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Amyloid β oligomers in Alzheimer’s disease pathogenesis, treatment, and diagnosis
Open accessAbstract
Protein aggregation is common to dozens of diseases including prionoses, diabetes, Parkinson's and Alzheimer's. Over the past 15 years, there has been a paradigm shift in understanding the structural basis for these proteinopathies. Precedent for this shift has come from investigation of soluble Aβ oligomers (AβOs), toxins now widely regarded as instigating neuron damage leading to Alzheimer's dementia. Toxic AβOs accumulate in AD brain and constitute long-lived alternatives to the disease-defining Aβ fibrils deposited in amyloid plaques. Key experiments using fibril-free AβO solutions demonstrated that while Aβ is essential for memory loss, the fibrillar Aβ in amyloid deposits is not the agent. The AD-like cellular pathologies induced by AβOs suggest their impact provides a unifying mechanism for AD pathogenesis, explaining why early stage disease is specific for memory and accounting for major facets of AD neuropathology. Alternative ideas for triggering mechanisms are being actively investigated. Some research favors insertion of AβOs into membrane, while other evidence supports ligand-like accumulation at particular synapses. Over a dozen candidate toxin receptors have been proposed. AβO binding triggers a redistribution of critical synaptic proteins and induces hyperactivity in metabotropic and ionotropic glutamate receptors. This leads to Ca(2+) overload and instigates major facets of AD neuropathology, including tau hyperphosphorylation, insulin resistance, oxidative stress, and synapse loss. Because different species of AβOs have been identified, a remaining question is which oligomer is the major pathogenic culprit. The possibility has been raised that more than one species plays a role. Despite some key unknowns, the clinical relevance of AβOs has been established, and new studies are beginning to point to co-morbidities such as diabetes and hypercholesterolemia as etiological factors. Because pathogenic AβOs appear early in the disease, they offer appealing targets for therapeutics and diagnostics. Promising therapeutic strategies include use of CNS insulin signaling enhancers to protect against the presence of toxins and elimination of the toxins through use of highly specific AβO antibodies. An AD-dependent accumulation of AβOs in CSF suggests their potential use as biomarkers and new AβO probes are opening the door to brain imaging. Overall, current evidence indicates that Aβ oligomers provide a substantive molecular basis for the cause, treatment and diagnosis of Alzheimer's disease.
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“Because pathogenic soluble aggregates of Aβ appear early in the sequence of AD, they can represent interesting targets for therapeutics and diagnostics [51].”
From Alzheimer's Disease: Treatment Strategies and Their Limitations. (2022) · cites this paper as [51]
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“It is suggested that oligomers are the most neurotoxic species in AD as levels of these species correlate much better with cognitive symptoms than presence of plaques or NFTs [166].”
From Alzheimer's disease: experimental models and reality (2017) · cites this paper as [166]
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“Strong correlation is observed between the severity of cognitive impairment in AD and the levels of oligomeric rather than aggregated Ab in senile plaques (2,3).”
From Differential protective effects of connective tissue growth factor against Aβ neurotoxicity on neurons and glia (2017) · cites this paper as [3]
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1 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
RetractedAmyloid 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
Imaging brain amyloid in Alzheimer's disease with Pittsburgh Compound‐B
Klunk, W. E., Engler, H., Nordberg, A., Wang, Y., Blomqvist, G., Holt, D. P., Bergström, M., Savitcheva, I., Huang, G., Estrada, S., et al. (2004) · Annals of Neurology · doi:10.1002/ana.20009 · Cited by 4,496
Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291
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
Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506
Self-citationJournal of Biological Chemistry
Kurkinensp, M., CondongT, M. R., Blumberg, B., Barlow, D. P., Quiñones, S., Sausg, J., & Pihlajaniemisyy, T. (2021) · Journal of Biological Chemistry · doi:10.1074/jbc · Cited by 3,427
Yang, F., Lim, G. P., Begum, A. N., Ubeda, O. J., Simmons, M. R., Ambegaokar, S. S., Chen, P. P., Kayed, R., Glabe, C. G., Frautschy, S. A., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m404751200 · Cited by 2,336
The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes
Benilova, I., Karran, E., & De Strooper, B. (2012) · Nature Neuroscience · doi:10.1038/nn.3028 · Cited by 1,962
Mucke, L., Masliah, E., Yu, G.-Q., Mallory, M., Rockenstein, E. M., Tatsuno, G., Hu, K., Kholodenko, D., Johnson-Wood, K., & McConlogue, L. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-11-04050.2000 · Cited by 1,856
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- Nigh AB, Vahedi S, Davis EG, Weintraub S, Bigio EH, Klein WL, Geula C (2014) Intracellular Amyloid-beta in cholinergic neurons. Brain J Neurol: In Press
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Olloquequi, J., Ettcheto, M., Cano, A. C., Sánchez‐López, E., Carrasco, M., Espinosa-Jiménez, T., Beas‐Zárate, C., Gudiño‐Cabrera, G., Ureña‐Guerrero, M. E., Verdaguer, E., et al. (2022) · Frontiers in Bioscience-Landmark · doi:10.31083/j.fbl2705146 · Cited by 25
Activatable small-molecule NIR fluorescent/photoacoustic probes for brain disease imaging
Zou, J., Kim, Y., Lee, Y., Hong, S. J., Lee, K., Zhang, F., Mao, Z., & Kim, J. S. (2025) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2025.217149 · Cited by 20
Benseny‐Cases, N., Álvarez-Marimon, E., Aso, E., Carmona, M., Klementieva, O. L., Appelhans, D., Ferrer, I., & Cladera, J. (2021) · Scientific Reports · doi:10.1038/s41598-021-96379-4 · Cited by 20
A review of autophagy mechanism of statins in the potential therapy of Alzheimer’s disease
Liu, L., Dai, W.-Z., Zhu, X., & Ma, T. (2022) · Journal of Integrative Neuroscience · doi:10.31083/j.jin2102046 · Cited by 20
Arendash, G. W., Abulaban, H., Steen, S., Andel, R., Wang, Y., Bai, Y., Baranowski, R., McGarity, J., Scritsmier, L., Lin, X., et al. (2022) · Medicines · doi:10.3390/medicines9080042 · Cited by 21
Treponema denticola Induces Neuronal Apoptosis by Promoting Amyloid-β Accumulation in Mice
Wu, L., Su, X., Tang, Z., Jian, L., Zhu, H., Cheng, X., & Wu, H. (2022) · Pathogens · doi:10.3390/pathogens11101150 · Cited by 19
Araki, W. (2023) · Cells · doi:10.3390/cells12101386 · Cited by 20
Targets, trials and tribulations in Alzheimer therapeutics
Gharat, R., Dixit, G., Khambete, M., & Prabhu, A. (2023) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2023.176230 · Cited by 18
Amyloid PET detects the deposition of brain Aβ earlier than CSF fluid biomarkers
Lowe, V. J., Mester, C. T., Lundt, E. S., Lee, J., Ghatamaneni, S., Algeciras‐Schimnich, A., Campbell, M. R., Graff‐Radford, J., Nguyen, A. T., Min, H.-K. P., et al. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.14317 · Cited by 20
Endocytosis Is a Key Mode of Interaction between Extracellular β-Amyloid and the Cell Membrane
Shi, J., Zhu, L., Lan, X., Zhao, D.-W., He, Y., Sun, Z.-Q., Wu, D., & Li, H. (2020) · Biophysical Journal · doi:10.1016/j.bpj.2020.07.035 · Cited by 19
Robbins, J., Busquets, O., Tong, M., & de la Monte, S. M. (2020) · Journal of Alzheimer s Disease Reports · doi:10.3233/adr-200238 · Cited by 19
Masuda, Y., Fujihara, K., Hayashi, S., Sasaki, H., Kino, Y., Kamauchi, H., Noji, M., Satoh, J., Takanami, T., Kinoshita, K., et al. (2021) · Journal of Natural Products · doi:10.1021/acs.jnatprod.0c01329 · Cited by 19
Liu, Q., Liu, X., Zhao, D., Ruan, X., Su, R. J., Shang, X., Wang, D., Yang, C., & Xue, Y. (2021) · Cell Death Discovery · doi:10.1038/s41420-021-00531-y · Cited by 19
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Condello, C., Merz, G. E., Aoyagi, A., DeGrado, W. F., & Prusiner, S. B. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2655-9_16 · Cited by 18
Mi, L., Fan, M., Liu, T., Wu, D., Wang, Y., Li, F., Cai, Y., Qiu, Z., Liu, D., & Cao, L. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.1074397 · Cited by 18
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León-Martínez, R., Gutiérrez, D. A., Pinto, C., Morales, C., de la Fuente, C., Riquelme, C., Cortés, B. I., González-Martín, A., Chamorro, D., Espinosa, N., et al. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1180987 · Cited by 19
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van Diggelen, F., Tepper, A. W. J. W., Apetri, M. M., & Otzen, D. E. (2016) · Israel Journal of Chemistry · doi:10.1002/ijch.201600116 · Cited by 18
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Pate, K. M., & Murphy, R. M. (2017) · Israel Journal of Chemistry · doi:10.1002/ijch.201600078 · Cited by 17
Przygońska, K., Pacewicz, M., Sadowska, W., Poznański, J. T., Bal, W., & Dadlez, M. (2019) · Scientific Reports · doi:10.1038/s41598-019-45988-1 · Cited by 18
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Gutiérrez, D. A., Vargas, L. M., Chandía-Cristi, A., de la Fuente, C., Leal, N. R., & Alvarez, A. R. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00526 · Cited by 19
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Zhang, J.-X., Lai, Y.-H., Mi, P., Dai, X., Zhang, R., Zhang, Z., Zhang, S., Zhang, X., Zhang, X., Yang, B., et al. (2019) · Alzheimer s Research & Therapy · doi:10.1186/s13195-019-0560-6 · Cited by 18
Chen, C., Xu, D., Zhang, Z.-H., Jia, S.-Z., Cao, X.-C., Chen, Y., Song, G.-L., Wong, M. S., & Li, H. (2020) · Experimental Neurology · doi:10.1016/j.expneurol.2020.113210 · Cited by 18
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Robinson, J., Sarangi, N. K., & Keyes, T. E. (2022) · Physical Chemistry Chemical Physics · doi:10.1039/d2cp03344e · Cited by 18
Li, H., Wang, X., Yu, H., Zhu, J., Jin, H., Wang, A., & Yang, Z. (2017) · Current Neuropharmacology · doi:10.2174/1570159x15666171030142108 · Cited by 21
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Mulumba, J., Duan, R., Luo, B., Wu, J., Sulaiman, M., Wang, F., & Yang, Y. (2025) · Exploration of neuroscience · doi:10.37349/en.2025.100675 · Cited by 23
Tong, M., Leão, R. A. C., Vimbela, G. V., Yalcin, E. B., Kay, J., Krotow, A., & de la Monte, S. M. (2017) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2017.04.010 · Cited by 17
Lee, B. Y., Attwood, S. J., Turnbull, S., & Leonenko, Z. (2018) · Molecules · doi:10.3390/molecules23123089 · Cited by 17
Pourhamzeh, M., Joghataei, M. T., Mehrabi, S., Ahadi, R., Hojjati, S. M. M., Fazli, N., Nabavi, S. M., Pakdaman, H., & Shahpasand, K. (2020) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-020-00906-2 · Cited by 18
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Sohn, E., Kim, Y. J., Kim, J., & Jeong, S. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02358-1 · Cited by 16
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Zhang, X., Huai, Y., Cai, J., Song, C., & Zhang, Y. (2018) · International Immunopharmacology · doi:10.1016/j.intimp.2018.12.014 · Cited by 16
Lana, D., Ugolini, F., & Giovannini, M. G. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249441 · Cited by 17
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Hu, Z., Yang, J., Zhang, S., Li, M., Zuo, C., Mao, C., Zhang, Z., Tang, M., Shi, C., & Xu, Y. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-23-01277 · Cited by 15
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Lv, Z., Tan, C., Yu, J., & Tan, L. (2017) · Neurotoxicity Research · doi:10.1007/s12640-017-9765-2 · Cited by 15
Zheng, Y.-P., Xu, L., Yang, J., Peng, X.-L., Wang, H., Yu, N., Hua, Y., Zhao, J., He, J., & Hong, T. (2018) · Biopolymers · doi:10.1002/bip.23237 · Cited by 15
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Yang, X., Du, W., Zhang, Y., Wang, H., & He, M. (2020) · Dose-Response · doi:10.1177/1559325820972205 · Cited by 16
Kumar, S., Kapadia, A., Theil, S., Joshi, P., Riffel, F., Heneka, M. T., & Walter, J. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.619639 · Cited by 16
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Shin, J., Kang, D. M., Yoo, J., Heo, J., Jeong, K., Chung, J. H., Han, Y. S., & Kim, S. (2021) · The Analyst · doi:10.1039/d1an00692d · Cited by 15
Danziger, R., Fuchs, D.-T., Koronyo, Y., Rentsendorj, A., Sheyn, J., Hayden, E. Y., Teplow, D. B., Black, K. L., Fuchs, S., Bernstein, K. E., et al. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1179315 · Cited by 16
Holcombe, B., Foes, A., Banerjee, S., Yeh, K. L., Wang, S. J., Bhargava, R., & Ghosh, A. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00400 · Cited by 13
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Yun, J., Kim, H. J., Kim, H., Lee, K. M., Hong, I. K., Kim, S. H., Rhee, H. Y., Jahng, G., Yoon, S. S., Park, K., et al. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.736937 · Cited by 14
Martins, S., Müller‐Schiffmann, A., Erichsen, L., Bohndorf, M., Wruck, W., Sleegers, K., Broeckhoven, C. V., Korth, C., & Adjaye, J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21124516 · Cited by 14
Song, S., Wu, J., Cheng, Y., Ma, L., Liu, T., Liu, J., Liu, J., Sotor, J. Z., & Luan, P. (2021) · Applied Materials Today · doi:10.1016/j.apmt.2021.101028 · Cited by 14
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Zheng, Y., Yang, J., Li, X., Qi, L., Zheng, Z., Kong, J., Zhang, G., & Guo, Y. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.106862 · Cited by 14
Chen, H., Xiang, S., Huang, L., Lin, J., Hu, S., Mak, S., Wang, C., Wang, Q., Cui, W., & Han, Y. (2018) · Metabolic Brain Disease · doi:10.1007/s11011-018-0221-7 · Cited by 13
Wang, J., Zhu, X., Li, Y., Zhang, P., Wang, T., & Li, M. (2022) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2022/6091671 · Cited by 14
Halder, B., Mitra, A., Dewangan, S., Gazi, R., Sarkar, N., Jana, M., & Chatterjee, S. (2022) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2022.134362 · Cited by 13
Kugaevskaya, E. V., Veselovsky, A., Indeykina, M., Solovyeva, N. I., Zharkova, M. S., Popov, I., Nikolaev, E., Mantsyzov, A., Makarov, A., & Kozin, S. (2018) · Scientific Reports · doi:10.1038/s41598-017-18567-5 · Cited by 14
Bartley, S. C., Proctor, M. T., Xia, H., Ho, E., Kang, D. S., Schuster, K. H., Bicca, M. A., Seckler, H. S., Viola, K. L., Patrie, S. M., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23042208 · Cited by 14
Self-citationLiu, Y., Gao, X., Zhang, Z., Lin, Z., & Zou, Q. (2016) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-016-0425-5 · Cited by 13
Hida, M., Yasuda, K., Toyokawa, M., Asada‐Utsugi, M., Toda, S., Yanagida, N., Takahashi, R., Kinoshita, A., & Maki, T. (2025) · Brain Research · doi:10.1016/j.brainres.2025.149601 · Cited by 12
Yang, X., Yao, K., Zhang, M., Zhang, W., & Zu, H. (2025) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2025.111321 · Cited by 12
Kopeć, K., Koziorowski, D., & Szlufik, S. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26157552 · Cited by 15
Natarajan, B., Zhou, Q., Maduraiveeran, G., & Kannan, P. (2026) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2026.217682 · Cited by 12
Randhawa, S., Dar, A. I., Saini, T. C., Bathla, M., & Acharya, A. (2024) · Nano Today · doi:10.1016/j.nantod.2024.102243 · Cited by 12
Hey, J. A., Yu, Y., Abushakra, S. R., Schaefer, J. F., Power, A., Kesslak, P. J., & Tolar, M. (2024) · Drugs · doi:10.1007/s40265-024-02068-7 · Cited by 15
Qu, W., Lam, M., McInvale, J. J., Mares, J. A., Kwon, S. H., Humala, N., Mahajan, A., Nguyen, T. T. T., Jakubiak, K. A., Mun, J.-Y., et al. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02755-5 · Cited by 13
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Abad, S., Ramon‐Duaso, C., López‐Arnau, R., Folch, J., Pubill, D., Camarasa, J., Camins, A., & Escubedo, E. (2019) · Journal of Psychopharmacology · doi:10.1177/0269881119855987 · Cited by 12
Cobalt(III) Schiff base complexes stabilize non-fibrillar amyloid-β aggregates with reduced toxicity
Roberts, K. F., Brue, C. R., Preston, A., Baxter, D., Herzog, E., Varelas, E. A., & Meade, T. J. (2020) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2020.111265 · Cited by 12
Ettcheto, M., Sánchez‐López, E., Cano, A. C., Carrasco, M., Herrera, K., Manzine, P. R., Espinosa-Jiménez, T., Busquets, O., Verdaguer, E., Olloquequi, J., et al. (2021) · Cell & Bioscience · doi:10.1186/s13578-021-00646-w · Cited by 12
Discovery of Novel Drug Candidates for Alzheimer’s Disease by Molecular Network Modeling
Zhou, J., Li, Q., Wu, W., Zhang, X., Zuo, Z., Lu, Y., Zhao, H., & Wang, Z. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.850217 · Cited by 12
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Strømland, Ø., Jakubec, M., Furse, S., & Halskau, Ø. (2016) · Journal of Clinical and Translational Research · doi:10.18053/jctres.02.201601.003 · Cited by 12
Lee, H. J., Savelieff, M. G., Kang, J., Brophy, M. B., Nakashige, T. G., Lee, S. J. C., Nolan, E. M., & Lim, M. H. (2018) · Metallomics · doi:10.1039/c8mt00091c · Cited by 12
Jara-Moreno, D., Castro-Torres, R. D., Ettcheto, M., Auladell, C., Kogan, M. J., Folch, J., Verdaguer, E., Cano, A. C., Busquets, O., Delporte, C. L., et al. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180174 · Cited by 12
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Llorente, P., Kristen, H., Sastre, I., Toledano‐Zaragoza, A., Aldudo, J., Recuero, M., & Bullido, M. J. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-170159 · Cited by 12
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Hilt, S., Tang, T., Walton, J. H., Budamagunta, M. S., Maezawa, I., Kálai, T., Hideg, K., Singh, V., Wulff, H., Gong, Q., et al. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160279 · Cited by 12
Wang, R., Peng, S., Zhu, J., Xu, Y., Wang, M., Zhang, L., Qiu, Y., Hou, D., Wang, Q., & Liu, R. (2025) · Frontiers in Neurology · doi:10.3389/fneur.2025.1651708 · Cited by 11
Lannfelt, L. (2023) · Upsala Journal of Medical Sciences · doi:10.48101/ujms.v128.10316 · Cited by 12
Rathee, S., Sen, D., Pandey, V., & Jain, S. (2024) · Current Drug Targets · doi:10.2174/0113894501320096240627071400 · Cited by 16
Panmanee, J., Phanchana, M., Pearngam, P., Petchyam, N., Promthep, K., Wisomka, P., Kutpruek, S., Pannengpetch, S., Prasertporn, T., Mukda, S., et al. (2025) · Cell Biology International · doi:10.1002/cbin.70013 · Cited by 11
Jin, S., Bellier, J., Wells, A. R., Llopis, P. D. L. M. M., Anekal, P. V., Tresback, J. S., Caldarone, B. J., Liu, L., Li, S., Dettmer, U., et al. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70194 · Cited by 11
Yu, Y., Liu, S., Wang, H., Shi, D., Xu, Q., Zhou, X., Sun, Z., & Huang, P. (2016) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-016-9678-5 · Cited by 11
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Dominguez, J. C., Yu, J. R. T., Guzman, M. F. D., Ampil, E. R., Guevarra, A. C., Joson, M. L. C., Reandelar, M., Martinez, M., Ligsay, A. D., Ocampo, F. F., et al. (2022) · International Journal of Alzheimer s Disease · doi:10.1155/2022/9960832 · Cited by 12
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Whitfield, J. F., Rennie, K., & Chakravarthy, B. (2023) · Cells · doi:10.3390/cells12121618 · Cited by 11
Zhao, J., Liu, F., Huang, C., Shentu, J., Wang, M., Sun, C., Chen, L., Yan, S., Fang, F., Wang, Y., et al. (2017) · Molecules · doi:10.3390/molecules22101651 · Cited by 13
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Tsubaki, Y., Akamatsu, G., Shimokawa, N., Katsube, S., Takashima, A., Sasaki, M., & Initiative, J. A. D. N. (2020) · EJNMMI Physics · doi:10.1186/s40658-020-00329-4 · Cited by 11
Duangjan, C., Rangsinth, P., Zhang, S., Gu, X., Wink, M., & Tencomnao, T. (2021) · Biology · doi:10.3390/biology10080800 · Cited by 11
Metadata
- Authors
- Viola, K. L., & Klein, W. L.
- Affiliations
- Northwestern University (US)
- Corresponding author
- Klein, William L.
- Venue
- Acta Neuropathologica
- Published
- 2015-01-22
- Volume
- 129
- Issue
- 2
- Pages
- 183-206
- ISSN
- 0001-6322 (ISSN-L)
- 1432-0533
- PMC
- PMC4390393
- OpenAlex
- W2055775253
- Cited by
- 628
- References
- 198
- Citations by year
- 2026: 42 · 2025: 45 · 2024: 55 · 2023: 51 · 2022: 75 · 2021: 69 · 2020: 66 · 2019: 58 · 2018: 60 · 2017: 53 · 2016: 42 · 2015: 10
- FWCI
- 6.76
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Acta Neuropathologica (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Institute on Aging (AG045637, AG029460, R01AG022547, AG022547, R01AG029460, R21AG045637)
- 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
- amyloid-beta oligomers, Alzheimer's disease pathogenesis, protein aggregation, neurotoxicity, synaptic dysfunction, glutamate receptors, calcium overload, tau hyperphosphorylation, insulin resistance, oxidative stress, synaptic loss, cerebrospinal fluid biomarkers, diabetes comorbidity, hypercholesterolemia, Alzheimer's disease therapeutics
- MeSH terms
- Alzheimer Disease, Animals, Humans, Neurons, Amyloid beta-Peptides
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