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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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Sorted by citations
Items 201–300 of 635
Current strategies of detecting Aβ species and inhibiting Aβ aggregation: Status and prospects
Li, J., Liao, W., Huang, D., Ou, M., Chen, T., Wang, X., Zhao, R., Zhang, L., Mei, L., Liu, J., et al. (2023) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2023.215375 · Cited by 37
Molecular basis of selective amyloid‐β degrading enzymes in Alzheimer's disease
Żukowska, J., Moss, S. J., Subramanian, V., & Acharya, K. R. (2023) · FEBS Journal · doi:10.1111/febs.16939 · Cited by 36
Lin, L., Huang, L., Huang, S., Chen, W., Huang, H., Li, C., Su, F., Liu, X., Yuan, K., Jiang, Q., et al. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-03914-1 · Cited by 36
Neuroimaging biomarkers and CSF sTREM2 levels in Alzheimer’s disease: a longitudinal study
Nabizadeh, F., Seyedmirzaei, H., & Karami, S. (2024) · Scientific Reports · doi:10.1038/s41598-024-66211-w · Cited by 36
Structural analysis of copper(I) interaction with amyloid β peptide
Gregorio, G. D., Biasotto, F., Hecel, A., Łuczkowski, M., Kozłowski, H., & Valensin, D. (2019) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2019.03.006 · Cited by 34
Habiba, U., Merlin, S., Lim, J. K. H., Wong, V. H. Y., Nguyen, C. T. O., Morley, J. W., Bui, B. V., & Tayebi, M. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-191346 · Cited by 33
Stem cell in neurodegenerative disorders; an emerging strategy
Ahani‐Nahayati, M., Shariati, A., Mahmoodi, M., Zekiy, A. O., Javidi-Aghdam, K., Shamlou, S., Mousakhani, A., Zamani, M., & Hassanzadeh, A. (2021) · International Journal of Developmental Neuroscience · doi:10.1002/jdn.10101 · Cited by 34
Kiss, É., Gorgas, K., Schlicksupp, A., Groß, D., Kins, S., Kirsch, J., & Kuhse, J. (2016) · American Journal Of Pathology · doi:10.1016/j.ajpath.2016.05.013 · Cited by 34
CRISPR/Cas9 system and its applications in nervous system diseases
Jiang, H., Tang, M.-Y., Xu, Z., Wang, Y., Li, M., Zheng, S., Zhu, J., Lin, Z., & Zhang, M. (2023) · Genes & Diseases · doi:10.1016/j.gendis.2023.03.017 · Cited by 41
Ribeiro, F. C., Cozachenco, D., Heimfarth, L., Fortuna, J. T. S., de Freitas, G. B., de Sousa, J. M., Alves‐Leon, S. V., Leite, R. E. P., Suemoto, C. K., Grinberg, L. T., et al. (2023) · Communications Biology · doi:10.1038/s42003-023-05511-9 · Cited by 34
Emerging Trends: Neurofilament Biomarkers in Precision Neurology
Sharma, P., Giri, A., & Tripathi, P. N. (2024) · Neurochemical Research · doi:10.1007/s11064-024-04244-3 · Cited by 33
Taniguchi, K., Yamamoto, F., Arai, T., Yang, J., Sakai, Y., Itoh, M., Mamada, N., Sekiguchi, M., Yamada, D., Saitoh, A., et al. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190098 · Cited by 34
Ettcheto, M., Sánchez‐López, E., Gómez-Mínguez, Y., Cabrera, H., Busquets, O., Beas‐Zárate, C., García, M. L., Carro, E., Casadesús, G., Auladell, C., et al. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-0868-4 · Cited by 32
Wang, X., Kastanenka, K. V., Arbel‐Ornath, M., Commins, C., Kuzuya, A., Lariviere, A., Krafft, G. A., Hefti, F. F., Jerecı̀ć, J., & Bacskai, B. J. (2018) · Scientific Reports · doi:10.1038/s41598-018-22979-2 · Cited by 32
Mendes, N. D., Fernandes, A., de Almeida, G. M., Santos, L. E., Sellés, M. C., Silva, N. M. L. E., Machado, C. D. M., Horta‐Júnior, J. D. A. C., Louzada, P. R., Felice, F. G. D., et al. (2018) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2018.05.021 · Cited by 35
Self-citationJia, H., Zhang, Y., & Huang, Y. H. (2018) · Neuroscience Letters · doi:10.1016/j.neulet.2018.07.033 · Cited by 32
Antonioni, A., Martorana, A., Santarnecchi, E., Hampel, H. J., & Koch, G. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70337 · Cited by 31
Shi, X., Zhang, H., Zhou, Z., Ruan, Y., Pang, J., Zhang, L., Zhai, W., & Hu, Y. (2017) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2017.12.099 · Cited by 30
Aβ pathology downregulates brain mGluR5 density in a mouse model of Alzheimer
Lee, M., Lee, H., Park, I. S., Park, J. A., Kwon, Y., Ryu, Y. H., Kim, C. H., Kang, J. H., Hyun, I. Y., Lee, K. C., et al. (2018) · Neuropharmacology · doi:10.1016/j.neuropharm.2018.02.003 · Cited by 30
On the Common Journey of Neural Cells through Ischemic Brain Injury and Alzheimer’s Disease
Kriška, J., Heřmanová, Z., Knotek, T., Turečková, J., & Anděrová, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22189689 · Cited by 33
Zhang, D., Qi, Y., Klyubin, I. V., Ondrejčák, T., Sarell, C. J., Cuello, A. C., Collinge, J., & Rowan, M. J. (2017) · Neuropharmacology · doi:10.1016/j.neuropharm.2017.03.036 · Cited by 32
Ettcheto, M., Abad, S., Petrov, D., Pedrós, I., Busquets, O., Sánchez‐López, E., Casadesús, G., Beas‐Zárate, C., Carro, E., Auladell, C., et al. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0690-4 · Cited by 28
Rhodamine-Based Metal Chelator: A Potent Inhibitor of Metal-Catalyzed Amyloid Toxicity
Pradhan, K., Das, G., Kar, C., Mukherjee, N., Khan, J., Mahata, T., Barman, S., & Ghosh, S. (2020) · ACS Omega · doi:10.1021/acsomega.0c02235 · Cited by 30
The Protective A673T Mutation of Amyloid Precursor Protein (APP) in Alzheimer’s Disease
Xia, Q., Yang, X., Shi, J., Liu, Z., Peng, Y., Wang, W., Li, B., Zhao, Y., Xiao, J., Huang, L. F., et al. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02385-y · Cited by 32
Mavroidi, B., Kaminari, A., Matiadis, D., Hadjipavlou‐Litina, D., Pelecanou, M., Tzinia, A. K., & Sagnou, M. (2022) · Brain Sciences · doi:10.3390/brainsci12060806 · Cited by 30
Gutiérrez, D. A., Chandía-Cristi, A., Yañez, M. J., Zanlungo, S., & Alvarez, A. R. (2022) · Neural Regeneration Research · doi:10.4103/1673-5374.346540 · Cited by 31
Baronio, C. M., Baldassarre, M., & Barth, A. (2019) · Physical Chemistry Chemical Physics · doi:10.1039/c9cp00717b · Cited by 30
A metabolic perspective of late onset Alzheimer’s disease
Ettcheto, M., Cano, A. C., Busquets, O., Manzine, P. R., Sánchez‐López, E., Castro-Torres, R. D., Beas‐Zárate, C., Verdaguer, E., García, M. L., Olloquequi, J., et al. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2019.104255 · Cited by 31
Amylin in Alzheimer's disease: Pathological peptide or potential treatment?
Mietlicki‐Baase, E. G. (2017) · Neuropharmacology · doi:10.1016/j.neuropharm.2017.12.016 · Cited by 30
Huang, L., Lin, M., Zhong, X., Yang, H., & Deng, M. (2019) · Molecular Medicine Reports · doi:10.3892/mmr.2019.9824 · Cited by 29
Khorasani, A., Abbasnejad, M., & Esmaeili‐Mahani, S. (2019) · International Journal of Neuroscience · doi:10.1080/00207454.2019.1634067 · Cited by 29
Nutraceutical based SIRT3 activators as therapeutic targets in Alzheimer's disease
Govindarajulu, M., Ramesh, S., Neel, L. T., Fabbrini, M., Buabeid, M. A., Fujihashi, A., Dwyer, D., Lynd, T. O., Shah, K., Mohanakumar, K. P., et al. (2021) · Neurochemistry International · doi:10.1016/j.neuint.2021.104958 · Cited by 31
Post-Translational Modifications of BACE1 in Alzheimer's Disease
Wen, W., Li, P., Liu, P., Xu, S., Wang, F., & Huang, J. H. (2021) · Current Neuropharmacology · doi:10.2174/1570159x19666210121163224 · Cited by 33
Viola, K. L., Bicca, M. A., Bebenek, A. M., Kranz, D. L., Nandwana, V., Waters, E. A., Haney, C. R., Lee, M. Y., Gupta, A., Brahmbhatt, Z., et al. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.768646 · Cited by 29
Self-citationWang, J. S.-H., Whitehead, S. N., & Yeung, K. K. ‐. (2018) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-018-1896-z · Cited by 31
Thy1-ApoE4/C/EBPβ double transgenic mice act as a sporadic model with Alzheimer’s disease
Qian, Z., Wang, Z., Li, B., Meng, X., Kuang, Z., Li, Y., Yang, Y., & Ye, K. (2024) · Molecular Psychiatry · doi:10.1038/s41380-024-02565-x · Cited by 28
Hu, T., Wang, S., Chen, C., Sun, J., & Yang, X. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.6b04950 · Cited by 28
van Dyck, C. H., Mecca, A. P., O’Dell, R. S., Bartlett, H. H., Diepenbrock, N. G., Huang, Y., Hamby, M. E., Grundman, M., Catalano, S. M., Caggiano, A. O., et al. (2024) · Alzheimer's Research & Therapy · doi:10.1186/s13195-024-01382-2 · Cited by 29
Alzheimer disease: Amyloid peptide controversies and challenges of anti-Aβ immunotherapy
Almohmadi, N. H., Al-Kuraishy, H. M., Albuhadily, A. K., Al-Gareeb, A. I., Abdelaziz, A. M., Alexiou, A. T., Papadakis, M., & Batiha, G. E. (2025) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/j.jpet.2025.103639 · Cited by 29
Zhi, Z., Tang, X., Wang, Y., Chen, R., & Ji, H. (2021) · Neurochemical Research · doi:10.1007/s11064-021-03406-x · Cited by 29
Xiong, J., Lu, D., Chen, B.-Q., Liu, T., & Wang, Z. (2022) · NeuroMolecular Medicine · doi:10.1007/s12017-022-08725-y · Cited by 29
LaBarbera, K. M., Sheline, Y. I., Izzo, N. J., Yuede, C. M., Waybright, L., Yurko, R., Edwards, H. M., Gardiner, W. D., Blennow, K., Zetterberg, H., et al. (2023) · Translational Neurodegeneration · doi:10.1186/s40035-023-00358-w · Cited by 25
Neuroepigenetics of ageing and neurodegeneration-associated dementia: An updated review
Mir, F. A., Amanullah, A., Jain, B. P., Hyderi, Z., & Gautam, A. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102067 · Cited by 30
Clearance of amyloid β-protein and its role in the spreading of Alzheimer's disease pathology
Thal, D. R. (2015) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2015.00025 · Cited by 28
Post-translational regulation of the β-secretase BACE1
Araki, W. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.04.009 · Cited by 26
Rosetta Stone for Amyloid Fibrils: The Key Role of Ring-Like Oligomers in Amyloidogenesis
Galzitskaya, O. V., & Selivanova, O. M. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170230 · Cited by 28
Yang, C.-N., Wu, M.-F., Liu, C.-C., Jung, W.-H., Chang, Y.-C., Lee, W.-P., Shiao, Y.-J., Wu, C.-L., Liou, H.-H., Lin, S.-K., et al. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx278 · Cited by 27
Sulforaphane Reverses the Amyloid-β Oligomers Induced Depressive-Like Behavior
Wang, W., Wei, C., Quan, M., Li, T., & Jia, J. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200397 · Cited by 27
Accumulation of cellular prion protein within β‐amyloid oligomer plaques in aged human brains
Takahashi, R. H., Yokotsuka, M., Tobiume, M., Sato, Y., Hasegawa, H., Nagao, T., & Gouras, G. K. (2021) · Brain Pathology · doi:10.1111/bpa.12941 · Cited by 27
Potential Novel Approaches to Understand the Pathogenesis and Treat Alzheimer’s Disease
Drummond, E., Goñi, F., Liu, S., Prelli, F., Scholtzova, H., & Wısnıewskı, T. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-179909 · Cited by 26
Huang, Y., Guo, B., Shi, B., Gao, Q., & Zhou, Q. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-170763 · Cited by 26
Alam, P., Siddiqi, M. K., Malik, S., Chaturvedi, S. K., Uddin, M., & Khan, R. H. (2019) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2019.01.134 · Cited by 26
β-Amyrin Ameliorates Alzheimer's Disease-Like Aberrant Synaptic Plasticity in the Mouse Hippocampus
Park, H. J., Kwon, H., Lee, J., Cho, E., Lee, Y. C., Moon, M., Jun, M., Kim, D. H., & Jung, J. W. (2019) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2019.024 · Cited by 27
Soluble Epoxide Hydrolase and Brain Cholesterol Metabolism
Domingues, M. F., Callai-Silva, N., Piovesan, A. R., & Carlini, C. R. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00325 · Cited by 26
Alzheimer’s protection effect of A673T mutation may be driven by lower Aβ oligomer binding affinity
Limegrover, C. S., LeVine, H., Izzo, N. J., Yurko, R., Mozzoni, K., Rehak, C., Sadlek, K., Safferstein, H., & Catalano, S. M. (2021) · Journal of Neurochemistry · doi:10.1111/jnc.15212 · Cited by 24
Protein Oligomer Engineering: A New Frontier for Studying Protein Structure, Function, and Toxicity
Liu, C., & Luo, J. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202216480 · Cited by 25
Umeda, T., Kimura, T., Yoshida, K., Takao, K., Fujita, Y., Matsuyama, S., Sakai, A., Yamashita, M., Yamashita, Y., Ohnishi, K., et al. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0461-5 · Cited by 26
Ning, C., Mo, L., Chen, X., Tu, W., Wu, J., Hou, S., & Xu, J. (2018) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2018.01.019 · Cited by 26
Özdemir, A. Y., Hofbauerová, K., Kopecký, V., Novotný, J., & Rudajev, V. (2024) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-024-00657-8 · Cited by 27
Versatile near-infrared fluorescent probe for in vivo detection of Aβ oligomers
Zeng, F., Yang, J., Li, X., Peng, K., Ran, C., Xu, Y., & Li, Y. (2020) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2020.115559 · Cited by 25
Pharmacological Strategies to Improve Dendritic Spines in Alzheimer’s Disease
Ettcheto, M., Busquets, O., Cano, A. C., Sánchez‐López, E., Manzine, P. R., Espinosa-Jiménez, T., Verdaguer, E., Sureda, F. X., Olloquequi, J., Castro-Torres, R. D., et al. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-201106 · Cited by 25
Melatonin: Regulation of Prion Protein Phase Separation in Cancer Multidrug Resistance
Loh, D., & Reiter, R. J. (2022) · Molecules · doi:10.3390/molecules27030705 · Cited by 25
Nazere, K., Takahashi, T., Hara, N., Muguruma, K., Nakamori, M., Yamazaki, Y., Morino, H., & Maruyama, H. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.804702 · Cited by 26
Matthes, D., & de Groot, B. L. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.103034 · Cited by 27
Calamai, M., Evangelisti, E., Cascella, R., Parenti, N., Cecchi, C., Stefani, M., & Pavone, F. S. (2015) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2015.12.009 · Cited by 27
DiChiara, T., DiNunno, N., Clark, J. R., Bu, R. L., Cline, E. N., Rollins, M. G., Gong, Y., Brody, D. L., Sligar, S. G., Velasco, P. T., et al. (2017) · PubMed · Cited by 25
Self-citationYin, X., Zhou, H., Cao, T., Yang, X., Meng, F., Dai, X., Wang, Y., Li, S., Zhai, W., Yang, Z., et al. (2024) · ACS Nano · doi:10.1021/acsnano.3c08823 · Cited by 26
Roterman, I., Banach, M., Kalinowska, B., & Konieczny, L. (2016) · Entropy · doi:10.3390/e18100351 · Cited by 24
Herline, K., Prelli, F., Mehta, P. D., MacMurray, C., Goñi, F., & Wısnıewskı, T. (2018) · Alzheimer s Research & Therapy · doi:10.1186/s13195-018-0384-9 · Cited by 24
Current Strategies for Real-Time Enzyme Activation
Wang, F., Liu, Y., Du, C., & Gao, R. (2022) · Biomolecules · doi:10.3390/biom12050599 · Cited by 24
Site specific NMR characterization of abeta-40 oligomers cross seeded by abeta-42 oligomers
Chang, H., Ma, H.-I., Wu, Y., Lee, M., Yuan, E. C., Huang, S., Cheng, Y.-S., Wu, M., Tu, L., & Chan, J. C. C. (2022) · Chemical Science · doi:10.1039/d2sc01555b · Cited by 23
Amyloid-β in Alzheimer’s disease – front and centre after all?
Weglinski, C., & Jeans, A. F. (2022) · Neuronal Signaling · doi:10.1042/ns20220086 · Cited by 24
Williams, S. M., Schulz, P., Rosenberry, T. L., Caselli, R. J., & Sierks, M. R. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-161116 · Cited by 24
Shin, N. N., Jeon, H., Jung, Y., Baek, S., Lee, S., Yoo, H. C., Bae, G. H., Park, K., Yang, S.-H., Han, J. M., et al. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00093 · Cited by 24
Itoh, N., Takada, E., Okubo, K., Yano, Y., Hoshino, M., Sasaki, A., Kinjo, M., & Matsuzaki, K. (2017) · ChemBioChem · doi:10.1002/cbic.201700576 · Cited by 24
Cichoń, N., Dziedzic, A., Gorniak, L., Miller, E. D., Bijak, M., Starosta, M., & Saluk, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910707 · Cited by 24
Jamuna, N. A., Kamalakshan, A., Dandekar, B. R., Devassy, A. M. C., Mondal, J., & Mandal, S. (2023) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.3c00274 · Cited by 23
Bhardwaj, S., Grewal, A. K., Singh, S., Dhankar, V., & Jindal, A. (2024) · Inflammopharmacology · doi:10.1007/s10787-024-01502-2 · Cited by 25
Chowdhury, S. R., Mondal, S., Balakrishnan, M., Balaji, S., Trivedi, V., & Iyer, P. K. (2018) · ACS Omega · doi:10.1021/acsomega.8b00764 · Cited by 22
Malishev, R., Nandi, S., Śmiłowicz, D., Bakavayev, S., Engel, S., Bujanover, N., Gazit, R., Metzler‐Nolte, N., & Jelinek, R. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00177 · Cited by 21
Ge, X., Wang, Y., Yu, S., Cao, X., Chen, Y., Cheng, Q., & Ding, F. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.716177 · Cited by 22
Wang, Y., Cheng, Q., Su, Q., Yu, X., Shen, T., Yang, X., & Jia, W. (2022) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2022.174755 · Cited by 23
Li, W., Gao, J.-Y., Lin, S.-Y., Pan, S.-T., Xiao, B., Ma, Y.-T., Xie, K., Shen, W., Liu, Z.-T., Li, G.-Y., et al. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-02784-9 · Cited by 23
BACE-1 Inhibitors Targeting Alzheimer's Disease
Monteiro, K. L. C., Alcântara, M. G. D. S., Freire, N. M. L., Brandão, E. M., do Nascimento, V. L., Viana, L. M. D. S., de Aquino, T. M., & da Silva‐Júnior, E. F. (2023) · Current Alzheimer Research · doi:10.2174/1567205020666230612155953 · Cited by 23
Pushie, M. J., Stefaniak, E., Sendzik, M. R., Sokaras, D., Kröll, T., & Haas, K. L. (2019) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.9b01940 · Cited by 22
Oxidative DNA Damage Signalling in Neural Stem Cells in Alzheimer’s Disease
Kieroń, M., Żekanowski, C., Falk, A., & Wężyk, M. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/2149812 · Cited by 22
Adult hippocampal neurogenesis: New avenues for treatment of brain disorders
Chen, L., Li, Z., Wang, W., Zhou, Y., Li, W., & Wang, Y. (2025) · Stem Cell Reports · doi:10.1016/j.stemcr.2025.102600 · Cited by 25
Tangeretin Inhibits BACE1 Activity and Attenuates Cognitive Impairments in AD Model Mice
Bao, J., Liang, Z., Gong, X., Zhao, Y., Wu, M., Liu, W., Tu, C., Wang, X., & Shu, X. (2022) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.1c07241 · Cited by 21
Miao, Y., Zhong, Q., & Ren, H. (2022) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-022-04367-y · Cited by 21
Alzheimer’s disease is an inherent, natural part of human brain aging: an integrated perspective
Ferrer, I. (2022) · Free Neuropathology · doi:10.17879/freeneuropathology-2022-3806 · Cited by 25
Xue, J., Li, J.-Q., Wang, C.-C., Ma, X., Dai, H., Xu, C., & Meng, X. (2023) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2023.116613 · Cited by 23
Zhang, H., Chen, Y., Yu, M., Xi, Y., Han, G., Jin, Y., Wang, G.-J., Sun, X., Zhou, J., & Ding, Y. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2304213120 · Cited by 21
Tolar, M., Hey, J. A., Power, A., & Abushakra, S. R. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25052727 · Cited by 23
Chen, L., Huang, C., Shentu, J., Wang, M., Yan, S., Fei, Z., Zhang, Z., Wang, C., Han, Y., Wang, Q., et al. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00393 · Cited by 21
Zhang, K., Yang, Q., Fan, Z., Zhao, J., & Li, H. (2019) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2019.111701 · Cited by 21
Enhancing α-secretase Processing for Alzheimer’s Disease—A View on SFRP1
Tang, B. L. (2020) · Brain Sciences · doi:10.3390/brainsci10020122 · Cited by 21
Martins, T. S., Marçalo, R., Ferreira, M., Vaz, M., Silva, R. M., Rosa, I. M., Vogelgsang, J. S., Wiltfang, J., Silva, O. A. B. D. C. E., & Henriques, A. G. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22083933 · Cited by 21
Flores‐Clemente, C., Nicolás‐Vázquez, M. I., Jiménez, E. M., & Rodríguez, M. H. (2021) · Biomolecules · doi:10.3390/biom11101408 · Cited by 21
Goñi, F., Martá-Ariza, M., Herline, K., Peyser, D. K., Boutajangout, A., Mehta, P. D., Drummond, E., Prelli, F., & Wısnıewskı, T. (2018) · Alzheimer s Research & Therapy · doi:10.1186/s13195-018-0337-3 · Cited by 20
Future horizons in Alzheimer's disease research
Wısnıewskı, T., & Drummond, E. (2019) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2019.08.001 · Cited by 20
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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