Amyloid-β/Fyn–Induced Synaptic, Network, and Cognitive Impairments Depend on Tau Levels in Multiple Mouse Models of Alzheimer's Disease
Open accessAbstract
Alzheimer's disease (AD), the most common neurodegenerative disorder, is a growing public health problem and still lacks effective treatments. Recent evidence suggests that microtubule-associated protein tau may mediate amyloid-β peptide (Aβ) toxicity by modulating the tyrosine kinase Fyn. We showed previously that tau reduction prevents, and Fyn overexpression exacerbates, cognitive deficits in human amyloid precursor protein (hAPP) transgenic mice overexpressing Aβ. However, the mechanisms by which Aβ, tau, and Fyn cooperate in AD-related pathogenesis remain to be fully elucidated. Here we examined the synaptic and network effects of this pathogenic triad. Tau reduction prevented cognitive decline induced by synergistic effects of Aβ and Fyn. Tau reduction also prevented synaptic transmission and plasticity deficits in hAPP mice. Using electroencephalography to examine network effects, we found that tau reduction prevented spontaneous epileptiform activity in multiple lines of hAPP mice. Tau reduction also reduced the severity of spontaneous and chemically induced seizures in mice overexpressing both Aβ and Fyn. To better understand these protective effects, we recorded whole-cell currents in acute hippocampal slices from hAPP mice with and without tau. hAPP mice with tau had increased spontaneous and evoked excitatory currents, reduced inhibitory currents, and NMDA receptor dysfunction. Tau reduction increased inhibitory currents and normalized excitation/inhibition balance and NMDA receptor-mediated currents in hAPP mice. Our results indicate that Aβ, tau, and Fyn jointly impair synaptic and network function and suggest that disrupting the copathogenic relationship between these factors could be of therapeutic benefit.
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
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?
In AD models, absence of tau rescues behavioral impairments and reduces neurotoxicity despite no significant changes in Aβ levels.
“For example, in AD models, the absence of tau has been shown to rescue behavioral impairments and reduce neurotoxicity, despite no significant changes in Aβ levels [75–79].”
From Tau Ablation Rewires Brain Cell Programs in Health and Restores Function in Disease (2026) · cites this paper as [76]
The Results section on behavioral abnormalities reports that tau-absent hAPPJ9/Fyn mice performed better on learning and memory tests, and the Discussion section on synaptic effects reports that tau reduction corrected neuronal dysfunction in hAPPJ20 mice (page numbers unavailable). However, the passages do not establish that these benefits occurred without significant changes in Aβ levels, or demonstrate reduced neuronal death if “neurotoxicity” means cell death. (LLM, conf=0.83)
Experimental — accuracy not yet measuredOnce tau is eliminated, glia appear better able to mount context and disease-appropriate responses, including elimination of toxic species, reduction in kinase activation, and modulation of downstream signaling, potentially explaining the broad protective effects of tau ablation across pathological models.
“Once tau is eliminated, glia appear better able to mount context and disease-appropriate responses, including elimination of toxic species [144], reduction in kinase activation, and modulation of downstream signaling [76, 78, 145], potentially explaining the broad protective effects of tau ablation across pathological models.”
From Tau Ablation Rewires Brain Cell Programs in Health and Restores Function in Disease (2026) · cites this paper as [76]
Split into 2 atoms — 0 confirmed, 1 partially supported, 0 disputed, 0 misattributed, 1 unverifiable. Expand the claim to see per-atom verdicts.
Experimental — accuracy not yet measuredTau ablation confers neuronal protection resulting in the recovery of behavioral deficits in neurodegenerative and neurodevelopmental models.
“Numerous studies across neurodegenerative and neurodevelopmental models have shown that tau ablation confers neuronal protection resulting in the recovery of behavioral deficits [56, 75, 76, 121–123].”
From Tau Ablation Rewires Brain Cell Programs in Health and Restores Function in Disease (2026) · cites this paper as [76]
The Results section reports that tau ablation improved learning and memory performance in hAPPJ9/Fyn mice, supporting protection against behavioral deficits in an Alzheimer’s disease model. The Discussion limits the benefit to specific AD-related circumstances: it reports no benefit in an ALS model and adverse effects in a Niemann–Pick type C model. This paper does not establish the claim across neurodevelopmental models. (LLM, conf=0.88)
Experimental — accuracy not yet measuredTau-induced hyperexcitability exacerbates synaptic and cognitive decline in a model of amyloid toxicity.
“This aligns with evidence that tau-induced hyperexcitability exacerbates synaptic and cognitive decline in a model of amyloid toxicity56.”
From The R136S mutation in the APOE3 gene confers resilience against tau pathology via inhibition of the cGAS-STING-IFN pathway (2025) · cites this paper as [56]
The Abstract and Discussion report that tau reduction prevented synaptic deficits, epileptiform activity, and cognitive impairment in amyloid-β mouse models. The Discussion suggests aberrant network activity contributes to cognitive impairment, but it does not establish that tau-induced hyperexcitability itself exacerbates both synaptic and cognitive decline; tau is described as enabling effects of amyloid-β and Fyn. (LLM, conf=0.84)
Experimental — accuracy not yet measuredIn multiple mouse disease models, tau ablation is associated with protective effects.
“Interestingly, in multiple mouse disease models, tau ablation has been associated with protective effects.”
From Tau Ablation Rewires Brain Cell Programs in Health and Restores Function in Disease (2026) · cites this paper as [76]
Reducing tau levels prevents Aβ-induced cognitive deficits and premature mortality, reduces spontaneous and induced seizure activity, and prevents synaptic impairment in mutant APP-expressing mouse models.
“Reducing tau levels prevents Aβ-induced cognitive deficits and premature mortality, reduces spontaneous and induced seizure activity, and prevents synaptic impairment in mutant APP-expressing mouse models (Roberson et al., 2007, 2011).”
From Wild-Type, but Not Mutant N296H, Human Tau Restores Aβ-Mediated Inhibition of LTP in Tau−/− mice (2017) · cites this paper as Roberson et al., 2011
Some data suggest that Aβ toxicity is partially mediated through tau, as tau knockout mice are protected against Aβ-induced insults including cognitive effects, seizures, survival, axonal transport, and DNA double-stranded breaks.
“Some data suggest that Aβ toxicity is partially mediated through tau (50–52) as the tau knockout mouse has proven to be protected against a growing number of Aβ-induced insults, including those affecting cognition (50, 53), seizures (14, 50, 51, 54, 55), survival (50, 51, 54), axonal transport (52), and double-stranded breaks in DNA (55).”
From Tau reduction prevents neuronal loss and reverses pathological tau deposition and seeding in mice with tauopathy (2017) · cites this paper as [51]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
The 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 · see citing works
Modification of seizure activity by electrical stimulation: II. Motor seizure
Racine, R. J. (1972) · Electroencephalography and Clinical Neurophysiology · doi:10.1016/0013-4694(72)90177-0 · Cited by 7,141 · see citing works
Alzheimer's Disease Is a Synaptic Failure
Selkoe, D. J. (2002) · Science · doi:10.1126/science.1074069 · Cited by 4,420 · see citing works
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 · see citing works
Motor Neuron Degeneration in Mice that Express a Human Cu,Zn Superoxide Dismutase Mutation
Gurney, M. E., Pu, H., Chiu, A. Y., Dal Canto, M. C., Polchow, C. Y., Alexander, D. D., Caliendo, J., Hentati, A., Kwon, Y. W., Deng, H.-X., et al. (1994) · Science · doi:10.1126/science.8209258 · Cited by 4,143 · see citing works
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 · see citing works
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 · see citing works
Reducing Endogenous Tau Ameliorates Amyloid ß-Induced Deficits in an Alzheimer's Disease Mouse Model
Roberson, E. D., Scearce-Levie, K., Palop, J. J., Yan, F., Cheng, I. H., Wu, T., Gerstein, H., Yu, G.-Q., & Mucke, L. (2007) · Science · doi:10.1126/science.1141736 · Cited by 1,892 · see citing works
Self-citationMucke, 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 · see citing works
Self-citationTwenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective
Tanzi, R. E., & Bertram, L. (2005) · Cell · doi:10.1016/j.cell.2005.02.008 · Cited by 1,849 · see citing works
Dendritic Function of Tau Mediates Amyloid-β Toxicity in Alzheimer's Disease Mouse Models
Ittner, L. M., Ke, Y. D., Delerue, F., Bi, M., Gladbach, A., van Eersel, J., Wölfing, H., Chieng, B. C., Christie, M. J., Napier, I. A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.06.036 · Cited by 1,821 · see citing works
Palop, J. J., Chin, J., Roberson, E. D., Wang, J., Thwin, M. T., Bien-Ly, N., Yoo, J., Ho, K. O., Yu, G.-Q., Kreitzer, A., et al. (2007) · Neuron · doi:10.1016/j.neuron.2007.07.025 · Cited by 1,653 · see citing works
Self-citationAmyloid-β–induced neuronal dysfunction in Alzheimer's disease: from synapses toward neural networks
Palop, J. J., & Mucke, L. (2010) · Nature Neuroscience · doi:10.1038/nn.2583 · Cited by 1,651 · see citing works
Self-citationAPP Processing and Synaptic Function
Kamenetz, F., Tomita, T., Hsieh, H., Seabrook, G., Borchelt, D., Iwatsubo, T., Sisodia, S., & Malinow, R. (2003) · Neuron · doi:10.1016/s0896-6273(03)00124-7 · Cited by 1,644 · see citing works
Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP
Lewis, J., Dickson, D. W., Lin, W.-L., Chisholm, L., Corral, A., Jones, G., Yen, S.-H., Sahara, N., Skipper, L., Yager, D., et al. (2001) · Science · doi:10.1126/science.1058189 · Cited by 1,611 · see citing works
Shankar, G. M., Bloodgood, B. L., Townsend, M., Walsh, D. M., Selkoe, D. J., & Sabatini, B. L. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4970-06.2007 · Cited by 1,592 · see citing works
Formation of Neurofibrillary Tangles in P301L Tau Transgenic Mice Induced by Aβ42 Fibrils
Götz, J., Chen, F., van Dorpe, J., & Nitsch, R. M. (2001) · Science · doi:10.1126/science.1062097 · Cited by 1,526 · see citing works
Clinical effects of Aβ immunization (AN1792) in patients with AD in an interrupted trial
Gilman, S., Koller, M., Black, R. S., Jenkins, L., Griffith, S. G., Fox, N. C., Eisner, L., Kirby, L., Rovira, M. B., Forette, F., et al. (2005) · Neurology · doi:10.1212/01.wnl.0000159740.16984.3c · Cited by 1,329 · see citing works
The GSK3 hypothesis of Alzheimer’s disease
Hooper, C., Killick, R., & Lovestone, S. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.05194.x · Cited by 1,191 · see citing works
Clusters of Hyperactive Neurons Near Amyloid Plaques in a Mouse Model of Alzheimer’s Disease
Busche, M. A., Eichhoff, G., Adelsberger, H., Abramowski, D., Wiederhold, K.-H., Haass, C., Staufenbiel, M., Konnerth, A., & Garaschuk, O. (2008) · Science · doi:10.1126/science.1162844 · Cited by 1,125 · see citing works
Plaque-independent disruption of neural circuits in Alzheimer’s disease mouse models
Hsia, A. Y., Masliah, E., McConlogue, L., Yu, G.-Q., Tatsuno, G., Hu, K., Kholodenko, D., Malenka, R. C., Nicoll, R. A., & Mucke, L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.3228 · Cited by 1,123 · see citing works
Self-citationLi, S., Hong, S., Shepardson, N. E., Walsh, D. M., Shankar, G. M., & Selkoe, D. (2009) · Neuron · doi:10.1016/j.neuron.2009.05.012 · Cited by 972 · see citing works
Impaired synaptic plasticity and learning in aged amyloid precursor protein transgenic mice
Chapman, P. F., White, G. L., Jones, M. W., Cooper-Blacketer, D., Marshall, V. J., Irizarry, M., Younkin, L., Good, M. A., Bliss, T. V. P., Hyman, B. T., et al. (1999) · Nature Neuroscience · doi:10.1038/6374 · Cited by 946 · see citing works
Tau is essential to β-amyloid-induced neurotoxicity
Rapoport, M., Dawson, H. N., Binder, L. I., Vitek, M. P., & Ferreira, A. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.092136199 · Cited by 807 · see citing works
Src kinases: a hub for NMDA receptor regulation
Salter, M. W., & Kalia, L. V. (2004) · Nature reviews. Neuroscience · doi:10.1038/nrn1368 · Cited by 777 · see citing works
Epilepsy and Cognitive Impairments in Alzheimer Disease
Palop, J. J. (2009) · Archives of Neurology · doi:10.1001/archneurol.2009.15 · Cited by 684 · see citing works
Self-citationMoechars, D., Dewachter, I., Lorent, K., Reversé, D., Baekelandt, V., Naidu, A., Tesseur, I., Spittaels, K., Haute, C. V. D., Checler, F., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.10.6483 · Cited by 668 · see citing works
Amyloid β-Induced Neuronal Hyperexcitability Triggers Progressive Epilepsy
Minkeviciene, R., Rheims, S., Dobszay, M. B., Zilberter, M. Y., Hartikainen, J., Fülöp, L., Penke, B., Zilberter, Y., Harkany, T., Pitkänen, A., et al. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.5215-08.2009 · Cited by 656 · see citing works
Inhibition of neuronal maturation in primary hippocampal neurons from tau deficient mice
Dawson, H. N., Ferreira, A., Eyster, M. V., Ghoshal, N., Binder, L. I., & Vitek, M. P. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.6.1179 · Cited by 527 · see citing works
Neurotrophins are required for nerve growth during development
Tucker, K. L., Meyer, M., & Barde, Y. (2001) · Nature Neuroscience · doi:10.1038/82868 · Cited by 526 · see citing works
Hsiao, K., Borchelt, D., Olson, K., Johannsdottir, R., Kitt, C. A., Yunis, W. S., Xu, S., Eckman, C., Younkin, S. G., Price, D., et al. (1995) · Neuron · doi:10.1016/0896-6273(95)90107-8 · Cited by 519 · see citing works
The Alzheimer's Aβ peptide induces neurodegeneration and apoptotic cell death in transgenic mice
LaFerla, F. M., Tinkle, B. T., Bieberich, C. J., Haudenschild, C. C., & Jay, G. (1995) · Nature Genetics · doi:10.1038/ng0195-21 · Cited by 513 · see citing works
Tau Reduction Prevents Aβ-Induced Defects in Axonal Transport
Vossel, K. A., Zhang, K., Brodbeck, J., Daub, A. C., Sharma, P., Finkbeiner, S., Cui, B., & Mucke, L. (2010) · Science · doi:10.1126/science.1194653 · Cited by 486 · see citing works
Self-citationNeuropeptide Y: emerging evidence for a functional role in seizure modulation
Vezzani, A., Sperk, G., & Colmers, W. F. (1999) · Trends in Neurosciences · doi:10.1016/s0166-2236(98)01284-3 · Cited by 469 · see citing works
Tau interacts with src-family non-receptor tyrosine kinases
Lee, G. S., Newman, S. T., Gard, D. L., Band, H., & Panchamoorthy, G. (1998) · Journal of Cell Science · doi:10.1242/jcs.111.21.3167 · Cited by 445 · see citing works
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 414 · see citing works
Mechanisms of neocortical epileptogenesis in vitro
Gutnick, M. J., Connors, B. W., & Prince, D. A. (1982) · Journal of Neurophysiology · doi:10.1152/jn.1982.48.6.1321 · Cited by 403 · see citing works
Löscher, W., Hönack, D., Fassbender, C. P., & Nolting, B. (1991) · Epilepsy Research · doi:10.1016/0920-1211(91)90062-k · Cited by 403 · see citing works
Chin, J., Palop, J. J., Puoliväli, J., Massaro, C., Bien-Ly, N., Gerstein, H., Scearce-Levie, K., Masliah, E., & Mucke, L. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.2980-05.2005 · Cited by 312 · see citing works
Self-citationThe dentate gyrus as a regulated gate for the propagation of epileptiform activity.
Heinemann, U., Beck, H., Dreier, J. P., et al. (1992) · PubMed · Cited by 290 · see citing works
Frontotemporal dementia progresses to death faster than Alzheimer disease
Roberson, E. D., Hesse, J., Rose, K. D., Slama, H., Johnson, J. K., Yaffe, K. S., Forman, M. S., Miller, C. A., Trojanowski, J. Q., Kramer, J. H., et al. (2005) · Neurology · doi:10.1212/01.wnl.0000173837.82820.9f · Cited by 290 · see citing works
Self-citationSurvival of Outpatients with Alzheimer-type Dementia
Walsh, J. S. A., Welch, H. G., & Larson, E. B. (1990) · Annals of Internal Medicine · doi:10.7326/0003-4819-113-6-429 · Cited by 267 · see citing works
Korn, S. J., Giacchino, J. L., Chamberlin, N. L., & Dingledine, R. J. (1987) · Journal of Neurophysiology · doi:10.1152/jn.1987.57.1.325 · Cited by 266 · see citing works
Park, S.-Y., & Ferreira, A. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.1125-05.2005 · Cited by 262 · see citing works
The dentate gyrus as a control point for seizures in the hippocampus and beyond.
Lothman, E. W., Stringer, J. L., & Bertram, E. H. (1992) · PubMed · Cited by 240 · see citing works
Williamson, T. L., Bruijn, L. I., Zhu, Q., Anderson, K. L., Anderson, S., Julien, J., & Cleveland, D. W. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.16.9631 · Cited by 238 · see citing works
Sun, B., Zhou, Y., Halabisky, B., Lo, I., Cho, S.-H., Mueller-Steiner, S., Devidze, N., Wang, X., Grubb, A., & Gan, L. (2008) · Neuron · doi:10.1016/j.neuron.2008.10.001 · Cited by 231 · see citing works
Self-citationWilliamson, R., Scales, T., Clark, B. R., Gibb, G., Reynolds, C. H., Kellie, S., Bird, I. N., Varndell, I. M., Sheppard, P. W., Everall, I., et al. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-01-00010.2002 · Cited by 227 · see citing works
Rockenstein, E. M., Mallory, M. E., Mante, M., Sisk, A., & Masliaha, E. (2001) · Journal of Neuroscience Research · doi:10.1002/jnr.1247 · Cited by 224 · see citing works
Tau-dependent microtubule disassembly initiated by prefibrillar β-amyloid
King, M. E., Kan, H.-M., Baas, P. W., Erişir, A., Glabe, C. G., & Bloom, G. S. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200605187 · Cited by 215 · see citing works
Axonal Transport RatesIn VivoAre Unaffected by Tau Deletion or Overexpression in Mice
Yuan, A., Kumar, A. R., Peterhoff, C. M., Duff, K., & Nixon, R. A. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.5242-07.2008 · Cited by 190 · see citing works
McKhann, G. M., Wenzel, H. J., Robbins, C. A., Sosunov, A. A., & Schwartzkroin, P. A. (2003) · Neuroscience · doi:10.1016/s0306-4522(03)00562-1 · Cited by 189 · see citing works
Rescuing impairment of long-term potentiation in fyn-deficient mice by introducing Fyn transgene
Kojima, N., Wang, J., Mansuy, I. M., Grant, S. G. N., Mayford, M. R., & Kandel, E. R. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.9.4761 · Cited by 188 · see citing works
Chin, J., Palop, J. J., Yu, G.-Q., Kojima, N., Masliah, E., & Mucke, L. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.0277-04.2004 · Cited by 161 · see citing works
Self-citationCarlson, G. A., Borchelt, D. R., Dake, A., Turner, S., Danielson, V., Coffin, J. D., Eckman, C., Meiners, J., Nilsen, S. P., Younkin, S. G., et al. (1997) · Human Molecular Genetics · doi:10.1093/hmg/6.11.1951 · Cited by 158 · see citing works
Loss of Neprilysin Function Promotes Amyloid Plaque Formation and Causes Cerebral Amyloid Angiopathy
Farris, W., Schütz, S. G., Cirrito, J. R., Shankar, G. M., Sun, X., George, A., Leissring, M. A., Walsh, D. M., Qiu, W. Q., Holtzman, D. M., et al. (2007) · American Journal Of Pathology · doi:10.2353/ajpath.2007.070105 · Cited by 155 · see citing works
Harris, J. A., Devidze, N., Halabisky, B., Lo, I., Thwin, M. T., Yu, G.-Q., Bredesen, D. E., Masliah, E., & Mucke, L. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.5341-09.2010 · Cited by 146 · see citing works
Self-citationLoss of tau elicits axonal degeneration in a mouse model of Alzheimer's disease
Dawson, H. N., Cantillana, V., Jansen, M., Wang, H., Vitek, M. P., Wilcock, D. M., Lynch, J., & Laskowitz, D. T. (2010) · Neuroscience · doi:10.1016/j.neuroscience.2010.04.037 · Cited by 137 · see citing works
Neurobehavioral characterization of APP23 transgenic mice with the SHIRPA primary screen
Lalonde, R., Dumont, M., Staufenbiel, M., & Strazielle, C. (2004) · Behavioural Brain Research · doi:10.1016/j.bbr.2004.06.020 · Cited by 116 · see citing works
Vogt, D. L., Thomas, D., Galván, V., Bredesen, D. E., Lamb, B. T., & Pimplikar, S. W. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.09.002 · Cited by 113 · see citing works
Tau-knockout mice show reduced GSK3-induced hippocampal degeneration and learning deficits
de Barreda, E. G., Pérez, M., Gómez‐Ramos, P., de Cristóbal, J., Martín-Maestro, P., Morán, A., Dawson, H. N., Vitek, M. P., Lucas, J. J., Hernández, F., et al. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.11.017 · Cited by 112 · see citing works
Fyn-Tau-Amyloid: A Toxic Triad
Haass, C., & Mandelkow�, E. (2010) · Cell · doi:10.1016/j.cell.2010.07.032 · Cited by 106 · see citing works
Kumar‐Singh, S., Dewachter, I., Moechars, D., Lübke, U., Jonghe, C. D., Ceuterick, C., Checler, F., Naidu, A., Cordell, B., Cras, P. P., et al. (2000) · Neurobiology of Disease · doi:10.1006/nbdi.1999.0272 · Cited by 105 · see citing works
Palop, J. J., Mucke, L., & Roberson, E. D. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-744-0_17 · Cited by 104 · see citing works
Self-citationIncreased seizure threshold and severity in young transgenic CRND8 mice
Vecchio, R. A. D., Gold, L. H., Novick, S. J., Wong, G., & Hyde, L. A. (2004) · Neuroscience Letters · doi:10.1016/j.neulet.2004.05.107 · Cited by 103 · see citing works
Somatostatin Acts in CA1 and CA3 to Reduce Hippocampal Epileptiform Activity
Tallent, M. K., & Siggins, G. R. (1999) · Journal of Neurophysiology · doi:10.1152/jn.1999.81.4.1626 · Cited by 93 · see citing works
神経フィラメントの欠如は,家族性筋萎縮性側索硬化症関連スーパオキジドジスムターゼ1変異に対する運動ニューロンの選択的易損性を低下させ,疾患を遅らせる
Williamson, T. L., Bruijn, L. I., Zhu, Q., et al. (1998) · Cited by 92 · see citing works
Kojima, N., Ishibashi, H., Obata, K., et al. (1998) · Learning & Memory · doi:10.1101/lm.5.6.429 · Cited by 91 · see citing works
Liu, T., Perry, G. L., Chan, H. W., Verdile, G., Martins, R. N., Smith, M. A., & Atwood, C. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02196.x · Cited by 84 · see citing works
Pacheco, C. D., Elrick, M. J., & Lieberman, A. P. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn423 · Cited by 75 · see citing works
Fyn tyrosine kinase is required for normal amygdala kindling
Cain, D. P., Grant, S. G. N., Saucier, D. M., et al. (1995) · Epilepsy Research · doi:10.1016/0920-1211(95)00029-1 · Cited by 50 · see citing works
Differences in two mice strains on kainic acid-induced amygdalar seizures
Kasugai, M., 赤池, 浩., Imamura, S.-I., et al. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.04.067 · Cited by 29 · see citing works
Krezowski, J. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh210 · Cited by 23 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Amyloid 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 · see citing works
Karran, E., Mercken, M., & Strooper, B. D. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3505 · Cited by 2,188 · see citing works
Verret, L., Mann, E. O., Hang, G. B., Barth, A. M. I., Cobos, I., Ho, K., Devidze, N., Masliah, E., Kreitzer, A. C., Mody, I., et al. (2012) · Cell · doi:10.1016/j.cell.2012.02.046 · Cited by 1,216 · see citing works
Self-citationSynergy between amyloid-β and tau in Alzheimer’s disease
Busche, M. A., & Hyman, B. T. (2020) · Nature Neuroscience · doi:10.1038/s41593-020-0687-6 · Cited by 1,242 · see citing works
Tau pathology and neurodegeneration
Spillantini, M. G., & Goedert, M. (2013) · The Lancet Neurology · doi:10.1016/s1474-4422(13)70090-5 · Cited by 1,133 · see citing works
Roles of tau protein in health and disease
Guo, T., Noble, W., & Hanger, D. P. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1707-9 · Cited by 1,003 · see citing works
Network abnormalities and interneuron dysfunction in Alzheimer disease
Palop, J. J., & Mucke, L. (2016) · Nature reviews. Neuroscience · doi:10.1038/nrn.2016.141 · Cited by 1,022 · see citing works
Self-citationNeurotoxicity of Amyloid -Protein: Synaptic and Network Dysfunction
Mucke, L., & Selkoe, D. J. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006338 · Cited by 1,000 · see citing works
Self-citationBeyond weight loss: a review of the therapeutic uses of very-low-carbohydrate (ketogenic) diets
Paoli, A., Rubini, A., Volek, J. S., & Grimaldi, K. A. (2013) · European Journal of Clinical Nutrition · doi:10.1038/ejcn.2013.116 · Cited by 885 · see citing works
Morris, M., Maeda, S., Vossel, K., & Mucke, L. (2011) · Neuron · doi:10.1016/j.neuron.2011.04.009 · Cited by 899 · see citing works
Self-citationTau and neurodegenerative disease: the story so far
Iqbal, K., Liu, F., & Gong, C.-X. (2016) · Nature Reviews Neurology · doi:10.1038/nrneurol.2015.225 · Cited by 806 · see citing works
Apolipoprotein E and Apolipoprotein E Receptors: Normal Biology and Roles in Alzheimer Disease
Holtzman, D. M., Herz, J., & Bu, G. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006312 · Cited by 782 · see citing works
Interaction between Aβ and Tau in the Pathogenesis of Alzheimer’s Disease
Zhang, H., Wei, W., Zhao, M., Ma, L., Jiang, X., Pei, H., Cao, Y., & Li, H. (2021) · International Journal of Biological Sciences · doi:10.7150/ijbs.57078 · Cited by 689 · see citing works
Arendt, T., Stieler, J. T., & Holzer, M. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.08.018 · Cited by 609 · see citing works
Aβ induces astrocytic glutamate release, extrasynaptic NMDA receptor activation, and synaptic loss
Talantova, M., Sanz-Blasco, S., Zhang, X., Xia, P., Akhtar, M. W., Okamoto, S.-I., Dziewczapolski, G., Nakamura, T., Cao, G., Pratt, A. E., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1306832110 · Cited by 600 · see citing works
Epileptic activity in Alzheimer’s disease: Causes and clinical relevance
Vossel, K. A., Tartaglia, M. C., Nygaard, H. B., Zeman, A. Z., & Miller, B. L. (2017) · The Lancet Neurology · doi:10.1016/s1474-4422(17)30044-3 · Cited by 590 · see citing works
Um, J. W., Kaufman, A. C., Kostylev, M., Heiss, J. K., Stagi, M., Takahashi, H., Kerrisk, M. E., Vortmeyer, A., Wisniewski, T., Koleske, A. J., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.06.036 · Cited by 572 · see citing works
DeVos, S. L., Miller, R. L., Schoch, K. M., Holmes, B. B., Kebodeaux, C. S., Wegener, A. J., Chen, G., Shen, T., Tran, H., Nichols, B., et al. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aag0481 · Cited by 516 · see citing works
Suberbielle, E., Sanchez, P. E., Kravitz, A. V., Wang, X., Ho, K., Eilertson, K., Devidze, N., Kreitzer, A. C., & Mucke, L. (2013) · Nature Neuroscience · doi:10.1038/nn.3356 · Cited by 487 · see citing works
Self-citationMorris, M., Knudsen, G. M., Maeda, S., Trinidad, J. C., Ioanoviciu, A., Burlingame, A. L., & Mucke, L. (2015) · Nature Neuroscience · doi:10.1038/nn.4067 · Cited by 472 · see citing works
Self-citationWang, 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 · see citing works
Synapses and Alzheimer's Disease
Sheng, M., Sabatini, B. L., & Sudhof, T. C. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005777 · Cited by 436 · see citing works
Synaptopathies: 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 · see citing works
The clinical promise of biomarkers of synapse damage or loss in Alzheimer’s disease
the Synaptic Health Endpoints Working Group, Colom-Cadena, M., Spires-Jones, T., Zetterberg, H., Blennow, K., Caggiano, A., DeKosky, S. T., Fillit, H., Harrison, J. E., Schneider, L. S., et al. (2020) · Alzheimer's Research & Therapy · doi:10.1186/s13195-020-00588-4 · Cited by 328 · see citing works
Soluble Aβ oligomer production and toxicity
Larson, M. E., & Lesné, S. E. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07478.x · Cited by 356 · see citing works
Mairet-Coello, G., Courchet, J., Pieraut, S., Courchet, V., Maximov, A., & Polleux, F. (2013) · Neuron · doi:10.1016/j.neuron.2013.02.003 · Cited by 351 · see citing works
Yamada, K., Cirrito, J. R., Stewart, F. R., Jiang, H., Finn, M. B., Holmes, B. B., Binder, L. I., Mandelkow, E.-M., Diamond, M. I., Lee, V. M.-Y., et al. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.2569-11.2011 · Cited by 351 · see citing works
<scp>F</scp>yn inhibition rescues established memory and synapse loss in <scp>A</scp>lzheimer mice
Kaufman, A. C., Salazar, S. V., Haas, L. T., Yang, J., Kostylev, M. A., Jeng, A. T., Robinson, S. A., Gunther, E. C., van Dyck, C. H., Nygaard, H. B., et al. (2015) · Annals of Neurology · doi:10.1002/ana.24394 · Cited by 314 · see citing works
Šišková, Z., Justus, D., Kaneko, H., Friedrichs, D., Henneberg, N., Beutel, T., Pitsch, J., Schoch, S., Becker, A., von der Kammer, H., et al. (2014) · Neuron · doi:10.1016/j.neuron.2014.10.024 · Cited by 320 · see citing works
Antisense Reduction of Tau in Adult Mice Protects against Seizures
DeVos, S. L., Goncharoff, D. K., Chen, G., Kebodeaux, C. S., Yamada, K., Stewart, F. R., Schuler, D. R., Maloney, S. E., Wozniak, D. F., Rigo, F., et al. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.2107-13.2013 · Cited by 311 · see citing works
Dendritic Tau in Alzheimer’s Disease
Ittner, A., & Ittner, L. M. (2018) · Neuron · doi:10.1016/j.neuron.2018.06.003 · Cited by 278 · see citing works
Hyperphosphorylation of Tau Associates With Changes in Its Function Beyond Microtubule Stability
Alonso, A. D., Cohen, L. S., Corbo, C., Morozova, V., ElIdrissi, A., Phillips, G., & Kleiman, F. E. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00338 · Cited by 278 · see citing works
Frandemiche, M. L., De Seranno, S., Rush, T., Borel, E., Elie, A., Arnal, I., Lanté, F., & Buisson, A. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.4261-13.2014 · Cited by 272 · see citing works
Tau: Enabler of diverse brain disorders and target of rapidly evolving therapeutic strategies
Chang, C.-W., Shao, E., & Mucke, L. (2021) · Science · doi:10.1126/science.abb8255 · Cited by 263 · see citing works
Self-citationModels of β-amyloid induced Tau-pathology: The long and “folded” road to understand the mechanism
Stancu, I.-C., Vasconcelos, B., Terwel, D., & Dewachter, I. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-51 · Cited by 256 · see citing works
Synaptic dysfunction in Alzheimer's disease: Mechanisms and therapeutic strategies
Chen, Y., Fu, A. K. Y., & Ip, N. Y. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2018.11.006 · Cited by 258 · see citing works
Tau in neurodegenerative disease
Gao, Y.-L., Wang, N., Sun, F.-R., Cao, X.-P., Zhang, W., & Yu, J.-T. (2018) · Annals of Translational Medicine · doi:10.21037/atm.2018.04.23 · Cited by 222 · see citing works
Wang, W., Zhou, Q., Jiang, T., Li, S., Ye, J., Zheng, J., Wang, X., Liu, Y., Deng, M., Ke, D., et al. (2021) · Theranostics · doi:10.7150/thno.55680 · Cited by 242 · see citing works
Analyzing dendritic spine pathology in Alzheimer’s disease: Problems and opportunities
Dorostkar, M. M., Zou, C., Blazquez-Llorca, L., & Herms, J. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1449-5 · Cited by 235 · see citing works
Soluble forms of tau are toxic in Alzheimer's disease
Kopeikina, K., Hyman, B., & Spires-Jones, T. (2012) · Translational Neuroscience · doi:10.2478/s13380-012-0032-y · Cited by 232 · see citing works
Human secreted tau increases amyloid-beta production
Bright, J., Hussain, S., Dang, V., Wright, S., Cooper, B., Byun, T., Ramos, C., Singh, A., Parry, G., Stagliano, N., et al. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.09.007 · Cited by 230 · see citing works
Dendritic Spine Pathology in Neurodegenerative Diseases
Herms, J., & Dorostkar, M. M. (2016) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-012615-044216 · Cited by 201 · see citing works
Tau Protein Interaction Partners and Their Roles in Alzheimer’s Disease and Other Tauopathies
Sinsky, J., Pichlerova, K., & Hanes, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179207 · Cited by 220 · see citing works
Peeraer, E., Bottelbergs, A., Van Kolen, K., Stancu, I.-C., Vasconcelos, B., Mahieu, M., Duytschaever, H., Ver Donck, L., Torremans, A., Sluydts, E., et al. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.08.032 · Cited by 214 · see citing works
Widman, A. J., & McMahon, L. L. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1718883115 · Cited by 204 · see citing works
The Perineuronal ‘Safety’ Net? Perineuronal Net Abnormalities in Neurological Disorders
Wen, T. H., Binder, D. K., Ethell, I. M., & Razak, K. A. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00270 · Cited by 170 · see citing works
A second X chromosome contributes to resilience in a mouse model of Alzheimer’s disease
Davis, E. J., Broestl, L., Abdulai-Saiku, S., Worden, K., Bonham, L. W., Miñones-Moyano, E., Moreno, A. J., Wang, D., Chang, K., Williams, G., et al. (2020) · Science Translational Medicine · doi:10.1126/scitranslmed.aaz5677 · Cited by 176 · see citing works
Self-citationBeagle, A. J., Darwish, S. M., Ranasinghe, K. G., La, A. L., Karageorgiou, E., & Vossel, K. A. (2017) · Journal of Alzheimer's Disease · doi:10.3233/jad-170031 · Cited by 173 · see citing works
Sohn, P. D., Tracy, T. E., Son, H.-I., Zhou, Y., Leite, R. E. P., Miller, B. L., Seeley, W. W., Grinberg, L. T., & Gan, L. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0109-0 · Cited by 160 · see citing works
Tau reduction prevents Aβ-induced axonal transport deficits by blocking activation of GSK3β
Vossel, K. A., Xu, J. C., Fomenko, V., Miyamoto, T., Suberbielle, E., Knox, J. A., Ho, K., Kim, D. H., Yu, G.-Q., & Mucke, L. (2015) · Journal of Cell Biology · doi:10.1083/jcb.201407065 · Cited by 167 · see citing works
Self-citationPathogenic Tau Impairs Axon Initial Segment Plasticity and Excitability Homeostasis
Sohn, P. D., Huang, C. T.-L., Yan, R., Fan, L., Tracy, T. E., Camargo, C. M., Montgomery, K. M., Arhar, T., Mok, S.-A., Freilich, R., et al. (2019) · Neuron · doi:10.1016/j.neuron.2019.08.008 · Cited by 148 · see citing works
Self-citationAntisense oligonucleotides: treating neurodegeneration at the level of RNA
DeVos, S. L., & Miller, T. M. (2013) · Neurotherapeutics · doi:10.1007/s13311-013-0194-5 · Cited by 164 · see citing works
Targeting Fyn Kinase in Alzheimer’s Disease
Nygaard, H. B. (2018) · Biological Psychiatry · doi:10.1016/j.biopsych.2017.06.004 · Cited by 162 · see citing works
Harris, S. S., Wolf, F., De Strooper, B., & Busche, M. A. (2020) · Neuron · doi:10.1016/j.neuron.2020.06.005 · Cited by 161 · see citing works
GSK3β and tau protein in Alzheimer's disease and epilepsy
Toral-Rios, D., Pichardo-Rojas, P. S., Alonso-Vanegas, M., & Campos-Peña, V. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.00019 · Cited by 158 · see citing works
Gourmaud, S., Shou, H., Irwin, D. J., Sansalone, K., Jacobs, L. M., Lucas, T. H., Marsh, E. D., Davis, K. A., Jensen, F. E., & Talos, D. M. (2020) · Brain · doi:10.1093/brain/awz381 · Cited by 155 · see citing works
Bazan, N. G. (2018) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2018.09.003 · Cited by 148 · see citing works
Pre‐synaptic C‐terminal truncated tau is released from cortical synapses in Alzheimer's disease
Sokolow, S., Henkins, K. M., Bilousova, T., Gonzalez, B., Vinters, H. V., Miller, C. A., Cornwell, L., Poon, W. W., & Gylys, K. H. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.12991 · Cited by 133 · see citing works
Is Alzheimer’s a disease of the white matter?
Sachdev, P. S., Zhuang, L., Braidy, N., & Wen, W. (2013) · Current Opinion in Psychiatry · doi:10.1097/yco.0b013e32835ed6e8 · Cited by 137 · see citing works
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 · see citing works
Alzheimer’s disease as oligomeropathy
Ono, K. (2018) · Neurochemistry International · doi:10.1016/j.neuint.2017.08.010 · Cited by 129 · see citing works
Connecting the dots between tau dysfunction and neurodegeneration
Frost, B., Götz, J., & Feany, M. B. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.07.005 · Cited by 124 · see citing works
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 · see citing works
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 · see citing works
Self-citationHippocampal 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 · see citing works
Amyloid-<i>β</i>-Induced Dysregulation of AMPA Receptor Trafficking
Guntupalli, S., Widagdo, J., & Anggono, V. (2016) · Neural Plasticity · doi:10.1155/2016/3204519 · Cited by 110 · see citing works
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 · see citing works
Cheng, J. S., Craft, R., Yu, G.-Q., Ho, K., Wang, X., Mohan, G., Mangnitsky, S., Ponnusamy, R., & Mucke, L. (2014) · PLoS ONE · doi:10.1371/journal.pone.0115765 · Cited by 100 · see citing works
Self-citationThe Deacetylase HDAC6 Mediates Endogenous Neuritic Tau Pathology
Tseng, J.-H., Xie, L., Song, S., Xie, Y., Allen, L., Ajit, D., Hong, J.-S., Chen, X., Meeker, R. B., & Cohen, T. J. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.07.082 · Cited by 93 · see citing works
Dendritic Spines: Mediators of Cognitive Resilience in Aging and Alzheimer’s Disease
Walker, C. K., & Herskowitz, J. H. (2021) · The Neuroscientist · doi:10.1177/1073858420945964 · Cited by 86 · see citing works
Chang, C.-W., Evans, M. D., Yu, X., Yu, G.-Q., & Mucke, L. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109855 · Cited by 81 · see citing works
Self-citationJohnson, E. C. B., Ho, K., Yu, G.-Q., Das, M., Sanchez, P. E., Djukic, B., Lopez, I., Yu, X., Gill, M., Zhang, W., et al. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00393-5 · Cited by 73 · see citing works
Self-citationSeizure resistance without parkinsonism in aged mice after tau reduction
Li, Z., Hall, A. M., Kelinske, M., & Roberson, E. D. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.05.001 · Cited by 71 · see citing works
Self-citationDysregulated Wnt Signalling in the Alzheimer’s Brain
Aghaizu, N. D., Jin, H., & Whiting, P. J. (2020) · Brain Sciences · doi:10.3390/brainsci10120902 · Cited by 70 · see citing works
Tau-induced pathology in epilepsy and dementia: notions from patients and animal models.
Sánchez, M., García-Cabrero, A., Sánchez-Elexpuru, G., Burgos, D., & Serratosa, J. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19041092 · Cited by 68 · see citing works
Network dysfunction in<i>α</i>‐synuclein transgenic mice and human Lewy body dementia
Morris, M., Sanchez, P. E., Verret, L., Beagle, A. J., Guo, W., Dubal, D., Ranasinghe, K. G., Koyama, A., Ho, K., Yu, G., et al. (2015) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.257 · Cited by 61 · see citing works
Self-citationSingh, A., Allen, D., Fracassi, A., Tumurbaatar, B., Natarajan, C., Scaduto, P., Woltjer, R., Kayed, R., Limon, A., Krishnan, B., et al. (2020) · Journal of Alzheimer's Disease · doi:10.3233/jad-200716 · Cited by 56 · see citing works
Tau acts as a mediator for<scp>A</scp>lzheimer's disease‐related synaptic deficits
Liao, D., Miller, E. C., & Teravskis, P. J. (2014) · European Journal of Neuroscience · doi:10.1111/ejn.12504 · Cited by 53 · see citing works
The Role of Amyloid-Beta and Tau in the Early Pathogenesis of Alzheimer’s Disease
Yin, X., Qiu, Y., Zhao, C., Zhou, Z., Bao, J., & Qian, W. (2021) · Medical Science Monitor · doi:10.12659/msm.933084 · Cited by 48 · see citing works
Tauopathy contributes to synaptic and cognitive deficits in a murine model for Alzheimer’s disease
Stancu, I., Ris, L., Vasconcelos, B., Marinangeli, C., Goeminne, L., Laporte, V., Haylani, L. E., Couturier, J., Schakman, O., Gailly, P., et al. (2014) · The FASEB Journal · doi:10.1096/fj.13-246702 · Cited by 48 · see citing works
Mechanisms of tau and Aβ-induced excitotoxicity
Pallo, S. P., DiMaio, J., Cook, A., Nilsson, B., & Johnson, G. V. W. (2016) · Brain Research · doi:10.1016/j.brainres.2015.12.048 · Cited by 46 · see citing works
Marcatti, M., Fracassi, A., Montalbano, M., Natarajan, C., Krishnan, B., Kayed, R., & Taglialatela, G. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04255-9 · Cited by 38 · see citing works
Miyamoto, T., Kim, D., Knox, J. A., Johnson, E., & Mucke, L. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.666529 · Cited by 33 · see citing works
Self-citationTau as a mediator of neurotoxicity associated to cerebral amyloid angiopathy
You, Y., Perkins, A., Cisternas, P., Muñoz, B., Taylor, X., You, Y., Garringer, H. J., Oblak, A. L., Atwood, B. K., Vidal, R., et al. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0680-z · Cited by 33 · see citing works
Naguib, S., Lopez-Lee, C., Torres, E. R., Lee, S.-I., Zhu, J., Zhu, D., Ye, P., Norman, K., Zhao, M., Wong, M. Y., et al. (2025) · Immunity · doi:10.1016/j.immuni.2025.05.023 · Cited by 32 · see citing works
Masitinib for the Treatment of Alzheimer’s Disease
Ettcheto, M., Cano, A., Sanchez-López, E., Verdaguer, E., Folch, J., Auladell, C., & Camins, A. (2021) · Neurodegenerative Disease Management · doi:10.2217/nmt-2021-0019 · Cited by 28 · see citing works
Chen, L., Christenson Wick, Z., Vetere, L. M., Vaughan, N., Jurkowski, A., Galas, A., Diego, K. S., Philipsberg, P. A., Soler, I., Feng, Y., et al. (2023) · The Journal of Neuroscience · doi:10.1523/jneurosci.1204-23.2023 · Cited by 21 · see citing works
DNA damage and neurodegeneration: the unusual suspect
Toiber, D., & Stein, D. (2017) · Neural Regeneration Research · doi:10.4103/1673-5374.215254 · Cited by 20 · see citing works
Wild-Type, but Not Mutant N296H, Human Tau Restores Aβ-Mediated Inhibition of LTP in Tau−/− mice
Vargas-Caballero, M., Denk, F., Wobst, H. J., Arch, E., Pegasiou, C.-M., Oliver, P. L., Shipton, O. A., Paulsen, O., & Wade-Martins, R. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00201 · Cited by 18 · see citing works
Tau Ablation Rewires Brain Cell Programs in Health and Restores Function in Disease
Chimal-Juárez, E., Patel, H., Jury-Garfe, N., Dabin, L. C., Vidal, R., Kim, J., & Lasagna-Reeves, C. A. (2026) · bioRxiv · doi:10.64898/2026.05.12.724684
- Authors
- Roberson, E. D., Halabisky, B., Yoo, J. W., Yao, J., Chin, J., Yan, F., Wu, T., Hamto, P., Devidze, N., Yu, G.-Q., Palop, J. J., Noebels, J. L., & Mucke, L.
- Affiliations
- Gladstone Institutes (US)
- Baylor College of Medicine (US)
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2011-01-12
- Volume
- 31
- Issue
- 2
- Pages
- 700-711
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC3325794
- OpenAlex
- W2118516203
- Cited by
- 654
- References
- 74
- Citations by year
- 2026: 22 · 2025: 23 · 2024: 37 · 2023: 30 · 2022: 31 · 2021: 50 · 2020: 53 · 2019: 46 · 2018: 45 · 2017: 46 · 2016: 41 · 2015: 50 · 2014: 54 · 2013: 55 · 2012: 42
- FWCI
- 39.27
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Gladstone Institutes
- National Institutes of Health (1c06rr018928-01, AG‐022074)
- National Institute on Aging (AG022074, P01AG022074)
- National Institute of Neurological Disorders and Stroke (NS054811, K08NS054811, R01NS041787, NS041787, NS29709, R01NS029709)
- National Center for Research Resources (C06-RR-018928, RR018928)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- Alzheimer's disease, amyloid-beta, tau protein, Fyn tyrosine kinase, synaptic transmission, synaptic plasticity, spontaneous epileptiform activity, seizures, excitation-inhibition balance, NMDA receptor dysfunction, cognitive impairment, hippocampus
- MeSH terms
- Alzheimer Disease, Amyotrophic Lateral Sclerosis, Animals, Cognition Disorders, Disease Models, Animal, Electroencephalography, Female, Hippocampus, Male, Mice, Mutant Strains, Nerve Net, Synaptic Transmission, Neuronal Plasticity, Seizures, Species Specificity, Synapses, Amyloid beta-Peptides, tau Proteins, Proto-Oncogene Proteins c-fyn, Mice, In Vitro Techniques
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
