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Amyloid Oligomers Exacerbate Tau Pathology in a Mouse Model of Tauopathy
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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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RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory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
Flagged first, then by citations
1 of the 186 references couldn’t be matched to a known paper.
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Items 401–500 of 1,639
A Recessive Mutation in the APP Gene with Dominant-Negative Effect on Amyloidogenesis
Fede, G. D., Catania, M., Morbin, M., Rossi, G., Suardi, S., Mazzoleni, G., Merlin, M., Gıovagnolı, A. R., Prioni, S., Erbetta, A., et al. (2009) · Science · doi:10.1126/science.1168979 · Cited by 429
Phosphorylation of Tau by Fyn: Implications for Alzheimer's Disease
Lee, G. S., Thangavel, R., Sharma, V. M., Litersky, J. M., Bhaskar, K., Fang, S. M., Lana, H., Andreadis, A., Hoesen, G. W. V., & Ksiȩżak-Reding, H. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.4162-03.2004 · Cited by 435
Norden, D. M., Muccigrosso, M. M., & Godbout, J. P. (2015) · Neuropharmacology · doi:10.1016/j.neuropharm.2014.10.028 · Cited by 413
Zhang, B., Maiti, A., Shively, S., Lakhani, F., McDonald-Jones, G., Bruce, J., Lee, E. B., Xie, S. X., Joyce, S., Li, C., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0406361102 · Cited by 413
A clinicopathological approach to the diagnosis of dementia
Elahi, F. M., & Miller, B. L. (2017) · Nature Reviews Neurology · doi:10.1038/nrneurol.2017.96 · Cited by 425
BACE1 inhibitor drugs in clinical trials for Alzheimer’s disease
Vassar, R. J. (2014) · Alzheimer s Research & Therapy · doi:10.1186/s13195-014-0089-7 · Cited by 421
Neuronal Cell Death Mechanisms in Major Neurodegenerative Diseases
Chi, H., Chang, H.-Y., & Sang, T.-K. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19103082 · Cited by 412
The crucial role of metal ions in neurodegeneration: the basis for a promising therapeutic strategy
Gaeta, A., & Hider, R. C. (2005) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0706416 · Cited by 411
Brain amyloid-β oligomers in ageing and Alzheimer’s disease
Lesné, S., Sherman, M. A., Grant, M. K. O., Kuskowski, M. A., Schneider, J. A., Bennett, D. A., & Ashe, K. H. (2013) · Brain · doi:10.1093/brain/awt062 · Cited by 430
Kim, T., Vidal, G. S., Djurisic, M., William, C. M., Birnbaum, M. E., Garcia, K. C., Hyman, B. T., & Shatz, C. J. (2013) · Science · doi:10.1126/science.1242077 · Cited by 410
Central role for PICALM in amyloid-β blood-brain barrier transcytosis and clearance
Zhao, Z., Sagare, A. P., Ma, Q., Halliday, M. R., Kong, P., Kisler, K., Winkler, E. A., Ramanathan, A., Kanekiyo, T., Bu, G., et al. (2015) · Nature Neuroscience · doi:10.1038/nn.4025 · Cited by 410
Glial contributions to neurodegeneration in tauopathies
Leyns, C. E. G., & Holtzman, D. M. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0192-x · Cited by 409
Calcium Signaling and Amyloid Toxicity in Alzheimer Disease
Demuro, A., Parker, I., & Stutzmann, G. E. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.r109.080895 · Cited by 426
Wu, Y., Wu, Z., Butko, P., Christen, Y., Lambert, M. P., Klein, W. L., Link, C. D., & Luo, Y. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.3448-06.2006 · Cited by 418
Forecasting the prevalence of preclinical and clinical Alzheimer's disease in the United States
Brookmeyer, R., Abdalla, N., Kawas, C. H., & Corrada, M. M. (2018) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2017.10.009 · Cited by 406
Kowalewski, T., & Holtzman, D. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.7.3688 · Cited by 406
Green, K. N., Steffan, J. S., Martinez-Coria, H., Sun, X., Schreiber, S. S., Thompson, L. M., & LaFerla, F. M. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.3203-08.2008 · Cited by 404
Therapeutic potential of mood stabilizers lithium and valproic acid:Beyond bipolar disorder
Chiu, C.-T., Wang, Z., Hunsberger, J. G., & Chuang, D.-M. (2013) · Pharmacological Reviews · doi:10.1124/pr.111.005512 · Cited by 404
Natural products as a source of Alzheimer's drug leads
Williams, P., Sorribas, A., & Howes, M.-J. R. (2011) · Nat. Prod. Rep. · doi:10.1039/c0np00027b · Cited by 404
Altered Lipid Metabolism in Brain Injury and Disorders
Rao, A. M., & Hatcher, J. F. (2008) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-1-4020-8831-5_9 · Cited by 413
Pathological mechanisms and therapeutic strategies for Alzheimer’s disease
Tam, K. Y., & Ju, Y. (2021) · Neural Regeneration Research · doi:10.4103/1673-5374.320970 · Cited by 422
Palop, J. J., Jones, B., Kekonius, L., Chin, J., Yu, G.-Q., Raber, J., Masliah, E., & Mucke, L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1133381100 · Cited by 402
Majumder, S., Richardson, A., Strong, R., & Oddo, S. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025416 · Cited by 365
The two faces of protein misfolding: gain‐ and loss‐of‐function in neurodegenerative diseases
Winklhofer, K. F., Tatzelt, J., & Haass, C. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601930 · Cited by 410
Liu, Y., Ying, Y., Li, Y., Eyo, U. B., Chen, T., Zheng, J., Umpierre, A. D., Zhu, J., Bosco, D. B., Dong, H., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-019-0511-3 · Cited by 401
Altered Insulin Signaling in Alzheimer’s Disease Brain – Special Emphasis on PI3K-Akt Pathway
Gabbouj, S., Ryhänen, S., Marttinen, M., Wittrahm, R., Takalo, M., Kemppainen, S., Martiskainen, H., Tanila, H., Haapasalo, A., Hiltunen, M., et al. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00629 · Cited by 401
Targa Dias Anastacio, H., Matosin, N., & Ooi, L. (2022) · Translational Psychiatry · doi:10.1038/s41398-022-02024-7 · Cited by 401
Allele-specific silencing of dominant disease genes
Miller, V. M., Xia, H., Marrs, G. L., Gouvion, C. M., Lee, G. S., Davidson, B. L., & Paulson, H. L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1231012100 · Cited by 402
Wang, C., Ward, M. E., Chen, R., Liu, K., Tracy, T. E., Chen, X., Xie, M., Sohn, P. D., Ludwig, C., Meyer-Franke, A., et al. (2017) · Stem Cell Reports · doi:10.1016/j.stemcr.2017.08.019 · Cited by 400
Casas, C., Sergeant, N., Itier, J.-M., Blanchard, V., Wirths, O., van der Kolk, N., Vingtdeux, V., van de Steeg, E., Ret, G., Canton, T., et al. (2004) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)63388-3 · Cited by 400
Caricasole, A., Copani, A., Caraci, F., Aronica, E., Rozemüller, A. J. M., Caruso, A., Storto, M., Gaviraghi, G., Terstappen, G. C., & Nicoletti, F. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.1381-04.2004 · Cited by 398
η-Secretase processing of APP inhibits neuronal activity in the hippocampus
Willem, M., Tahirovic, S., Busche, M. A., Ovsepian, S. V., Chafai, M., Kootar, S., Hornburg, D., Evans, L. D. B., Moore, S., Daria, A., et al. (2015) · Nature · doi:10.1038/nature14864 · Cited by 398
Decreased synaptic proteins in neuronal exosomes of frontotemporal dementia and Alzheimer's disease
Goetzl, E. J., Kapogiannis, D., Schwartz, J. B., Lobach, I. V., Goetzl, L., Abner, E. L., Jicha, G. A., Karydas, A. M., Boxer, A., & Miller, B. L. (2016) · The FASEB Journal · doi:10.1096/fj.201600816r · Cited by 398
Hamaguchi, T., Ono, K., Murase, A., & Yamada, M. (2009) · American Journal Of Pathology · doi:10.2353/ajpath.2009.090417 · Cited by 403
Diversity in NMDA Receptor Composition
Sanz-Clemente, A., Nicoll, R. A., & Roche, K. W. (2012) · The Neuroscientist · doi:10.1177/1073858411435129 · Cited by 424
Integrated multimodal cell atlas of Alzheimer’s disease
Gabitto, M. I., Travaglini, K. J., Rachleff, V. M., Kaplan, E. S., Long, B., Ariza, J., Ding, Y., Mahoney, J. T., Dee, N., Goldy, J., et al. (2024) · Nature Neuroscience · doi:10.1038/s41593-024-01774-5 · Cited by 397
Schindowski, K., Bretteville, A., Leroy, K., Bégard, S., Brion, J., Hamdane, M., & Buée, L. (2006) · American Journal Of Pathology · doi:10.2353/ajpath.2006.060002 · Cited by 438
Varnum, M. M., & Ikezu, T. (2012) · Archivum Immunologiae et Therapiae Experimentalis · doi:10.1007/s00005-012-0181-2 · Cited by 412
Ontogeny and homeostasis of CNS myeloid cells
Prinz, M., Erny, D., & Hagemeyer, N. (2017) · Nature Immunology · doi:10.1038/ni.3703 · Cited by 413
Expression profiles for macrophage alternative activation genes in AD and in mouse models of AD.
(2006) · Journal of Neuroinflammation · doi:10.1186/1742-2094-3-27 · Cited by 393
The role of microbial amyloid in neurodegeneration
Friedland, R. P., & Chapman, M. R. (2017) · PLoS Pathogens · doi:10.1371/journal.ppat.1006654 · Cited by 398
Microglial Activation in Stroke: Therapeutic Targets
Yenari, M. A., Kauppinen, T. M., & Swanson, R. A. (2010) · Neurotherapeutics · doi:10.1016/j.nurt.2010.07.005 · Cited by 398
He, P., Zhong, Z., Lindholm, K., Berning, L., Lee, W., Lemere, C., Staufenbiel, M., Li, R., & Shen, Y. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200705042 · Cited by 390
The role of cerebral amyloid accumulation in common forms of Alzheimer disease
Gandy, S. (2005) · Journal of Clinical Investigation · doi:10.1172/jci25100 · Cited by 407
Epigenetic mechanisms in neurogenesis
Yao, B., Christian, K. M., He, C., Jin, P., Ming, G., & Song, H. (2016) · Nature reviews. Neuroscience · doi:10.1038/nrn.2016.70 · Cited by 406
Wilcock, D. M., Rojiani, A. M., Rosenthal, A., Subbarao, S., Freeman, M. J., Gordon, M. N., & Morgan, D. (2004) · Journal of Neuroinflammation · doi:10.1186/1742-2094-1-24 · Cited by 392
Self-citationSynaptopathies: synaptic dysfunction in neurological disorders – A review from students to students
Lepeta, K., Lourenco, M. V., Schweitzer, B. C., Martino Adami, P. V., Banerjee, P., Catuara‐Solarz, S., de La Fuente Revenga, M., Guillem, A. M., Haidar, M., Ijomone, O. M., et al. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13713 · Cited by 386
The epigenetics of aging and neurodegeneration
Lardenoije, R., Iatrou, A., Kenis, G., Kompotis, K., Steinbusch, H. W. M., Mastroeni, D., Coleman, P., Lemere, C. A., Hof, P. R., van den Hove, D. L. A., et al. (2015) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.05.002 · Cited by 381
Do glia drive synaptic and cognitive impairment in disease?
Chung, W.-S., Welsh, C. A., Barres, B. A., & Stevens, B. (2015) · Nature Neuroscience · doi:10.1038/nn.4142 · Cited by 385
Spittaels, K., den Haute, C. V., Dorpe, J. V., Bruynseels, K., Vandezande, K., Laenen, I., Geerts, H., Mercken, M. H., Sciot, R., Lommel, A. V., et al. (1999) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)65533-2 · Cited by 390
Aβ inhibits the proteasome and enhances amyloid and tau accumulation
Tseng, B. P., Green, K. N., Chan, J. L., Blurton-Jones, M., & LaFerla, F. M. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.04.014 · Cited by 384
What is the evidence that tau pathology spreads through prion-like propagation?
Mudher, A., Colin, M., Dujardin, S., Medina, M., Dewachter, I., Alavi Naini, S. M., Mandelkow, E.-M., Mandelkow, E., Buée, L., Goedert, M., et al. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0488-7 · Cited by 384
Phosphorylation of different tau sites during progression of Alzheimer’s disease
Neddens, J., Temmel, M., Flunkert, S., Kerschbaumer, B., Hoeller, C., Loeffler, T., Niederkofler, V., Daum, G., Attems, J., & Hutter-Paier, B. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0557-6 · Cited by 384
Neuropathology of Alzheimer's Disease
Trejo‐Lopez, J. A., Yachnis, A. T., & Prokop, S. (2021) · Neurotherapeutics · doi:10.1007/s13311-021-01146-y · Cited by 419
Jimenez, S., Baglietto-Vargas, D., Caballero, C., Moreno-Gonzalez, I., Torres, M., Sanchez-Varo, R., Ruano, D., Vizuete, M., Gutierrez, A., & Vitorica, J. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.3024-08.2008 · Cited by 383
Frontotemporal dementia and its subtypes: a genome-wide association study
Ferrari, R., Hernandez, D. G., Nalls, M. A., Rohrer, J. D., Ramasamy, A., Kwok, J. B. J., Dobson-Stone, C., Brooks, W. S., Schofield, P. R., Halliday, G. M., et al. (2014) · The Lancet Neurology · doi:10.1016/s1474-4422(14)70065-1 · Cited by 383
GWAS of Cerebrospinal Fluid Tau Levels Identifies Risk Variants for Alzheimer’s Disease
Cruchaga, C., Kauwe, J. S. K., Harari, O., Jin, S. C., Cai, Y., Karch, C. M., Benitez, B. A., Jeng, A. T., Skorupa, T., Carrell, D., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.02.026 · Cited by 383
Anti-Aβ Therapeutics in Alzheimer's Disease: The Need for a Paradigm Shift
Golde, T. E., Schneider, L. S., & Koo, E. H. (2011) · Neuron · doi:10.1016/j.neuron.2011.01.002 · Cited by 382
Kotler, S. A., Walsh, P. J., Brender, J., & Ramamoorthy, A. (2014) · Chemical Society Reviews · doi:10.1039/c3cs60431d · Cited by 384
Directed differentiation of human pluripotent stem cells to microglia
Douvaras, P., Sun, B., Wang, M., Kruglikov, I., Lallos, G., Zimmer, M., Terrenoire, C., Zhang, B., Gandy, S., Schadt, E., et al. (2017) · Stem Cell Reports · doi:10.1016/j.stemcr.2017.04.023 · Cited by 381
Matrix Metalloproteinases Expressed by Astrocytes Mediate Extracellular Amyloid-β Peptide Catabolism
Yin, K.-J., Cirrito, J. R., Yan, P., Hu, X., Xiao, Q., Pan, X., Bateman, R., Song, H., Hsu, F.-F., Turk, J., et al. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.2085-06.2006 · Cited by 381
The Amyloid Cascade Hypothesis in Alzheimer’s Disease: It’s Time to Change Our Mind
Ricciarelli, R., & Fedele, E. (2017) · Current Neuropharmacology · doi:10.2174/1570159x15666170116143743 · Cited by 380
Liu, Y., Zhou, L., Jun, W., Li, D., Ren, W.-J., Peng, J., Xiao, W., Xu, T., Xin, W., Pang, R., et al. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.2235-16.2016 · Cited by 391
Treusch, S., Hamamichi, S., Goodman, J. L., Matlack, K. E. S., Chung, C. Y., Baru, V., Shulman, J. M., Parrado, A., Bevis, B. J., Valastyan, J. S., et al. (2011) · Science · doi:10.1126/science.1213210 · Cited by 379
Neurodegeneration and defective neurotransmission in a Caenorhabditis elegans model of tauopathy
Kraemer, B. C., Zhang, B., Leverenz, J. B., Thomas, J. H., Trojanowski, J. Q., & Schellenberg, G. D. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1533448100 · Cited by 379
Jordão, J. F., Ayala‐Grosso, C. A., Markham, K. A., Huang, Y., Chopra, R., McLaurin, J., Hynynen, K., & Aubert, I. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010549 · Cited by 390
Monzio Compagnoni, G., Di Fonzo, A., Corti, S., Comi, G. P., Bresolin, N., & Masliah, E. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-01926-1 · Cited by 378
CircRNAs: role in human diseases and potential use as biomarkers
Verduci, L., Tarcitano, E., Strano, S., Yarden, Y., & Blandino, G. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03743-3 · Cited by 382
Alzheimer's Disease and the Amyloid Cascade Hypothesis: A Critical Review
Reitz, C. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/369808 · Cited by 398
Amyloid-β and tau complexity — towards improved biomarkers and targeted therapies
Polanco, J. C., Li, C., Bodea, L., Martínez‐Mármol, R., Meunier, F. A., & Götz, J. (2017) · Nature Reviews Neurology · doi:10.1038/nrneurol.2017.162 · Cited by 386
Dickerson, B. C., & Sperling, R. A. (2007) · Neuropsychologia · doi:10.1016/j.neuropsychologia.2007.11.030 · Cited by 389
Glial response during cuprizone-induced de- and remyelination in the CNS: lessons learned
Gudi, V., Gingele, S., Skripuletz, T., & Stangel, M. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00073 · Cited by 375
Goedert, M., Jakes, R., Crowther, R. A., Cohen, P., Vanmechelen, E., Vandermeeren, M., & Cras, P. (1994) · Biochemical Journal · doi:10.1042/bj3010871 · Cited by 375
May, P. C., Dean, R. A., Lowe, S. L., Martenyi, F., Sheehan, S. M., Boggs, L. N., Monk, S. A., Mathes, B. M., Mergott, D. J., Watson, B. M., et al. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.3647-11.2011 · Cited by 336
How Can Hearing Loss Cause Dementia?
Griffiths, T. D., Lad, M., Kumar, S., Holmes, E., McMurray, B., Maguire, E. A., Billig, A. J., & Sedley, W. (2020) · Neuron · doi:10.1016/j.neuron.2020.08.003 · Cited by 389
Narasimhan, S., Guo, J. L., Changolkar, L., Stieber, A., McBride, J. D., Silva, L. V., He, Z., Zhang, B., Gathagan, R. J., Trojanowski, J. Q., et al. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.1230-17.2017 · Cited by 374
The complexity of tau in Alzheimer’s disease
Naseri, N. N., Wang, H., Guo, J. D., Sharma, M., & Luo, W. (2019) · Neuroscience Letters · doi:10.1016/j.neulet.2019.04.022 · Cited by 393
Buckley, R. F., Mormino, E. C., Rabin, J. S., Hohman, T. J., Landau, S., Hanseeuw, B. J., Jacobs, H. I. L., Papp, K. V., Amariglio, R. E., Properzi, M. J., et al. (2019) · JAMA Neurology · doi:10.1001/jamaneurol.2018.4693 · Cited by 373
Ferreira, S. T., Lourenco, M. V., Oliveira, M. M., & De Felice, F. G. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00191 · Cited by 373
Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease
Gouras, G. K., Tampellini, D., Takahashi, R. H., & Capetillo-Zarate, E. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0679-9 · Cited by 372
Updated TDP-43 in Alzheimer’s disease staging scheme
Josephs, K. A., Murray, M. E., Whitwell, J. L., Tosakulwong, N., Weigand, S. D., Petrucelli, L., Liesinger, A. M., Petersen, R. C., Parisi, J. E., & Dickson, D. W. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1537-1 · Cited by 382
An Overview of the Role of Lipofuscin in Age-Related Neurodegeneration
Moreno-García, A., Kun, A., Calero, O., Medina, M., & Calero, M. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00464 · Cited by 372
Takeda, S., Wegmann, S., Cho, H., DeVos, S. L., Commins, C., Roe, A. D., Nicholls, S. B., Carlson, G. A., Pitstick, R., Nobuhara, C. K., et al. (2015) · Nature Communications · doi:10.1038/ncomms9490 · Cited by 371
Tau-targeting therapies for Alzheimer disease: Current status and future directions
Congdon, E. E., Ji, C., Tetlow, A. M., Jiang, Y., & Sigurdsson, E. M. (2023) · Nature Reviews Neurology · doi:10.1038/s41582-023-00883-2 · Cited by 371
Apolipoprotein E, Receptors, and Modulation of Alzheimer’s Disease
Zhao, N., Liu, C.-C., Qiao, W., & Bu, G. (2018) · Biological Psychiatry · doi:10.1016/j.biopsych.2017.03.003 · Cited by 370
Young-Pearse, T. L., Bai, J., Chang, R., Zheng, J. B., LoTurco, J. J., & Selkoe, D. J. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4701-07.2007 · Cited by 369
Phospholipase A2 reduction ameliorates cognitive deficits in a mouse model of Alzheimer's disease
Sanchez-Mejia, R. O., Newman, J. W. I., Toh, S., Yu, G.-Q., Zhou, Y., Halabisky, B., Cissé, M., Scearce-Levie, K. A., Cheng, I. H.-J., Gan, L., et al. (2008) · Nature Neuroscience · doi:10.1038/nn.2213 · Cited by 362
Selective clearance of aberrant tau proteins and rescue of neurotoxicity by transcription factor EB
Polito, V. A., Li, H., Martini‐Stoica, H., Wang, B., Li, Y., Xu, Y., Swartzlander, D. B., Palmieri, M., di Ronza, A., Lee, V. M. ‐., et al. (2014) · EMBO Molecular Medicine · doi:10.15252/emmm.201303671 · Cited by 356
Alquezar, C., Arya, S., & Kao, A. W. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2020.595532 · Cited by 367
Microglia: Architects of the Developing Nervous System
Frost, J. L., & Schafer, D. P. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.02.006 · Cited by 385
Locus coeruleus imaging as a biomarker for noradrenergic dysfunction in neurodegenerative diseases
Betts, M. J., Kirilina, E. P., Otaduy, M. C. G., Ivanov, D., Acosta‐Cabronero, J., Callaghan, M. F., Lambert, C., Cárdenas‐Blanco, A., Pine, K., Passamonti, L., et al. (2019) · Brain · doi:10.1093/brain/awz193 · Cited by 367
Astrocyte Heterogeneity: Impact to Brain Aging and Disease
Matias, I., Morgado, J., & Gomes, F. C. A. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00059 · Cited by 387
Garay, P. A., Hsiao, E. Y., Patterson, P. H., & McAllister, A. K. (2013) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2012.07.008 · Cited by 366
Zhao, J., Fu, Y., Yasvoina, M., Shao, P., Hitt, B., O'Connor, T., Logan, S., Maus, E., Citron, M., Berry, R., et al. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4396-06.2007 · Cited by 365
Microglia: Agents of the CNS Pro-Inflammatory Response
Rodríguez-Gómez, J. A., Kavanagh, E., Engskog-Vlachos, P., Engskog, M. K. R., Herrera, A. J., Espinosa-Oliva, A. M., Joseph, B., Hajji, N., Venero, J. L., & Burguillos, M. A. (2020) · Cells · doi:10.3390/cells9071717 · Cited by 365
Kawarabayashi, T., Shoji, M., Younkin, L. H., Wen-Lang, L., Dickson, D. W., Murakami, T., Matsubara, E., Abe, K., Ashe, K. H., & Younkin, S. G. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.5543-03.2004 · Cited by 320
Glucose Transporters at the Blood-Brain Barrier: Function, Regulation and Gateways for Drug Delivery
Patching, S. G. (2016) · Molecular Neurobiology · doi:10.1007/s12035-015-9672-6 · Cited by 376
Luo, R., Su, L.-Y., Li, G., Yang, J., Liu, Q., Yang, L.-X., Zhang, D.-F., Zhou, H., Xu, M., Fan, Y., et al. (2020) · Autophagy · doi:10.1080/15548627.2019.1596488 · Cited by 364
Interactions between β-amyloid and central cholinergic neurons: implications for Alzheimer’s disease
Kar, S., Slowikowski, S. P. M., Westaway, D. A., & Mount, H. T. J. (2004) · Journal of Psychiatry and Neuroscience · doi:10.1139/jpn.0442 · Cited by 366
Mitochondrial Oxidative Stress Causes Hyperphosphorylation of Tau
Melov, S., Adlard, P. A., Morten, K., Johnson, F., Golden, T. R., Hinerfeld, D., Schilling, B., Mavros, C., Masters, C. L., Volitakis, I., et al. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000536 · Cited by 363
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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