{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,14]],"date-time":"2026-10-14T02:29:17Z","timestamp":1791944957031,"version":"4.3.4"},"reference-count":229,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2026,6,3]],"date-time":"2026-06-03T00:00:00Z","timestamp":1780444800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Dement."],"abstract":"<jats:p>Tau is an intrinsically disordered microtubule-associated protein that performs diverse roles in neuronal physiology, including regulation of microtubule stability, intracellular transport, and synaptic signaling. These functions are dynamically regulated by an extensive array of post-translational modifications (PTMs) that collectively shape tau conformation, interactions, localization, and turnover. Under physiological conditions, PTMs act as a regulatory system that enables tau to transition between functional states in response to cellular cues. In neurodegenerative diseases collectively known as tauopathies, however, this finely balanced modification landscape becomes disrupted, leading to tau mislocalization, impaired clearance, and assembly into toxic oligomers and fibrillar aggregates. Although phosphorylation has historically dominated the tau field, growing evidence indicates that multiple PTMs, including acetylation, ubiquitination, truncation, oxidation, nitration, methylation, and glycosylation, cooperatively influence tau structure and pathogenic potential. Recent proteomic studies reveal that tau can harbor dozens of modifications simultaneously, highlighting the importance of understanding PTMs as an integrated regulatory network rather than independent events. Crosstalk between modifications can generate synergistic or antagonistic effects that influence tau aggregation, proteostasis, and propagation. In this review, we synthesize current knowledge of major tau PTMs and highlight emerging principles governing their interactions. We discuss how dysregulation of PTM networks contributes to tau state transitions during aging and neurodegeneration and consider how targeting PTM-regulating enzymes may provide therapeutic strategies for Alzheimer\u2019s disease and related tauopathies.<\/jats:p>","DOI":"10.3389\/frdem.2026.1834737","type":"journal-article","created":{"date-parts":[[2026,6,3]],"date-time":"2026-06-03T04:50:57Z","timestamp":1780462257000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":4,"title":["Post-translational modifications as a regulatory code for tau function in health and disease"],"prefix":"10.3389","volume":"5","author":[{"given":"Abigail J.","family":"Nordbeck","sequence":"first","affiliation":[{"name":"Arizona State University-Banner Neurodegenerative Disease Research Center at the Biodesign Institute","place":["Tempe, AZ, United States"]},{"name":"School of Life Sciences, Arizona State University","place":["Tempe, AZ, United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bhirisha","family":"Sharma","sequence":"additional","affiliation":[{"name":"Arizona State University-Banner Neurodegenerative Disease Research Center at the Biodesign Institute","place":["Tempe, AZ, United States"]},{"name":"School of Life Sciences, Arizona State University","place":["Tempe, AZ, United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Charles A.","family":"Garcia","sequence":"additional","affiliation":[{"name":"Arizona State University-Banner Neurodegenerative Disease Research Center at the Biodesign Institute","place":["Tempe, AZ, United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jui-Heng","family":"Tseng","sequence":"additional","affiliation":[{"name":"Arizona State University-Banner Neurodegenerative Disease Research Center at the Biodesign Institute","place":["Tempe, AZ, United States"]},{"name":"School of Life Sciences, Arizona State University","place":["Tempe, AZ, United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2026,6,3]]},"reference":[{"key":"ref1","doi-asserted-by":"publisher","first-page":"251","DOI":"10.1038\/s42003-024-05920-4","article-title":"Phosphorylation regulates tau\u2019s phase separation behavior and interactions with chromatin","volume":"7","author":"Abasi","year":"2024","journal-title":"Communications Biology"},{"key":"ref2","doi-asserted-by":"publisher","first-page":"7905","DOI":"10.1074\/jbc.RA119.012517","article-title":"Phosphorylation of the overlooked tyrosine 310 regulates the structure, aggregation, and microtubule- and lipid-binding properties of tau","volume":"295","author":"Ait-Bouziad","year":"2020","journal-title":"J. Biol. Chem."},{"key":"ref3","doi-asserted-by":"publisher","first-page":"301","DOI":"10.1042\/BST20230596","article-title":"Biochemical approaches to assess the impact of post-translational modifications on pathogenic tau conformations using recombinant protein","volume":"52","author":"Alhadidy","year":"2024","journal-title":"Biochem. Soc. Trans."},{"key":"ref4","doi-asserted-by":"publisher","first-page":"699","DOI":"10.2174\/1389203721666200507091952","article-title":"Non-histone arginine methylation by protein arginine methyltransferases","volume":"21","author":"Al-Hamashi","year":"2020","journal-title":"Curr. Protein Pept. Sci."},{"key":"ref5","doi-asserted-by":"publisher","first-page":"1216","DOI":"10.1021\/acs.chemrev.7b00181","article-title":"Lysine acetylation Goes global: from epigenetics to metabolism and therapeutics","volume":"118","author":"Ali","year":"2018","journal-title":"Chem. Rev."},{"key":"ref6","doi-asserted-by":"publisher","first-page":"595532","DOI":"10.3389\/fneur.2020.595532","article-title":"Tau post-translational modifications: dynamic transformers of tau function, degradation, and aggregation","volume":"11","author":"Alquezar","year":"2020","journal-title":"Front. Neurol."},{"key":"ref7","doi-asserted-by":"publisher","first-page":"295","DOI":"10.1007\/s00726-003-0018-8","article-title":"Peroxynitrite reactivity with amino acids and proteins","volume":"25","author":"Alvarez","year":"2003","journal-title":"Amino Acids"},{"key":"ref8","doi-asserted-by":"publisher","first-page":"685","DOI":"10.1016\/j.freeradbiomed.2024.09.021","article-title":"The effect of tau K677 lactylation on ferritinophagy and ferroptosis in Alzheimer's disease","volume":"224","author":"An","year":"2024","journal-title":"Free Radic. Biol. Med."},{"key":"ref9","doi-asserted-by":"publisher","first-page":"91","DOI":"10.1016\/j.bbadis.2004.08.010","article-title":"Tau gene alternative splicing: expression patterns, regulation and modulation of function in normal brain and neurodegenerative diseases","volume":"1739","author":"Andreadis","year":"2005","journal-title":"Biochim. Biophys. Acta"},{"key":"ref10","doi-asserted-by":"publisher","first-page":"1510","DOI":"10.1021\/acs.jproteome.2c00131","article-title":"Profiling the human Phosphoproteome to estimate the true extent of protein phosphorylation","volume":"21","author":"Anton Kalyuzhnyy","year":"2022","journal-title":"J. Proteome Res."},{"key":"ref11","doi-asserted-by":"publisher","first-page":"72","DOI":"10.1038\/s41593-017-0022-z","article-title":"Reducing the RNA binding protein TIA1 protects against tau-mediated neurodegeneration in vivo","volume":"21","author":"Apicco","year":"2018","journal-title":"Nat. Neurosci."},{"key":"ref12","doi-asserted-by":"publisher","first-page":"633","DOI":"10.1016\/j.cell.2020.01.027","article-title":"Posttranslational modifications mediate the structural diversity of Tauopathy strains","volume":"180","author":"Arakhamia","year":"2020","journal-title":"Cell"},{"key":"ref13","doi-asserted-by":"publisher","first-page":"271","DOI":"10.3892\/ijmm.2017.3036","article-title":"The crucial role of protein phosphorylation in cell signaling and its use as targeted therapy (review)","volume":"40","author":"Ardito","year":"2017","journal-title":"Int. J. Mol. Med."},{"key":"ref14","doi-asserted-by":"publisher","first-page":"28741","DOI":"10.1074\/jbc.271.46.28741","article-title":"The microtubule-associated protein tau is extensively modified with O-linked N-acetylglucosamine","volume":"271","author":"Arnold","year":"1996","journal-title":"J. Biol. Chem."},{"key":"ref15","doi-asserted-by":"publisher","first-page":"358","DOI":"10.1038\/s42003-022-03312-0","article-title":"Failure of DNA double-strand break repair by tau mediates Alzheimer's disease pathology in vitro","volume":"5","author":"Asada-Utsugi","year":"2022","journal-title":"Commun Biol"},{"key":"ref16","doi-asserted-by":"publisher","first-page":"709","DOI":"10.1007\/s00401-021-02275-6","article-title":"Plasma p-tau231: a new biomarker for incipient Alzheimer's disease pathology","volume":"141","author":"Ashton","year":"2021","journal-title":"Acta Neuropathol."},{"key":"ref17","doi-asserted-by":"publisher","first-page":"130014","DOI":"10.1016\/j.bbagen.2021.130014","article-title":"Characterizing the role of the dark kinome in neurodegenerative disease \u2013 a mini review","volume":"1865","author":"Axtman","year":"2021","journal-title":"Biochim. Biophys. Acta Gen. Subj."},{"key":"ref18","doi-asserted-by":"publisher","first-page":"51","DOI":"10.1186\/s12964-021-00732-z","article-title":"Methylation as a key regulator of tau aggregation and neuronal health in Alzheimer's disease","volume":"19","author":"Balmik","year":"2021","journal-title":"Cell Commun. Signal"},{"key":"ref19","doi-asserted-by":"publisher","first-page":"836","DOI":"10.1021\/tx9501445","article-title":"Oxidative damage and tyrosine nitration from peroxynitrite","volume":"9","author":"Beckman","year":"1996","journal-title":"Chem. Res. Toxicol."},{"key":"ref20","doi-asserted-by":"publisher","first-page":"D529","DOI":"10.1093\/nar\/gkaa853","article-title":"The dark kinase knowledgebase: an online compendium of knowledge and experimental results of understudied kinases","volume":"49","author":"Berginski","year":"2020","journal-title":"Nucleic Acids Res."},{"key":"ref21","doi-asserted-by":"publisher","first-page":"20","DOI":"10.1006\/bbrc.2001.5116","article-title":"Role of cysteine-291 and cysteine-322 in the polymerization of human tau into Alzheimer-like filaments","volume":"285","author":"Bhattacharya","year":"2001","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref22","doi-asserted-by":"publisher","first-page":"14569","DOI":"10.1074\/jbc.M114.563031","article-title":"Lysine 27 ubiquitination of the mitochondrial transport protein Miro is dependent on serine 65 of the Parkin ubiquitin ligase","volume":"289","author":"Birsa","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref23","doi-asserted-by":"publisher","first-page":"2884","DOI":"10.3390\/biomedicines13122884","article-title":"Unlocking the sugar code: implications and consequences of glycosylation in Alzheimer's disease and other Tauopathies","volume":"13","author":"Bondar","year":"2025","journal-title":"Biomedicine"},{"key":"ref24","doi-asserted-by":"publisher","first-page":"702788","DOI":"10.3389\/fnins.2021.702788","article-title":"Human tau isoforms and proteolysis for production of toxic tau fragments in neurodegeneration","volume":"15","author":"Boyarko","year":"2021","journal-title":"Front. Neurosci."},{"key":"ref25","doi-asserted-by":"publisher","first-page":"163","DOI":"10.1186\/s40478-024-01865-1","article-title":"Development and characterization of novel anti-acetylated tau monoclonal antibodies to probe pathogenic tau species in Alzheimer's disease","volume":"12","author":"BryanIii","year":"2024","journal-title":"Acta Neuropathol. Commun."},{"key":"ref26","doi-asserted-by":"publisher","first-page":"3606","DOI":"10.1002\/alz.13784","article-title":"The six brain-specific TAU isoforms and their role in Alzheimer's disease and related neurodegenerative dementia syndromes","volume":"20","author":"Buchholz","year":"2024","journal-title":"Alzheimers Dement."},{"key":"ref27","doi-asserted-by":"publisher","first-page":"e12692","DOI":"10.1111\/acel.12692","article-title":"Interplay of pathogenic forms of human tau with different autophagic pathways","volume":"17","author":"Caballero","year":"2018","journal-title":"Aging Cell"},{"key":"ref28","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.neuroscience.2025.08.048","article-title":"Lactate lactylation in neural pathophysiology: bridging metabolism and neurodegeneration","volume":"585","author":"Cao","year":"2025","journal-title":"Neuroscience"},{"key":"ref29","doi-asserted-by":"publisher","first-page":"15277","DOI":"10.1074\/jbc.M117.794602","article-title":"An acetylation-phosphorylation switch that regulates tau aggregation propensity and function","volume":"292","author":"Carlomagno","year":"2017","journal-title":"J. Biol. Chem."},{"key":"ref30","doi-asserted-by":"publisher","first-page":"1678595","DOI":"10.3389\/fneur.2025.1678595","article-title":"The metabolic-epigenetic interface: lysine succinylation orchestrates bidirectional crosstalk in neurodegenerative disorders","volume":"16","author":"Chai","year":"2025","journal-title":"Front. Neurol."},{"key":"ref31","doi-asserted-by":"publisher","first-page":"34457","DOI":"10.1074\/jbc.M111.229633","article-title":"Passive immunization with anti-tau antibodies in two transgenic models: reduction of tau pathology and delay of disease progression","volume":"286","author":"Chai","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref32","doi-asserted-by":"publisher","first-page":"5919","DOI":"10.1038\/s41467-023-41672-1","article-title":"Acetylation discriminates disease-specific tau deposition","volume":"14","author":"Chakraborty","year":"2023","journal-title":"Nat. Commun."},{"key":"ref33","doi-asserted-by":"publisher","first-page":"21","DOI":"10.3390\/antiox13010021","article-title":"Role of oxidative stress, methionine oxidation and methionine sulfoxide reductases (MSR) in Alzheimer's disease","volume":"13","author":"Chandran","year":"2023","journal-title":"Antioxidants (Basel)"},{"key":"ref34","doi-asserted-by":"publisher","first-page":"2","DOI":"10.1186\/s13024-019-0354-0","article-title":"Promoting tau secretion and propagation by hyperactive p300\/CBP via autophagy-lysosomal pathway in tauopathy","volume":"15","author":"Chen","year":"2020","journal-title":"Mol. Neurodegener."},{"key":"ref35","doi-asserted-by":"publisher","first-page":"275","DOI":"10.1016\/j.molcel.2009.01.014","article-title":"Nonproteolytic functions of ubiquitin in cell signaling","volume":"33","author":"Chen","year":"2009","journal-title":"Mol. Cell"},{"key":"ref36","doi-asserted-by":"publisher","first-page":"355","DOI":"10.1016\/bs.apcsb.2025.02.001","article-title":"SUMO inhibits tau aggregation in Alzheimer's disease","volume":"147","author":"Chinnathambi","year":"2025","journal-title":"Adv. Protein Chem. Struct. Biol."},{"key":"ref37","doi-asserted-by":"publisher","first-page":"e13081","DOI":"10.1111\/acel.13081","article-title":"Acetylation changes tau interactome to degrade tau in Alzheimer's disease animal and organoid models","volume":"19","author":"Choi","year":"2020","journal-title":"Aging Cell"},{"key":"ref38","doi-asserted-by":"publisher","first-page":"1221","DOI":"10.4103\/1673-5374.385853","article-title":"Tau truncation in the pathogenesis of Alzheimer's disease: a narrative review","volume":"19","author":"Chu","year":"2024","journal-title":"Neural Regen. Res."},{"key":"ref39","doi-asserted-by":"publisher","first-page":"61","DOI":"10.1016\/j.bbrc.2022.08.093","article-title":"Emerging role of protein modification by UFM1 in cancer","volume":"633","author":"Chung","year":"2022","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref40","doi-asserted-by":"publisher","first-page":"179","DOI":"10.1016\/j.molcel.2010.09.019","article-title":"The DNA damage response: making it safe to play with knives","volume":"40","author":"Ciccia","year":"2010","journal-title":"Mol. Cell"},{"key":"ref41","doi-asserted-by":"publisher","first-page":"207","DOI":"10.1016\/0022-2836(77)90213-3","article-title":"Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin","volume":"116","author":"Cleveland","year":"1977","journal-title":"J. Mol. Biol."},{"key":"ref42","doi-asserted-by":"publisher","first-page":"756","DOI":"10.1038\/nsmb.2555","article-title":"The microtubule-associated tau protein has intrinsic acetyltransferase activity","volume":"20","author":"Cohen","year":"2013","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref43","doi-asserted-by":"publisher","first-page":"252","DOI":"10.1038\/ncomms1255","article-title":"The acetylation of tau inhibits its function and promotes pathological tau aggregation","volume":"2","author":"Cohen","year":"2011","journal-title":"Nat. Commun."},{"key":"ref44","doi-asserted-by":"publisher","first-page":"689","DOI":"10.1038\/174689a0","article-title":"Free radicals in biological materials","volume":"174","author":"Commoner","year":"1954","journal-title":"Nature"},{"key":"ref45","doi-asserted-by":"publisher","first-page":"104","DOI":"10.1093\/hmg\/ddt402","article-title":"Acetylation of the KXGS motifs in tau is a critical determinant in modulation of tau aggregation and clearance","volume":"23","author":"Cook","year":"2014","journal-title":"Hum. Mol. Genet."},{"key":"ref46","doi-asserted-by":"publisher","first-page":"15383","DOI":"10.3390\/ijms232315383","article-title":"Tau isoforms: gaining insight into MAPT alternative splicing","volume":"23","author":"Corsi","year":"2022","journal-title":"Int. J. Mol. Sci."},{"key":"ref47","doi-asserted-by":"publisher","first-page":"10825","DOI":"10.1074\/jbc.M512786200","article-title":"Alzheimer disease-specific conformation of hyperphosphorylated paired helical filament-tau is polyubiquitinated through Lys-48, Lys-11, and Lys-6 ubiquitin conjugation","volume":"281","author":"Cripps","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref49","doi-asserted-by":"publisher","first-page":"160","DOI":"10.1038\/ncb3097","article-title":"USP30 and parkin homeostatically regulate atypical ubiquitin chains on mitochondria","volume":"17","author":"Cunningham","year":"2015","journal-title":"Nat. Cell Biol."},{"key":"ref50","doi-asserted-by":"publisher","first-page":"423","DOI":"10.1038\/s41418-020-00703-w","article-title":"The ubiquitin system: from cell signalling to disease biology and new therapeutic opportunities","volume":"28","author":"Damgaard","year":"2021","journal-title":"Cell Death Differ."},{"key":"ref51","doi-asserted-by":"publisher","first-page":"2419","DOI":"10.1021\/cr500452k","article-title":"Protein lysine acetylation by p300\/CBP","volume":"115","author":"Dancy","year":"2015","journal-title":"Chem. Rev."},{"key":"ref52","doi-asserted-by":"publisher","first-page":"17290","DOI":"10.7554\/eLife.17290","article-title":"Functional CRISPR screening identifies the ufmylation pathway as a regulator of SQSTM1\/p62","volume":"5","author":"DeJesus","year":"2016","journal-title":"eLife"},{"key":"ref53","first-page":"244","article-title":"Tauopathies: recent insights into old diseases","volume":"43","author":"Delacourte","year":"2005","journal-title":"Folia Neuropathol."},{"key":"ref54","doi-asserted-by":"publisher","first-page":"138","DOI":"10.1096\/fj.07-8309com","article-title":"Regulation between O-GlcNAcylation and phosphorylation of neurofilament-M and their dysregulation in Alzheimer disease","volume":"22","author":"Deng","year":"2008","journal-title":"FASEB J."},{"key":"ref55","doi-asserted-by":"publisher","first-page":"238","DOI":"10.1021\/acschembio.0c00771","article-title":"Non-histone protein methylation: biological significance and bioengineering potential","volume":"16","author":"Di Blasi","year":"2021","journal-title":"ACS Chem. Biol."},{"key":"ref56","doi-asserted-by":"publisher","first-page":"766","DOI":"10.1039\/B704905F","article-title":"O-GlcNAc modification in diabetes and Alzheimer's disease","volume":"3","author":"Dias","year":"2007","journal-title":"Mol. BioSyst."},{"key":"ref57","doi-asserted-by":"publisher","first-page":"1043","DOI":"10.3389\/fimmu.2019.01043","article-title":"Cellular specificity of NF-kappaB function in the nervous system","volume":"10","author":"Dresselhaus","year":"2019","journal-title":"Front. Immunol."},{"key":"ref58","doi-asserted-by":"publisher","first-page":"1027","DOI":"10.3390\/cells3041027","article-title":"Versatile roles of k63-linked ubiquitin chains in trafficking","volume":"3","author":"Erpapazoglou","year":"2014","journal-title":"Cells"},{"key":"ref59","doi-asserted-by":"publisher","first-page":"655","DOI":"10.1038\/s41419-018-0688-5","article-title":"The novel histone de acetylase 6 inhibitor, MPT0G211, ameliorates tau phosphorylation and cognitive deficits in an Alzheimer's disease model","volume":"9","author":"Fan","year":"2018","journal-title":"Cell Death Dis."},{"key":"ref61","doi-asserted-by":"publisher","first-page":"167","DOI":"10.3389\/fnmol.2017.00167","article-title":"Cysteines as redox molecular switches and targets of disease","volume":"10","author":"Fra","year":"2017","journal-title":"Front. Mol. Neurosci."},{"key":"ref62","doi-asserted-by":"publisher","first-page":"927630","DOI":"10.3389\/fragi.2022.927630","article-title":"Proteolysis dysfunction in the process of aging and age-related diseases","volume":"3","author":"Frankowska","year":"2022","journal-title":"Front Aging"},{"key":"ref63","doi-asserted-by":"publisher","first-page":"6","DOI":"10.1038\/s41421-020-00237-y","article-title":"Emerging functions of branched ubiquitin chains","volume":"7","author":"French","year":"2021","journal-title":"Cell Discov."},{"key":"ref64","doi-asserted-by":"publisher","first-page":"77","DOI":"10.1042\/BJ20140372","article-title":"Lysine methylation is an endogenous post-translational modification of tau protein in human brain and a modulator of aggregation propensity","volume":"462","author":"Funk","year":"2014","journal-title":"Biochem. J."},{"key":"ref65","doi-asserted-by":"publisher","first-page":"226","DOI":"10.1016\/j.celrep.2014.12.021","article-title":"RNF168 promotes noncanonical K27 ubiquitination to signal DNA damage","volume":"10","author":"Gatti","year":"2015","journal-title":"Cell Rep."},{"key":"ref66","doi-asserted-by":"publisher","first-page":"29","DOI":"10.3389\/fgene.2018.00029","article-title":"A comprehensive atlas of E3 ubiquitin ligase mutations in neurological disorders","volume":"9","author":"George","year":"2018","journal-title":"Front. Genet."},{"key":"ref67","doi-asserted-by":"publisher","first-page":"974","DOI":"10.1016\/j.tcb.2019.09.005","article-title":"The UFMylation system in Proteostasis and beyond","volume":"29","author":"Gerakis","year":"2019","journal-title":"Trends Cell Biol."},{"key":"ref68","doi-asserted-by":"publisher","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":"Alzheimers Dement."},{"key":"ref69","doi-asserted-by":"publisher","first-page":"fcaf221","DOI":"10.1093\/braincomms\/fcaf221","article-title":"The potential dual role of tau phosphorylation: plasma phosphorylated-tau217 in newborns and Alzheimer's disease","volume":"7","author":"Gonzalez-Ortiz","year":"2025","journal-title":"Brain Commun"},{"key":"ref70","doi-asserted-by":"publisher","first-page":"9984","DOI":"10.1038\/s41598-017-10225-0","article-title":"Pseudo-acetylation of multiple sites on human tau proteins alters tau phosphorylation and microtubule binding, and ameliorates amyloid beta toxicity","volume":"7","author":"Gorsky","year":"2017","journal-title":"Sci. Rep."},{"key":"ref71","doi-asserted-by":"publisher","first-page":"307","DOI":"10.1016\/j.neuropharm.2013.11.025","article-title":"Increased O-GlcNAcylation reduces pathological tau without affecting its normal phosphorylation in a mouse model of tauopathy","volume":"79","author":"Graham","year":"2014","journal-title":"Neuropharmacology"},{"key":"ref72","doi-asserted-by":"publisher","first-page":"4913","DOI":"10.1073\/pnas.83.13.4913","article-title":"Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology","volume":"83","author":"Grundke-Iqbal","year":"1986","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref73","doi-asserted-by":"publisher","first-page":"510","DOI":"10.2174\/156720511796391836","article-title":"Dietary patterns in Alzheimer's disease and cognitive aging","volume":"8","author":"Gu","year":"2011","journal-title":"Curr. Alzheimer Res."},{"key":"ref74","doi-asserted-by":"publisher","first-page":"13812","DOI":"10.1074\/jbc.RA120.012587","article-title":"Truncation of tau selectively facilitates its pathological activities","volume":"295","author":"Gu","year":"2020","journal-title":"J. Biol. Chem."},{"key":"ref75","doi-asserted-by":"publisher","first-page":"5440","DOI":"10.1523\/JNEUROSCI.0147-12.2012","article-title":"G9a\/GLP histone lysine dimethyltransferase complex activity in the hippocampus and the entorhinal cortex is required for gene activation and silencing during memory consolidation","volume":"32","author":"Gupta-Agarwal","year":"2012","journal-title":"J. Neurosci."},{"key":"ref76","doi-asserted-by":"publisher","first-page":"351","DOI":"10.1101\/lm.035105.114","article-title":"NMDA receptor- and ERK-dependent histone methylation changes in the lateral amygdala bidirectionally regulate fear memory formation","volume":"21","author":"Gupta-Agarwal","year":"2014","journal-title":"Learn. Mem."},{"key":"ref77","doi-asserted-by":"publisher","first-page":"213","DOI":"10.1038\/s41420-025-02408-w","article-title":"The role of protein lactylation in brain health and disease: current advances and future directions","volume":"11","author":"Han","year":"2025","journal-title":"Cell Death Discov."},{"key":"ref78","doi-asserted-by":"publisher","first-page":"EMBJ2018100847","DOI":"10.15252\/embj.2018100847","article-title":"Strong anion exchange-mediated phosphoproteomics reveals extensive human non-canonical phosphorylation","volume":"38","author":"Hardman Gemma","year":"2019","journal-title":"Scopus"},{"key":"ref79","doi-asserted-by":"publisher","first-page":"39","DOI":"10.1186\/s13024-017-0181-0","article-title":"Inhibition of O-GlcNAcase leads to elevation of O-GlcNAc tau and reduction of tauopathy and cerebrospinal fluid tau in rTg4510 mice","volume":"12","author":"Hastings","year":"2017","journal-title":"Mol. Neurodegener."},{"key":"ref80","doi-asserted-by":"publisher","first-page":"102927","DOI":"10.1016\/j.arr.2025.102927","article-title":"Tau post-translational modifications in Alzheimer's disease: insights into pathogenesis, therapeutic strategies, and diagnostic advances","volume":"113","author":"Huiwen Lei","year":"2026","journal-title":"Ageing Res. Rev."},{"key":"ref81","doi-asserted-by":"publisher","first-page":"979","DOI":"10.3233\/JAD-190604","article-title":"Quantification of tau protein lysine methylation in aging and Alzheimer's disease","volume":"71","author":"Huseby","year":"2019","journal-title":"J. Alzheimer's Dis"},{"key":"ref82","doi-asserted-by":"publisher","first-page":"536","DOI":"10.1038\/embor.2008.93","article-title":"Atypical ubiquitin chains: new molecular signals. 'Protein modifications: beyond the usual suspects' review series","volume":"9","author":"Ikeda","year":"2008","journal-title":"EMBO Rep."},{"key":"ref83","doi-asserted-by":"publisher","first-page":"2375","DOI":"10.1097\/00001756-199807130-00041","article-title":"Levels of tau phosphorylation at different sites in Alzheimer disease brain","volume":"9","author":"Ikura","year":"1998","journal-title":"Neuroreport"},{"key":"ref84","doi-asserted-by":"publisher","first-page":"656","DOI":"10.2174\/156720510793611592","article-title":"Tau in Alzheimer disease and related tauopathies","volume":"7","author":"Iqbal","year":"2010","journal-title":"Curr. Alzheimer Res."},{"key":"ref85","doi-asserted-by":"publisher","first-page":"344","DOI":"10.1016\/j.ajpath.2013.04.025","article-title":"Acetylated tau neuropathology in sporadic and hereditary tauopathies","volume":"183","author":"Irwin","year":"2013","journal-title":"Am. J. Pathol."},{"key":"ref86","doi-asserted-by":"publisher","first-page":"807","DOI":"10.1093\/brain\/aws013","article-title":"Acetylated tau, a novel pathological signature in Alzheimer's disease and other tauopathies","volume":"135","author":"Irwin","year":"2012","journal-title":"Brain"},{"key":"ref87","doi-asserted-by":"publisher","first-page":"1019","DOI":"10.1111\/jnc.15975","article-title":"Site-specific phosphorylation of tau impacts mitochondrial function and response to stressors","volume":"168","author":"Isei","year":"2024","journal-title":"J. Neurochem."},{"key":"ref88","doi-asserted-by":"publisher","first-page":"387","DOI":"10.1016\/j.cell.2010.06.036","article-title":"Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer's disease mouse models","volume":"142","author":"Ittner","year":"2010","journal-title":"Cell"},{"key":"ref89","doi-asserted-by":"publisher","first-page":"7827","DOI":"10.3390\/ijms25147827","article-title":"The interplay between endogenous and foodborne pro-oxidants and antioxidants in shaping redox homeostasis","volume":"25","author":"Jakubek","year":"2024","journal-title":"Int. J. Mol. Sci."},{"key":"ref90","doi-asserted-by":"publisher","first-page":"7747","DOI":"10.1007\/s12035-025-04739-2","article-title":"Roles of ubiquitin ligases and Deubiquitylases in Alzheimer's disease","volume":"62","author":"Jia","year":"2025","journal-title":"Mol. Neurobiol."},{"key":"ref91","doi-asserted-by":"publisher","first-page":"e1008939","DOI":"10.1371\/journal.pcbi.1008939","article-title":"How multisite phosphorylation impacts the conformations of intrinsically disordered proteins","volume":"17","author":"Jin","year":"2021","journal-title":"PLoS Comput. Biol."},{"key":"ref92","doi-asserted-by":"publisher","first-page":"1025473","DOI":"10.3389\/fnagi.2022.1025473","article-title":"The role of altered protein acetylation in neurodegenerative disease","volume":"14","author":"Kabir","year":"2022","journal-title":"Front. Aging Neurosci."},{"key":"ref93","doi-asserted-by":"publisher","first-page":"826.e15","DOI":"10.1016\/j.neurobiolaging.2011.06.006","article-title":"Phosphorylation in the amino terminus of tau prevents inhibition of anterograde axonal transport","volume":"33","author":"Kanaan","year":"2012","journal-title":"Neurobiol. Aging"},{"key":"ref94","doi-asserted-by":"publisher","first-page":"1275","DOI":"10.1038\/s12276-020-00494-7","article-title":"Delta-secretase cleavage of tau mediates its pathology and propagation in Alzheimer's disease","volume":"52","author":"Kang","year":"2020","journal-title":"Exp. Mol. Med."},{"key":"ref95","doi-asserted-by":"publisher","first-page":"17","DOI":"10.29245\/2572.942X\/2016\/3.1016","article-title":"DNA-PK deficiency in Alzheimer's disease","volume":"1","author":"Kanungo","year":"2016","journal-title":"J Neurol Neuromedicine"},{"key":"ref96","doi-asserted-by":"publisher","first-page":"2269","DOI":"10.1111\/jcmm.12910","article-title":"Oxidative stress induces transient O-GlcNAc elevation and tau dephosphorylation in SH-SY5Y cells","volume":"20","author":"Katai","year":"2016","journal-title":"J. Cell. Mol. Med."},{"key":"ref97","doi-asserted-by":"publisher","first-page":"44","DOI":"10.1007\/s00401-025-02881-8","article-title":"The interactome of tau phosphorylated at T217 in Alzheimer's disease human brain tissue","volume":"149","author":"Kavanagh","year":"2025","journal-title":"Acta Neuropathol."},{"key":"ref1102","doi-asserted-by":"publisher","first-page":"e70020","DOI":"10.1002\/trc2.70020","article-title":"Discovery and clinical translation of ceperognastat, an O-GlcNAcase (OGA) inhibitor, for the treatment of Alzheimer\u2019s disease","volume":"10","author":"Kielbasa","year":"2024","journal-title":"Alzheimers Dement (N Y)"},{"key":"ref98","doi-asserted-by":"publisher","first-page":"12014","DOI":"10.1074\/jbc.M112.436113","article-title":"Identification of a novel anti-apoptotic E3 ubiquitin ligase that ubiquitinates antagonists of inhibitor of apoptosis proteins SMAC, HtrA2, and ARTS","volume":"288","author":"Kim","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref99","doi-asserted-by":"publisher","first-page":"2417","DOI":"10.1038\/s41593-024-01777-2","article-title":"TYK2 regulates tau levels, phosphorylation and aggregation in a tauopathy mouse model","volume":"27","author":"Kim","year":"2024","journal-title":"Nat. Neurosci."},{"key":"ref100","doi-asserted-by":"publisher","first-page":"901","DOI":"10.1016\/j.bbagen.2013.04.038","article-title":"Methionine oxidation and reduction in proteins","volume":"1840","author":"Kim","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"ref101","doi-asserted-by":"publisher","first-page":"181","DOI":"10.1002\/2211-5463.13667","article-title":"Novel aspects of the phosphorylation and structure of pathological tau: implications for tauopathy biomarkers","volume":"14","author":"Kimura","year":"2024","journal-title":"FEBS Open Bio"},{"key":"ref102","doi-asserted-by":"publisher","first-page":"203","DOI":"10.1146\/annurev-biochem-060310-170328","article-title":"The ubiquitin code","volume":"81","author":"Komander","year":"2012","journal-title":"Annu. Rev. Biochem."},{"key":"ref103","doi-asserted-by":"publisher","first-page":"1977","DOI":"10.1038\/sj.emboj.7600205","article-title":"A novel protein-conjugating system for Ufm1, a ubiquitin-fold modifier","volume":"23","author":"Komatsu","year":"2004","journal-title":"EMBO J."},{"key":"ref104","doi-asserted-by":"publisher","first-page":"156","DOI":"10.1016\/j.molcel.2023.11.034","article-title":"The UFM1 system: working principles, cellular functions, and pathophysiology","volume":"84","author":"Komatsu","year":"2024","journal-title":"Mol. Cell"},{"key":"ref105","doi-asserted-by":"publisher","first-page":"56","DOI":"10.3389\/fmolb.2017.00056","article-title":"Lysine-directed post-translational modifications of tau protein in Alzheimer's disease and related Tauopathies","volume":"4","author":"Kontaxi","year":"2017","journal-title":"Front. Mol. Biosci."},{"key":"ref106","doi-asserted-by":"publisher","first-page":"263","DOI":"10.1038\/nrneurol.2011.43","article-title":"Corticobasal degeneration: a pathologically distinct 4R tauopathy","volume":"7","author":"Kouri","year":"2011","journal-title":"Nat. Rev. Neurol."},{"key":"ref107","doi-asserted-by":"publisher","first-page":"956","DOI":"10.1016\/j.cell.2025.12.036","article-title":"Molecular features of human pathological tau distinguish tauopathy-associated dementias","volume":"189","author":"Kumar","year":"2026","journal-title":"Cell"},{"key":"ref108","doi-asserted-by":"publisher","first-page":"1836","DOI":"10.3390\/biomedicines12081836","article-title":"P-tau217 as a reliable blood-based marker of Alzheimer's disease","volume":"12","author":"Lai","year":"2024","journal-title":"Biomedicine"},{"key":"ref109","doi-asserted-by":"publisher","first-page":"e15098","DOI":"10.15252\/emmm.202115098","article-title":"P-tau235: a novel biomarker for staging preclinical Alzheimer's disease","volume":"13","author":"Lantero-Rodriguez","year":"2021","journal-title":"EMBO Mol. Med."},{"key":"ref110","doi-asserted-by":"publisher","first-page":"3409","DOI":"10.1016\/j.jmb.2017.05.029","article-title":"Molecular basis for K63-linked ubiquitination processes in double-Strand DNA break repair: a focus on kinetics and dynamics","volume":"429","author":"Lee","year":"2017","journal-title":"J. Mol. Biol."},{"key":"ref111","doi-asserted-by":"publisher","first-page":"2304","DOI":"10.1523\/JNEUROSCI.4162-03.2004","article-title":"Phosphorylation of tau by fyn: implications for Alzheimer's disease","volume":"24","author":"Lee","year":"2004","journal-title":"J. Neurosci."},{"key":"ref112","doi-asserted-by":"publisher","first-page":"11","DOI":"10.1523\/JNEUROSCI.2872-20.2020","article-title":"A pictorial history of the neuronal cytoskeleton","volume":"41","author":"Leterrier","year":"2021","journal-title":"J. Neurosci."},{"key":"ref113","doi-asserted-by":"publisher","first-page":"1025","DOI":"10.1016\/j.str.2023.05.020","article-title":"Disease-associated patterns of acetylation stabilize tau fibril formation","volume":"31","author":"Li","year":"2023","journal-title":"Structure"},{"key":"ref114","doi-asserted-by":"publisher","first-page":"61","DOI":"10.1007\/s00401-025-02965-5","article-title":"Probing tau citrullination in Alzheimer's disease brains and mouse models of tauopathy","volume":"150","author":"Liang","year":"2025","journal-title":"Acta Neuropathol."},{"key":"ref115","doi-asserted-by":"publisher","first-page":"655","DOI":"10.1136\/jnnp-2014-308577","article-title":"CSF lactate levels, tau proteins, cognitive decline: a dynamic relationship in Alzheimer's disease","volume":"86","author":"Liguori","year":"2015","journal-title":"J. Neurol. Neurosurg. Psychiatry"},{"key":"ref116","doi-asserted-by":"publisher","first-page":"148","DOI":"10.1186\/s12943-024-02046-3","article-title":"Ubiquitination and deubiquitination in cancer: from mechanisms to novel therapeutic approaches","volume":"23","author":"Liu","year":"2024","journal-title":"Mol. Cancer"},{"key":"ref117","doi-asserted-by":"publisher","first-page":"10804","DOI":"10.1073\/pnas.0400348101","article-title":"O-GlcNAcylation regulates phosphorylation of tau: a mechanism involved in Alzheimer's disease","volume":"101","author":"Liu","year":"2004","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref118","doi-asserted-by":"publisher","first-page":"4304","DOI":"10.1038\/s41467-021-24319-x","article-title":"Phosphorylated tau181 in plasma as a potential biomarker for Alzheimer's disease in adults with down syndrome","volume":"12","author":"Lle\u00f3","year":"2021","journal-title":"Nat. Commun."},{"key":"ref119","doi-asserted-by":"publisher","first-page":"75","DOI":"10.3233\/jad-141959","article-title":"A phase II trial of tideglusib in Alzheimer's disease","volume":"45","author":"Lovestone","year":"2015","journal-title":"J. Alzheimer's Dis"},{"key":"ref120","doi-asserted-by":"publisher","first-page":"458","DOI":"10.1021\/acschemneuro.2c00611","article-title":"Phosphorylation of tau R2 repeat destabilizes its binding to microtubules: a molecular dynamics simulation study","volume":"14","author":"Man","year":"2023","journal-title":"ACS Chem. Neurosci."},{"key":"ref121","doi-asserted-by":"publisher","first-page":"7520","DOI":"10.3390\/ijms26157520","article-title":"Antioxidants and reactive oxygen species: shaping human health and disease outcomes","volume":"26","author":"Manful","year":"2025","journal-title":"Int. J. Mol. Sci."},{"key":"ref122","doi-asserted-by":"publisher","first-page":"289","DOI":"10.1016\/j.arr.2012.06.003","article-title":"Tau protein kinases: involvement in Alzheimer's disease","volume":"12","author":"Martin","year":"2013","journal-title":"Ageing Res. Rev."},{"key":"ref123","doi-asserted-by":"publisher","first-page":"116291","DOI":"10.1016\/j.celrep.2025.116291","article-title":"Clearing truncated tau protein restores neuronal function and prevents microglia activation in tauopathy mice","volume":"44","author":"Mart\u00edn-\u00c1vila","year":"2025","journal-title":"Cell Rep."},{"key":"ref124","doi-asserted-by":"publisher","first-page":"477","DOI":"10.1016\/j.molcel.2010.07.001","article-title":"K11-linked polyubiquitination in cell cycle control revealed by a K11 linkage-specific antibody","volume":"39","author":"Matsumoto","year":"2010","journal-title":"Mol. Cell"},{"key":"ref1101","doi-asserted-by":"publisher","first-page":"100456","DOI":"10.1016\/j.tjpad.2025.100456","article-title":"Synaptic Toxicity of OGA Inhibitors and the Failure of Ceperognastat","volume":"13","author":"Meade","year":"2026","journal-title":"J Prev Alzheimers Dis."},{"key":"ref125","doi-asserted-by":"publisher","first-page":"687","DOI":"10.3233\/JAD-150298","article-title":"Identification of novel tau interactions with endoplasmic reticulum proteins in Alzheimer's disease brain","volume":"48","author":"Meier","year":"2015","journal-title":"J. Alzheimer's Dis"},{"key":"ref126","doi-asserted-by":"publisher","first-page":"910","DOI":"10.1016\/j.cell.2014.03.037","article-title":"Enhanced protein degradation by branched ubiquitin chains","volume":"157","author":"Meyer","year":"2014","journal-title":"Cell"},{"key":"ref127","doi-asserted-by":"publisher","first-page":"95","DOI":"10.1016\/j.molcel.2015.01.042","article-title":"Assembly and specific recognition of k29- and k33-linked polyubiquitin","volume":"58","author":"Michel","year":"2015","journal-title":"Mol. Cell"},{"key":"ref128","doi-asserted-by":"publisher","first-page":"5040","DOI":"10.1111\/febs.16730","article-title":"A guide to UFMylation, an emerging posttranslational modification","volume":"290","author":"Millrine","year":"2023","journal-title":"FEBS J."},{"key":"ref129","doi-asserted-by":"publisher","first-page":"953","DOI":"10.1016\/j.neuron.2010.08.044","article-title":"Acetylation of tau inhibits its degradation and contributes to tauopathy","volume":"67","author":"Min","year":"2010","journal-title":"Neuron"},{"key":"ref130","doi-asserted-by":"publisher","first-page":"1151","DOI":"10.1016\/0896-6273(93)90063-W","article-title":"Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments","volume":"10","author":"Morishima-Kawashima","year":"1993","journal-title":"Neuron"},{"key":"ref131","doi-asserted-by":"publisher","first-page":"1183","DOI":"10.1038\/nn.4067","article-title":"Tau post-translational modifications in wild-type and human amyloid precursor protein transgenic mice","volume":"18","author":"Morris","year":"2015","journal-title":"Nat. Neurosci."},{"key":"ref132","doi-asserted-by":"publisher","first-page":"647054","DOI":"10.3389\/fnmol.2021.647054","article-title":"Tau: A Signaling Hub Protein","volume":"14","author":"Mueller","year":"2021","journal-title":"Front. Mol. Neurosci."},{"key":"ref133","doi-asserted-by":"publisher","first-page":"4400","DOI":"10.3390\/ijms21124400","article-title":"Semisynthetic modification of tau protein with Di-ubiquitin chains for aggregation studies","volume":"21","author":"Munari","year":"2020","journal-title":"Int. J. Mol. Sci."},{"key":"ref134","doi-asserted-by":"publisher","first-page":"107286","DOI":"10.1016\/j.nlm.2020.107286","article-title":"The diversity of linkage-specific polyubiquitin chains and their role in synaptic plasticity and memory formation","volume":"174","author":"Musaus","year":"2020","journal-title":"Neurobiol. Learn. Mem."},{"key":"ref135","doi-asserted-by":"publisher","first-page":"7972","DOI":"10.1038\/s41467-024-52075-1","article-title":"Phosphorylation of tau at a single residue inhibits binding to the E3 ubiquitin ligase, CHIP","volume":"15","author":"Nadel","year":"2024","journal-title":"Nat. Commun."},{"key":"ref136","doi-asserted-by":"publisher","first-page":"1934","DOI":"10.1093\/brain\/awy135","article-title":"Biallelic UFM1 and UFC1 mutations expand the essential role of ufmylation in brain development","volume":"141","author":"Nahorski","year":"2018","journal-title":"Brain"},{"key":"ref137","doi-asserted-by":"publisher","first-page":"156","DOI":"10.1038\/s41580-018-0081-3","article-title":"Functions and mechanisms of non-histone protein acetylation","volume":"20","author":"Narita","year":"2019","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref138","doi-asserted-by":"publisher","first-page":"362","DOI":"10.1097\/NEN.0b013e31825018f7","article-title":"Correlation of Alzheimer disease neuropathologic changes with cognitive status: a review of the literature","volume":"71","author":"Nelson","year":"2012","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"ref139","doi-asserted-by":"publisher","first-page":"702404","DOI":"10.3389\/fcell.2021.702404","article-title":"Caspases in the developing central nervous system: apoptosis and beyond","volume":"9","author":"Nguyen","year":"2021","journal-title":"Front. Cell Dev. Biol."},{"key":"ref140","doi-asserted-by":"publisher","first-page":"900","DOI":"10.1038\/s41436-020-01071-z","article-title":"A pathogenic UFSP2 variant in an autosomal recessive form of pediatric neurodevelopmental anomalies and epilepsy","volume":"23","author":"Ni","year":"2021","journal-title":"Genet. Med."},{"key":"ref141","doi-asserted-by":"publisher","first-page":"35","DOI":"10.1186\/s13195-015-0119-0","article-title":"A phase Ib multiple ascending dose study of the safety, tolerability, and central nervous system availability of AZD0530 (saracatinib) in Alzheimer's disease","volume":"7","author":"Nygaard","year":"2015","journal-title":"Alzheimer's Res. Ther."},{"key":"ref142","doi-asserted-by":"publisher","first-page":"325","DOI":"10.5483\/BMBRep.2025-0077","article-title":"Decoding tau acetylation in Alzheimer's disease and tauopathies: from site-specific mechanisms to therapeutic horizons","volume":"58","author":"Oh","year":"2025","journal-title":"BMB Rep."},{"key":"ref143","doi-asserted-by":"publisher","first-page":"5691","DOI":"10.1007\/s12035-023-03434-4","article-title":"Pathological impact of tau Proteolytical process on neuronal and mitochondrial function: a crucial role in Alzheimer's disease","volume":"60","author":"Olesen","year":"2023","journal-title":"Mol. Neurobiol."},{"key":"ref144","doi-asserted-by":"publisher","first-page":"106905","DOI":"10.1016\/j.isci.2023.106905","article-title":"Activity-dependent tau cleavage by caspase-3 promotes neuronal dysfunction and synaptotoxicity","volume":"26","author":"Opland","year":"2023","journal-title":"iScience"},{"key":"ref145","doi-asserted-by":"publisher","first-page":"205","DOI":"10.1016\/j.neulet.2009.05.074","article-title":"Immunoreactivity to Lys63-linked polyubiquitin is a feature of neurodegeneration","volume":"460","author":"Paine","year":"2009","journal-title":"Neurosci. Lett."},{"key":"ref146","doi-asserted-by":"publisher","first-page":"204","DOI":"10.1038\/s12276-020-0382-4","article-title":"A short guide to histone deacetylases including recent progress on class II enzymes","volume":"52","author":"Park","year":"2020","journal-title":"Exp. Mol. Med."},{"key":"ref147","doi-asserted-by":"publisher","first-page":"107839","DOI":"10.1016\/j.celrep.2020.107839","article-title":"Caspase activation and caspase-mediated cleavage of APP is associated with amyloid beta-protein-induced synapse loss in Alzheimer's disease","volume":"31","author":"Park","year":"2020","journal-title":"Cell Rep."},{"key":"ref148","doi-asserted-by":"publisher","first-page":"2446","DOI":"10.1016\/j.cell.2024.03.015","article-title":"Human iPSC 4R tauopathy model uncovers modifiers of tau propagation","volume":"187","author":"Parra Bravo","year":"","journal-title":"Cell"},{"key":"ref149","doi-asserted-by":"publisher","first-page":"845","DOI":"10.1038\/s41580-024-00753-9","article-title":"Cellular and pathological functions of tau","volume":"25","author":"Parra Bravo","year":"","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref150","doi-asserted-by":"publisher","first-page":"103","DOI":"10.1152\/physrev.00030.2022","article-title":"Oxidative damage in neurodegeneration: roles in the pathogenesis and progression of Alzheimer disease","volume":"104","author":"Perluigi","year":"2024","journal-title":"Physiol. Rev."},{"key":"ref151","doi-asserted-by":"publisher","first-page":"11","DOI":"10.1007\/s12291-014-0446-0","article-title":"Free radicals: properties, sources, targets, and their implication in various diseases","volume":"30","author":"Phaniendra","year":"2015","journal-title":"Indian J. Clin. Biochem."},{"key":"ref152","doi-asserted-by":"publisher","first-page":"588","DOI":"10.1007\/s004010050565","article-title":"Pick's disease: hyperphosphorylated tau protein segregates to the somatoaxonal compartment","volume":"92","author":"Probst","year":"1996","journal-title":"Acta Neuropathol."},{"key":"ref153","doi-asserted-by":"publisher","first-page":"101766","DOI":"10.1016\/j.jbc.2022.101766","article-title":"Lysine 63-linked ubiquitination of tau oligomers contributes to the pathogenesis of Alzheimer's disease","volume":"298","author":"Puangmalai","year":"2022","journal-title":"J. Biol. Chem."},{"key":"ref154","doi-asserted-by":"publisher","first-page":"e1004358","DOI":"10.1371\/journal.ppat.1004358","article-title":"RNF26 temporally regulates virus-triggered type I interferon induction by two distinct mechanisms","volume":"10","author":"Qin","year":"2014","journal-title":"PLoS Pathog."},{"key":"ref155","doi-asserted-by":"publisher","first-page":"13","DOI":"10.3233\/JAD-170959","article-title":"Tau proteolysis in the pathogenesis of Tauopathies: neurotoxic fragments and novel biomarkers","volume":"63","author":"Quinn","year":"2018","journal-title":"J. Alzheimer's Dis"},{"key":"ref156","doi-asserted-by":"publisher","first-page":"2275","DOI":"10.1016\/j.ajpath.2011.01.030","article-title":"Tyrosine nitration within the proline-rich region of tau in Alzheimer's disease","volume":"178","author":"Reyes","year":"2011","journal-title":"Am. J. Pathol."},{"key":"ref157","doi-asserted-by":"publisher","first-page":"119","DOI":"10.1007\/s00401-011-0898-8","article-title":"Selective tau tyrosine nitration in non-AD tauopathies","volume":"123","author":"Reyes","year":"2012","journal-title":"Acta Neuropathol."},{"key":"ref158","doi-asserted-by":"publisher","first-page":"198","DOI":"10.1016\/j.nbd.2008.04.005","article-title":"A possible link between astrocyte activation and tau nitration in Alzheimer's disease","volume":"31","author":"Reyes","year":"2008","journal-title":"Neurobiol. Dis."},{"key":"ref159","doi-asserted-by":"publisher","first-page":"fcaf091","DOI":"10.1093\/braincomms\/fcaf091","article-title":"Vulnerability of the entorhinal cortex II to neurodegeneration in Alzheimer's disease","volume":"7","author":"Reyes-Pablo","year":"2025","journal-title":"Brain Commun"},{"key":"ref160","doi-asserted-by":"publisher","first-page":"1690","DOI":"10.1021\/bi047982v","article-title":"Site-specific nitration and oxidative dityrosine bridging of the tau protein by peroxynitrite: implications for Alzheimer's disease","volume":"44","author":"Reynolds","year":"","journal-title":"Biochemistry"},{"key":"ref161","doi-asserted-by":"publisher","first-page":"13997","DOI":"10.1021\/bi051028w","article-title":"Site-specific nitration differentially influences tau assembly in vitro","volume":"44","author":"Reynolds","year":"","journal-title":"Biochemistry"},{"key":"ref162","doi-asserted-by":"publisher","first-page":"7325","DOI":"10.1021\/bi700430y","article-title":"Nitration in neurodegeneration: deciphering the \"Hows\" \"nYs\"","volume":"46","author":"Reynolds","year":"2007","journal-title":"Biochemistry"},{"key":"ref163","doi-asserted-by":"publisher","first-page":"10636","DOI":"10.1523\/JNEUROSCI.2143-06.2006","article-title":"Tau nitration occurs at tyrosine 29 in the fibrillar lesions of Alzheimer's disease and other tauopathies","volume":"26","author":"Reynolds","year":"2006","journal-title":"J. Neurosci."},{"key":"ref164","doi-asserted-by":"publisher","first-page":"489","DOI":"10.3233\/jad-2004-6505","article-title":"The potential role of tau protein O-glycosylation in Alzheimer's disease","volume":"6","author":"Robertson","year":"2004","journal-title":"J. Alzheimer's Dis"},{"key":"ref165","doi-asserted-by":"publisher","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":"ref166","doi-asserted-by":"publisher","DOI":"10.1101\/2023.06.16.545386","article-title":"CRISPR screens in iPSC-derived neurons reveal principles of tau proteostasis","author":"Samelson","year":"2024","journal-title":"bioRxiv"},{"key":"ref167","doi-asserted-by":"publisher","first-page":"678","DOI":"10.1016\/j.neuron.2009.11.019","article-title":"Control of cognition and adaptive behavior by the GLP\/G9a epigenetic suppressor complex","volume":"64","author":"Schaefer","year":"2009","journal-title":"Neuron"},{"key":"ref168","doi-asserted-by":"publisher","first-page":"13","DOI":"10.1016\/j.bbamcr.2013.08.012","article-title":"Regulation of proteasome activity in health and disease","volume":"1843","author":"Schmidt","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"ref169","doi-asserted-by":"publisher","first-page":"e16221","DOI":"10.1111\/jnc.16221","article-title":"Mass spectrometry identifies tau C-terminal phosphorylation cluster during neuronal hyperexcitation","volume":"169","author":"Schneeweis","year":"2025","journal-title":"J. Neurochem."},{"key":"ref170","doi-asserted-by":"publisher","first-page":"8463","DOI":"10.1073\/pnas.92.18.8463","article-title":"Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments","volume":"92","author":"Schweers","year":"1995","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref171","doi-asserted-by":"publisher","first-page":"596","DOI":"10.1016\/j.neurobiolaging.2005.03.009","article-title":"DNA end joining activity is reduced in Alzheimer's disease","volume":"27","author":"Shackelford","year":"2006","journal-title":"Neurobiol. Aging"},{"key":"ref172","doi-asserted-by":"publisher","first-page":"21","DOI":"10.1038\/cdd.2012.72","article-title":"Ubiquitination and selective autophagy","volume":"20","author":"Shaid","year":"2013","journal-title":"Cell Death Differ."},{"key":"ref173","doi-asserted-by":"publisher","first-page":"20365","DOI":"10.1074\/jbc.M414356200","article-title":"Lys6-modified ubiquitin inhibits ubiquitin-dependent protein degradation","volume":"280","author":"Shang","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref174","doi-asserted-by":"publisher","first-page":"106280","DOI":"10.1016\/j.compbiomed.2022.106280","article-title":"In silico approaches uncovering the systematic function of N-phosphorylated proteins in human cells","volume":"151","author":"Shanshan Wang","year":"2022","journal-title":"Comput. Biol. Med."},{"key":"ref175","doi-asserted-by":"publisher","first-page":"157","DOI":"10.1093\/procel\/pwad045","article-title":"The ubiquitin codes in cellular stress responses","volume":"15","author":"Sheng","year":"2024","journal-title":"Protein Cell"},{"key":"ref176","doi-asserted-by":"publisher","first-page":"1125","DOI":"10.3389\/fneur.2019.01125","article-title":"Frontrunner in translation: progressive Supranuclear palsy","volume":"10","author":"Shoeibi","year":"2019","journal-title":"Front. Neurol."},{"key":"ref177","doi-asserted-by":"publisher","first-page":"1420","DOI":"10.1039\/C0MB00337A","article-title":"Identification of O-GlcNAc sites within peptides of the tau protein and their impact on phosphorylation","volume":"7","author":"Smet-Nocca","year":"2011","journal-title":"Mol. BioSyst."},{"key":"ref178","doi-asserted-by":"publisher","first-page":"e70221","DOI":"10.1111\/jnc.70221","article-title":"Acetylation mimetic and null mutations within the filament Core of P301L tau have varied effects on susceptibility to seeding and aggregation","volume":"169","author":"Smith","year":"2025","journal-title":"J. Neurochem."},{"key":"ref179","doi-asserted-by":"publisher","first-page":"43R","DOI":"10.1093\/glycob\/12.4.43R","article-title":"Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds","volume":"12","author":"Spiro","year":"2002","journal-title":"Glycobiology"},{"key":"ref180","doi-asserted-by":"publisher","first-page":"eabl8809","DOI":"10.1126\/sciadv.abl8809","article-title":"Alzheimer's disease: ablating single master site abolishes tau hyperphosphorylation","volume":"8","author":"Stefanoska","year":"2022","journal-title":"Sci. Adv."},{"key":"ref181","doi-asserted-by":"publisher","first-page":"1458038","DOI":"10.3389\/frdem.2024.1458038","article-title":"Tyrosine kinases: multifaceted receptors at the intersection of several neurodegenerative disease-associated processes","volume":"3","author":"Stevenson","year":"2024","journal-title":"Front Dement"},{"key":"ref182","doi-asserted-by":"publisher","first-page":"110415","DOI":"10.1016\/j.jbc.2025.110415","article-title":"Molecular choreography of E1 enzymes in ubiquitin-like protein cascades: new insights into dynamics and specificity","volume":"301","author":"Stratton","year":"2025","journal-title":"J. Biol. Chem."},{"key":"ref183","doi-asserted-by":"publisher","first-page":"2358","DOI":"10.1097\/00001756-199411000-00037","article-title":"Early phosphorylation of tau in Alzheimer's disease occurs at Ser-202 and is preferentially located within neurites","volume":"5","author":"Su","year":"1994","journal-title":"Neuroreport"},{"key":"ref184","doi-asserted-by":"publisher","first-page":"399","DOI":"10.1038\/cr.2016.39","article-title":"Ubiquitin modifications","volume":"26","author":"Swatek","year":"2016","journal-title":"Cell Res."},{"key":"ref60","first-page":"1","volume-title":"Tau Protein: Physiological Functions and Multifaceted roles in Neurodegenerative and Psychiatric Disorders","author":"Tang","year":"2025"},{"key":"ref185","doi-asserted-by":"publisher","first-page":"497","DOI":"10.1093\/jb\/mvt028","article-title":"The ubiquitin code and its decoding machinery in the endocytic pathway","volume":"153","author":"Tanno","year":"2013","journal-title":"J. Biochem."},{"key":"ref186","doi-asserted-by":"publisher","first-page":"5417","DOI":"10.1074\/jbc.M109.036814","article-title":"A novel type of E3 ligase for the Ufm1 conjugation system","volume":"285","author":"Tatsumi","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref187","doi-asserted-by":"publisher","first-page":"7","DOI":"10.1007\/s00401-023-02667-w","article-title":"P-tau Ser356 is associated with Alzheimer's disease pathology and is lowered in brain slice cultures using the NUAK inhibitor WZ4003","volume":"147","author":"Taylor","year":"2024","journal-title":"Acta Neuropathol."},{"key":"ref188","doi-asserted-by":"publisher","first-page":"e12819","DOI":"10.1111\/nan.12819","article-title":"Caspase-6-cleaved tau is relevant in Alzheimer's disease and marginal in four-repeat tauopathies: diagnostic and therapeutic implications","volume":"48","author":"Theofilas","year":"2022","journal-title":"Neuropathol. Appl. Neurobiol."},{"key":"ref189","doi-asserted-by":"publisher","first-page":"986","DOI":"10.1016\/j.tibs.2024.08.004","article-title":"The expanding landscape of canonical and non-canonical protein phosphorylation","volume":"49","author":"Thibault Houles","year":"2024","journal-title":"Trends Biochem. Sci."},{"key":"ref190","doi-asserted-by":"publisher","first-page":"105","DOI":"10.1007\/s00401-011-0893-0","article-title":"Dual modification of Alzheimer's disease PHF-tau protein by lysine methylation and ubiquitylation: a mass spectrometry approach","volume":"123","author":"Thomas","year":"2012","journal-title":"Acta Neuropathol."},{"key":"ref191","doi-asserted-by":"publisher","first-page":"134","DOI":"10.1016\/j.conb.2018.04.027","article-title":"Tau-mediated synaptic and neuronal dysfunction in neurodegenerative disease","volume":"51","author":"Tracy","year":"2018","journal-title":"Curr. Opin. Neurobiol."},{"key":"ref192","doi-asserted-by":"publisher","first-page":"44102","DOI":"10.1038\/srep44102","article-title":"A dual pathogenic mechanism links tau acetylation to sporadic Tauopathy","volume":"7","author":"Trzeciakiewicz","year":"2017","journal-title":"Sci. Rep."},{"key":"ref193","doi-asserted-by":"publisher","first-page":"740","DOI":"10.1038\/s41580-024-00729-9","article-title":"Targeted protein degradation: from mechanisms to clinic","volume":"25","author":"Tsai","year":"2024","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref194","doi-asserted-by":"publisher","first-page":"109037","DOI":"10.1016\/j.celrep.2021.109037","article-title":"Tau seeds are subject to aberrant modifications resulting in distinct signatures","volume":"35","author":"Tseng","year":"2021","journal-title":"Cell Rep."},{"key":"ref195","doi-asserted-by":"publisher","first-page":"89","DOI":"10.1002\/cm.21811","article-title":"The emerging nontraditional roles for tau in the brain","volume":"81","author":"Tseng","year":"2024","journal-title":"Cytoskeleton"},{"key":"ref196","doi-asserted-by":"publisher","first-page":"44","DOI":"10.1016\/j.biocel.2006.07.001","article-title":"Free radicals and antioxidants in normal physiological functions and human disease","volume":"39","author":"Valko","year":"2007","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref197","doi-asserted-by":"publisher","first-page":"1219","DOI":"10.1001\/jamaneurol.2019.2050","article-title":"Effect of AZD0530 on cerebral metabolic decline in Alzheimer disease: a randomized clinical trial","volume":"76","author":"van Dyck","year":"2019","journal-title":"JAMA Neurol."},{"key":"ref198","doi-asserted-by":"publisher","first-page":"1203","DOI":"10.1021\/bi101735m","article-title":"Peroxynitrite-induced nitrative and oxidative modifications alter tau filament formation","volume":"50","author":"Vana","year":"2011","journal-title":"Biochemistry"},{"key":"ref199","doi-asserted-by":"publisher","first-page":"2514","DOI":"10.3390\/ijms22052514","article-title":"The tumor proteolytic landscape: a challenging frontier in Cancer diagnosis and therapy","volume":"22","author":"Vizovisek","year":"2021","journal-title":"Int. J. Mol. Sci."},{"key":"ref200","doi-asserted-by":"publisher","first-page":"5","DOI":"10.3389\/fonc.2012.00005","article-title":"K63-linked ubiquitination in kinase activation and cancer","volume":"2","author":"Wang","year":"2012","journal-title":"Front. Oncol."},{"key":"ref201","doi-asserted-by":"publisher","first-page":"241","DOI":"10.3233\/JAD-200529","article-title":"Tau acetylation in entorhinal cortex induces its chronic hippocampal propagation and cognitive deficits in mice","volume":"77","author":"Wang","year":"2020","journal-title":"J. Alzheimer's Dis"},{"key":"ref202","doi-asserted-by":"publisher","first-page":"5","DOI":"10.1038\/nrn.2015.1","article-title":"Tau in physiology and pathology","volume":"17","author":"Wang","year":"2016","journal-title":"Nat. Rev. Neurosci."},{"key":"ref203","first-page":"13","article-title":"In vitro analysis of tau phosphorylation sites and its biological activity","volume":"17","author":"Wang","year":"2002","journal-title":"Chin. Med. Sci. J."},{"key":"ref204","doi-asserted-by":"publisher","first-page":"131","DOI":"10.1016\/j.conb.2021.03.003","article-title":"A current view on tau protein phosphorylation in Alzheimer's disease","volume":"69","author":"Wegmann","year":"2021","journal-title":"Curr. Opin. Neurobiol."},{"key":"ref205","doi-asserted-by":"publisher","first-page":"e98049","DOI":"10.15252\/embj.201798049","article-title":"Tau protein liquid-liquid phase separation can initiate tau aggregation","volume":"37","author":"Wegmann","year":"2018","journal-title":"EMBO J."},{"key":"ref206","doi-asserted-by":"publisher","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":"ref207","doi-asserted-by":"publisher","first-page":"e54217","DOI":"10.15252\/embr.202154217","article-title":"Mechanisms of DNA damage-mediated neurotoxicity in neurodegenerative disease","volume":"23","author":"Welch","year":"2022","journal-title":"EMBO Rep."},{"key":"ref208","doi-asserted-by":"publisher","first-page":"1699","DOI":"10.1016\/j.cell.2020.10.029","article-title":"Tau PTM profiles identify patient heterogeneity and stages of Alzheimer's disease","volume":"183","author":"Wesseling","year":"2020","journal-title":"Cell"},{"key":"ref209","doi-asserted-by":"publisher","first-page":"133","DOI":"10.1016\/j.cell.2009.01.041","article-title":"Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation","volume":"137","author":"Xu","year":"2009","journal-title":"Cell"},{"key":"ref210","doi-asserted-by":"publisher","first-page":"97","DOI":"10.1186\/s13024-024-00784-y","article-title":"The UFMylation pathway is impaired in Alzheimer's disease","volume":"19","author":"Yan","year":"2024","journal-title":"Mol. Neurodegener."},{"key":"ref211","doi-asserted-by":"publisher","first-page":"452","DOI":"10.1038\/nrm.2017.22","article-title":"Protein O-GlcNAcylation: emerging mechanisms and functions","volume":"18","author":"Yang","year":"2017","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref212","doi-asserted-by":"publisher","first-page":"4712","DOI":"10.1007\/s12035-023-03867-x","article-title":"Complicated role of post-translational modification and protease-cleaved fragments of tau in Alzheimer's disease and other Tauopathies","volume":"61","author":"Yang","year":"2024","journal-title":"Mol. Neurobiol."},{"key":"ref213","doi-asserted-by":"publisher","first-page":"261","DOI":"10.1016\/j.molcel.2014.08.007","article-title":"Modification of ASC1 by UFM1 is crucial for ERalpha transactivation and breast cancer development","volume":"56","author":"Yoo","year":"2014","journal-title":"Mol. Cell"},{"key":"ref214","doi-asserted-by":"publisher","first-page":"e71354","DOI":"10.1096\/fj.202503324R","article-title":"Ubiquitination and acetylation in cellular senescence: mechanisms, crosstalk, and therapeutic implications","volume":"39","author":"Yu","year":"2025","journal-title":"FASEB J."},{"key":"ref215","doi-asserted-by":"publisher","first-page":"586","DOI":"10.1016\/j.molcel.2014.03.035","article-title":"K33-linked Polyubiquitination of Coronin 7 by Cul3-KLHL20 ubiquitin E3 ligase regulates protein trafficking","volume":"54","author":"Yuan","year":"2014","journal-title":"Mol. Cell"},{"key":"ref216","doi-asserted-by":"publisher","first-page":"1736","DOI":"10.1016\/j.jmb.2014.01.004","article-title":"O-GlcNAc modification of tau directly inhibits its aggregation without perturbing the conformational properties of tau monomers","volume":"426","author":"Yuzwa","year":"2014","journal-title":"J. Mol. Biol."},{"key":"ref217","doi-asserted-by":"publisher","first-page":"393","DOI":"10.1038\/nchembio.797","article-title":"Increasing O-GlcNAc slows neurodegeneration and stabilizes tau against aggregation","volume":"8","author":"Yuzwa","year":"2012","journal-title":"Nat. Chem. Biol."},{"key":"ref218","doi-asserted-by":"publisher","first-page":"857","DOI":"10.1007\/s00726-010-0705-1","article-title":"Mapping O-GlcNAc modification sites on tau and generation of a site-specific O-GlcNAc tau antibody","volume":"40","author":"Yuzwa","year":"2011","journal-title":"Amino Acids"},{"key":"ref219","doi-asserted-by":"publisher","first-page":"288","DOI":"10.1111\/jnc.16053","article-title":"Acetylated tau exacerbates apoptosis by disturbing mitochondrial dynamics in HEK293 cells","volume":"168","author":"Zhang","year":"2024","journal-title":"J. Neurochem."},{"key":"ref220","doi-asserted-by":"publisher","first-page":"898574","DOI":"10.3389\/fphar.2022.898574","article-title":"The involvement of caspases in Neuroinflammation and neuronal apoptosis in chronic pain and potential therapeutic targets","volume":"13","author":"Zhang","year":"2022","journal-title":"Front. Pharmacol."},{"key":"ref221","doi-asserted-by":"publisher","first-page":"e14481","DOI":"10.1002\/alz.14481","article-title":"Lactylation of tau in human Alzheimer's disease brains","volume":"21","author":"Zhang","year":"2025","journal-title":"Alzheimers Dement."},{"key":"ref222","doi-asserted-by":"publisher","first-page":"2421","DOI":"10.1016\/j.febslet.2005.03.041","article-title":"Nitration and oligomerization of tau induced by peroxynitrite inhibit its microtubule-binding activity","volume":"579","author":"Zhang","year":"2005","journal-title":"FEBS Lett."},{"key":"ref223","doi-asserted-by":"publisher","first-page":"1431","DOI":"10.1096\/fj.05-5223com","article-title":"Peroxynitrite induces Alzheimer-like tau modifications and accumulation in rat brain and its underlying mechanisms","volume":"20","author":"Zhang","year":"2006","journal-title":"FASEB J."},{"key":"ref224","doi-asserted-by":"publisher","first-page":"bbaf627","DOI":"10.1093\/bib\/bbaf627","article-title":"Decoding protein N-phosphorylation functionality and sequence patterns","volume":"26","author":"Zhao","year":"2025","journal-title":"Brief. Bioinform."},{"key":"ref225","doi-asserted-by":"publisher","first-page":"113","DOI":"10.1038\/s41392-022-00966-4","article-title":"Targeted protein degradation: mechanisms, strategies and application","volume":"7","author":"Zhao","year":"2022","journal-title":"Signal Transduct. Target. Ther."},{"key":"ref226","doi-asserted-by":"publisher","first-page":"1046","DOI":"10.1101\/gad.215681.113","article-title":"The p97-UBXD8 complex destabilizes mRNA by promoting release of ubiquitinated HuR from mRNP","volume":"27","author":"Zhou","year":"2013","journal-title":"Genes Dev."},{"key":"ref227","doi-asserted-by":"publisher","first-page":"909","DOI":"10.1152\/physrev.00026.2013","article-title":"Mitochondrial reactive oxygen species (ROS) and ROS-induced ROS release","volume":"94","author":"Zorov","year":"2014","journal-title":"Physiol. Rev."},{"key":"ref228","doi-asserted-by":"publisher","first-page":"3386","DOI":"10.1021\/acs.jcim.3c01929","article-title":"Molecular insights into the differential effects of acetylation on the aggregation of tau microtubule-binding repeats","volume":"64","author":"Zou","year":"2024","journal-title":"J. Chem. Inf. Model."}],"container-title":["Frontiers in Dementia"],"original-title":[],"link":[{"URL":"https:\/\/www.frontiersin.org\/articles\/10.3389\/frdem.2026.1834737\/full","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,6,3]],"date-time":"2026-06-03T04:51:01Z","timestamp":1780462261000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.frontiersin.org\/articles\/10.3389\/frdem.2026.1834737\/full"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,6,3]]},"references-count":229,"alternative-id":["10.3389\/frdem.2026.1834737"],"URL":"https:\/\/doi.org\/10.3389\/frdem.2026.1834737","relation":{},"ISSN":["2813-3919"],"issn-type":[{"value":"2813-3919","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,6,3]]},"article-number":"1834737"}}