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Tau Oligomers: The Toxic Player at Synapses in Alzheimer’s Disease
Open accessAbstract
Alzheimer's disease (AD) is a progressive disorder in which the most noticeable symptoms are cognitive impairment and memory loss. However, the precise mechanism by which those symptoms develop remains unknown. Of note, neuronal loss occurs at sites where synaptic dysfunction is observed earlier, suggesting that altered synaptic connections precede neuronal loss. The abnormal accumulation of amyloid-β (Aβ) and tau protein is the main histopathological feature of the disease. Several lines of evidence suggest that the small oligomeric forms of Aβ and tau may act synergistically to promote synaptic dysfunction in AD. Remarkably, tau pathology correlates better with the progression of the disease than Aβ. Recently, a growing number of studies have begun to suggest that missorting of tau protein from the axon to the dendrites is required to mediate the detrimental effects of Aβ. In this review we discuss the novel findings regarding the potential mechanisms by which tau oligomers contribute to synaptic dysfunction in AD.
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“Pathogenic tau has been linked to synaptic dysfunction and loss (69).”
From Modeling late-onset Alzheimer’s disease neuropathology via direct neuronal reprogramming (2024) · cites this paper as [69]
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2 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., & Ashe, K. H. (2006) · Nature · doi:10.1038/nature04533 · Cited by 2,769 · cited 1×
“It seems likely that the increase in trimers in treated mice may be a consequence of Aβ∗56 disassembly which has been suggested to be comprised of four Aβ trimers (Lesne et al., 2006).”
BackgroundRetractedRETRACTED: Soluble α-Synuclein Is a Novel Modulator of Alzheimer's Disease Pathophysiology
Larson, M. E., Sherman, M. A., Greimel, S., Kuskowski, M., Schneider, J. A., Bennett, D. A., & Lesné, S. E. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.0581-12.2012 · Cited by 128
RetractedNeuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123
Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064
Hearing loss and cognitive decline in older adults
Lin, F. R., Yaffe, K., Xia, J., Xue, Q.-L., Harris, T. B., Purchase-Helzner, E., Satterfield, S., Ayonayon, H. N., Ferrucci, L., Simonsick, E. M., et al. (2013) · JAMA Internal Medicine · doi:10.1001/jamainternmed.2013.1868 · Cited by 4,017
Neuropathological alterations in Alzheimer disease
Serrano-Pozo, A., Frosch, M. P., Masliah, E., & Hyman, B. T. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006189 · Cited by 3,345
Amyloid deposition as the central event in the aetiology of Alzheimer’s disease
Hardy, J., & Allsop, D. (1991) · Trends in Pharmacological Sciences · doi:10.1016/0165-6147(91)90609-v · Cited by 2,538
Synapse Loss and Microglial Activation Precede Tangles in a P301S Tauopathy Mouse Model
Yoshiyama, Y., Higuchi, M., Zhang, B., Huang, S.-M., Iwata, N., Saido, T. C., Maeda, J., Suhara, T., Trojanowski, J. Q., & Lee, V. M.-Y. (2007) · Neuron · doi:10.1016/j.neuron.2007.01.010 · Cited by 2,208
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Items 101–169 of 169
Jester, H. M., Gosrani, S. P., Ding, H., Zhou, X., Ko, M., & Ma, T. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-215303 · Cited by 15
Internalization of extracellular Tau oligomers in Alzheimer’s disease
Chinnathambi, S., Rangappa, N., & Chandrashekar, M. (2025) · Advances in clinical chemistry · doi:10.1016/bs.acc.2025.01.005 · Cited by 14
Timofeeva, A. M., Aulova, K. S., & Nevinsky, G. A. (2025) · Brain Sciences · doi:10.3390/brainsci15050486 · Cited by 17
Liu, Z., Cheng, L., Cao, W., Shen, C., Qiu, Y., Li, C., Xiong, Y., Yang, S., Chen, Z., Yin, X., et al. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.135826 · Cited by 13
Varma, N., Singh, I., Dahiya, M. S., Ravi, V. K., & Kumar, S. (2017) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2017.11.096 · Cited by 13
Modulation of tau protein aggregation using ‘Trojan’ sequences
Pandey, G., Morla, S., Kumar, S., & Ramakrishnan, V. (2020) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2020.129569 · Cited by 13
Multistep molecular mechanism of amyloid‐like aggregation of nucleic acid‐binding domain of TDP ‐43
Pillai, M., & Jha, S. K. (2022) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26455 · Cited by 12
Hossen, F., Geng, X. H., Sun, G. Y., Yao, X., & Lee, J. C. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04138-z · Cited by 13
Areche, C., Zapata, F., González, M., Díaz, E., Montecinos, R., Hernández, M., Melo, F., & Cornejo, A. (2019) · ChemistryOpen · doi:10.1002/open.201800222 · Cited by 12
Scialò, C., & Legname, G. (2020) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2020.08.008 · Cited by 12
Jarero-Basulto, J. J., Gasca-Martínez, Y., Rivera-Cervantes, M. C., Gasca‐Martínez, D., González, N., Beas‐Zárate, C., & Gudiño‐Cabrera, G. (2024) · NeuroSci · doi:10.3390/neurosci5020010 · Cited by 11
RetractedArendash, G. W., Lin, X., & Cao, C. (2024) · Journal of Alzheimer s Disease · doi:10.3233/jad-240600 · Cited by 12
Nipecotic Acid Derivatives as Potent Agents against Neurodegeneration: A Preliminary Study
Papagiouvannis, G., Theodosis‐Nobelos, P., & Rekka, E. A. (2022) · Molecules · doi:10.3390/molecules27206984 · Cited by 11
Alzheimer’s Disease and Its Possible Evolutionary Origin: Hypothesis
Whitfield, J. F., Rennie, K., & Chakravarthy, B. (2023) · Cells · doi:10.3390/cells12121618 · Cited by 11
Inflammation in Alzheimer’s disease: A friend or foe?
Chiroma, S. M., Baharuldin, M. T. H., Taib, C. N. M., Amom, Z., Jagadeesan, S., & Moklas, M. A. M. (2018) · Biomedical Research and Therapy · doi:10.15419/bmrat.v5i8.464 · Cited by 11
Extracellular PHF-tau modulates astrocyte mitochondrial dynamics and mediates neuronal connectivity
Zufferey, V., Barve, A., Parietti, E., Belinga, L. N., Bringaud, A., Varisco, Y., Fabbri, K., Capotosti, F., Bezzi, P., Déglon, N., et al. (2025) · Translational Neurodegeneration · doi:10.1186/s40035-025-00474-9 · Cited by 11
Detrez, J. R., Ben-Nejma, I. R. H., Kolen, K. V., Dam, D. V., Deyn, P. P. D., Fransén, E., Verhoye, M., Timmermans, J., Nuydens, R., der Linden, A. V., et al. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.105011 · Cited by 10
Oligomer Formation and Cross‐Seeding: The New Frontier
Farmer, K. M., Gerson, J. E., & Kayed, R. (2016) · Israel Journal of Chemistry · doi:10.1002/ijch.201600103 · Cited by 10
Self-citationÖzsoy, Ş., ÇAKIR, Z., AKÇAY, E., & Gevrek, F. (2023) · TURKISH JOURNAL OF MEDICAL SCIENCES · doi:10.55730/1300-0144.5653 · Cited by 9
Effect of memantine on expression of Bace1-as and Bace1 genes in STZ-induced Alzheimeric rats
Azadfar, P., Noormohammadi, Z., Noroozıan, M., Eidi, A., & Mortazavi, P. (2020) · Molecular Biology Reports · doi:10.1007/s11033-020-05629-7 · Cited by 8
Oligomeropathies, inflammation and prion protein binding
Forloni, G., Vitola, P. L., & Balducci, C. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.822420 · Cited by 8
Gabapentin Antioxidant Derivatives with Anti-Inflammatory and Neuroprotective Potency
Papagiouvannis, G., Theodosis‐Nobelos, P., Tziona, P., Gavalas, A. M., Kourounakis, P. N., & Rekka, E. A. (2021) · Letters in Drug Design & Discovery · doi:10.2174/1570180818666211210161922 · Cited by 8
Liu, J., Jiang, J., He, C., Zhou, L., Zhang, Y., Zhao, S., & Yang, Z. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1451766 · Cited by 6
Langkilde, A. E., Herranz-Trillo, F., Bernadó, P., & Vestergaard, B. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-7816-8_14 · Cited by 6
Vu, K. H. P., Blankenburg, G. H., Lesser‐Rojas, L., & Chou, C. (2022) · Molecules · doi:10.3390/molecules27196448 · Cited by 6
Understanding molecular features of aggregation-resistant tau conformer using oxidized monomer
Jebarupa, B., Mathew, B., Srinivasu, B. Y., Sasikumaran, A., Joseph, S., Mandal, A. K., Thomas, T. S., & Mitra, G. (2019) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2019.03.006 · Cited by 6
Divergent disruptive effects of soluble recombinant tau assemblies on synaptic plasticity in vivo
Yang, Y., Ondrejčák, T., Hu, N., Klyubin, I. V., & Rowan, M. J. (2025) · Molecular Brain · doi:10.1186/s13041-025-01208-8 · Cited by 5
Jafarian, A., Karadag, M., Kocagöncü, E., Lanskey, J. H., Fye, H. K. S., Williams, R., Quinn, A. J., Pitt, J., Raymont, V., Lowe, S. L., et al. (2025) · Human Brain Mapping · doi:10.1002/hbm.70234 · Cited by 6
Mécanismes, facteurs de risque et stratégies thérapeutiques dans la maladie d’Alzheimer
Maître, M., Klein, C., & Mensah‐Nyagan, A. G. (2017) · NPG. Neurologie, psychiatrie, gériatrie/NPG · doi:10.1016/j.npg.2016.12.006 · Cited by 5
Galushkin, A., & Gozes, I. (2024) · Current Research in Biotechnology · doi:10.1016/j.crbiot.2024.100254 · Cited by 4
For better or worse: Immune system involvement in Alzheimer's Disease
Walton, E. L. (2018) · Biomedical Journal · doi:10.1016/j.bj.2018.03.001 · Cited by 4
Tau Protein in Drug-Resistant Epilepsy and Cognitive Decline
Thom, M., & Koepp, M. J. (2021) · Progress in inflammation research · doi:10.1007/978-3-030-67403-8_7 · Cited by 3
Monnet‐Tschudi, F., & FitzGerald, R. (2018) · OECD series on adverse outcome pathways · doi:10.1787/95f569ad-en · Cited by 4
Haque, M. A., Montalbano, M., Khan, S., Puangmalai, N., Bhatt, N. N., Shchankin, N., Jerez, C., & Kayed, R. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2025.167995 · Cited by 2
Hossen, F., Hung, J., Odeh, H., Sun, G. Y., & Lee, J. C. (2025) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2025.1671986 · Cited by 2
Selective vulnerability of human synapses to soluble tau oligomers
Kadamangudi, S., Sánchez-Sánchez, L., Kayed, R., Limón, A., & Taglialatela, G. (2026) · Journal of Alzheimer s Disease · doi:10.1177/13872877261416539 · Cited by 2
Khan, N., De, S., Boddu, S., & Pravala, N. (2026) · The Journal of Prevention of Alzheimer s Disease · doi:10.1016/j.tjpad.2026.100498 · Cited by 3
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Barrantes, F. J. (2026) · Brain · doi:10.1093/brain/awag117 · Cited by 2
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Grinberg, L. T. (2023) · JAMA Neurology · doi:10.1001/jamaneurol.2023.3539 · Cited by 2
Kara, B., Beck, J. S., Fu, Z., Hickey, S. L., Kanaan, N. M., Mufson, E. J., Ginsberg, S. D., & Counts, S. (2025) · Acta Neuropathologica Communications · doi:10.1186/s40478-025-02080-2 · Cited by 1
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Chowdhury, R., Das, A. C., van Deventer, R., Shlyakhtenko, L. S., & Lyubchenko, Y. L. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262412128 · Cited by 1
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Khanal, P., Chand, J., Patil, V. S., Singh, L., & Bhattacharya, K. (2026) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.6c00026 · Cited by 1
Skrehot, J. T., & Kurouski, D. (2026) · Protein Science · doi:10.1002/pro.70635 · Cited by 2
Chemicals and Rodent Models for the Safety Study of Alzheimer’s Disease
Varghese, N., & Vijayan, V. (2023) · Springer eBooks · doi:10.1007/978-981-19-7834-0_23 · Cited by 1
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Damasceno, B. P. (2020) · Springer eBooks · doi:10.1007/978-3-030-57267-9_20 · Cited by 1
Imaging in Neurology Research III: Neurodegenerative Diseases
Endepols, H., & Neumaier, B. (2017) · Springer eBooks · doi:10.1007/978-3-319-42202-2_30
Adhikari, R. (2019) · Digital Commons - Michigan Tech (Michigan Technological University) · doi:10.37099/mtu.dc.etdr/891
Jadhav, V. (2021) · IUScholarWorks (Indiana University) · doi:10.7912/c2/2086
Memantine for Treatment of Dementia
Müller, T. H., & Kuhn, W. (2022) · Springer eBooks · doi:10.1007/978-3-319-56015-1_200-1
Brain Imaging for Alzheimer’s Disease Clinical Trials
Matthews, D. C., & Schmidt, M. E. (2022) · Cambridge University Press eBooks · doi:10.1017/9781108975759.034
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Du, F., Yu, Q., Chen, D., Yan, S. F., & Yan, S. S. (2020) · doi:10.21203/rs.3.rs-40746/v1
Alzheimer’s disease as a syndrome of overloaded amyloidic synaptic tagging in memory networksPreprint
Murphy, N. (2021) · OSF Preprints (OSF Preprints) · doi:10.31219/osf.io/7gsaz
Memantine for Treatment of Dementia
Müller, T. H., & Kuhn, W. (2022) · Springer eBooks · doi:10.1007/978-3-030-62059-2_200
Montecinos-Oliva, C. (2018) · theses.fr (ABES) · doi:10.70675/1cb0a505zb904z4045z83b4z7ec8f3bc62b9
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Bansal, S., Yadav, M., Bisht, P., Bansal, D., Tushir, S., & Rathore, D. (2025) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/0118715273382447250526062100
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Hoang, D. A., Le, D. A., Do, T. M. H., & Than, V. T. (2025) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2025.06.024
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Chinnathambi, S., & Rangappa, N. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2025.10.015
Rissardo, J. P., & Caprara, A. L. F. (2025) · Preprints.org · doi:10.20944/preprints202512.2722.v1
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Barbereau, C. (2020) · theses.fr (ABES) · doi:10.70675/dfe1802ez70f2z4da6zb3e5z63d1de7a429c
García, L. G. (2026) · Gredos (University of Salamanca) · doi:10.14201/gredos.171270
Luo, P., Travis, Z. D., Lenahan, C., Wu, H., Zhang, J., Yu, J., & Xu, W. (2026) · International Journal of Biological Sciences · doi:10.7150/ijbs.127431
Distinct roles of AMPA receptor subunits as potential therapeutic targets in Alzheimer’s disease
Seo, J., Kim, K., & Park, M. (2026) · Pharmacological Research · doi:10.1016/j.phrs.2026.108394
Targeting soluble misfolded oligomers in anti-amyloid research
Vosbein, P., Mao, H., & Lou, C. (2026) · Nature Reviews Chemistry · doi:10.1038/s41570-026-00867-y
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Rentsendorj, A., Vit, J., Hutton, A., Koronyo, Y., Shahin, S., Robinson, E., Barrón, E., Rodriguez, A., Jallow, O., Sheyn, J., et al. (2026) · Advanced Science · doi:10.1002/advs.202600020
Metadata
- Authors
- Guerrero-Muñoz, M. J., Gerson, J., & Castillo-Carranza, D. L.
- Affiliations
- The University of Texas Medical Branch at Galveston (US)
- ORCID
- Gerson, Julia
- Venue
- Frontiers in Cellular Neuroscience
- Publisher
- Frontiers Media SA
- Published
- 2015-12-02
- Volume
- 9
- Pages
- 464-464
- ISSN
- 1662-5102 (ISSN-L)
- PMC
- PMC4667007
- OpenAlex
- W2228598504
- Cited by
- 168
- References
- 142
- Citations by year
- 2026: 9 · 2025: 14 · 2024: 13 · 2023: 13 · 2022: 23 · 2021: 12 · 2020: 23 · 2019: 20 · 2018: 25 · 2017: 9 · 2016: 7
- FWCI
- 1.68
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Frontiers in Cellular Neuroscience (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Mitchell Center for Neurodegenerative Diseases, University of Texas Medical Branch
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- tau oligomers, Alzheimer's disease, synaptic dysfunction, amyloid-beta, tau protein, neurotoxicity, cognitive impairment, memory loss, neuronal loss
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