotes APP Processing Involving Meprin \u03b2","volume":"294","author":"Menon","year":"2019","journal-title":"J. Biol. Chem."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1111\/febs.16586","article-title":"MT1-MMPand ADAM10 \/17 Exhibit a Remarkable Overlap of Shedding Properties","volume":"290","author":"Werny","year":"2023","journal-title":"FEBS J."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"27741","DOI":"10.1074\/jbc.M111.252718","article-title":"Metalloprotease Meprin \u03b2 Generates Nontoxic N-Terminal Amyloid Precursor Protein Fragments in Vivo","volume":"286","author":"Jefferson","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1007\/s00018-022-04205-5","article-title":"Meprin \u03b2 Knockout Reduces Brain A\u03b2 Levels and Rescues Learning and Memory Impairments in the APP\/Lon Mouse Model for Alzheimer\u2019s Disease","volume":"79","author":"Marengo","year":"2022","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_149","first-page":"2","article-title":"Broadening Horizons: Exploring the Cathepsin Family as Therapeutic Targets for Alzheimer\u2019s Disease","volume":"16","author":"Liu","year":"2024","journal-title":"Aging Dis."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"340","DOI":"10.1007\/s11481-016-9721-6","article-title":"Cathepsin B Improves SS-Amyloidosis and Learning and Memory in Models of Alzheimer\u2019s Disease","volume":"12","author":"Embury","year":"2017","journal-title":"J. Neuroimmune Pharmacol."},{"key":"ref_151","doi-asserted-by":"crossref","unstructured":"Oberstein, T.J., Utz, J., Spitzer, P., Klafki, H.W., Wiltfang, J., Lewczuk, P., Kornhuber, J., and Maler, J.M. (2021). The Role of Cathepsin B in the Degradation of A\u03b2 and in the Production of A\u03b2 Peptides Starting With Ala2 in Cultured Astrocytes. Front. Mol. Neurosci., 13.","DOI":"10.3389\/fnmol.2020.615740"},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"314","DOI":"10.1038\/s41420-023-01617-5","article-title":"New Insight into Protein Glycosylation in the Development of Alzheimer\u2019s Disease","volume":"9","author":"Zhao","year":"2023","journal-title":"Cell Death Discov."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"21304","DOI":"10.1074\/jbc.M117.814202","article-title":"The Small Molecule Luteolin Inhibits N-Acetyl-\u03b1-Galactosaminyltransferases and Reduces Mucin-Type O-Glycosylation of Amyloid Precursor Protein","volume":"292","author":"Liu","year":"2017","journal-title":"J. Biol. Chem."},{"key":"ref_154","doi-asserted-by":"crossref","unstructured":"Haukedal, H., and Freude, K.K. (2021). Implications of Glycosylation in Alzheimer\u2019s Disease. Front. Neurosci., 14.","DOI":"10.3389\/fnins.2020.625348"},{"key":"ref_155","doi-asserted-by":"crossref","unstructured":"Goettig, P. (2016). Effects of Glycosylation on the Enzymatic Activity and Mechanisms of Proteases. Int. J. Mol. Sci., 17.","DOI":"10.3390\/ijms17121969"},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1016\/j.tibs.2018.02.005","article-title":"Fine-Tuning Limited Proteolysis: A Major Role for Regulated Site-Specific O-Glycosylation","volume":"43","author":"Goth","year":"2018","journal-title":"Trends Biochem. Sci."},{"key":"ref_157","doi-asserted-by":"crossref","unstructured":"Kang, Y., Zhang, Q., Xu, S., and Yu, Y. (2024). The Alteration and Role of Glycoconjugates in Alzheimer\u2019s Disease. Front. Aging Neurosci., 16.","DOI":"10.3389\/fnagi.2024.1398641"},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"6277","DOI":"10.1074\/jbc.273.11.6277","article-title":"Cleavage of Alzheimer\u2019s Amyloid Precursor Protein (APP) by Secretases Occurs after O-Glycosylation of APP in the Protein Secretory Pathway","volume":"273","author":"Tomita","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1093\/jb\/mvy121","article-title":"Mucin-Type Glycosylation as a Regulatory Factor of Amyloid Precursor Protein Processing","volume":"165","author":"Nakamura","year":"2019","journal-title":"J. Biochem."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1093\/jb\/mvw056","article-title":"Excess APP O. -Glycosylation by GalNAc-T6 Decreases A\u03b2 Production","volume":"161","author":"Kawamura","year":"2017","journal-title":"J. Biochem."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1016\/j.brainresbull.2021.05.009","article-title":"The Significance of Sialylation on the Pathogenesis of Alzheimer\u2019s Disease","volume":"173","author":"Yang","year":"2021","journal-title":"Brain Res. Bull."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"e13267","DOI":"10.1111\/bpa.13267","article-title":"Distinct Patterns of Plaque and Microglia Glycosylation in Alzheimer\u2019s Disease","volume":"34","author":"Fastenau","year":"2024","journal-title":"Brain Pathol."},{"key":"ref_163","doi-asserted-by":"crossref","unstructured":"Cai, Y., Liu, J., Wang, B., Sun, M., and Yang, H. (2022). Microglia in the Neuroinflammatory Pathogenesis of Alzheimer\u2019s Disease and Related Therapeutic Targets. Front. Immunol., 13.","DOI":"10.3389\/fimmu.2022.856376"},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"e714","DOI":"10.1002\/mco2.714","article-title":"The Interaction of Innate Immune and Adaptive Immune System","volume":"5","author":"Wang","year":"2024","journal-title":"MedComm"},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1186\/s13223-018-0278-1","article-title":"An Introduction to Immunology and Immunopathology","volume":"14","author":"Marshall","year":"2018","journal-title":"Allergy Asthma Clin. Immunol."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"1096","DOI":"10.1038\/nn.3161","article-title":"Immune Surveillance in the Central Nervous System","volume":"15","author":"Ousman","year":"2012","journal-title":"Nat. Neurosci."},{"key":"ref_167","doi-asserted-by":"crossref","unstructured":"Morimoto, K., and Nakajima, K. (2019). Role of the Immune System in the Development of the Central Nervous System. Front. Neurosci., 13.","DOI":"10.3389\/fnins.2019.00916"},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"594","DOI":"10.1186\/1742-2094-9-155","article-title":"Neuroimmune Crosstalk in the Central Nervous System and Its Significance for Neurological Diseases","volume":"9","author":"Tian","year":"2012","journal-title":"J. Neuroinflamm."},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"987","DOI":"10.1038\/nn.4338","article-title":"A Polarizing Question: Do M1 and M2 Microglia Exist?","volume":"19","author":"Ransohoff","year":"2016","journal-title":"Nat. Neurosci."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"826","DOI":"10.1002\/glia.22966","article-title":"Dark Microglia: A New Phenotype Predominantly Associated with Pathological States","volume":"64","author":"Bisht","year":"2016","journal-title":"Glia"},{"key":"ref_171","doi-asserted-by":"crossref","unstructured":"Wang, C., Zong, S., Cui, X., Wang, X., Wu, S., Wang, L., Liu, Y., and Lu, Z. (2023). The Effects of Microglia-Associated Neuroinflammation on Alzheimer\u2019s Disease. Front. Immunol., 14.","DOI":"10.3389\/fimmu.2023.1117172"},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1186\/s12979-024-00445-0","article-title":"Neuroinflammation in Alzheimer\u2019s Disease: Insights from Peripheral Immune Cells","volume":"21","author":"Zhang","year":"2024","journal-title":"Immun. Ageing"},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1186\/1750-1326-6-45","article-title":"Microglial Phagocytosis Induced by Fibrillar \u03b2-Amyloid Is Attenuated by Oligomeric \u03b2-Amyloid: Implications for Alzheimer\u2019s Disease","volume":"6","author":"Pan","year":"2011","journal-title":"Mol. Neurodegener."},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1523\/JNEUROSCI.1698-16.2016","article-title":"Large Soluble Oligomers of Amyloid \u03b2-Protein from Alzheimer Brain Are Far Less Neuroactive Than the Smaller Oligomers to Which They Dissociate","volume":"37","author":"Yang","year":"2017","journal-title":"J. Neurosci."},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1038\/s41593-021-00951-0","article-title":"Microglia Contribute to the Propagation of A\u03b2 into Unaffected Brain Tissue","volume":"25","author":"Aires","year":"2022","journal-title":"Nat. Neurosci."},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"a024398","DOI":"10.1101\/cshperspect.a024398","article-title":"The Prion-Like Properties of Amyloid-\u03b2 Assemblies: Implications for Alzheimer\u2019s Disease","volume":"6","author":"Walker","year":"2016","journal-title":"Cold Spring Harb. Perspect. Med."},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"849","DOI":"10.3233\/JAD-131843","article-title":"Tau Oligomers and Fibrils Induce Activation of Microglial Cells","volume":"37","author":"Morales","year":"2013","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_178","doi-asserted-by":"crossref","unstructured":"Long, H.-Z., Zhou, Z.-W., Cheng, Y., Luo, H.-Y., Li, F.-J., Xu, S.-G., and Gao, L.-C. (2022). The Role of Microglia in Alzheimer\u2019s Disease From the Perspective of Immune Inflammation and Iron Metabolism. Front. Aging Neurosci., 14.","DOI":"10.3389\/fnagi.2022.888989"},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"1283","DOI":"10.1016\/j.neuron.2021.02.010","article-title":"Trem2 Restrains the Enhancement of Tau Accumulation and Neurodegeneration by \u03b2-Amyloid Pathology","volume":"109","author":"Lee","year":"2021","journal-title":"Neuron"},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"416","DOI":"10.1016\/S1474-4422(21)00133-2","article-title":"TREM2-Mediated Activation of Microglia Breaks Link between Amyloid and Tau","volume":"20","author":"Hardy","year":"2021","journal-title":"Lancet Neurol."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"1472","DOI":"10.1042\/BST0361472","article-title":"Galectin\u2013Glycan Lattices Regulate Cell-Surface Glycoprotein Organization and Signalling","volume":"36","author":"Garner","year":"2008","journal-title":"Biochem. Soc. Trans."},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"1101","DOI":"10.1038\/s41423-023-01074-1","article-title":"Immune Regulatory Networks Coordinated by Glycans and Glycan-Binding Proteins in Autoimmunity and Infection","volume":"20","author":"Pinho","year":"2023","journal-title":"Cell. Mol. Immunol."},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"1383","DOI":"10.1073\/pnas.72.4.1383","article-title":"A Beta-D-Galactoside Binding Protein from Electric Organ Tissue of Electrophorus Electricus","volume":"72","author":"Teichberg","year":"1975","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1038\/s41577-022-00829-7","article-title":"The Role of Galectins in Immunity and Infection","volume":"23","author":"Liu","year":"2023","journal-title":"Nat. Rev. Immunol."},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1038\/nrc1527","article-title":"Galectins as Modulators of Tumour Progression","volume":"5","author":"Liu","year":"2005","journal-title":"Nat. Rev. Cancer"},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"7842","DOI":"10.1021\/bi201121m","article-title":"When Galectins Recognize Glycans: From Biochemistry to Physiology and Back Again","volume":"50","author":"Sundblad","year":"2011","journal-title":"Biochemistry"},{"key":"ref_187","doi-asserted-by":"crossref","unstructured":"Tazhitdinova, R., and Timoshenko, A.V. (2020). The Emerging Role of Galectins and O-GlcNAc Homeostasis in Processes of Cellular Differentiation. Cells, 9.","DOI":"10.3390\/cells9081792"},{"key":"ref_188","doi-asserted-by":"crossref","unstructured":"Troncoso, M.F., Elola, M.T., Blidner, A.G., Sarrias, L., Espelt, M.V., and Rabinovich, G.A. (2023). The Universe of Galectin-Binding Partners and Their Functions in Health and Disease. J. Biol. Chem., 299.","DOI":"10.1016\/j.jbc.2023.105400"},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"20249","DOI":"10.1074\/jbc.RA118.004636","article-title":"Galectin Binding to Cells and Glycoproteins with Genetically Modified Glycosylation Reveals Galectin\u2013Glycan Specificities in a Natural Context","volume":"293","author":"Nielsen","year":"2018","journal-title":"J. Biol. Chem."},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"3195","DOI":"10.1158\/0008-5472.CAN-15-0834","article-title":"Galectin-Binding O-Glycosylations as Regulators of Malignancy","volume":"75","author":"Dimitroff","year":"2015","journal-title":"Cancer Res."},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"5697","DOI":"10.4049\/jimmunol.167.10.5697","article-title":"CD45 Modulates Galectin-1-Induced T Cell Death: Regulation by Expression of Core 2 O-Glycans","volume":"167","author":"Nguyen","year":"2001","journal-title":"J. Immunol."},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"4635","DOI":"10.1182\/blood-2012-06-438234","article-title":"Galectin-3 Binds to CD45 on Diffuse Large B-Cell Lymphoma Cells to Regulate Susceptibility to Cell Death","volume":"120","author":"Clark","year":"2012","journal-title":"Blood"},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"981","DOI":"10.1038\/ni.1772","article-title":"Tolerogenic Signals Delivered by Dendritic Cells to T Cells through a Galectin-1-Driven Immunoregulatory Circuit Involving Interleukin 27 and Interleukin 10","volume":"10","author":"Ilarregui","year":"2009","journal-title":"Nat. Immunol."},{"key":"ref_194","doi-asserted-by":"crossref","unstructured":"Siew, J.J., and Chern, Y. (2018). Microglial Lectins in Health and Neurological Diseases. Front. Mol. Neurosci., 11.","DOI":"10.3389\/fnmol.2018.00158"},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1007\/s00401-022-02469-6","article-title":"Galectin-3 Is Elevated in CSF and Is Associated with A\u03b2 Deposits and Tau Aggregates in Brain Tissue in Alzheimer\u2019s Disease","volume":"144","author":"Vrillon","year":"2022","journal-title":"Acta Neuropathol."},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1038\/s41418-019-0348-z","article-title":"Galectin-3 Promotes A\u03b2 Oligomerization and A\u03b2 Toxicity in a Mouse Model of Alzheimer\u2019s Disease","volume":"27","author":"Tao","year":"2020","journal-title":"Cell Death Differ."},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"e165523","DOI":"10.1172\/JCI165523","article-title":"Galectin-3 Aggravates Microglial Activation and Tau Transmission in Tauopathy","volume":"134","author":"Siew","year":"2024","journal-title":"J. Clin. Investig."},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"101117","DOI":"10.1016\/j.mam.2022.101117","article-title":"Discovery, Classification, Evolution and Diversity of Siglecs","volume":"90","author":"Angata","year":"2023","journal-title":"Mol. Aspects Med."},{"key":"ref_199","doi-asserted-by":"crossref","unstructured":"Ayyalasomayajula, R., and Cudic, M. (2024). Targeting Siglec\u2013Sialylated MUC1 Immune Axis in Cancer. Cancers, 16.","DOI":"10.3390\/cancers16071334"},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1038\/nri2056","article-title":"Siglecs and Their Roles in the Immune System","volume":"7","author":"Crocker","year":"2007","journal-title":"Nat. Rev. Immunol."},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"3637","DOI":"10.4049\/jimmunol.166.6.3637","article-title":"Cutting Edge: CD43 Functions as a T Cell Counterreceptor for the Macrophage Adhesion Receptor Sialoadhesin (Siglec-1)","volume":"166","author":"Nath","year":"2001","journal-title":"J. Immunol."},{"key":"ref_202","doi-asserted-by":"crossref","unstructured":"Stewart, N., Daly, J., Drummond-Guy, O., Krishnamoorthy, V., Stark, J.C., Riley, N.M., Williams, K.C., Bertozzi, C.R., and Wisnovsky, S. (2024). The Glycoimmune Checkpoint Receptor Siglec-7 Interacts with T-Cell Ligands and Regulates T-Cell Activation. J. Biol. Chem., 300.","DOI":"10.1016\/j.jbc.2023.105579"},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1093\/glycob\/cws139","article-title":"The Interaction between Siglec-15 and Tumor-Associated Sialyl-Tn Antigen Enhances TGF- Secretion from Monocytes\/Macrophages through the DAP12-Syk Pathway","volume":"23","author":"Takamiya","year":"2013","journal-title":"Glycobiology"},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"e2026102118","DOI":"10.1073\/pnas.2026102118","article-title":"Probing the Binding Specificities of Human Siglecs by Cell-Based Glycan Arrays","volume":"118","author":"Nason","year":"2021","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"101141","DOI":"10.1016\/j.mam.2022.101141","article-title":"Roles of Siglecs in Neurodegenerative Diseases","volume":"90","author":"Siew","year":"2023","journal-title":"Mol. Aspects Med."},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"101111","DOI":"10.1016\/j.mam.2022.101111","article-title":"CD33 Isoforms in Microglia and Alzheimer\u2019s Disease: Friend and Foe","volume":"90","author":"Jung","year":"2023","journal-title":"Mol. Aspects Med."},{"key":"ref_207","doi-asserted-by":"crossref","first-page":"eabm5667","DOI":"10.1126\/sciadv.abm5667","article-title":"Associations of Plasma Soluble CD22 Levels with Brain Amyloid Burden and Cognitive Decline in Alzheimer\u2019s Disease","volume":"8","author":"Bu","year":"2022","journal-title":"Sci. Adv."},{"key":"ref_208","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1111\/neup.12277","article-title":"Hypersialylation Is a Common Feature of Neurofibrillary Tangles and Granulovacuolar Degenerations in Alzheimer\u2019s Disease and Tauopathy Brains","volume":"36","author":"Nagamine","year":"2016","journal-title":"Neuropathology"},{"key":"ref_209","doi-asserted-by":"crossref","first-page":"6179","DOI":"10.1111\/j.1742-4658.2005.05031.x","article-title":"The C-type Lectin-like Domain Superfamily","volume":"272","author":"Zelensky","year":"2005","journal-title":"FEBS J."},{"key":"ref_210","doi-asserted-by":"crossref","first-page":"5790","DOI":"10.1016\/j.csbj.2022.10.019","article-title":"From Structure to Function\u2014Ligand Recognition by Myeloid C-Type Lectin Receptors","volume":"20","author":"Fischer","year":"2022","journal-title":"Comput. Struct. Biotechnol. J."},{"key":"ref_211","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1038\/35092620","article-title":"A New Receptor for \u03b2-Glucans","volume":"413","author":"Brown","year":"2001","journal-title":"Nature"},{"key":"ref_212","doi-asserted-by":"crossref","first-page":"700","DOI":"10.1016\/j.immuni.2024.03.005","article-title":"Myeloid C-Type Lectin Receptors in Innate Immune Recognition","volume":"57","author":"Yamasaki","year":"2024","journal-title":"Immunity"},{"key":"ref_213","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1111\/j.1749-6632.2012.06492.x","article-title":"Glycobiology of Immune Responses","volume":"1253","author":"Rabinovich","year":"2012","journal-title":"Ann. N. Y Acad. Sci."},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"1200","DOI":"10.1038\/ni1390","article-title":"Regulation of Effector T Cells by Antigen-Presenting Cells via Interaction of the C-Type Lectin MGL with CD45","volume":"7","author":"Gringhuis","year":"2006","journal-title":"Nat. Immunol."},{"key":"ref_215","doi-asserted-by":"crossref","first-page":"250","DOI":"10.1111\/ane.13196","article-title":"C-type Lectin-like Receptor 2 and Zonulin Are Associated with Mild Cognitive Impairment and Alzheimer\u2019s Disease","volume":"141","author":"Wang","year":"2020","journal-title":"Acta Neurol. Scand."},{"key":"ref_216","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1007\/s12640-020-00295-w","article-title":"A Role of the Podoplanin-CLEC-2 Axis in Promoting Inflammatory Response After Ischemic Stroke in Mice","volume":"39","author":"Meng","year":"2021","journal-title":"Neurotox. Res."},{"key":"ref_217","doi-asserted-by":"crossref","unstructured":"Szczykutowicz, J. (2023). Ligand Recognition by the Macrophage Galactose-Type C-Type Lectin: Self or Non-Self?\u2014A Way to Trick the Host\u2019s Immune System. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms242317078"},{"key":"ref_218","doi-asserted-by":"crossref","first-page":"879","DOI":"10.1093\/glycob\/cwad083","article-title":"Tn Antigen Interactions of Macrophage Galactose-Type Lectin (MGL) in Immune Function and Disease","volume":"33","author":"Tumoglu","year":"2023","journal-title":"Glycobiology"},{"key":"ref_219","doi-asserted-by":"crossref","first-page":"2172","DOI":"10.1021\/acschembio.7b00471","article-title":"GalNAc-Tyrosine Is a Ligand of Plant Lectins, Antibodies, and Human and Murine Macrophage Galactose-Type Lectins","volume":"12","author":"Gibadullin","year":"2017","journal-title":"ACS Chem. Biol."},{"key":"ref_220","doi-asserted-by":"crossref","first-page":"1300","DOI":"10.1074\/jbc.RA118.004957","article-title":"Identification of a Secondary Binding Site in Human Macrophage Galactose-Type Lectin by Microarray Studies: Implications for the Molecular Recognition of Its Ligands","volume":"294","author":"Marcelo","year":"2019","journal-title":"J. Biol. Chem."},{"key":"ref_221","doi-asserted-by":"crossref","first-page":"1327","DOI":"10.1021\/acs.biochem.1c00009","article-title":"Crystal Structure of the Carbohydrate Recognition Domain of the Human Macrophage Galactose C-Type Lectin Bound to GalNAc and the Tumor-Associated Tn Antigen","volume":"60","author":"Gabba","year":"2021","journal-title":"Biochemistry"}],"container-title":["Molecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1420-3049\/30\/9\/1895\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,9]],"date-time":"2025-10-09T17:20:43Z","timestamp":1760030443000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1420-3049\/30\/9\/1895"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,4,24]]},"references-count":221,"journal-issue":{"issue":"9","published-online":{"date-parts":[[2025,5]]}},"alternative-id":["molecules30091895"],"URL":"https:\/\/doi.org\/10.3390\/molecules30091895","relation":{},"ISSN":["1420-3049"],"issn-type":[{"value":"1420-3049","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,4,24]]}}}