The DOI matches its Crossref record; 52 of the 52 references it cites were found in a registry or an index.
A Mouse Model of Amyloid β Oligomers: Their Contribution to Synaptic Alteration, Abnormal Tau Phosphorylation, Glial Activation, and Neuronal Loss In Vivo
Open accessAbstract
Although amyloid β (Aβ) oligomers are presumed to cause synaptic and cognitive dysfunction in Alzheimer's disease (AD), their contribution to other pathological features of AD remains unclear. To address the latter, we generated APP transgenic mice expressing the E693Δ mutation, which causes AD by enhanced Aβ oligomerization without fibrillization. The mice displayed age-dependent accumulation of intraneuronal Aβ oligomers from 8 months but no extracellular amyloid deposits even at 24 months. Hippocampal synaptic plasticity and memory were impaired at 8 months, at which time the presynaptic marker synaptophysin began to decrease. Furthermore, we detected abnormal tau phosphorylation from 8 months, microglial activation from 12 months, astrocyte activation from 18 months, and neuronal loss at 24 months. These findings suggest that Aβ oligomers cause not only synaptic alteration but also other features of AD pathology and that these mice are a useful model of Aβ oligomer-induced pathology in the absence of amyloid plaques.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“In the E693Delta APP mutation discovered in a Japanese kindred (Nishitsuji et al., 2009), the presence of intracellular oligomers is essentially identical in patients and in the transgenic mouse model (Tomiyama et al., 2010).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Tomiyama et al., 2010
In the citing paper
“This idea is confirmed by studies reporting a transgenic mouse model bearing APP with a recently described AD-associated mutation that exhibits intraneuronal Aβ accumulation in the absence of plaques and still shows signs of AD-related neurodegeneration [113].”
From Senescence-related impairment of autophagy induces toxic intraneuronal amyloid-β accumulation in a mouse model of amyloid pathology (2023) · cites this paper as [113]
In the citing paper
“The other major limitation of these mouse models was that while some showed evidence of localized hyperphosphylated tau that may represent “pretangles”[107, 118, 151, 159], none developed neurofibrillary tangles.”
From Alzheimer's disease: experimental models and reality (2017) · cites this paper as [159]
In the citing paper
“The APP E693Δ-Tg model expresses the Osaka (APPE693Δ) mutation, which results in a unique phenotype of significantly increased expression of Aβ oligomers, synaptic impairment and cognitive impairments from 8 months of age, but no plaque or tau pathology formation [159].”
From Alzheimer's disease: experimental models and reality (2017) · cites this paper as [159]
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 · cited 4×
“…mice A oligomers have been demonstrated to cause synaptic and cognitive dysfunction (Lambert et al., 1998; Walsh et al., 2002; Cleary et al., 2005; Lesné et al., 2006; Shankar et al., 2008; Tomiyama et al., 2008) and loss of synapses (Lacor et al., 2007; Shankar et al., 2007; Takuma et al.,…”
BackgroundInfluentialRetractedAlzheimer's Disease Is a Synaptic Failure
Selkoe, D. J. (2002) · Science · doi:10.1126/science.1074069 · Cited by 4,420
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
Correlative Memory Deficits, Aβ Elevation, and Amyloid Plaques in Transgenic Mice
Hsiao, K., Chapman, P., Nilsen, S., Eckman, C., Harigaya, Y., Younkin, S., Yang, F., & Cole, G. (1996) · Science · doi:10.1126/science.274.5284.99 · Cited by 4,210
Triple-Transgenic Model of Alzheimer’s Disease with Plaques and Tangles
Oddo, S., Caccamo, A., Shepherd, J. D., Murphy, M. P., Golde, T. E., Kayed, R., Metherate, R., Mattson, M. P., Akbari, Y., & LaFerla, F. M. (2003) · Neuron · doi:10.1016/s0896-6273(03)00434-3 · Cited by 4,126
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
Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685
Oakley, H., Cole, S. L., Logan, S., Maus, E., Shao, P., Craft, J., Guillozet-Bongaarts, A., Ohno, M., Disterhoft, J., Van Eldik, L., et al. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.1202-06.2006 · Cited by 3,530 · cited 4×
“The finding that A oligomers were largely recovered in insoluble fractions suggests the possibility that intraneuronal A in the APPE693 -Tg mice may form fibrils, as reported in other APP-Tg mice (Casas et al., 2004; Oakley et al., 2006).”
BackgroundMethodResultInfluentialDiffusible, 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-citationNeuN, a neuronal specific nuclear protein in vertebratesxs
Mullen, R. J., Buck, C. R., & Smith, A. M. (1992) · Development · doi:10.1242/dev.116.1.201 · Cited by 2,351
Cited by
Sorted by citations
Items 301–396 of 396
Challenges in understanding the structure/activity relationship of Aβ oligomers
Pilkington, A. W., & Legleiter, J. A. (2019) · AIMS Biophysics · doi:10.3934/biophy.2019.1.1 · Cited by 7
Matsushima, Y., Irie, Y., Kageyama, Y., Bellier, J., Tooyama, I., Maki, T., Kume, T., Yanagita, R. C., & Irie, K. (2022) · ChemBioChem · doi:10.1002/cbic.202200029 · Cited by 8
Recombinant Integrin β1 Signal Peptide Blocks Gliosis Induced by Aβ Oligomers
Ortiz-Sanz, C., Llavero, F., Zuazo-Ibarra, J., Balantzategi, U., Quintela‐López, T., Wyssenbach, A., Capetillo‐Zarate, E., Matute, C., Alberdi, E. M., & Zugaza, J. L. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23105747 · Cited by 7
Maki, T., Sawahata, M., Akutsu, I., Amaike, S., Hiramatsu, G., Uta, D., Izuo, N., Shimizu, T., Irie, K., & Kume, T. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232113259 · Cited by 7
Aβ oligomer induced cognitive impairment and evaluation of ACU193‐MNS‐based MRI in rabbit
Rozema, N. B., Procissi, D., Bertolino, N., Viola, K. L., Nandwana, V., Abdul, N., Pribus, S. J., Dravid, V. P., Klein, W. L., Disterhoft, J. F., et al. (2020) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1002/trc2.12087 · Cited by 6
Self-citationImaging organelle transport in primary hippocampal neurons treated with amyloid-β oligomers
Gan, K. J., & Silverman, M. A. (2015) · Methods in cell biology · doi:10.1016/bs.mcb.2015.06.012 · Cited by 7
Schützmann, M. P., & Hoyer, W. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169048 · Cited by 7
Aβ∗56 is a stable oligomer that impairs memory function in mice
Liu, P., Lapcinski, I. P., Hlynialuk, C. J. W., Steuer, E. L., Loude, T. J., Shapiro, S. L., Kemper, L. J., & Ashe, K. H. (2024) · iScience · doi:10.1016/j.isci.2024.109239 · Cited by 6
Armbrust, F., Bickenbach, K., Altmeppen, H. C., Foggetti, A., Winkelmann, A., Wulff, P., Glatzel, M., Pietrzik, C. U., & Becker‐Pauly, C. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05139-w · Cited by 9
Célestine, M., Jacquier‐Sarlin, M. R., Borel, E., Petit, F., Pérot, J., Hérard, A., Bousset, L., Buisson, A., & Dhénain, M. (2023) · Acta Neuropathologica Communications · doi:10.1186/s40478-023-01559-0 · Cited by 7
Falangola, M. F., Dhiman, S., Voltin, J. R., & Jensen, J. H. (2023) · Magnetic Resonance Imaging · doi:10.1016/j.mri.2023.06.017 · Cited by 6
Aβ Oligomers-Induced Toxicity is Attenuated in Cells Cultured with NbActiv4™ Medium
Zhou, Y., & Klein, W. L. (2012) · Neurotoxicity Research · doi:10.1007/s12640-012-9318-7 · Cited by 6
Self-citationAmyloid-β oligomers unveil a novel primate model of sporadic Alzheimer's disease
Jebelli, J. D., & Piers, T. M. (2015) · Frontiers in Neuroscience · doi:10.3389/fnins.2015.00047 · Cited by 6
Cyclin Dependent Kinase 11, Neuroinflammation and Alzheimer's Disease: A Review
Bajić, V. (2015) · Journal of Clinical & Cellular Immunology · doi:10.4172/2155-9899.1000305 · Cited by 6
Mrđenović, D., Lipkowski, J., & Pięta, P. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1843-1_18 · Cited by 6
Braak Staging in Mouse Models of Alzheimer's Disease
Granic, I., Masman, M. F., Luiten, P. G. M., & Eisel, U. L. M. (2010) · American Journal Of Pathology · doi:10.2353/ajpath.2010.100656 · Cited by 7
Kawarabayashi, T., Terakawa, T., Takahashi, A., Hasegawa, H., Narita, S., Sato, K., Nakamura, T., Seino, Y., Hirohata, M., Baba, N., et al. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190023 · Cited by 6
Fukuda, A., Nakashima, S., Oda, Y., Nishimura, K., Kawashima, H., Kimura, H., Ohgita, T., Kawashita, E., Ishihara, K., Hanaki, A., et al. (2023) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b22-00797 · Cited by 5
Malik, N., Miah, M.-U., Galgani, A., McAleese, K. E., Walker, L., LeBeau, F. E. N., Attems, J., Outeiro, T. F., Thomas, A. J., & Koss, D. J. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02691-4 · Cited by 5
Johnson, E. A., Nowar, R., Viola, K. L., Huang, W., Zhou, S., Bicca, M. A., Zhu, W., Kranz, D. L., Klein, W. L., & Silverman, R. B. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2402117122 · Cited by 5
Self-citationGu, S., & Ran, C. (2025) · iRadiology · doi:10.1002/ird3.70002 · Cited by 5
Velázquez-Delgado, C., Hernández-Ortiz, E., Landa‐Navarro, L., Rodríguez, M. T., Moreno‐Castilla, P., & Bermúdez‐Rattoni, F. (2024) · Psychopharmacology · doi:10.1007/s00213-024-06650-5 · Cited by 5
Memory rescue and learning in synaptic impaired neuronal circuits
Li, K. T., Ji, D., & Zhou, C. (2023) · iScience · doi:10.1016/j.isci.2023.106931 · Cited by 6
PET Applications in Animal Models of Neurodegenerative and Neuroinflammatory Disorders
Higuchi, M., Maeda, J., Ji, B., Tokunaga, M., Zhang, M., Maruyama, M., Ono, M., Fukumura, T., & Suhara, T. (2011) · Current topics in behavioral neurosciences · doi:10.1007/7854_2011_167 · Cited by 5
The role of amyloid beta 4-42 in the etiology of Alzheimer's disease
Bouter, Y. (2015) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-4849 · Cited by 5
Uchiumi, O., Zou, J., Yamaki, S., Hori, Y., Ono, M., Yamamoto, R., & Kato, N. (2024) · Brain Research · doi:10.1016/j.brainres.2024.148934 · Cited by 4
Zhang, T., Sun, J., Jiao, Q., Li, S., Meng, X., Shi, J., & Wang, B. (2024) · IBRO Neuroscience Reports · doi:10.1016/j.ibneur.2024.08.004 · Cited by 4
Zhao, W., Toolan, D. M., Hepler, R. W., Wolfe, A. L., Yu, Y., Price, E. A., Uebele, V. N., Schachter, J. B., Reynolds, I. J., Renger, J. J., et al. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-102022 · Cited by 4
Green Tea and Neurodegeneration in Alzheimer’s Disease
Ho, J. Y. S., Hung, C. H.-L., & Chang, R. C. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-384937-3.00058-6 · Cited by 4
The Role of Aβ in Alzheimer's Disease
Ryan, T. M., Roberts, B. R., Streltsov, V. A., Nuttall, S. D., & Masters, C. L. (2013) · doi:10.1002/9783527654185.ch13 · Cited by 4
Colettis, N. C., Oberholzer, M. V., Cercato, M. C., Habif, M., Sellés, M. C., Salas, D. A., Sebollela, A. S., Klein, W. L., Epstein, A. L., Salvetti, A., et al. (2023) · Journal of Applied Cognitive Neuroscience · doi:10.17981/jacn.4.1.2023.2 · Cited by 3
Self-citationRen, Q., Wang, S., Li, J., Cao, K., Zhuang, M., Wu, M., Geng, J., Jia, Z., Xie, W., & Liu, A. (2024) · Journal of Neuroscience · doi:10.1523/jneurosci.1689-23.2024 · Cited by 3
Review of Alzheimer’s Disease’s Animal Model with it’s Pathophysiology and Drug Discovery
Pal, T., & Das, M. (2024) · Asian Journal of Research in Pharmaceutical Sciences · doi:10.52711/2231-5659.2024.00006 · Cited by 4
Salahuddin, P., Khan, R. H., & Uversky, V. N. (2019) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2019.1697367 · Cited by 4
Murakami, K., Yamaguchi, T., Izuo, N., Kume, T., Hara, H., & Irie, K. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00331 · Cited by 3
Riffo-Lepe, N., González-Sanmiguel, J., Armijo‐Weingart, L., Saavedra, P., Hernandez, D., Ramos, G., Martín, L. S., & Aguayo, L. G. (2025) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-24-01052 · Cited by 2
A Novel Missense Variant in SORBS2 Is Causative With Familial Alzheimer's Disease
Wang, Q., Wang, S., Cao, S., Wang, Q., Wei, Y., Li, Y., Wang, Y., Li, Y., Qin, W., Quan, M., et al. (2025) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.70256 · Cited by 2
Asai, M., Shirotani, K., Kondo, T., Inoue, H., & Iwata, N. (2014) · Folia Pharmacologica Japonica · doi:10.1254/fpj.143.23 · Cited by 2
Neurodegenerative Diseases and Dementia
Janus, C., & Welzl, H. (2016) · Springer eBooks · doi:10.1007/978-1-4939-3777-6_6 · Cited by 2
Bu, R. L., Clark, J. R., DiChiara, T., Sligar, S. G., & Klein, W. L. (2018) · Neuromethods · doi:10.1007/978-1-4939-8739-9_13 · Cited by 2
Self-citationShivakumar, A. B., Mehak, S. F., Kumari, S., Saraf, V., & Gangadharan, G. (2022) · Springer eBooks · doi:10.1007/978-981-19-1352-5_14 · Cited by 2
Yamakuni, T., & Kawahata, K. (2015) · Folia Pharmacologica Japonica · doi:10.1254/fpj.145.229 · Cited by 2
Chen, T., Wang, Y., Wang, K., Zhu, P., Guo, Y., Yang, L., & Nie, W. (2025) · BMC Pregnancy and Childbirth · doi:10.1186/s12884-025-08553-5 · Cited by 1
Biological Targeting and Activity of Pre-fibrillar Aβ Assemblies
Wilcox, K. C., Pitt, J. E., Sebollela, A. S., Martirosova, H., Lacor, P. N., & Klein, W. L. (2011) · Springer eBooks · doi:10.1007/978-94-007-2774-8_4 · Cited by 1
Self-citationMolecular Mechanism Underlying Aβ Immunotherapy: Implications for the Toxic Action of Aβ Oligomers
Matsubara, E. (2013) · Journal of Gerontology & Geriatric Research · doi:10.4172/2167-7182.s2-001 · Cited by 1
Yoshida, H., Hashimoto, Y., Fukushima, T., Tanji, K., Matsumiya, T., Seya, K., Kawaguchi, S., & Imaizumi, T. (2019) · Institutional Repositories DataBase (IRDB) · doi:10.32216/hirosakiigaku.70.1_24 · Cited by 1
Intracellular Amyloid β: A Modification to the Amyloid Hypothesis in Alzheimer's Disease
Zhang, Y. (2011) · Wiley eBooks · doi:10.1002/9783527634323.ch6 · Cited by 1
SERF deletion modifies amyloid aggregation in a mouse model of Alzheimer’s diseasePreprint
Stroo, E., Janssen, L., Sin, O., Hogewerf, W., Koster, M. H., Harkema, L., Youssef, S. A., Beschörner, N., Wolters, A. H. G., Bakker, B., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.01.05.423442 · Cited by 1
Célestine, M., Jacquier‐Sarlin, M. R., Borel, E., Petit, F., Pérot, J., Hérard, A., Bousset, L., Buisson, A., & Dhénain, M. (2022) · Research Square · doi:10.21203/rs.3.rs-2334976/v1 · Cited by 1
Aβ*56 is present in brain extracts enriched for extracellular proteinsPreprint
Liu, P., Lapcinski, I. P., & Ashe, K. H. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.09.617424 · Cited by 1
Blutbasierte Mikrozirkulationsmarker bei der Alzheimer-Demenz
Knauer, K. (2010) · Electronic Theses of LMU Munich (Ludwig-Maximilians-Universität München) · doi:10.5282/edoc.12369
15. Therapeutic Application of iPS Cells
Kondo, T., Inoue, H., & Takahashi, R. (2013) · Nihon Naika Gakkai Zasshi · doi:10.2169/naika.102.2015
Panegyres, P. K., & Atkins, E. (2011) · Neuroscience & Medicine · doi:10.4236/nm.2011.23033
The involvement of degradation pathways and neuron-to-neuron transmission in Alzheimer’s disease
Agholme, L. (2012) · KTH Publication Database DiVA (KTH Royal Institute of Technology)
Molecular changes during the development of Alzheimer's disease
Wirz, K. T. S. (2013) · Data Archiving and Networked Services (DANS)
Conformational Disease and RNA Disease Theory in the Context of Neurodegenerative Diseases
Ishihara, T., Nishizawa, M., & Onodera, O. (2015) · Springer eBooks · doi:10.1007/978-4-431-54541-5_1
Synapse- and cell-specific plasticity in the mature hippocampus
Queenan, B. N. (2014) · DigitalGeorgetown (Georgetown University Library)
Farooqui, A. A. (2016) · Springer eBooks · doi:10.1007/978-3-319-15889-1_2
Immunocytochemical Detection of Intraneuronal Aβ Peptides in Mouse Models of Alzheimer’s Disease
Wirths, O., & Saul, A. (2015) · Neuromethods · doi:10.1007/978-1-4939-2313-7_10
Lorette, A. (2012)
Modeling of Alzheimer’s Disease and Outlooks for its Therapy Using Induced Pluripotent Stem Cells
Хаспеков, Л. Г. (2019) · Neurochemical Journal · doi:10.1134/s181971241902003x
The interaction of neutrophils and amyloid-ß in Alzheimer’s disease
Hill, M. J. (2020) · Otago University Research Archive (University of Otago)
Exercise-Mediated Autophagy and Alzheimer’s Disease
Kou, X., Zhang, M., Zhang, H., Kirberger, M., & Chen, N. (2021) · Springer eBooks · doi:10.1007/978-981-16-4525-9_7
Sasidharakurup, H., Menon, A. S., Sabeen, A. S., & Diwakar, S. (2021) · Advances in intelligent systems and computing · doi:10.1007/978-981-16-4369-9_19
Zampar, S. (2021) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-9004
Tracking Neurodegeneration: Advancement in Experimental Study Models
Arumugam, M., & Sugin Lal Jabaris, S. (2022) · Springer eBooks · doi:10.1007/978-981-16-6703-9_3
Functional spreading of hyperexcitability induced by human and synthetic intracellular Aβ oligomersPreprint
Fernández-Pérez, E. J., Muñoz, B., Bascuñán, D., Peters, C., Riffo-Lepe, N., Espinoza, M. P., Morgan, P. J., Filippi, C., Bourboulou, R., Sengupta, U., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.10.16.332445
Motoi, Y. (2010) · Juntendō Igaku/Juntendo igaku · doi:10.14789/pjmj.56.447
Aβ*56 is a Stable Oligomer That Correlates with Age-Related Memory Loss in Tg2576 MicePreprint
Liu, P., Lapcinski, I. P., Shapiro, S. L., Kemper, L. J., & Ashe, K. H. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.03.20.533414
Malik, N., Miah, M.-U., Galgani, A., McAleese, K. E., Walker, L., LeBeau, F. E. N., Attems, J., Outeiro, T. F., Thomas, A. J., & Koss, D. J. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.09.27.559720
Animal Models and Ethics in the Testing of Drugs for Alzheimer’s Disease
Roychowdhury, P., Justin, A., Gobinath, M., Karri, V. V. S. R., & Kuppusamy, G. (2024) · Springer eBooks · doi:10.1007/978-981-96-0259-9_17
Lapcinski, I. P., Petersen, A. J., Ashe, K. H., & Liu, P. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.04.11.648457
Gonzalo‐Ruiz, A., Delso, M., Carrero, I., Vicente, P. G., Anquela, J. M. S., Rodríguez, M. J., & Arévalo‐Serrano, J. (2011) · European Journal of Anatomy
Li, W., Pang, Y., Wang, Y., Mei, F., Guo, M., Wei, Y., Li, X., Qin, W., Wang, W., Jia, L., et al. (2023) · Figshare · doi:10.6084/m9.figshare.23583691
Amano, A., Sanjo, N., Araki, W., Anraku, Y., Nakakido, M., Matsubara, E., Tomiyama, T., Nagata, T., Tsumoto, K., Kataoka, K., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26565342
Self-citationAmano, A., Sanjo, N., Araki, W., Anraku, Y., Nakakido, M., Matsubara, E., Tomiyama, T., Nagata, T., Tsumoto, K., Kataoka, K., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26565345
Self-citationAmano, A., Sanjo, N., Araki, W., Anraku, Y., Nakakido, M., Matsubara, E., Tomiyama, T., Nagata, T., Tsumoto, K., Kataoka, K., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26565348
Self-citationLi, W., Pang, Y., Wang, Y., Mei, F., Guo, M., Wei, Y., Li, X., Qin, W., Wang, W., Jia, L., et al. (2023) · Figshare · doi:10.6084/m9.figshare.23583694
The influence of the liposomal form of curcumin and microRNA on the course of Alzheimer’s disease
Kot, Y. G., Kot, K., Андріяш, Г. С., Tigunova, O., Blume, Y. B., & Shulga, S. (2025) · Regulatory Mechanisms in Biosystems · doi:10.15421/0225187
Rôle des ADAM dans le processus physiopathologique de la maladie d'Alzheimer
Laumet, G. O. (2010) · theses.fr (ABES) · doi:10.70675/94126786zf990z488ezb471z5f1d5686766c
Etude préclinique et clinique de la phase précoce de la maladie d'Alzheimer
Epelbaum, S. (2015) · theses.fr (ABES) · doi:10.70675/ea81e5c2z5032z4474z9f96z59f62125a629
Hanbouch, L. (2017) · theses.fr (ABES) · doi:10.70675/c4d2c894zf69dz4ae4z9ab1zf4135d0efa12
Souchet, B. (2018) · theses.fr (ABES) · doi:10.70675/5510ef76zecf1z41f2z9496z015aa6a093be
Bergeron, S. (2018) · theses.fr (ABES) · doi:10.70675/36a54739zd120z440bzac6aze1ff3180f9f1
Développement d’un test sanguin pour le dépistage de la maladie d’Alzheimer
Torres, F. D. (2022) · theses.fr (ABES) · doi:10.70675/afbb97a5z1636z46abz844czb340616aeda1
The role of the α7 nicotinic acetylcholine receptor in a model of amyloid pathology
Santos, D. G. (2024) · theses.fr (ABES) · doi:10.70675/b3ed4de5zcd9ez4421za129z0a05130d86b9
Advanced glycation end-products in the pathogenesis of Alzheimer’s disease: a review
Mazur, K., & Smoleń, A. (2026) · Psychiatria i Psychologia Kliniczna · doi:10.15557/pipk.2026.0011
Jing, Z., Jiang, B., Li, W., Zhang, C., Xu, J., Zhang, T. A., Liu, D., Yu, L., Luo, D., & Guo, Z. (2026) · Journal of Natural Products · doi:10.1021/acs.jnatprod.6c00302
Yu, X., Ren, Q., Gao, Y., Xie, S., Dang, R., Meng, J., Su, Z., Li, M., Ao, Y., Liu, A., et al. (2026) · Cell Reports · doi:10.1016/j.celrep.2026.118063
Metadata
- Authors
- Tomiyama, T., Matsuyama, S., Iso, H., Umeda, T., Takuma, H., Ohnishi, K., Ishibashi, K., Teraoka, R., Sakama, N., Yamashita, T., Nishitsuji, K., Ito, K., Shimada, H., Lambert, M. P., Klein, W. L., & Mori, H.
- Affiliations
- Osaka City University (JP)
- Himeji Dokkyo University (JP)
- Hyogo University of Health Sciences (JP)
- Northwestern University (US)
- ORCID
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2010-04-06
- Volume
- 30
- Issue
- 14
- Pages
- 4845-4856
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC6632783
- OpenAlex
- W2095031277
- Semantic Scholar
- 599d4363741ebd4649dc5b7f2de2da4503720038
- Cited by
- 396
- References
- 52
- Citations by year
- 2026: 3 · 2025: 13 · 2024: 21 · 2023: 26 · 2022: 20 · 2021: 24 · 2020: 21 · 2019: 23 · 2018: 20 · 2017: 19 · 2016: 18 · 2015: 33 · 2014: 22 · 2013: 27 · 2012: 39
- FWCI
- 28.82
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Alzheimer's Association (IIRG-09-132098)
- Ministry of Education, Culture, Sports, Science and Technology (18023033, 17300114, 20023026, IIRG-09-132098)
- Ministry of Health, Labour and Welfare
- Japan Society for the Promotion of Science (18023033, 20023026, 17300114)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- amyloid-beta oligomers, Alzheimer's disease, APP transgenic mice, synaptic plasticity, memory impairment, synaptophysin, tau phosphorylation, microglial activation, astrocyte activation, neuronal loss, mouse model
- MeSH terms
- Alzheimer Disease, Animals, Disease Models, Animal, Humans, Male, Mice, Inbred C3H, Mice, Inbred C57BL, Mice, Transgenic, Neuroglia, Neurons, Phosphorylation, Synapses, Amyloid beta-Peptides, tau Proteins, Cell Death, Mice
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