{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,21]],"date-time":"2026-10-21T01:12:48Z","timestamp":1792545168279,"version":"4.5.0"},"reference-count":152,"publisher":"MDPI AG","issue":"1","license":[{"start":{"date-parts":[[2026,2,3]],"date-time":"2026-02-03T00:00:00Z","timestamp":1770076800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Pathophysiology"],"abstract":"<jats:p>Alzheimer\u2019s disease (AD) is characterized by progressive cognitive decline, with amyloid beta oligomers (A\u03b2Os) emerging as the most neurotoxic species and acting as early triggers of cellular alterations. Before the appearance of other protein aggregates, A\u03b2Os disrupt the dynamics and stability of the neuronal cytoskeleton, a structure essential for maintaining neuronal morphology, axonal transport, and synaptic plasticity. Experimental evidence demonstrates that A\u03b2Os promote microtubule disassembly, Tau hyperphosphorylation, reduced kinesin levels, impaired axonal transport, and alterations in actin dynamics through the LIMK\u2013cofilin signaling pathway. In addition, increased levels of neurofilament light chain have been identified as an early biomarker of axonal damage. Notably, these cytoskeletal disturbances arise in the absence of extensive neuronal death, underscoring the cytoskeleton as a critical early target in AD pathogenesis. In this review, we analyze cytoskeletal alterations induced by A\u03b2Os in neurons and discuss how these changes may contribute to disrupted neuronal communication, a defining early hallmark of AD pathology.<\/jats:p>","DOI":"10.3390\/pathophysiology33010014","type":"journal-article","created":{"date-parts":[[2026,2,3]],"date-time":"2026-02-03T10:03:29Z","timestamp":1770113009000},"page":"14","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Amyloid Beta Oligomers as Early Triggers of Neuronal Cytoskeleton Dysfunction in Alzheimer\u2019s Disease"],"prefix":"10.3390","volume":"33","author":[{"ORCID":"https:\/\/orcid.org\/0009-0006-2010-8635","authenticated-orcid":false,"given":"Yadira","family":"Gasca-Mart\u00ednez","sequence":"first","affiliation":[{"name":"Departamento de Biolog\u00eda Celular y Molecular, Universidad de Guadalajara, Zapopan 45200, Jalisco, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Miguel Angel","family":"Ontiveros-Torres","sequence":"additional","affiliation":[{"name":"Escuela de Ingenier\u00eda y Ciencias, Tecnol\u00f3gico de Monterrey, Monterrey 64849, Nuevo Le\u00f3n, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Isa\u00edas","family":"L\u00f3pez-Gallegos","sequence":"additional","affiliation":[{"name":"Departamento de Biolog\u00eda Celular y Molecular, Universidad de Guadalajara, Zapopan 45200, Jalisco, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3294-0243","authenticated-orcid":false,"given":"Jos\u00e9 Jaime","family":"Jarero-Basulto","sequence":"additional","affiliation":[{"name":"Departamento de Biolog\u00eda Celular y Molecular, Universidad de Guadalajara, Zapopan 45200, Jalisco, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,2,3]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Safiri, S., Ghaffari Jolfayi, A., Fazlollahi, A., Morsali, S., Sarkesh, A., Daei Sorkhabi, A., Golabi, B., Aletaha, R., Motlagh Asghari, K., and Hamidi, S. (2024). Alzheimer\u2019s disease: A comprehensive review of epidemiology, risk factors, symptoms diagnosis, management, caregiving, advanced treatments and associated challenges. Front. Med., 11.","DOI":"10.3389\/fmed.2024.1474043"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1038\/s41572-021-00269-y","article-title":"Alzheimer disease","volume":"7","author":"Knopman","year":"2021","journal-title":"Nat. Rev. Dis. Primers"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1001\/jamaneurol.2013.5847","article-title":"Amyloid-\u03b2 and tau: The trigger and bullet in Alzheimer disease pathogenesis","volume":"71","author":"Bloom","year":"2014","journal-title":"JAMA Neurol."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"975","DOI":"10.3233\/JAD-160612","article-title":"Amyloid-Beta and Phosphorylated Tau Accumulations Cause Abnormalities at Synapses of Alzheimer\u2019s disease Neurons","volume":"57","author":"Rajmohan","year":"2017","journal-title":"J. Alzheimers Dis."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1007\/s00401-015-1386-3","article-title":"Amyloid \u03b2 oligomers in Alzheimer\u2019s disease pathogenesis, treatment, and diagnosis","volume":"129","author":"Viola","year":"2015","journal-title":"Acta Neuropathol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"1227","DOI":"10.1038\/nn.3178","article-title":"Alzheimer amyloid-\u03b2 oligomer bound to postsynaptic prion protein activates Fyn to impair neurons","volume":"15","author":"Um","year":"2012","journal-title":"Nat. Neurosci."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1159\/000332816","article-title":"Linking amyloid-\u03b2 and tau: Amyloid-\u03b2 induced synaptic dysfunction via local wreckage of the neuronal cytoskeleton","volume":"10","author":"Zempel","year":"2012","journal-title":"Neurodegener. Dis."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/j.jbiomech.2019.01.046","article-title":"Dynamic effect of beta-amyloid 42 on cell mechanics","volume":"86","author":"Gao","year":"2019","journal-title":"J. Biomech."},{"key":"ref_9","doi-asserted-by":"crossref","unstructured":"Varshavskaya, K.B., Barykin, E.P., Timoshenko, R.V., Kolmogorov, V.S., Erofeev, A.S., Gorelkin, P.V., Mitkevich, V.A., and Makarov, A.A. (2024). Post-translational modifications of beta-amyloid modulate its effect on cell mechanical properties and influence cytoskeletal signaling cascades. Front. Mol. Neurosci., 17.","DOI":"10.3389\/fnmol.2024.1501874"},{"key":"ref_10","first-page":"2764","article-title":"Experimental study on the neurotoxic effect of \u03b2-amyloid on the cytoskeleton of PC12 cells","volume":"41","author":"Wang","year":"2018","journal-title":"Int. J. Mol. Med."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1016\/j.cell.2022.12.032","article-title":"Hallmarks of neurodegenerative diseases","volume":"186","author":"Wilson","year":"2023","journal-title":"Cell"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1146\/annurev.neuro.26.010302.081142","article-title":"Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders","volume":"26","author":"Caughey","year":"2003","journal-title":"Annu. Rev. Neurosci."},{"key":"ref_13","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_14","doi-asserted-by":"crossref","unstructured":"Uddin, M.S., Kabir, M.T., Rahman, M.S., Behl, T., Jeandet, P., Ashraf, G.M., Najda, A., Bin-Jumah, M.N., El-Seedi, H.R., and Abdel-Daim, M.M. (2020). Revisiting the Amyloid Cascade Hypothesis: From Anti-A\u03b2 Therapeutics to Auspicious New Ways for Alzheimer\u2019s Disease. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21165858"},{"key":"ref_15","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_16","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1007\/s00221-011-2894-6","article-title":"The role of APP and APLP for synaptic transmission, plasticity, and network function: Lessons from genetic mouse models","volume":"217","author":"Korte","year":"2012","journal-title":"Exp. Brain Res."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"1661","DOI":"10.4103\/1673-5374.257511","article-title":"Physiological effects of amyloid precursor protein and its derivatives on neural stem cell biology and signaling pathways involved","volume":"14","author":"Coronel","year":"2019","journal-title":"Neural Regen. Res."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"21948","DOI":"10.1038\/srep21948","article-title":"Impaired theta-gamma coupling in APP-deficient mice","volume":"6","author":"Zhang","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.mcn.2016.09.002","article-title":"Amyloid \u03b2 precursor protein regulates neuron survival and maturation in the adult mouse brain","volume":"77","author":"Wang","year":"2016","journal-title":"Mol. Cell Neurosci."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"877","DOI":"10.1126\/science.3810169","article-title":"Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer\u2019s disease","volume":"235","author":"Goldgaber","year":"1987","journal-title":"Science"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"1680","DOI":"10.1016\/j.neurobiolaging.2012.12.004","article-title":"Differential processing of amyloid precursor protein in brain and in peripheral blood leukocytes","volume":"34","author":"Delvaux","year":"2013","journal-title":"Neurobiol. Aging"},{"key":"ref_22","doi-asserted-by":"crossref","unstructured":"Sehar, U., Rawat, P., Reddy, A.P., Kopel, J., and Reddy, P.H. (2022). Amyloid Beta in Aging and Alzheimer\u2019s Disease. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms232112924"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1007\/s11011-019-00516-y","article-title":"Mechanisms of action of amyloid-beta and its precursor protein in neuronal cell death","volume":"35","author":"Leong","year":"2020","journal-title":"Metab. Brain Dis."},{"key":"ref_24","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_25","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1186\/scrt77","article-title":"Soluble amyloid precursor protein: A novel proliferation factor of adult progenitor cells of ectodermal and mesodermal origin","volume":"2","author":"Demars","year":"2011","journal-title":"Stem Cell Res. Ther."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1016\/j.pneurobio.2017.05.005","article-title":"Small things matter: Implications of APP intracellular domain AICD nuclear signaling in the progression and pathogenesis of Alzheimer\u2019s disease","volume":"156","author":"Bukhari","year":"2017","journal-title":"Prog. Neurobiol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"103760","DOI":"10.1016\/j.mcn.2022.103760","article-title":"The AICD fragment of APP initiates a FoxO3a mediated response via FANCD2","volume":"122","author":"Greenwood","year":"2022","journal-title":"Mol. Cell Neurosci."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1016\/j.mehy.2010.12.013","article-title":"Peptide p3 may play a neuroprotective role in the brain","volume":"76","author":"Han","year":"2011","journal-title":"Med. Hypotheses"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1146\/annurev-neuro-061010-113613","article-title":"Amyloid precursor protein processing and Alzheimer\u2019s disease","volume":"34","author":"Wong","year":"2011","journal-title":"Annu. Rev. Neurosci."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/S0896-6273(03)00810-9","article-title":"BACE1 deficiency rescues memory deficits and cholinergic dysfunction in a mouse model of Alzheimer\u2019s disease","volume":"41","author":"Ohno","year":"2004","journal-title":"Neuron"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1111\/j.1460-9568.2005.04551.x","article-title":"Temporal memory deficits in Alzheimer\u2019s mouse models: Rescue by genetic deletion of BACE1","volume":"23","author":"Ohno","year":"2006","journal-title":"Eur. J. Neurosci."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1111\/j.1582-4934.2004.tb00267.x","article-title":"\u03b2-secretase-cleaved amyloid precursor protein in Alzheimer brain: A morphologic study","volume":"8","author":"Sennvik","year":"2004","journal-title":"J. Cell Mol. Med."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1096\/fj.10-157230","article-title":"Mitochondrial \u03b3-secretase participates in the metabolism of mitochondria-associated amyloid precursor protein","volume":"25","author":"Pavlov","year":"2011","journal-title":"FASEB J."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"827","DOI":"10.1515\/hsz-2016-0146","article-title":"Membrane trafficking and proteolytic activity of \u03b3-secretase in Alzheimer\u2019s disease","volume":"397","author":"Kanatsu","year":"2016","journal-title":"Biol. Chem."},{"key":"ref_35","doi-asserted-by":"crossref","unstructured":"Fourriere, L., and Gleeson, P.A. (2025). Organelle perturbation in Alzheimer\u2019s disease: Do intracellular amyloid-ss and the fragmented Golgi mediate early intracellular neurotoxicity?. Front. Cell Dev. Biol., 13.","DOI":"10.3389\/fcell.2025.1550211"},{"key":"ref_36","first-page":"1549","article-title":"Localization and Processing of the Amyloid-\u03b2 Protein Precursor in Mitochondria-Associated Membranes","volume":"55","author":"Suski","year":"2017","journal-title":"J. Alzheimers Dis."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"6075","DOI":"10.1073\/pnas.89.13.6075","article-title":"Beta-amyloid precursor protein cleavage by a membrane-bound protease","volume":"89","author":"Sisodia","year":"1992","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"E559","DOI":"10.1073\/pnas.1100745108","article-title":"ADP ribosylation factor 6 (ARF6) controls amyloid precursor protein (APP) processing by mediating the endosomal sorting of BACE1","volume":"108","author":"Sannerud","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_39","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_40","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1002\/psc.2975","article-title":"Comparison of neurotoxicity of different aggregated forms of A\u03b240, A\u03b242 and A\u03b243 in cell cultures","volume":"23","author":"Fu","year":"2017","journal-title":"J. Pept. Sci."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"9384","DOI":"10.1073\/pnas.1401564111","article-title":"Differences in nucleation behavior underlie the contrasting aggregation kinetics of the A\u03b240 and A\u03b242 peptides","volume":"111","author":"Meisl","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_42","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_43","doi-asserted-by":"crossref","first-page":"800","DOI":"10.1038\/nn.4018","article-title":"Three dimensions of the amyloid hypothesis: Time, space and \u2018wingmen\u2019","volume":"18","author":"Musiek","year":"2015","journal-title":"Nat. Neurosci."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1136\/jnnp.57.4.419","article-title":"Beta amyloid protein deposition in the brain after severe head injury: Implications for the pathogenesis of Alzheimer\u2019s disease","volume":"57","author":"Roberts","year":"1994","journal-title":"J. Neurol. Neurosurg. Psychiatry"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"37111","DOI":"10.1074\/jbc.274.52.37111","article-title":"Cu(II) potentiation of alzheimer A\u03b2 neurotoxicity. Correlation with cell-free hydrogen peroxide production and metal reduction","volume":"274","author":"Huang","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"1188","DOI":"10.1016\/j.cell.2012.02.022","article-title":"The amyloid state of proteins in human diseases","volume":"148","author":"Eisenberg","year":"2012","journal-title":"Cell"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"e2305823120","DOI":"10.1073\/pnas.2305823120","article-title":"Quantitative NMR analysis of the mechanism and kinetics of chaperone Hsp104 action on amyloid-\u03b242 aggregation and fibril formation","volume":"120","author":"Ghosh","year":"2023","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1021\/ar050063s","article-title":"Elucidating amyloid \u03b2-protein folding and assembly: A multidisciplinary approach","volume":"39","author":"Teplow","year":"2006","journal-title":"Acc. Chem. Res."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"4897","DOI":"10.1073\/pnas.97.9.4897","article-title":"Fiber diffraction of synthetic \u03b1-synuclein filaments shows amyloid-like cross-\u03b2 conformation","volume":"97","author":"Serpell","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1038\/s42004-025-01537-8","article-title":"Structural convergence and membrane interactions of A\u03b21\u201342 along the primary nucleation process studied by solid state NMR","volume":"8","author":"Kengwerere","year":"2025","journal-title":"Commun. Chem."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"688","DOI":"10.1016\/j.csbj.2023.12.015","article-title":"Helix-to-sheet transition of the A\u03b242 peptide revealed using an enhanced sampling strategy and Markov state model","volume":"23","author":"Wen","year":"2024","journal-title":"Comput. Struct. Biotechnol. J."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"22364","DOI":"10.1074\/jbc.272.35.22364","article-title":"Amyloid \u03b2-protein fibrillogenesis. Detection of a protofibrillar intermediate","volume":"272","author":"Walsh","year":"1997","journal-title":"J. Biol. Chem."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"105208","DOI":"10.1016\/j.neuint.2021.105208","article-title":"Aggregation and structure of amyloid \u03b2-protein","volume":"151","author":"Ono","year":"2021","journal-title":"Neurochem. Int."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"e202400277","DOI":"10.1002\/chem.202400277","article-title":"Aggregation Mechanisms and Molecular Structures of Amyloid-\u03b2 in Alzheimer\u2019s Disease","volume":"30","author":"Niu","year":"2024","journal-title":"Chemistry"},{"key":"ref_55","doi-asserted-by":"crossref","unstructured":"Zampar, S., Di Gregorio, S.E., Grimmer, G., Watts, J.C., and Ingelsson, M. (2024). \u201cPrion-like\u201d seeding and propagation of oligomeric protein assemblies in neurodegenerative disorders. Front. Neurosci., 18.","DOI":"10.3389\/fnins.2024.1436262"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"4352","DOI":"10.1039\/C7SC00215G","article-title":"Modulation of electrostatic interactions to reveal a reaction network unifying the aggregation behaviour of the A\u03b242 peptide and its variants","volume":"8","author":"Meisl","year":"2017","journal-title":"Chem. Sci."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"e200007","DOI":"10.2142\/biophysico.bppb-v20.0007","article-title":"Molecular mechanisms of amyloid-\u03b2 peptide fibril and oligomer formation: NMR-based challenges","volume":"20","author":"Hiroaki","year":"2023","journal-title":"Biophys. Physicobiol."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1126\/science.abm7285","article-title":"Cryo-EM structures of amyloid-\u03b2 42 filaments from human brains","volume":"375","author":"Yang","year":"2022","journal-title":"Science"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"5468","DOI":"10.1073\/pnas.1219476110","article-title":"Atomic structure and hierarchical assembly of a cross-\u03b2 amyloid fibril","volume":"110","author":"Fitzpatrick","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"6606","DOI":"10.1021\/ja0342042","article-title":"Constraints on supramolecular structure in amyloid fibrils from two-dimensional solid-state NMR spectroscopy with uniform isotopic labeling","volume":"125","author":"Tycko","year":"2003","journal-title":"J. Am. Chem. Soc."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"e2200086","DOI":"10.1002\/bies.202200086","article-title":"Amyloid fibrils act as a reservoir of soluble oligomers, the main culprits in protein deposition diseases","volume":"44","author":"Bigi","year":"2022","journal-title":"Bioessays"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1016\/j.tibs.2006.01.002","article-title":"Amyloids, prions and the inherent infectious nature of misfolded protein aggregates","volume":"31","author":"Soto","year":"2006","journal-title":"Trends Biochem. Sci."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"8667","DOI":"10.1039\/C8CC02204F","article-title":"Secondary nucleation in amyloid formation","volume":"54","author":"Tornquist","year":"2018","journal-title":"Chem. Commun."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"e2404916","DOI":"10.1002\/advs.202404916","article-title":"Secondary Nucleation of A\u03b2 Revealed by Single-Molecule and Computational Approaches","volume":"11","author":"Meyer","year":"2024","journal-title":"Adv. Sci."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1515\/revneuro-2017-0063","article-title":"Amyloid toxicity in Alzheimer\u2019s disease","volume":"29","author":"Reiss","year":"2018","journal-title":"Rev. Neurosci."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1016\/S1474-4422(17)30037-6","article-title":"The prion model for progression and diversity of neurodegenerative diseases","volume":"16","author":"Stopschinski","year":"2017","journal-title":"Lancet Neurol."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"1255555","DOI":"10.1126\/science.1255555","article-title":"Neurodegeneration. Alzheimer\u2019s and Parkinson\u2019s diseases: The prion concept in relation to assembled A\u03b2, tau, and \u03b1-synuclein","volume":"349","author":"Goedert","year":"2015","journal-title":"Science"},{"key":"ref_68","doi-asserted-by":"crossref","unstructured":"Liu, L., Drouet, V., Wu, J.W., Witter, M.P., Small, S.A., Clelland, C., and Duff, K. (2012). Trans-synaptic spread of tau pathology in vivo. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0031302"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"8767","DOI":"10.1523\/JNEUROSCI.0615-12.2012","article-title":"Spreading of neurodegenerative pathology via neuron-to-neuron transmission of beta-amyloid","volume":"32","author":"Nath","year":"2012","journal-title":"J. Neurosci."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"223","DOI":"10.3233\/JAD-2011-110182","article-title":"Targeting oligomers in neurodegenerative disorders: Lessons from \u03b1-synuclein, tau, and amyloid-\u03b2 peptide","volume":"24","author":"Gadad","year":"2011","journal-title":"J. Alzheimers Dis."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"9319","DOI":"10.1523\/JNEUROSCI.3246-05.2005","article-title":"Amyloid plaques and amyloid-\u03b2 oligomers: An ongoing debate","volume":"25","author":"Lesne","year":"2005","journal-title":"J. Neurosci."},{"key":"ref_72","doi-asserted-by":"crossref","unstructured":"Hohmann, T., and Dehghani, F. (2019). The Cytoskeleton-A Complex Interacting Meshwork. Cells, 8.","DOI":"10.3390\/cells8040362"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/j.ceb.2016.09.003","article-title":"Microtubule-organizing centers: From the centrosome to non-centrosomal sites","volume":"44","author":"Sanchez","year":"2017","journal-title":"Curr. Opin. Cell Biol."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"2168","DOI":"10.4161\/cc.8.14.9074","article-title":"Microtubule network asymmetry in motile cells: Role of Golgi-derived array","volume":"8","author":"Vinogradova","year":"2009","journal-title":"Cell Cycle"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1007\/978-1-0716-3969-6_16","article-title":"Analysis of Microtubule Polymerization During Axon Outgrowth Using Fluorescently Labeled Microtubule Plus-End Tracking Proteins","volume":"2831","year":"2024","journal-title":"Methods Mol. Biol."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/j.tcb.2014.10.004","article-title":"Post-translational modifications of tubulin: Pathways to functional diversity of microtubules","volume":"25","author":"Song","year":"2015","journal-title":"Trends Cell Biol."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"388","DOI":"10.1096\/fj.201800604R","article-title":"Kinesin-dependent transport of keratin filaments: A unified mechanism for intermediate filament transport","volume":"33","author":"Robert","year":"2019","journal-title":"FASEB J."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"1675","DOI":"10.1091\/mbc.E14-09-1398","article-title":"Microtubule-dependent transport and dynamics of vimentin intermediate filaments","volume":"26","author":"Hookway","year":"2015","journal-title":"Mol. Biol. Cell"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1002\/(SICI)1097-4652(199612)169:3<439::AID-JCP4>3.0.CO;2-P","article-title":"Balanced mechanical forces and microtubule contribution to fibroblast contraction","volume":"169","author":"Brown","year":"1996","journal-title":"J. Cell Physiol."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1146\/annurev-biochem-060815-014528","article-title":"Mechanisms of Mitotic Spindle Assembly","volume":"85","author":"Petry","year":"2016","journal-title":"Annu. Rev. Biochem."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1038\/nrm2816","article-title":"Unleashing formins to remodel the actin and microtubule cytoskeletons","volume":"11","author":"Chesarone","year":"2010","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1080\/19490992.2015.1090670","article-title":"Competition and collaboration between different actin assembly pathways allows for homeostatic control of the actin cytoskeleton","volume":"5","author":"Rotty","year":"2014","journal-title":"Bioarchitecture"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1038\/s44303-024-00054-y","article-title":"Super-resolution imaging of the neuronal cytoskeleton","volume":"2","author":"Leterrier","year":"2024","journal-title":"npj Imaging"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1016\/j.devcel.2014.09.002","article-title":"Cofilin-2 controls actin filament length in muscle sarcomeres","volume":"31","author":"Kremneva","year":"2014","journal-title":"Dev. Cell"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"102534","DOI":"10.1016\/j.conb.2022.102534","article-title":"Structural LTP: Signal transduction, actin cytoskeleton reorganization, and membrane remodeling of dendritic spines","volume":"74","author":"Yang","year":"2022","journal-title":"Curr. Opin. Neurobiol."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1091\/mbc.e09-07-0596","article-title":"Molecular architecture of synaptic actin cytoskeleton in hippocampal neurons reveals a mechanism of dendritic spine morphogenesis","volume":"21","author":"Korobova","year":"2010","journal-title":"Mol. Biol. Cell"},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1038\/nrm1438","article-title":"Intermediate filaments mediate cytoskeletal crosstalk","volume":"5","author":"Chang","year":"2004","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"re1","DOI":"10.1091\/mbc.E23-11-0438","article-title":"Neurofilament Biophysics: From Structure to Biomechanics","volume":"35","author":"Ding","year":"2024","journal-title":"Mol. Biol. Cell"},{"key":"ref_89","doi-asserted-by":"crossref","unstructured":"Sainio, M.T., Rasila, T., Molchanova, S.M., Jarvilehto, J., Torregrosa-Munumer, R., Harjuhaahto, S., Pennonen, J., Huber, N., Herukka, S.K., and Haapasalo, A. (2021). Neurofilament Light Regulates Axon Caliber, Synaptic Activity, and Organelle Trafficking in Cultured Human Motor Neurons. Front. Cell Dev. Biol., 9.","DOI":"10.3389\/fcell.2021.820105"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1016\/j.ceb.2015.01.003","article-title":"Neurofilament assembly and function during neuronal development","volume":"32","author":"Kornreich","year":"2015","journal-title":"Curr. Opin. Cell Biol."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"161","DOI":"10.2147\/JIR.S391325","article-title":"Review of Neurofilaments as Biomarkers in Sepsis-Associated Encephalopathy","volume":"16","author":"Zhang","year":"2023","journal-title":"J. Inflamm. Res."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"1975","DOI":"10.1093\/brain\/awaa098","article-title":"Neurofilaments: Neurobiological foundations for biomarker applications","volume":"143","author":"Gafson","year":"2020","journal-title":"Brain"},{"key":"ref_93","doi-asserted-by":"crossref","unstructured":"Pelucchi, S., Stringhi, R., and Marcello, E. (2020). Dendritic Spines in Alzheimer\u2019s Disease: How the Actin Cytoskeleton Contributes to Synaptic Failure. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21030908"},{"key":"ref_94","doi-asserted-by":"crossref","unstructured":"Jiang, G., Xie, G., Li, X., and Xiong, J. (2025). Cytoskeletal Proteins and Alzheimer\u2019s Disease Pathogenesis: Focusing on the Interplay with Tau Pathology. Biomolecules, 15.","DOI":"10.3390\/biom15060831"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1007\/978-3-030-25650-0_12","article-title":"The Cytoskeleton as a Modulator of Aging and Neurodegeneration","volume":"1178","author":"Kounakis","year":"2019","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"5819","DOI":"10.1073\/pnas.1017033108","article-title":"Soluble amyloid \u03b2-protein dimers isolated from Alzheimer cortex directly induce Tau hyperphosphorylation and neuritic degeneration","volume":"108","author":"Jin","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"11938","DOI":"10.1523\/JNEUROSCI.2357-10.2010","article-title":"A\u03b2 oligomers cause localized Ca2+ elevation, missorting of endogenous Tau into dendrites, Tau phosphorylation, and destruction of microtubules and spines","volume":"30","author":"Zempel","year":"2010","journal-title":"J. Neurosci."},{"key":"ref_98","first-page":"1068","article-title":"Dynamic Microtubules in Alzheimer\u2019s Disease: Association with Dendritic Spine Pathology","volume":"83","author":"Pchitskaya","year":"2018","journal-title":"Biochemistry"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"565","DOI":"10.3233\/JAD-2011-110423","article-title":"Amyloid-\u03b2-induced mitochondrial dysfunction impairs the autophagic lysosomal pathway in a tubulin dependent pathway","volume":"26","author":"Silva","year":"2011","journal-title":"J. Alzheimers Dis."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"1623","DOI":"10.1016\/S0002-9440(10)64296-4","article-title":"Microtubule reduction in Alzheimer\u2019s disease and aging is independent of tau filament formation","volume":"162","author":"Cash","year":"2003","journal-title":"Am. J. Pathol."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"3227","DOI":"10.1016\/j.febslet.2010.06.014","article-title":"Microtubule destruction induces tau liberation and its subsequent phosphorylation","volume":"584","author":"Miyasaka","year":"2010","journal-title":"FEBS Lett."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1186\/s40478-019-0857-5","article-title":"Kinesin light chain-1 serine-460 phosphorylation is altered in Alzheimer\u2019s disease and regulates axonal transport and processing of the amyloid precursor protein","volume":"7","author":"Morotz","year":"2019","journal-title":"Acta Neuropathol. Commun."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"844","DOI":"10.2174\/156720512802455322","article-title":"Amyloid-Beta peptide 1\u201342 causes microtubule deregulation through N-methyl-D-aspartate receptors in mature hippocampal cultures","volume":"9","author":"Mota","year":"2012","journal-title":"Curr. Alzheimer Res."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1111\/jnc.14011","article-title":"Microtubule dynamics and the neurodegenerative triad of Alzheimer\u2019s disease: The hidden connection","volume":"143","author":"Brandt","year":"2017","journal-title":"J. Neurochem."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"9166","DOI":"10.1523\/JNEUROSCI.1074-10.2010","article-title":"Amyloid-\u03b2 peptide oligomers disrupt axonal transport through an NMDA receptor-dependent mechanism that is mediated by glycogen synthase kinase 3\u03b2 in primary cultured hippocampal neurons","volume":"30","author":"Decker","year":"2010","journal-title":"J. Neurosci."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"2118","DOI":"10.1021\/acs.jmedchem.8b00028","article-title":"Radiosynthesis and in vivo evaluation of [11C]MPC-6827, the First Brain Penetrant Microtubule PET Ligand","volume":"61","author":"Kumar","year":"2018","journal-title":"J. Med. Chem."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"3745","DOI":"10.1021\/acschemneuro.3c00527","article-title":"Preliminary PET imaging of microtubule-based PET radioligand [11C]MPC-6827 in a nonhuman primate model of Alzheimer\u2019s disease","volume":"14","author":"Bhoopal","year":"2023","journal-title":"ACS Chem. Neurosci."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1186\/s13550-022-00912-z","article-title":"Preliminary mechanistic insights of a brain-penetrant microtubule imaging PET ligand in a tau-knockout mouse model","volume":"12","author":"Damuka","year":"2022","journal-title":"EJNMMI Res."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"e70670","DOI":"10.1002\/alz.70670","article-title":"Imaging microtubule dynamics: A new frontier in biomarker development for neurodegenerative diseases","volume":"21","author":"Damuka","year":"2025","journal-title":"Alzheimers Dement."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"6082","DOI":"10.1002\/alz.14083","article-title":"Exploring microtubule dynamics in Alzheimer\u2019s disease: Longitudinal assessment using [11C]MPC-6827 PET imaging in rodent models of Alzheimer\u2019s-related pathology","volume":"20","author":"Damuka","year":"2024","journal-title":"Alzheimers Dement."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1007\/s00401-016-1558-9","article-title":"Presynaptic dystrophic neurites surrounding amyloid plaques are sites of microtubule disruption, BACE1 elevation, and increased A\u03b2 generation in Alzheimer\u2019s disease","volume":"132","author":"Sadleir","year":"2016","journal-title":"Acta Neuropathol."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"3161","DOI":"10.1083\/jcb.201701045","article-title":"Stabilization of dynamic microtubules by mDia1 drives Tau-dependent A\u03b21\u201342 synaptotoxicity","volume":"216","author":"Qu","year":"2017","journal-title":"J. Cell Biol."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1016\/j.nbd.2006.02.010","article-title":"Soluble oligomers of amyloid-\u03b2 peptide induce neuronal apoptosis by activating a cPLA2-dependent sphingomyelinase-ceramide pathway","volume":"23","author":"Youssef","year":"2006","journal-title":"Neurobiol. Dis."},{"key":"ref_114","first-page":"1117","article-title":"The A\u03b21\u201342 peptide regulates microtubule stability independently of tau","volume":"127","author":"Pianu","year":"2014","journal-title":"J. Cell Sci."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"2486","DOI":"10.1093\/brain\/awab436","article-title":"Tubulin tyrosination regulates synaptic function and is disrupted in Alzheimer\u2019s disease","volume":"145","author":"Peris","year":"2022","journal-title":"Brain"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1016\/j.neuropharm.2016.01.002","article-title":"A\u03b2-mediated spine changes in the hippocampus are microtubule-dependent and can be reversed by a subnanomolar concentration of the microtubule-stabilizing agent Epothilone D","volume":"105","author":"Penazzi","year":"2016","journal-title":"Neuropharmacology"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"14776","DOI":"10.1038\/s41598-020-71767-4","article-title":"Enhancing microtubule stabilization rescues cognitive deficits and ameliorates pathological phenotype in an amyloidogenic alzheimer\u2019s disease model","volume":"10","author":"Navarro","year":"2020","journal-title":"Sci. Rep."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1186\/s13041-021-00833-3","article-title":"Overexpression of LIMK1 in hippocampal excitatory neurons improves synaptic plasticity and social recognition memory in APP\/PS1 mice","volume":"14","author":"Zhang","year":"2021","journal-title":"Mol. Brain"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1002\/cm.21037","article-title":"The Ca2+ and Rho GTPase signaling pathways underlying activity-dependent actin remodeling at dendritic spines","volume":"69","author":"Saneyoshi","year":"2012","journal-title":"Cytoskeleton"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"2190","DOI":"10.1091\/mbc.e05-11-1016","article-title":"Enhancement of actin-depolymerizing factor\/cofilin-dependent actin disassembly by actin-interacting protein 1 is required for organized actin filament assembly in the Caenorhabditis elegans body wall muscle","volume":"17","author":"Mohri","year":"2006","journal-title":"Mol. Biol. Cell"},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"921","DOI":"10.1038\/cdd.2015.5","article-title":"Slingshot-Cofilin activation mediates mitochondrial and synaptic dysfunction via A\u03b2 ligation to \u03b21-integrin conformers","volume":"22","author":"Woo","year":"2015","journal-title":"Cell Death Differ."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"1399","DOI":"10.1126\/science.1242077","article-title":"Human LilrB2 is a beta-amyloid receptor and its murine homolog PirB regulates synaptic plasticity in an Alzheimer\u2019s model","volume":"341","author":"Kim","year":"2013","journal-title":"Science"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1186\/1750-1326-6-10","article-title":"Amyloid \u03b2 dimers\/trimers potently induce cofilin-actin rods that are inhibited by maintaining cofilin-phosphorylation","volume":"6","author":"Davis","year":"2011","journal-title":"Mol. Neurodegener."},{"key":"ref_124","doi-asserted-by":"crossref","unstructured":"Tahtamouni, L.H., Alderfer, S.A., Kuhn, T.B., Minamide, L.S., Chanda, S., Ruff, M.R., and Bamburg, J.R. (2023). Characterization of a Human Neuronal Culture System for the Study of Cofilin-Actin Rod Pathology. Biomedicines, 11.","DOI":"10.3390\/biomedicines11112942"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1038\/s41419-025-07741-7","article-title":"Role of LIMK1-cofilin-actin axis in dendritic spine dynamics in Alzheimer\u2019s disease","volume":"16","author":"Paciello","year":"2025","journal-title":"Cell Death Dis."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"1676","DOI":"10.1038\/cddis.2015.37","article-title":"RanBP9 at the intersection between cofilin and A\u03b2 pathologies: Rescue of neurodegenerative changes by RanBP9 reduction","volume":"6","author":"Woo","year":"2015","journal-title":"Cell Death Dis."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"12994","DOI":"10.1523\/JNEUROSCI.3531-09.2009","article-title":"Activated actin-depolymerizing factor\/cofilin sequesters phosphorylated microtubule-associated protein during the assembly of alzheimer-like neuritic cytoskeletal striations","volume":"29","author":"Whiteman","year":"2009","journal-title":"J. Neurosci."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"750","DOI":"10.1126\/science.1141736","article-title":"Reducing endogenous tau ameliorates amyloid \u03b2-induced deficits in an Alzheimer\u2019s disease mouse model","volume":"316","author":"Roberson","year":"2007","journal-title":"Science"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"1329","DOI":"10.1242\/jcs.065698","article-title":"Overlapping and distinct functions for cofilin, coronin and Aip1 in actin dynamics in vivo","volume":"123","author":"Lin","year":"2010","journal-title":"J. Cell Sci."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"S131","DOI":"10.3233\/JAD-190585","article-title":"Cofilin, a Master Node Regulating Cytoskeletal Pathogenesis in Alzheimer\u2019s Disease","volume":"72","author":"Kang","year":"2019","journal-title":"J. Alzheimers Dis."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1152\/physrev.00014.2003","article-title":"Long-term potentiation and memory","volume":"84","author":"Lynch","year":"2004","journal-title":"Physiol. Rev."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"5146","DOI":"10.1074\/jbc.M115.713495","article-title":"Actin-interacting Protein 1 Promotes Disassembly of Actin-depolymerizing Factor\/Cofilin-bound Actin Filaments in a pH-dependent Manner","volume":"291","author":"Nomura","year":"2016","journal-title":"J. Biol. Chem."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"2500","DOI":"10.1016\/j.bbadis.2014.10.004","article-title":"Inactivation of brain Cofilin-1 by age, Alzheimer\u2019s disease and \u03b3-secretase","volume":"1842","author":"Barone","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1111\/jnc.13688","article-title":"Rho-associated protein kinase 1 (ROCK1) is increased in Alzheimer\u2019s disease and ROCK1 depletion reduces amyloid-\u03b2 levels in brain","volume":"138","author":"Henderson","year":"2016","journal-title":"J. Neurochem."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"1910","DOI":"10.1523\/JNEUROSCI.2983-18.2018","article-title":"Pyk2 Signaling through Graf1 and RhoA GTPase Is Required for Amyloid-\u03b2 Oligomer-Triggered Synapse Loss","volume":"39","author":"Lee","year":"2019","journal-title":"J. Neurosci."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"63","DOI":"10.3233\/JAD-2012-101575","article-title":"Fibrillar amyloid-\u03b21\u201342 modifies actin organization affecting the cofilin phosphorylation state: A role for Rac1\/cdc42 effector proteins and the slingshot phosphatase","volume":"29","author":"Henriquez","year":"2012","journal-title":"J. Alzheimers Dis."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1016\/j.jalz.2017.09.008","article-title":"Amyloid \u03b2 synaptotoxicity is wnt-pcp dependent and blocked by fasudil","volume":"14","author":"Sellers","year":"2018","journal-title":"Alzheimers Dement."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"eaaw9318","DOI":"10.1126\/scisignal.aaw9318","article-title":"Pharmacologic inhibition of limk1 provides dendritic spine resilience against beta-amyloid","volume":"12","author":"Henderson","year":"2019","journal-title":"Sci. Signal"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/j.jns.2005.03.015","article-title":"Neurofilament phosphoforms: Surrogate markers for axonal injury, degeneration and loss","volume":"233","author":"Petzold","year":"2005","journal-title":"J. Neurol. Sci."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"650","DOI":"10.1523\/JNEUROSCI.06-03-00650.1986","article-title":"Expression of neurofilament subunits in neurons of the central and peripheral nervous system: An immunohistochemical study with monoclonal antibodies","volume":"6","author":"Trojanowski","year":"1986","journal-title":"J. Neurosci."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1038\/s41591-018-0304-3","article-title":"Serum neurofilament dynamics predicts neurodegeneration and clinical progression in presymptomatic Alzheimer\u2019s disease","volume":"25","author":"Preische","year":"2019","journal-title":"Nat. Med."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1001\/jamaneurol.2015.3037","article-title":"Association of Cerebrospinal Fluid Neurofilament Light Concentration With Alzheimer Disease Progression","volume":"73","author":"Zetterberg","year":"2016","journal-title":"JAMA Neurol."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1016\/j.neuron.2016.05.018","article-title":"Neurofilament Light Chain in Blood and CSF as Marker of Disease Progression in Mouse Models and in Neurodegenerative Diseases","volume":"91","author":"Bacioglu","year":"2016","journal-title":"Neuron"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/j.nbd.2017.04.007","article-title":"NF-L in cerebrospinal fluid and serum is a biomarker of neuronal damage in an inducible mouse model of neurodegeneration","volume":"104","author":"Brureau","year":"2017","journal-title":"Neurobiol. Dis."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1001\/jamaneurol.2016.6117","article-title":"Association of Plasma Neurofilament Light with Neurodegeneration in Patients With Alzheimer Disease","volume":"74","author":"Mattsson","year":"2017","journal-title":"JAMA Neurol."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"5989","DOI":"10.1038\/s41380-020-0818-1","article-title":"Amyloid-\u03b2 modulates the association between neurofilament light chain and brain atrophy in Alzheimer\u2019s disease","volume":"26","author":"Kang","year":"2021","journal-title":"Mol. Psychiatry"},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"1944","DOI":"10.1111\/febs.12224","article-title":"Redox regulation of protein kinases","volume":"280","author":"Corcoran","year":"2013","journal-title":"FEBS J."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"36","DOI":"10.3390\/diseases1010036","article-title":"The nervous system cytoskeleton under oxidative stress","volume":"1","author":"Gardiner","year":"2013","journal-title":"Diseases"},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"1691","DOI":"10.1056\/NEJMoa2100708","article-title":"Donanemab in early alzheimer\u2019s disease","volume":"384","author":"Mintun","year":"2021","journal-title":"N. Engl. J. Med."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1056\/NEJMoa2212948","article-title":"Lecanemab in early alzheimer\u2019s disease","volume":"388","author":"Swanson","year":"2023","journal-title":"N. Engl. J. Med."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"e12791","DOI":"10.1111\/acel.12791","article-title":"Impaired AMPA signaling and cytoskeletal alterations induce early synaptic dysfunction in a mouse model of Alzheimer\u2019s disease","volume":"17","author":"Prieto","year":"2018","journal-title":"Aging Cell"},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"2149","DOI":"10.1016\/S0042-6989(01)00090-6","article-title":"The premotor region essential for rapid vertical eye movements shows early involvement in Alzheimer\u2019s disease-related cytoskeletal pathology","volume":"41","author":"Rub","year":"2001","journal-title":"Vis. Res."}],"container-title":["Pathophysiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1873-149X\/33\/1\/14\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,2,3]],"date-time":"2026-02-03T10:43:20Z","timestamp":1770115400000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1873-149X\/33\/1\/14"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,2,3]]},"references-count":152,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2026,3]]}},"alternative-id":["pathophysiology33010014"],"URL":"https:\/\/doi.org\/10.3390\/pathophysiology33010014","relation":{},"ISSN":["1873-149X"],"issn-type":[{"value":"1873-149X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,2,3]]}}}