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Amyloid Oligomers Exacerbate Tau Pathology in a Mouse Model of Tauopathy
Open accessAbstract
BACKGROUND: We aimed to investigate the influence of oligomeric forms of β-amyloid (Aβ) and the influence of the duration of exposure on the development of tau phosphorylation. METHODS: Aβ oligomers were injected intracranially either acutely into 5-month-old rTg4510 mice and tissue was collected 3 days later, or chronically into 3-month-old mice and tissue was collected 2 months later. Several forms of phosphorylated tau (p-tau), GSK3 (glycogen synthase kinase-3) and microglial and astrocyte activation were measured. RESULTS: Acute injections of Aβ oligomers had no effect on p-tau epitopes but did result in elevation of phosphorylated/activated GSK3 (pGSK3). Chronic infusion of Aβ oligomers into the right hippocampus resulted in 3- to 4-fold elevations in several p-tau isoforms with no changes in total tau levels. A significant elevation in pGSK3 accompanied these changes. Microglial staining with CD68 paralleled the increase in tau phosphorylation, however, CD45 staining was unaffected by Aβ. Control experiments revealed that the infusion of Aβ from the minipumps was largely complete by 10 days after implantation. Thus, the elevation in p-tau 2 months after implantation implies that the changes are quite persistent. CONCLUSION: Soluble Aβ(1-42) oligomers have long-lasting effects on tau phosphorylation in the rTg4510 model, possibly due to elevations in GSK3. These data suggest that even brief elevations in Aβ production, may have enduring impact on the risk for tauopathy.
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“The relationship between DTI-detected WM changes and histologically detected axonal loss has been observed in several animal and human studies 25, 51–54”
From Amyloid-beta induced retrograde axonal degeneration in a mouse tauopathy model (2019) · cites this paper as [52]
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“Similar to our findings, reductions in FA and increases in RAD were found to correlate with axon loss in abnormal WM in both MCI and AD patients 25,51–54”
From Amyloid-beta induced retrograde axonal degeneration in a mouse tauopathy model (2019) · cites this paper as [52]
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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RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory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
RetractedThe Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
Alzheimer'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
Grundke-Iqbal, I., Iqbal, K., Tung, Y. C., Quinlan, M., Wisniewski, H. M., & Binder, L. I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.13.4913 · Cited by 3,676
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
Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17
Hutton, M., Lendon, C. L., Rizzu, P., Baker, M., Froelich, S., Houlden, H., Pickering-Brown, S., Chakraverty, S., Isaacs, A., Grover, A., et al. (1998) · Nature · doi:10.1038/31508 · Cited by 3,498
A simplified system for generating recombinant adenoviruses
He, T., Zhou, S., da Costa, L. T., Yu, J., Kinzler, K. W., & Vogelstein, B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.5.2509 · Cited by 3,209
Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse
Schenk, D., Barbour, R., Dunn, W., Gordon, G., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., Khan, K., et al. (1999) · Nature · doi:10.1038/22124 · Cited by 3,160
A protein factor essential for microtubule assembly
Weingarten, M. D., Lockwood, A. H., Hwo, S. Y., & Kirschner, M. W. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.5.1858 · Cited by 3,089
Cited by
Sorted by citations
Items 1,201–1,300 of 1,639
Hsu, P.-H., Wei, K.-C., Huang, C.-Y., Wen, C.-J., Yen, T.-C., Liu, C.-L., Lin, Y.-T., Chen, J.-C., Shen, C.-R., & Liu, H.-L. (2013) · PLoS ONE · doi:10.1371/journal.pone.0057682 · Cited by 136
Roberts, M., Sevastou, I., Imaizumi, Y., Mistry, K., Talma, S., Dey, M., Gartlon, J., Ochiai, H., Zhou, Z., Akasofu, S., et al. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-0884-2 · Cited by 135
Drug development for alzheimer’s disease: Microglia induced neuroinflammation as a target
Dong, Y., Li, X., Cheng, J., & Hou, L. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20030558 · Cited by 136
Early axonopathy preceding neurofibrillary tangles in mutant tau transgenic mice
Leroy, K., Bretteville, A., Schindowski, K., Gilissen, E., Authelet, M., De Decker, R., Yilmaz, Z., Buée, L., & Brion, J.-P. (2007) · The American Journal of Pathology · doi:10.2353/ajpath.2007.070345 · Cited by 135
Mosconi, L., Rinne, J. O., Tsui, W. H., Berti, V., Li, Y., Wang, H., Murray, J., Scheinin, N., Någren, K., Williams, S., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914141107 · Cited by 135
The effect of Cu2+ and Zn2+ on the Aβ42 peptide aggregation and cellular toxicity
Sharma, A. K., Pavlova, S. T., Kim, J., Kim, J., & Mirica, L. M. (2013) · Metallomics · doi:10.1039/c3mt00161j · Cited by 135
Kommaddi, R. P., Das, D., Karunakaran, S., Nanguneri, S., Bapat, D., Ray, A., Shaw, E., Bennett, D. A., Nair, D., & Ravindranath, V. (2018) · The Journal of Neuroscience · doi:10.1523/jneurosci.2127-17.2017 · Cited by 135
Cognitive defects are reversible in inducible mice expressing pro-aggregant full-length human Tau
Van der Jeugd, A., Hochgräfe, K., Ahmed, T., Decker, J. M., Sydow, A., Hofmann, A., Wu, D., Messing, L., Balschun, D., D’Hooge, R., et al. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-0987-3 · Cited by 135
Microglial Malfunction: The Third Rail in the Development of Alzheimer's Disease
Mhatre, S. D., Tsai, C. A., Rubin, A. J., James, M. L., & Andreasson, K. I. (2015) · Trends in Neurosciences · doi:10.1016/j.tins.2015.08.006 · Cited by 134
Critical review: involvement of endoplasmic reticulum stress in the aetiology of Alzheimer's disease
Hashimoto, S., & Saido, T. C. (2018) · Open Biology · doi:10.1098/rsob.180024 · Cited by 129
β-amyloid redirects norepinephrine signaling to activate the pathogenic GSK3β/tau cascade
Zhang, F., Gannon, M., Chen, Y., Yan, S., Zhang, S., Feng, W., Tao, J., Sha, B., Liu, Z., Saito, T., et al. (2020) · Science Translational Medicine · doi:10.1126/scitranslmed.aay6931 · Cited by 133
The endocytic pathway in microglia during health, aging and Alzheimer’s disease
Solé-Domènech, S., Cruz, D. L., Capetillo-Zarate, E., & Maxfield, F. R. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.07.002 · Cited by 133
Zerbinatti, C. V., Wozniak, D. F., Cirrito, J., Cam, J. A., Osaka, H., Bales, K. R., Zhuo, M., Paul, S. M., Holtzman, D. M., & Bu, G. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0305803101 · Cited by 133
Frank, M. G., Weber, M. D., Fonken, L. K., Hershman, S. A., Watkins, L. R., & Maier, S. F. (2016) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2015.10.009 · Cited by 133
Baker, S. L., Harrison, T. M., Maass, A., La Joie, R., & Jagust, W. J. (2019) · Journal of Nuclear Medicine · doi:10.2967/jnumed.118.224113 · Cited by 132
Tejeda, G., & Díaz-Guerra, M. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18020268 · Cited by 126
Scheltens, P., Hallikainen, M., Grimmer, T., Duning, T., Gouw, A. A., Teunissen, C. E., Wink, A. M., Maruff, P., Harrison, J., van Baal, C. M., et al. (2018) · Alzheimer's Research & Therapy · doi:10.1186/s13195-018-0431-6 · Cited by 129
Leon, J., Moreno, A. J., Garay, B. I., Chalkley, R. J., Burlingame, A. L., Wang, D., & Dubal, D. B. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.07.024 · Cited by 123
Developing Effective Alzheimer’s Disease Therapies: Clinical Experience and Future Directions
Elmaleh, D. R., Farlow, M. R., Conti, P. S., Tompkins, R. G., Kundakovic, L., & Tanzi, R. E. (2019) · Journal of Alzheimer’s Disease · doi:10.3233/jad-190507 · Cited by 129
ATP-binding cassette transporter A7 (ABCA7) loss of function alters Alzheimer amyloid processing
Satoh, K., Abe-Dohmae, S., Yokoyama, S., St George-Hyslop, P., & Fraser, P. E. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.655076 · Cited by 128
Sex dimorphism profile of Alzheimer’s disease-type pathologies in an APP/PS1 mouse model
Jiao, S.-S., Bu, X.-L., Liu, Y.-H., Zhu, C., Wang, Q.-H., Shen, L.-L., Liu, C.-H., Wang, Y.-R., Yao, X.-Q., & Wang, Y.-J. (2016) · Neurotoxicity Research · doi:10.1007/s12640-015-9589-x · Cited by 129
Alzheimer’s disease: Ablating single master site abolishes tau hyperphosphorylation
Stefanoska, K., Gajwani, M., Tan, A. R. P., Ahel, H. I., Asih, P. R., Volkerling, A., Poljak, A., & Ittner, A. (2022) · Science Advances · doi:10.1126/sciadv.abl8809 · Cited by 128
RETRACTED: Soluble α-Synuclein Is a Novel Modulator of Alzheimer's Disease Pathophysiology
Larson, M. E., Sherman, M. A., Greimel, S., Kuskowski, M., Schneider, J. A., Bennett, D. A., & Lesné, S. E. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.0581-12.2012 · Cited by 128
RetractedTariot, P. N., Lopera, F., Langbaum, J. B., Thomas, R. G., Hendrix, S., Schneider, L. S., Rios‐Romenets, S., Giraldo, M., Acosta, N., Tobon, C., et al. (2018) · Alzheimer's & Dementia: Translational Research & Clinical Interventions · doi:10.1016/j.trci.2018.02.002 · Cited by 128
The Inflammatory Continuum of Traumatic Brain Injury and Alzheimer’s Disease
Kokiko-Cochran, O. N., & Godbout, J. P. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00672 · Cited by 128
Liu, D., Tang, H., Li, X.-Y., Deng, M.-F., Wei, N., Wang, X., Zhou, Y.-F., Wang, D.-Q., Fu, P., Wang, J.-Z., et al. (2017) · Molecular Therapy · doi:10.1016/j.ymthe.2017.01.018 · Cited by 127
Nobuhara, C. K., DeVos, S. L., Commins, C., Wegmann, S., Moore, B. D., Roe, A. D., Costantino, I., Frosch, M. P., Pitstick, R., Carlson, G. A., et al. (2017) · The American Journal of Pathology · doi:10.1016/j.ajpath.2017.01.022 · Cited by 120
Nitric Oxide: Exploring the Contextual Link with Alzheimer’s Disease
Asiimwe, N., Yeo, S. G., Kim, M.-S., Jung, J., & Jeong, N. Y. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/7205747 · Cited by 125
Cystatin C in aging and in Alzheimer’s disease
Mathews, P. M., & Levy, E. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.06.003 · Cited by 133
In vivo rate-determining steps of tau seed accumulation in Alzheimer’s disease
Meisl, G., Hidari, E., Allinson, K., Rittman, T., DeVos, S. L., Sanchez, J. S., Xu, C. K., Duff, K. E., Johnson, K. A., Rowe, J. B., et al. (2021) · Science Advances · doi:10.1126/sciadv.abh1448 · Cited by 127
Rangaraju, S., Raza, S. A., Li, N. X., Betarbet, R., Dammer, E. B., Duong, D., Lah, J. J., Seyfried, N. T., & Levey, A. I. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00405 · Cited by 126
Metformin promotes tau aggregation and exacerbates abnormal behavior in a mouse model of tauopathy
Barini, E., Antico, O., Zhao, Y., Asta, F., Tucci, V., Catelani, T., Marotta, R., Xu, H., & Gasparini, L. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0082-7 · Cited by 126
Nilotinib Effects on Safety, Tolerability, and Biomarkers in Alzheimer’s Disease
Turner, R. S., Hebron, M. L., Lawler, A., Mundel, E. E., Yusuf, N., Starr, J. N., Anjum, M., Pagan, F., Torres‐Yaghi, Y., Shi, W., et al. (2020) · Annals of Neurology · doi:10.1002/ana.25775 · Cited by 126
Microglia in Aging and Alzheimer’s Disease: A Comparative Species Review
Edler, M. K., Mhatre-Winters, I., & Richardson, J. R. (2021) · Cells · doi:10.3390/cells10051138 · Cited by 126
Targeting innate immunity for neurodegenerative disorders of the central nervous system
Andreasson, K. I., Bachstetter, A. D., Colonna, M., Ginhoux, F., Holmes, C., Lamb, B., Landreth, G., Lee, D. C., Low, D., Lynch, M. A., et al. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13667 · Cited by 126
Self-citationBACE inhibition-dependent repair of Alzheimer’s pathophysiology
Keskin, A. D., Kekuš, M., Adelsberger, H., Neumann, U., Shimshek, D. R., Song, B., Zott, B., Peng, T., Förstl, H., Staufenbiel, M., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1708106114 · Cited by 125
Alasmari, F., Alshammari, M. A., Alasmari, A. F., Alanazi, W. A., & Alhazzani, K. (2018) · BioMed Research International · doi:10.1155/2018/3087475 · Cited by 125
Genome instability in Alzheimer disease
Hou, Y., Song, H., Croteau, D. L., Akbari, M., & Bohr, V. A. (2017) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2016.04.005 · Cited by 120
Giovanoli, S., Notter, T., Richetto, J., Labouesse, M. A., Vuillermot, S., Riva, M. A., & Meyer, U. (2015) · Journal of Neuroinflammation · doi:10.1186/s12974-015-0437-y · Cited by 124
Cerebral Microvascular Accumulation of Tau Oligomers in Alzheimer’s Disease and Related Tauopathies
Castillo-Carranza, D. L., Nilson, A. N., Van Skike, C. E., Jahrling, J. B., Patel, K., Garach, P., Gerson, J. E., Sengupta, U., Abisambra, J., Nelson, P., et al. (2017) · Aging and disease · doi:10.14336/ad.2017.0112 · Cited by 118
Gray, N. E., Harris, C. J., Quinn, J. F., & Soumyanath, A. (2016) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2016.01.013 · Cited by 123
Baas, P. W., & Qiang, L. (2019) · Trends in Cell Biology · doi:10.1016/j.tcb.2019.02.007 · Cited by 123
Baligács, N., Albertini, G., Borrie, S. C., Serneels, L., Pridans, C., Balusu, S., & De Strooper, B. (2024) · Nature Communications · doi:10.1038/s41467-024-54779-w · Cited by 123
Alić, I., Goh, P. A., Murray, A., Portelius, E., Gkanatsiou, E., Gough, G., Mok, K. Y., Koschut, D., Brunmeir, R., Yeap, Y. J., et al. (2021) · Molecular Psychiatry · doi:10.1038/s41380-020-0806-5 · Cited by 123
Accumulation of Filamentous Tau in the Cerebral Cortex of Human Tau R406W Transgenic Mice
Ikeda, M., Kawarai, T., Kawarabayashi, T., Matsubara, E., Murakami, T., Sasaki, A., Tomidokoro, Y., Ikarashi, Y., Kuribara, H., Ishiguro, K., et al. (2005) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)62274-2 · Cited by 120
Schaffert, J., LoBue, C., White, C. L., Chiang, H.-S., Didehbani, N., Lacritz, L., Rossetti, H., Dieppa, M., Hart, J., & Cullum, C. M. (2018) · Neuropsychology · doi:10.1037/neu0000423 · Cited by 120
Tau drives translational selectivity by interacting with ribosomal proteins
Koren, S. A., Hamm, M. J., Meier, S. E., Weiss, B. E., Nation, G. K., Chishti, E. A., Arango, J. P., Chen, J., Zhu, H., Blalock, E. M., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-01970-9 · Cited by 122
Developing therapeutic approaches to tau, selected kinases, and related neuronal protein targets
Lee, V. M.-Y., Brunden, K. R., Hutton, M., & Trojanowski, J. Q. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006437 · Cited by 122
Parkinsonism, movement disorders and genetics in frontotemporal dementia
Baizabal-Carvallo, J. F., & Jankovic, J. (2016) · Nature Reviews Neurology · doi:10.1038/nrneurol.2016.14 · Cited by 121
Disease-Modifying Therapies for Alzheimer’s Disease: More Questions than Answers
Golde, T. E. (2022) · Neurotherapeutics · doi:10.1007/s13311-022-01201-2 · Cited by 119
Alzheimer's disease pathology is attenuated in a CD 38‐deficient mouse model
Blacher, E., Dadali, T., Bespalko, A., Haupenthal, V. J., Grimm, M. O. W., Hartmann, T., Lund, F. E., Stein, R., & Levy, A. (2015) · Annals of Neurology · doi:10.1002/ana.24425 · Cited by 117
The dendritic hypothesis for Alzheimer's disease pathophysiology
Cochran, J. N., Hall, A. M., & Roberson, E. D. (2014) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2013.12.004 · Cited by 114
An update on the novel and approved drugs for Alzheimer disease
Alhazmi, H. A., & Albratty, M. (2022) · Saudi Pharmaceutical Journal · doi:10.1016/j.jsps.2022.10.004 · Cited by 122
Young, M. L., & Franklin, J. L. (2019) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2019.103409 · Cited by 120
A comprehensive resource for induced pluripotent stem cells from patients with primary tauopathies
Karch, C. M., Kao, A. W., Karydas, A., Onanuga, K., Martinez, R., Argouarch, A., Wang, C., Huang, C., Sohn, P. D., Bowles, K. R., et al. (2019) · Stem Cell Reports · doi:10.1016/j.stemcr.2019.09.006 · Cited by 119
Gómez de San José, N., Massa, F., Halbgebauer, S., Oeckl, P., Steinacker, P., & Otto, M. (2022) · Journal of Neural Transmission · doi:10.1007/s00702-021-02411-2 · Cited by 112
Genetic variability in response to amyloid beta deposition influences Alzheimer’s disease risk
Salih, D. A., Bayram, S., Guelfi, S., Reynolds, R. H., Shoai, M., Ryten, M., Brenton, J. W., Zhang, D., Matarin, M., Botia, J. A., et al. (2019) · Brain Communications · doi:10.1093/braincomms/fcz022 · Cited by 110
Bassil, R., Shields, K., Granger, K., Zein, I., Ng, S., & Chih, B. (2021) · Nature Communications · doi:10.1038/s41467-021-25344-6 · Cited by 106
Takeda, S., Commins, C., DeVos, S. L., Nobuhara, C. K., Wegmann, S., Roe, A. D., Costantino, I., Fan, Z., Nicholls, S. B., Sherman, A. E., et al. (2016) · Annals of Neurology · doi:10.1002/ana.24716 · Cited by 113
Microbial involvement in Alzheimer disease development and progression
Bulgart, H. R., Neczypor, E. W., Wold, L. E., & Mackos, A. R. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00378-4 · Cited by 116
Nelson, M. R., Liu, P., Agrawal, A., Yip, O., Blumenfeld, J., Traglia, M., Kim, M. J., Koutsodendris, N., Rao, A., Grone, B., et al. (2023) · Nature Neuroscience · doi:10.1038/s41593-023-01480-8 · Cited by 120
Propagation of Tau via Extracellular Vesicles
Pérez, M., Avila, J., & Hernández, F. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00698 · Cited by 118
Poudel, P., & Park, S. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14040835 · Cited by 124
Immunotherapy Targeting Pathological Tau Protein in Alzheimer's Disease and Related Tauopathies
Sigurdsson, E. M. (2008) · Journal of Alzheimer's Disease · doi:10.3233/jad-2008-15202 · Cited by 116
Hippocampal activation is associated with longitudinal amyloid accumulation and cognitive decline
Leal, S. L., Landau, S. M., Bell, R. K., & Jagust, W. J. (2017) · eLife · doi:10.7554/elife.22978 · Cited by 117
Contributions of DNA Damage to Alzheimer’s Disease
Lin, X., Kapoor, A., Gu, Y., Chow, M. J., Peng, J., Zhao, K., & Tang, D. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21051666 · Cited by 117
DebBurman, S. K. (2002) · Cell Biology Education · doi:10.1187/cbe.02-07-0024 · Cited by 117
Age and Alzheimer’s disease gene expression profiles reversed by the glutamate modulator riluzole
Pereira, A. C., Gray, J. D., Kogan, J. F., Davidson, R. L., Rubin, T. G., Okamoto, M., Morrison, J. H., & McEwen, B. S. (2017) · Molecular Psychiatry · doi:10.1038/mp.2016.33 · Cited by 116
The keystone of Alzheimer pathogenesis might be sought in Aβ physiology
Puzzo, D., Gulisano, W., Arancio, O., & Palmeri, A. (2015) · Neuroscience · doi:10.1016/j.neuroscience.2015.08.039 · Cited by 116
Guedes, J. R., Lao, T., Cardoso, A. L., & El Khoury, J. (2018) · Frontiers in Neurology · doi:10.3389/fneur.2018.00549 · Cited by 115
Neumann, U., Rueeger, H., Machauer, R., Veenstra, S. J., Lueoend, R. M., Tintelnot-Blomley, M., Laue, G., Beltz, K., Vogg, B., Schmid, P., et al. (2015) · Molecular Neurodegeneration · doi:10.1186/s13024-015-0033-8 · Cited by 113
The neuritic plaque facilitates pathological conversion of tau in an Alzheimer’s disease mouse model
Li, T., Braunstein, K. E., Zhang, J., Lau, A., Sibener, L., Deeble, C., & Wong, P. C. (2016) · Nature Communications · doi:10.1038/ncomms12082 · Cited by 114
Rojas, J. C., Wang, P., Staffaroni, A. M., Heller, C., Cobigo, Y., Wolf, A., Goh, S.-Y. M., Ljubenkov, P. A., Heuer, H. W., Fong, J. C., et al. (2021) · Neurology · doi:10.1212/wnl.0000000000011848 · Cited by 106
Kontsekova, E., Zilka, N., Kovacech, B., Skrabana, R., & Novak, M. (2014) · Alzheimer's Research & Therapy · doi:10.1186/alzrt277 · Cited by 112
Grace, E. A., & Busciglio, J. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-02-00493.2003 · Cited by 113
DNA damage in the oligodendrocyte lineage and its role in brain aging
Tse, K.-H., & Herrup, K. (2017) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2016.05.006 · Cited by 108
The informed road map to prevention of Alzheimer Disease: a call to arms
McDade, E., Llibre-Guerra, J. J., Holtzman, D. M., Morris, J. C., & Bateman, R. J. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00467-y · Cited by 89
Conway, O. J., Carrasquillo, M. M., Wang, X., Bredenberg, J. M., Reddy, J. S., Strickland, S. L., Younkin, C. S., Burgess, J. D., Allen, M., Lincoln, S. J., et al. (2018) · Molecular Neurodegeneration · doi:10.1186/s13024-018-0289-x · Cited by 112
Central role of glucocorticoid receptors in Alzheimer's disease and depression
Canet, G., Chevallier, N., Zussy, C., Desrumaux, C., & Givalois, L. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00739 · Cited by 106
Lacosta, A.-M., Pascual-Lucas, M., Pesini, P., Casabona, D., Pérez-Grijalba, V., Marcos-Campos, I., Sarasa, L., Canudas, J., Badi, H., Monleón, I., et al. (2018) · Alzheimer's Research & Therapy · doi:10.1186/s13195-018-0340-8 · Cited by 111
Role of the Immune System in the Pathogenesis, Prevention and Treatment of Alzheimer??s Disease
Blasko, I., & Grubeck-Loebenstein, B. (2003) · Drugs & Aging · doi:10.2165/00002512-200320020-00002 · Cited by 108
Amyloid-β-Induced Dysregulation of AMPA Receptor Trafficking
Guntupalli, S., Widagdo, J., & Anggono, V. (2016) · Neural Plasticity · doi:10.1155/2016/3204519 · Cited by 110
Fractalkine overexpression suppresses tau pathology in a mouse model of tauopathy
Nash, K. R., Lee, D. C., Hunt, J. B., Morganti, J. M., Selenica, M.-L., Moran, P., Reid, P., Brownlow, M., Guang-Yu Yang, C., Savalia, M., et al. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.12.011 · Cited by 108
Self-citationZheng, H., Liu, C.-C., Atagi, Y., Chen, X.-F., Jia, L., Yang, L., He, W., Zhang, X., Kang, S. S., Rosenberry, T. L., et al. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2016.03.004 · Cited by 110
Distinct Signaling Pathways Regulate TREM2 Phagocytic and NFκB Antagonistic Activities
Yao, H., Coppola, K., Schweig, J. E., Crawford, F., Mullan, M., & Paris, D. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00457 · Cited by 110
Tau biology, tauopathy, traumatic brain injury, and diagnostic challenges
Castellani, R. J., & Perry, G. (2019) · Journal of Alzheimer’s Disease · doi:10.3233/jad-180721 · Cited by 110
Rovelet-Lecrux, A., Charbonnier, C., Wallon, D., Nicolas, G., Seaman, M. N. J., Pottier, C., Breusegem, S. Y., Mathur, P. P., Jenardhanan, P., Le Guennec, K., et al. (2015) · Molecular Psychiatry · doi:10.1038/mp.2015.100 · Cited by 106
Delineating the Mechanism of Alzheimer’s Disease Aβ Peptide Neurotoxicity
Cappai, R., & Barnham, K. J. (2008) · Neurochemical Research · doi:10.1007/s11064-007-9469-8 · Cited by 108
Antisense drugs make sense for neurological diseases
Bennett, C. F., Kordasiewicz, H. B., & Cleveland, D. W. (2021) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010919-023738 · Cited by 108
Li, H., Liu, C.-C., Zheng, H., & Huang, T. Y. (2018) · Translational Neurodegeneration · doi:10.1186/s40035-018-0139-3 · Cited by 103
Tau reduction in the presence of amyloid-β prevents tau pathology and neuronal death in vivo
DeVos, S. L., Corjuc, B. T., Commins, C., Dujardin, S., Bannon, R. N., Corjuc, D., Moore, B. D., Bennett, R. E., Jorfi, M., Gonzales, J. A., et al. (2018) · Brain · doi:10.1093/brain/awy117 · Cited by 106
Driscoll, I., Troncoso, J. C., Rudow, G., Sojkova, J., Pletnikova, O., Zhou, Y., Kraut, M. A., Ferrucci, L., Mathis, C. A., Klunk, W. E., et al. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-1025-1 · Cited by 104
Pan, R.-Y., Zhang, J., Wang, J., Wang, Y., Li, Z., Liao, Y., Liao, Y., Zhang, C., Liu, Z., Song, L., et al. (2022) · Nature Aging · doi:10.1038/s43587-022-00311-y · Cited by 107
Li, Z., Farias, F. H. G., Dube, U., Del-Aguila, J. L., Mihindukulasuriya, K. A., Fernandez, M. V., Ibanez, L., Budde, J. P., Wang, F., Lake, A. M., et al. (2020) · Acta Neuropathologica · doi:10.1007/s00401-019-02066-0 · Cited by 85
A New Understanding of TMEM119 as a Marker of Microglia
Ruan, C., & Elyaman, W. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.902372 · Cited by 95
Dai, C.-L., Hu, W., Tung, Y. C., Liu, F., Gong, C.-X., & Iqbal, K. (2018) · Alzheimer's Research & Therapy · doi:10.1186/s13195-018-0341-7 · Cited by 99
Microglial large extracellular vesicles propagate early synaptic dysfunction in Alzheimer’s disease
Gabrielli, M., Prada, I., Joshi, P., Falcicchia, C., D’Arrigo, G., Rutigliano, G., Battocchio, E., Zenatelli, R., Tozzi, F., Radeghieri, A., et al. (2022) · Brain · doi:10.1093/brain/awac083 · Cited by 106
Anti‐amyloid antibody treatments for Alzheimer's disease
Perneczky, R., Dom, G., Chan, A., Falkai, P., & Bassetti, C. (2024) · European Journal of Neurology · doi:10.1111/ene.16049 · Cited by 106
APP Function and Lipids: A Bidirectional Link
Grimm, M. O. W., Mett, J., Grimm, H. S., & Hartmann, T. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00063 · Cited by 104
Zhao, Y., Tseng, I.-C., Heyser, C. J., Rockenstein, E., Mante, M., Adame, A., Zheng, Q., Huang, T., Wang, X., Arslan, P. E., et al. (2015) · Neuron · doi:10.1016/j.neuron.2015.08.020 · Cited by 98
Metadata
- Authors
- Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D.
- Affiliations
- University of South Florida (US)
- Venue
- Neurodegenerative Diseases
- Publisher
- S. Karger AG
- Published
- 2012-07-10
- Volume
- 11
- Issue
- 4
- Pages
- 165-181
- ISSN
- 1660-2854 (ISSN-L)
- 1660-2862
- PMC
- PMC3739054
- OpenAlex
- W2082429191
- Cited by
- 10,359
- References
- 186
- Citations by year
- 2026: 7 · 2025: 280 · 2024: 673 · 2023: 878 · 2022: 924 · 2021: 753 · 2020: 704 · 2019: 697 · 2018: 812 · 2017: 836 · 2016: 793 · 2015: 823 · 2014: 330 · 2013: 215 · 2012: 191
- FWCI
- 334.15
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Neurodegenerative Diseases (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Institute on Aging (AG 15490, R01AG015490, R29AG010282)
- National Institute of Neurological Disorders and Stroke (R01NS030352, NS76308, R01NS076308, R01NS073899)
- National Center for Research Resources (S10RR025633)
- 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, tau phosphorylation, tauopathy, glycogen synthase kinase-3, rTg4510 mice, microglial activation, astrocyte activation, hippocampus, Alzheimer's disease
- MeSH terms
- CD68 Molecule, Animals, Disease Models, Animal, Hippocampus, Mice, Transgenic, Neurons, Peptide Fragments, Phosphorylation, Antigens, Differentiation, Myelomonocytic, Antigens, CD, Amyloid beta-Peptides, tau Proteins, Leukocyte Common Antigens, Microglia, Tauopathies, Glycogen Synthase Kinase 3, Mice
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