The DOI matches its Crossref record; 197 of the 200 references it cites were found in a registry or an index, and 3 are not checked yet.
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The cited source says what the claim attributes to it.
In the citing paper
“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]
In the citing paper
“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]
In the citing paper
“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]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
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
Flagged first, then by citations
Research works printed but not linked: 1
- 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
Cited by
Sorted by citations
Items 101–200 of 635
Aβ42 pentamers/hexamers are the smallest detectable oligomers in solution
Wolff, M., Zhang-Haagen, B., Decker, C., Barz, B., Schneider, M., Biehl, R., Rădulescu, A., Strodel, B., Willbold, D., & Nagel‐Steger, L. (2017) · Scientific Reports · doi:10.1038/s41598-017-02370-3 · Cited by 58
de la Monte, S. M. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-3540-2_4 · Cited by 59
Biosensors on the road to early diagnostic and surveillance of Alzheimer's disease
Carneiro, P., Morais, S., & Pereira, M. D. C. (2020) · Talanta · doi:10.1016/j.talanta.2019.120700 · Cited by 59
Österlund, N., Lundqvist, M., Ilag, L. L., Gräslund, A., & Emanuelsson, C. S. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.013459 · Cited by 57
Alternative processing of the amyloid precursor protein family by rhomboid protease RHBDL4.
Paschkowsky, S., Hamzé, M., Oestereich, F., & Munter, L. M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.753582 · Cited by 58
Jiang, L., Chen, B.-C., Chen, B., Li, X.-J., Liao, H., Huang, H., Guo, Z., Zhang, W., & Wu, L. H. (2017) · Talanta · doi:10.1016/j.talanta.2017.04.021 · Cited by 57
Liu, S., Park, S.-A., Allington, G., Prelli, F., Sun, Y., Martá-Ariza, M., Scholtzova, H., Biswas, G. K., Brown, B., Verghese, P. B., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-08604-8 · Cited by 58
de la Monte, S. M., Tong, M., Daiello, L. A., & Ott, B. R. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-180906 · Cited by 63
Zhu, C., Xu, B., Sun, X., Zhu, Q., & Sui, Y. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-0269-5 · Cited by 59
The neurotoxicity of amyloid β-protein oligomers is reversible in a primary neuron model
Tanokashira, D., Mamada, N., Yamamoto, F., Taniguchi, K., Tamaoka, A., Lakshmana, M. K., & Araki, W. (2017) · Molecular Brain · doi:10.1186/s13041-016-0284-5 · Cited by 59
Liu, Y., Wang, S., Kan, J., Zhang, J., Zhou, L., Huang, Y., & Zhang, Y. (2019) · Current Neuropharmacology · doi:10.2174/1570159x17666191101125530 · Cited by 56
Emre, C., Arroyo-García, L. E., Do, K. V., Jun, B., Ohshima, M., Alcalde, S. G., Cothern, M. L., Maioli, S., Nilsson, P., Hjorth, E., et al. (2022) · Communications Biology · doi:10.1038/s42003-022-03169-3 · Cited by 55
Bigi, A., Cascella, R., Chiti, F., & Cecchi, C. (2022) · BioEssays · doi:10.1002/bies.202200086 · Cited by 56
Huang, L., Lin, J., Xiang, S., Zhao, K., Yu, J., Zheng, J., Xu, D., Mak, S., Hu, S., Nirasha, S., et al. (2016) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5b00329 · Cited by 55
Liu, X.-G., Zhang, L., Lu, S., Liu, D.-Q., Zhang, L.-X., Yu, X.-L., & Liu, R.-T. (2020) · International Journal of Nanomedicine · doi:10.2147/ijn.s240953 · Cited by 55
The Role of Lipid Environment in Ganglioside GM1-Induced Amyloid β Aggregation
Rudajev, V., & Novotný, J. (2020) · Membranes · doi:10.3390/membranes10090226 · Cited by 55
Wang, J., Zheng, J., Huang, C., Zhao, J., Lin, J., Zhou, X., Naman, C. B., Wang, N., Gerwick, W. H., Wang, Q., et al. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00527 · Cited by 54
Wei, H., Zhang, H., Wang, X., Xie, J., An, D., Wan, L., Wang, J., Zeng, Y., Shu, X., Westermarck, J. K., et al. (2020) · Neurotherapeutics · doi:10.1007/s13311-020-00841-6 · Cited by 54
Engeletin Attenuates Aβ1–42-Induced Oxidative Stress and Neuroinflammation by Keap1/Nrf2 Pathway
Huang, Z., Ji, H., Shi, J., Zhu, X., & Zhi, Z. (2020) · Inflammation · doi:10.1007/s10753-020-01250-9 · Cited by 54
Benefits in Alzheimer’s Disease of Sensory and Multisensory Stimulation
Yang, H., Luo, Y., Hu, Q., Tian, X., & Wen, H. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-201554 · Cited by 54
ACU193: An Immunotherapeutic Poised to Test the Amyloid β Oligomer Hypothesis of Alzheimer’s Disease
Krafft, G. A., Jerecı̀ć, J., Siemers, E., & Cline, E. N. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.848215 · Cited by 54
Necroptosis and Alzheimer’s Disease: Pathogenic Mechanisms and Therapeutic Opportunities
Zhang, R., Song, Y., & Su, X. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-220809 · Cited by 56
Garcia‐Esparcia, P., López‐González, I., Grau‐Rivera, O., Garrido, M. G., Koneti, A., Llorens, F., Zafar, S., Carmona, M., del Río, J. A., Zerr, I., et al. (2017) · Frontiers in Neurology · doi:10.3389/fneur.2017.00089 · Cited by 54
Impact of GM1 on Membrane-Mediated Aggregation/Oligomerization of β-Amyloid: Unifying View
Cebecauer, M., Hof, M., & Amaro, M. (2017) · Biophysical Journal · doi:10.1016/j.bpj.2017.03.009 · Cited by 51
Cao, K., Dong, Y., Xiang, J., Xu, Y., Hong, W., Song, H., & Guan, Z.-Z. (2018) · Journal of Clinical Pathology · doi:10.1136/jclinpath-2018-205320 · Cited by 53
Yildirimer, L., Zhang, Q., Kuang, S., Cheung, J. C., Chu, K. A., He, Y., Yang, M., & Zhao, X. (2019) · Biofabrication · doi:10.1088/1758-5090/ab17aa · Cited by 54
VEGF counteracts amyloid-β-induced synaptic dysfunction
Martin, L., Bouvet, P., Chounlamountri, N., Watrin, C., Besançon, R., Pinatel, D., Meyronet, D., Honnorat, J., Buisson, A., Salin, P. A., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109121 · Cited by 52
Taniguchi, K., Yamamoto, F., Amano, A., Tamaoka, A., Sanjo, N., Yokota, T., Kametani, F., & Araki, W. (2022) · Neuroscience Research · doi:10.1016/j.neures.2022.03.001 · Cited by 57
Peng, C., Wang, X., Li, Y., Li, H., & Wong, M. S. (2019) · Journal of Materials Chemistry B · doi:10.1039/c9tb00161a · Cited by 51
BACE1 SUMOylation increases its stability and escalates the protease activity in Alzheimer’s disease
Bao, J., Qin, M., Mahaman, Y. A. R., Zhang, B., Huang, F., Zeng, K., Xia, Y., Ke, D., Wang, Q., Liu, R., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1800498115 · Cited by 50
Pate, K. M., Rogers, M., Reed, J. W., van der Munnik, N. P., Vance, S. Z., & Moss, M. A. (2016) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.12659 · Cited by 51
Brain Inflammation Connects Cognitive and Non-Cognitive Symptoms in Alzheimer’s Disease
Sellés, M. C., Oliveira, M. M., & Ferreira, S. T. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-179925 · Cited by 51
Observation of β-Amyloid Peptide Oligomerization by Pressure-Jump NMR Spectroscopy
Barnes, C. A., Robertson, A. J., Louis, J. M., Anfinrud, P., & Bax, A. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b06970 · Cited by 50
Chai, A. B., Hartz, A. M. S., Gao, X., Yang, A., Callaghan, R., & Gelissen, I. C. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms22010246 · Cited by 51
Liu, D., Li, W., Jiang, X., Bai, S., Liu, J., Liu, X., Shi, Y., Kuai, Z., Kong, W., Gao, R., et al. (2019) · Theranostics · doi:10.7150/thno.30649 · Cited by 49
Nanotechnology for the diagnosis and treatment of Alzheimer's disease: A bibliometric analysis
Li, L., He, R., Yan, H., Leng, Z., Zhu, S., & Gu, Z. (2022) · Nano Today · doi:10.1016/j.nantod.2022.101654 · Cited by 49
Key Peptides and Proteins in Alzheimer’s Disease
Penke, B., Bogár, F., Paragi, G., Gera, J., & Fülöp, L. (2019) · Current Protein and Peptide Science · doi:10.2174/1389203720666190103123434 · Cited by 51
Frost, P. S., Barros‐Aragão, F. G. Q., da Silva, R. T., Venancio, A. M., Matias, I. C. P., Silva, N. M. L. E., Kincheski, G. C., Pimentel‐Coelho, P. M., Felice, F. G. D., Gomes, F. C. A., et al. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1529-x · Cited by 51
Arendash, G. W., Cao, C., Abulaban, H., Baranowski, R., Wisniewski, G., Becerra, L. R., Andel, R., Lin, X., Zhang, X., Wittwer, D., et al. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190367 · Cited by 52
Interaction of Aβ42 with Membranes Triggers the Self-Assembly into Oligomers
Banerjee, S., Hashemi, M., Zagorski, K., & Lyubchenko, Y. L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21031129 · Cited by 51
Molecular Mechanism of Vitamin K2 Protection against Amyloid-β-Induced Cytotoxicity
Huang, S.-H., Fang, S.-T., & Chen, Y.-C. (2021) · Biomolecules · doi:10.3390/biom11030423 · Cited by 49
Sharma, A., Angnes, L., Sattarahmady, N., Negahdary, M., & Heli, H. (2023) · Biosensors · doi:10.3390/bios13070742 · Cited by 48
Yang, X., Chen, Y.-H., Liu, L., Gu, Z., You, Y., Hao, J., Sun, N., & Gao, C. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107357 · Cited by 49
Opportunities and challenges in developing relevant animal models for Alzheimer’s disease
Felice, F. G. D., & Munoz, D. P. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.01.006 · Cited by 50
Kelly, L., Seifi, M., Ma, R., Mitchell, S. J., Rudolph, U., Viola, K. L., Klein, W. L., Lambert, J. J., & Swinny, J. D. (2020) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12674 · Cited by 48
Self-citationRole of Intracellular Amyloid β as Pathway Modulator, Biomarker, and Therapy Target
Villarejo, L. G., Bachmann, L., Marks, D., Brachthäuser, M., Geidies, A., & Müller, T. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23094656 · Cited by 48
C3N nanodots inhibits Aβ peptides aggregation pathogenic path in Alzheimer’s disease
Yin, X., Zhou, H., Zhang, M., Su, J., Wang, X. L., Li, S., Yang, Z., Kang, Z., & Zhou, R. (2023) · Nature Communications · doi:10.1038/s41467-023-41489-y · Cited by 50
Kawanishi, S., Takata, K., Itezono, S., Nagayama, H., Konoya, S., Chisaki, Y., Toda, Y., Nakata, S., Yano, Y., Kitamura, Y., et al. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-170994 · Cited by 47
Transition metal complexes as imaging or therapeutic agents for neurodegenerative diseases
Ma, D., Wu, C., Li, G., Yung, T.-L., & Leung, C. (2020) · Journal of Materials Chemistry B · doi:10.1039/c9tb02669j · Cited by 47
Su, X., Tang, Z., Lu, Z.-Y., Liu, Y., He, W., Jiang, J., Zhang, Y., & Wu, H. (2021) · Journal of Molecular Neuroscience · doi:10.1007/s12031-021-01827-5 · Cited by 47
Linking in domain-swapped protein dimers
Baiesi, M., Orlandini, E., Trovato, A., & Seno, F. (2016) · Scientific Reports · doi:10.1038/srep33872 · Cited by 46
Jha, S. K., Jha, N. K., Kumar, D., Sharma, R., Shrivastava, A., Ambasta, R. K., & Kumar, P. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160623 · Cited by 48
Tremblay, C., François, A., Delay, C., Freland, L., Vandal, M., Bennett, D. A., & Calon, F. (2017) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlw109 · Cited by 49
Jarosz-Griffiths, H., Corbett, N. J., Rowland, H. A., Fisher, K., Jones, A. C., Baron, J., Howell, G. J., Cowley, S. A., Chintawar, S., Cader, M. Z., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005364 · Cited by 45
Rishton, G. M., Look, G. C., Ni, Z., Zhang, J. Y., Wang, Y., Huang, Y., Wu, X., Izzo, N. J., Mozzoni, K., Limegrover, C. S., et al. (2021) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.1c00048 · Cited by 45
Recent advancements toward therapeutic vaccines against Alzheimer’s disease
Herline, K., Drummond, E., & Wısnıewskı, T. (2018) · Expert Review of Vaccines · doi:10.1080/14760584.2018.1500905 · Cited by 46
Toxic amyloid-β oligomers induced self-replication in astrocytes triggering neuronal injury
Wang, W., Hou, T., Jia, L.-F., Wu, Q., Quan, M., & Jia, J. (2019) · EBioMedicine · doi:10.1016/j.ebiom.2019.03.049 · Cited by 42
Emerging roles of N- and C-terminally truncated Aβ species in Alzheimer’s disease
Wirths, O., & Zampar, S. (2019) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2019.1702972 · Cited by 44
Jia, W., Su, Q., Cheng, Q., Peng, Q., Qiao, A., Luo, X., Zhang, J., & Wang, Y. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/9966223 · Cited by 45
Neuropathology of the Alzheimer's continuum: an update
Jellinger, K. A. (2020) · Free Neuropathology · doi:10.17879/freeneuropathology-2020-3050 · Cited by 52
Inhibiting Aβ toxicity in Alzheimer's disease by a pyridine amine derivative
Zhu, Z., Yang, T., Zhang, L., Liu, L., Yin, E., Zhang, C., Guo, Z., Chen, X., & Wang, X. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.02.052 · Cited by 44
Wang, X., Li, J., Ma, C., Huang, C., & Li, Z. (2019) · Biochemical Pharmacology · doi:10.1016/j.bcp.2019.113674 · Cited by 45
Detection of retinal and blood Aβ oligomers with nanobodies
Habiba, U., Descallar, J., Kreilaus, F., Adhikari, U. K., Kumar, S., Morley, J. W., Bui, B. V., Koronyo‐Hamaoui, M., & Tayebi, M. (2021) · Alzheimer s & Dementia Diagnosis Assessment & Disease Monitoring · doi:10.1002/dad2.12193 · Cited by 43
Guo, H.-D., Zhu, J., Tian, J.-X., Shao, S.-J., Xu, Y., Mou, F.-F., Han, X.-J., Yu, Z., Chen, J., Zhang, D., et al. (2016) · Acupuncture in Medicine · doi:10.1136/acupmed-2015-010894 · Cited by 42
Ren, J.-M., Zhang, S.-L., Wang, X., Guan, Z., & Qi, X. (2020) · Molecular Medicine Reports · doi:10.3892/mmr.2020.11253 · Cited by 43
β-Amyloid fibrils catalyze neurotransmitter degradation
Arad, E., Leshem, A. B., Rapaport, H., & Jelinek, R. (2021) · Chem Catalysis · doi:10.1016/j.checat.2021.07.005 · Cited by 42
Intranasal rifampicin for Alzheimer's disease prevention
Umeda, T., Tanaka, A., Sakai, A., Yamamoto, A., Sakane, T., & Tomiyama, T. (2018) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1016/j.trci.2018.06.012 · Cited by 40
Alzheimer’s disease pathological lesions activate the spleen tyrosine kinase
Schweig, J. E., Yao, H., Beaulieu‐Abdelahad, D., Ait‐Ghezala, G., Mouzon, B., Crawford, F., MULLAN, M. J., & Paris, D. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0472-2 · Cited by 40
Sellés, M. C., Fortuna, J. T. S., Zappa-Villar, M. F., de Faria, Y. P. R., de Souza, A. S., Suemoto, C. K., Leite, R. E. P., Rodriguez, R. D., Grinberg, L. T., Reggiani, P. C., et al. (2019) · Molecular Neurobiology · doi:10.1007/s12035-019-01827-y · Cited by 42
A review on α-mangostin as a potential multi-target-directed ligand for Alzheimer's disease
Yang, A., Liu, C., Wu, J., Kou, X., & Shen, R. (2021) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2021.173950 · Cited by 41
Metformin a Potential Pharmacological Strategy in Late Onset Alzheimer’s Disease Treatment
Poor, S. R., Ettcheto, M., Cano, A. C., Sánchez‐López, E., Manzine, P. R., Olloquequi, J., Camins, A., & Javan, M. (2021) · Pharmaceuticals · doi:10.3390/ph14090890 · Cited by 41
Yue, F., Feng, S., Lu, C., Zhang, T., Tao, G., Liu, J., Yue, C., & Jing, N. (2021) · iScience · doi:10.1016/j.isci.2021.103207 · Cited by 41
Potjewyd, F., & Axtman, A. D. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.768655 · Cited by 37
Therapeutic Potential of Targeting Mitochondria for Alzheimer’s Disease Treatment
Atlante, A., Amadoro, G., Latina, V., & Valenti, D. (2022) · Journal of Clinical Medicine · doi:10.3390/jcm11226742 · Cited by 40
Mani, S., Dubey, R., Lai, I., Babu, M. A., Tyagi, S., Swargiary, G., Mody, D., Singh, M., Agarwal, S., Iqbal, D., et al. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-220700 · Cited by 43
Mamada, N., Tanokashira, D., Hosaka, A., Kametani, F., Tamaoka, A., & Araki, W. (2015) · Molecular Brain · doi:10.1186/s13041-015-0163-5 · Cited by 40
Otophylloside B Protects Against Aβ Toxicity in Caenorhabditis elegans Models of Alzheimer’s Disease
Yang, J., Huang, X., Wan, Q.-L., Ding, A.-J., Yang, Z., Qiu, M., Sun, H., Qi, S., & Luo, H. (2017) · Natural Products and Bioprospecting · doi:10.1007/s13659-017-0122-1 · Cited by 41
Ettcheto, M., Sánchez‐López, E., Pons, L., Busquets, O., Olloquequi, J., Beas‐Zárate, C., Pallàs, M., García, M. L., Auladell, C., Folch, J., et al. (2017) · Redox Biology · doi:10.1016/j.redox.2017.06.003 · Cited by 39
Amyloid β-peptides 1–40 and 1–42 form oligomers with mixed β-sheets
Baldassarre, M., Baronio, C. M., Morozova‐Roche, L. A., & Barth, A. (2017) · Chemical Science · doi:10.1039/c7sc01743j · Cited by 39
Bowroju, S. K., Mainali, N., Ayyadevara, S., Penthala, N. R., Krishnamachari, S., Kakraba, S., Reis, R. J. S., & Crooks, P. A. (2020) · Molecules · doi:10.3390/molecules25163610 · Cited by 37
Abushakra, S. R., Porsteinsson, A. P., Sabbagh, M. N., Bracoud, L., Schaerer, J., Power, A., Hey, J. A., Scott, D., Suhy, J., Tolar, M., et al. (2020) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1002/trc2.12117 · Cited by 40
Xu, J., Ni, B., Ma, C., Rong, S., Gao, H. Y., Zhang, L., Xia, X., Huang, Q., Deng, Q., & Huang, F. (2022) · Journal of Advanced Research · doi:10.1016/j.jare.2022.04.015 · Cited by 39
Ong, L. K., Walker, F. R., & Nilsson, M. (2017) · AIMS Medical Science · doi:10.3934/medsci.2017.1.1 · Cited by 37
A small molecule Nec-1 directly induces amyloid clearance in the brains of aged APP/PS1 mice
Yang, S., Shin, J., Shin, N. N., Hwang, J., Hong, S.-C., Park, K., Lee, J. W., Lee, S., Baek, S., Kim, K., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-40205-5 · Cited by 38
Endosomal dysfunction impacts extracellular vesicle release: Central role in Aβ pathology
Arbo, B. D., Cechinel, L. R., Palazzo, R. P., & Siqueira, I. R. (2019) · Ageing Research Reviews · doi:10.1016/j.arr.2019.101006 · Cited by 40
Insulin Resistance as a Common Link Between Current Alzheimer’s Disease Hypotheses
Alves, S. S., da Silva-Júnior, R. M. P., Servilha‐Menezes, G., Homolak, J., Šalković‐Petrišić, M., & Garcia‐Cairasco, N. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-210234 · Cited by 39
Apolipoprotein E isoform-dependent effects on the processing of Alzheimer's amyloid-β
Chai, A. B., Lam, H. H. J., Kockx, M., & Gelissen, I. C. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2021.158980 · Cited by 41
Companys‐Alemany, J., Turcu, A. L., Schneider, M., Müller, C. E., Vázquez, S., Griñán‐Ferré, C., & Pallàs, M. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04438-4 · Cited by 43
Guo, Y., Huang, F., Sun, W., Zhou, Y., Chen, C., Qi, C., Yang, J., Li, X.-N., Luo, Z., Zhu, H., et al. (2021) · Chemical Science · doi:10.1039/d1sc03356e · Cited by 37
Hotsumi, M., Tajiri, M., Nikaido, Y., Sato, T., Makabe, K., & Konno, H. (2019) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2019.06.052 · Cited by 36
Bartolomé, F. B., Krzyzanowska, A., de la Cueva, M., Pascual, C., Antequera, D., Spuch, C., Villarejo‐Galende, A., Rábano, A., Fortea, J., Alcolea, D. A., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-66177-5 · Cited by 35
Genetic variants for personalised management of very low carbohydrate ketogenic diets
Aronica, L., Volek, J. S., Poff, A. M., & D’Agostino, D. P. (2020) · BMJ Nutrition Prevention & Health · doi:10.1136/bmjnph-2020-000167 · Cited by 37
Axonal Transport and Local Translation of mRNA in Neurodegenerative Diseases
Nagano, S., & Araki, T. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.697973 · Cited by 36
Coskuner‐Weber, O., & Uversky, V. N. (2019) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2019.05.007 · Cited by 35
Wang, D., Gu, X. Q., Ma, X., Chen, J., Zhang, Q., Yu, Z., Li, J., Meng, H., Tan, X., Tang, Y., et al. (2022) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2022.07.014 · Cited by 35
Senapati, S., Tripathi, K. K., Awad, K., & Rahimipour, S. (2024) · Small · doi:10.1002/smll.202311670 · Cited by 39
Gallo-Orive, Á., Moreno‐Guzmán, M., Sánchez-Paniagua, M., Montero‐Calle, A., Barderas, R., & Escarpa, A. (2024) · Analytical Chemistry · doi:10.1021/acs.analchem.3c05665 · Cited by 35
López‐Sánchez, N., Fontán‐Lozano, Á., Pallé, A., González-Álvarez, V., Rábano, A., Trejo, J. L., & Frade, J. M. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2017.04.008 · Cited by 33
Sebollela, A. S., Cline, E. N., Popova, I. A., Luo, K., Sun, X., Ahn, J., Barcelos, M. A., Bezerra, V. N., Silva, N. M. L. E., Patel, J., et al. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.14118 · Cited by 38
Self-citationLopez‐Grancha, M., Bernardelli, P., Moindrot, N., Genet, E., Vincent, C., Roudières, V., Krick, A., Sabuco, J.-F., Machnik, D., Ibghi, D., et al. (2021) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.121.000590 · Cited by 34
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review