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Transmission and spreading of tauopathy in transgenic mouse brain
Open accessAbstract
Hyperphosphorylated tau makes up the filamentous intracellular inclusions of several neurodegenerative diseases, including Alzheimer's disease. In the disease process, neuronal tau inclusions first appear in the transentorhinal cortex from where they seem to spread to the hippocampal formation and neocortex. Cognitive impairment becomes manifest when inclusions reach the hippocampus, with abundant neocortical tau inclusions and extracellular beta-amyloid deposits being the defining pathological hallmarks of Alzheimer's disease. An abundance of tau inclusions, in the absence of beta-amyloid deposits, defines Pick's disease, progressive supranuclear palsy, corticobasal degeneration and other diseases. Tau mutations cause familial forms of frontotemporal dementia, establishing that tau protein dysfunction is sufficient to cause neurodegeneration and dementia. Thus, transgenic mice expressing mutant (for example, P301S) human tau in nerve cells show the essential features of tauopathies, including neurodegeneration and abundant filaments made of hyperphosphorylated tau protein. By contrast, mouse lines expressing single isoforms of wild-type human tau do not produce tau filaments or show neurodegeneration. Here we have used tau-expressing lines to investigate whether experimental tauopathy can be transmitted. We show that injection of brain extract from mutant P301S tau-expressing mice into the brain of transgenic wild-type tau-expressing animals induces assembly of wild-type human tau into filaments and spreading of pathology from the site of injection to neighbouring brain regions.
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In the citing paper
“The pathogenic tau can be released from diseased neurons, then uptake by previously unaffected normal neurons, inducing pathogenic tau production in normal neurons.”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [42]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Proteopathic tau seeds are capable of entering a cell and promoting aggregation in a prion-like manner (Clavaguera et al., 2009; Frost et al., 2009).”
From Network analysis identifies strain-dependent response to tau and tau seeding-associated genes (2023) · cites this paper as Clavaguera et al., 2009
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“inoculation of mice with tauopathy homogenates produces local pathology that spreads beyond the injection site (Clavaguera et al., 2009).”
From Spontaneous pathology in PS19 tauopathy mice progresses via brain networks (2025) · cites this paper as Clavaguera et al., 2009
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“This may be important as we know that tau aggregates can transfer and propagate/spread within synaptic circuits (Clavaguera et al., 2009, de Calignon et al., 2012).”
From In vivo imaging of tau pathology using multi-parametric quantitative MRI (2015) · cites this paper as Clavaguera et al., 2009
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“We are thus unable to explain how Aβ peptides—despite being a part of the amyloid cascade—may participate in the neuron-to-neuron propagation of Tau pathology [20].”
From The new genetic landscape of Alzheimer’s disease: from amyloid cascade to genetically driven synaptic failure hypothesis? (2019) · cites this paper as [20]
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“According to the amyloid cascade hypothesis, Aβ peptides are neurotoxic and supposed to lead to or accentuate neuron-to-neuron propagation of Tau pathology—leading to neuronal death—by a still unknown mechanism [20].”
From The new genetic landscape of Alzheimer’s disease: from amyloid cascade to genetically driven synaptic failure hypothesis? (2019) · cites this paper as [20]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
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“Several lines of evidence indicate tau propagates pathology among neurons.”
From Spontaneous pathology in PS19 tauopathy mice progresses via brain networks (2025) · cites this paper as Clavaguera et al., 2009
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In the citing paper
“The failure of these candidate drugs to date to show any improvements in the human condition has caused a shift in interest to other therapeutic pathways (Clavaguera et al., 2009).”
From In vivo imaging of tau pathology using multi-parametric quantitative MRI (2015) · cites this paper as Clavaguera et al., 2009
Experimental — accuracy not yet measuredIn the citing paper
“Increasing evidence suggests the transmission of tau pathology is mediated by the release, uptake, and trafficking of pathogenic or misfolded tau aggregates within synaptically connected neurons9,10.”
From Tau Internalization is Regulated by 6-O Sulfation on Heparan Sulfate Proteoglycans (HSPGs) (2018) · cites this paper as [9]
In the citing paper
“seeded synthetic tau fibrils, or brain extracts from tau transgenic mice or human patients with tauopathy injected into the brain of tau transgenic or WT mice was found to induce pathological tau spreading at sites distal to the injection site [232–235].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [232]
In the citing paper
“The transfer of abnormal misfolded proteins, including tau and Aβ, has a common feature of the pathological propagation between cells [42, 56].”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [42]
In the citing paper
“Another recent study reported that brain extracts from NFT-bearing mouse brain injected in wild-type tau expressing mice induces seeding of tau fibrils in neurons (Clavaguera et al., 2009).”
From Propagation of Tau Pathology in a Model of Early Alzheimer's Disease (2012) · cites this paper as Clavaguera et al., 2009
In the citing paper
“In living mouse brain, intracortical injections of tau aggregates seed tau fibrillization in neurons carrying the human transgene (Clavaguera et al., 2009).”
From Propagation of Tau Pathology in a Model of Early Alzheimer's Disease (2012) · cites this paper as Clavaguera et al., 2009
In the citing paper
“Using a paradigm similar to in vivo Aβ-seeding, neurofibrillary (tau) tangles can be exogenously induced by the intracerebral infusion of brain extract containing abnormal tau filaments into mice bearing a human tau transgene63.”
From Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders (2011) · cites this paper as [63]
In the citing paper
“The current clinical trial literature is compatible with the idea that AβP-related substances kindle a self-propagating process related to neocortical NFTs, as has been hypothesized (266-269).”
From Correlation of Alzheimer Disease Neuropathologic Changes With Cognitive Status: A Review of the Literature (2012) · cites this paper as [268]
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Citations
Cites
Neuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123
The Mouse Brain in Stereotaxic Coordinates
Paxinos, G. (2001) · Cited by 12,859
Staging of brain pathology related to sporadic Parkinson’s disease
Braak, H., Tredici, K. D., Rüb, U., de Vos, R. A. I., Jansen Steur, E. N. H., & Braak, E. (2003) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00065-9 · Cited by 10,777
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
Prusiner, S. B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13363 · Cited by 5,373
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
Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D., & Crowther, R. A. (1989) · Neuron · doi:10.1016/0896-6273(89)90210-9 · Cited by 2,492
Self-citationLee, V. M.-Y., Goedert, M., & Trojanowski, J. Q. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1121 · Cited by 2,480
Self-citationA Century of Alzheimer's Disease
Goedert, M., & Spillantini, M. G. (2006) · Science · doi:10.1126/science.1132814 · Cited by 2,153
Self-citationFormation 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
Cited by
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Items 601–700 of 1,006
Intracellular and extracellular tau
Ávila, J. (2010) · Frontiers in Neuroscience · doi:10.3389/fnins.2010.00049 · Cited by 63
Interaction between -Synuclein and Other Proteins in Neurodegenerative Disorders
Jellinger, K. A. (2011) · The Scientific World JOURNAL · doi:10.1100/2011/371893 · Cited by 64
Aggregated proteins in schizophrenia and other chronic mental diseases
Korth, C. (2012) · Prion · doi:10.4161/pri.18989 · Cited by 64
Carbonell, F., Iturria‐Medina, Y., & Evans, A. C. (2018) · Frontiers in Neurology · doi:10.3389/fneur.2018.00037 · Cited by 65
In vivoimaging reveals reduced activity of neuronal circuits in a mouse tauopathy model
Marinković, P., Blumenstock, S., Goltstein, P. M., Korzhova, V., Peters, F., Knebl, A., & Herms, J. W. (2019) · Brain · doi:10.1093/brain/awz035 · Cited by 63
Lee, S., Kim, W., Li, Z., & Hall, G. F. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/172837 · Cited by 67
Goedert, M., Crowther, R. A., Scheres, S. H. W., & Spillantini, M. G. (2023) · Cytoskeleton · doi:10.1002/cm.21812 · Cited by 64
Self-citationIntracellular and Extracellular Roles for Tau in Neurodegenerative Disease
Hanger, D. P., Lau, D. H. W., Phillips, E. C., Bondulich, M. K., Guo, T., Woodward, B. W., Pooler, A. M., & Noble, W. J. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-132054 · Cited by 66
Cellular Aspects of Prion Replication In Vitro
Grassmann, A., Wolf, H., Hofmann, J. P., Graham, J. F., & Vorberg, I. M. (2013) · Viruses · doi:10.3390/v5010374 · Cited by 62
The ordered assembly of tau is the gain‐of‐toxic function that causes human tauopathies
Goedert, M. (2016) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2016.09.001 · Cited by 67
Self-citationFerrer, I. (2018) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.07.004 · Cited by 65
FRET-based Tau seeding assay does not represent prion-like templated assembly of Tau filaments
Kaniyappan, S., Tepper, K., Biernat, J., Chandupatla, R., Hübschmann, S., Irsen, S. H., Bicher, S., Klatt, C., Mandelkow, E., & Mandelkow�, E. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00389-1 · Cited by 65
Tau-targeting therapy in Alzheimer’s disease: Critical advances and future opportunities
Guo, Y., Li, S., Zeng, L.-H., & Tan, J. (2022) · Ageing and Neurodegenerative Diseases · doi:10.20517/and.2022.16 · Cited by 61
From nucleation to widespread propagation: A prion-like concept for ALS
Maniecka, Z., & Polymenidou, M. (2015) · Virus Research · doi:10.1016/j.virusres.2014.12.032 · Cited by 65
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Pao, P., Seo, J., Lee, A., Kritskiy, O., Patnaik, D., Penney, J., Raju, R. M., Geigenmüller, U., Silva, M. C., Lucente, D. E., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2217864120 · Cited by 62
Protein aggregation and its affecting mechanisms in neurodegenerative diseases
Wu, J., Wu, J., Chen, T., Cai, J., & Ren, R. (2024) · Neurochemistry International · doi:10.1016/j.neuint.2024.105880 · Cited by 62
Physiological and environmental control of yeast prions
Chernova, T. A., Wilkinson, K. D., & Chernoff, Y. O. (2013) · FEMS Microbiology Reviews · doi:10.1111/1574-6976.12053 · Cited by 62
Nussbaum-Krammer, C. I., & Morimoto, R. I. (2014) · Disease Models & Mechanisms · doi:10.1242/dmm.013011 · Cited by 68
Hu, W. H., Wu, F., Zhang, Y., Gong, C., Iqbal, K., & Liu, F. (2017) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00311 · Cited by 63
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Orru, C. D., Soldau, K., Cordano, C., Llibre‐Guerra, J. J., Green, A., Sanchez, H. C., Groveman, B. R., Edland, S. D., Safar, J., Lin, J. H., et al. (2018) · mBio · doi:10.1128/mbio.02095-18 · Cited by 62
Microglia: Friend and foe in tauopathy
Odfalk, K. F., Bieniek, K. F., & Hopp, S. C. (2022) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2022.102306 · Cited by 60
Tangles, Toxicity, and Tau Secretion in AD – New Approaches to a Vexing Problem
Gendreau, K. L., & Hall, G. F. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00160 · Cited by 67
Tau neurotoxicity and rescue in animal models of human Tauopathies
Krüger, L., & Mandelkow, E. (2015) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2015.09.004 · Cited by 63
Tau and Membranes: Interactions That Promote Folding and Condensation
Sallaberry, C. A., Voss, B. J., Majewski, J. P., Biernat, J., Mandelkow�, E., Chi, E. Y., & Zanden, C. M. V. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.725241 · Cited by 64
Clavaguera, F., Grueninger, F., & Tolnay, M. (2013) · Neuropharmacology · doi:10.1016/j.neuropharm.2013.08.037 · Cited by 68
Self-citationTransglutaminase 2: Biology, Relevance to Neurodegenerative Diseases and Therapeutic Implications
Grosso, H., & Mouradian, M. M. (2011) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2011.12.003 · Cited by 60
Therapeutic Strategies to Target Calcium Dysregulation in Alzheimer’s Disease
Calvo-Rodríguez, M., Kharitonova, E. K., & Bacskai, B. J. (2020) · Cells · doi:10.3390/cells9112513 · Cited by 60
Protein with tau-like repeats regulates neuronal integrity and lifespan inC. elegans
Chew, Y. L., Fan, X., Götz, J., & Nicholas, H. (2013) · Journal of Cell Science · doi:10.1242/jcs.jcs124404 · Cited by 59
Beta-Amyloid and Tau-Protein: Structure, Interaction, and Prion-Like Properties
Tatarnikova, O. G., Орлов, М. А., & Bobkova, N. V. (2015) · Biochemistry (Moscow) · doi:10.1134/s000629791513012x · Cited by 62
Croft, C. L., Wade, M. A., Kurbatskaya, K., Mastrandreas, P., Hughes, M. M., Phillips, E. C., Pooler, A. M., Perkinton, M. S., Hanger, D. P., & Noble, W. J. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.97 · Cited by 62
Clustering of Tau fibrils impairs the synaptic composition of α3‐Na+/K+‐ATPase and AMPA receptors
Shrivastava, A. N., Redeker, V., Pieri, L., Bousset, L., Renner, M. L., Madiona, K., Mailhes‐Hamon, C., Coens, A., Buée, L., Hantraye, P., et al. (2019) · The EMBO Journal · doi:10.15252/embj.201899871 · Cited by 62
Tau misfolding efficiently propagates between individual intact hippocampal neurons
Hallinan, G. I., Vargas-Caballero, M., West, J., & Deinhardt, K. (2019) · The Journal of Neuroscience · doi:10.1523/jneurosci.1590-19.2019 · Cited by 59
Alzheimer’s disease brain contains tau fractions with differential prion-like activities
Li, L., Shi, R., Gu, J., Tung, Y. C., Zhou, Y., Zhou, D., Wu, R., Chu, D., Jin, N., Deng, K., et al. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01127-4 · Cited by 60
Topography of FUS pathology distinguishes late-onset BIBD from aFTLD-U
Lee, E. B., Russ, J., Jung, H., Elman, L. B., Chahine, L. M., Kremens, D. E., Miller, B. L., Coslett, H. B., Trojanowski, J. Q., Deerlin, V. M. V., et al. (2013) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-1-9 · Cited by 58
The anesthetic sevoflurane induces tau trafficking from neurons to microglia
Dong, Y., Liang, F., Huang, L., Fang, F., Yang, G., Tanzi, R. E., Zhang, Y., Quan, Q., & Xie, Z. (2021) · Communications Biology · doi:10.1038/s42003-021-02047-8 · Cited by 59
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Liang, S., Wang, Z.-T., Tan, L., & Yu, J. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-02809-3 · Cited by 61
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Nussbaum-Krammer, C. I., Park, K.-W., Li, L., Melki, R., & Morimoto, R. I. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003351 · Cited by 58
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Walls, K. C., Ager, R. R., Vasilevko, V., Cheng, D., Medeiros, R., & LaFerla, F. M. (2014) · Neuroscience Letters · doi:10.1016/j.neulet.2014.05.047 · Cited by 62
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Wısnıewskı, T., & Drummond, E. (2015) · Expert Review of Vaccines · doi:10.1586/14760584.2016.1121815 · Cited by 60
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Niedowicz, D. M., Nelson, P. T., & Murphy, M. P. (2011) · Current Neuropharmacology · doi:10.2174/157015911798376181 · Cited by 62
Alterations in hippocampal activity and Alzheimer’s disease.
Setti, S. E., Hunsberger, H. C., & Reed, M. N. (2017) · Translational Issues in Psychological Science · doi:10.1037/tps0000124 · Cited by 65
The Cell Biology of Tau Secretion
Merezhko, M., Uronen, R., & Huttunen, H. J. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.569818 · Cited by 65
Patel, H., Martínez, P., Perkins, A., Taylor, X., Jury, N., McKinzie, D. L., & Lasagna‐Reeves, C. A. (2021) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2021.09.006 · Cited by 58
Gomes, P., Tzouanou, F., Skolariki, K., Vamvaka-Iakovou, A., Nogueras‐Ortiz, C. J., Tsirtsaki, K., Waites, C. L., Vlamos, P., Sousa, N., Costa‐Silva, B., et al. (2022) · Experimental Neurology · doi:10.1016/j.expneurol.2022.114183 · Cited by 60
Progression of Seed‐Induced A β Deposition within the Limbic Connectome
Ye, L., Hamaguchi, T., Fritschi, S. K., Eisele, Y. S., Obermüller, U., Jucker, M., & Walker, L. C. (2015) · Brain Pathology · doi:10.1111/bpa.12252 · Cited by 60
Self-citationFerrer, I., Andrés‐Benito, P., Zelaya, M. V., Aguirre, M. E. E., Carmona, M., Ausín, K., Lachén‐Montes, M., Fernández‐Irigoyen, J., Santamaría, E., & del Río, J. A. (2020) · Acta Neuropathologica · doi:10.1007/s00401-019-02122-9 · Cited by 58
Tau Filament Self-Assembly and Structure: Tau as a Therapeutic Target
Oakley, S. S., Maina, M. B., Marshall, K. E., Al‐Hilaly, Y. K., Harrington, C., Wischik, C. M., & Serpell, L. C. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.590754 · Cited by 59
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Sprunger, M. L., & Jackrel, M. E. (2021) · Biomolecules · doi:10.3390/biom11071014 · Cited by 60
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Panegyres, P. K., & Burchell, J. T. (2016) · ImmunoTargets and Therapy · doi:10.2147/itt.s64795 · Cited by 57
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Chalermpalanupap, T., Weinshenker, D., & Rorabaugh, J. M. (2017) · Neural Plasticity · doi:10.1155/2017/7829507 · Cited by 59
Liu, M., Dexheimer, T. S., Sui, D., Hovde, S., Deng, X., Kwok, R. P. S., Bochar, D. A., & Kuo, M. (2020) · Scientific Reports · doi:10.1038/s41598-020-73680-2 · Cited by 59
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Gadhe, L. G., Sakunthala, A., Mukherjee, S., Gahlot, N., Bera, R., Sawner, A. S., Kadu, P., & Maji, S. K. (2021) · Biophysical Chemistry · doi:10.1016/j.bpc.2021.106736 · Cited by 56
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Tuck, B. J., Miller, L. V. C., Katsinelos, T., Smith, A. E., Wilson, E. L., Keeling, S., Cheng, S., Vaysburd, M. J., Knox, C., Tredgett, L., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110776 · Cited by 57
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Li, A., Paudel, R., Johnson, R. M., Courtney, R. J., Lees, A. J., Holton, J. L., Hardy, J., Révész, T., & Houlden, H. (2012) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2012.01269.x · Cited by 56
Ramachandran, G., & Udgaonkar, J. B. (2013) · Biochemistry · doi:10.1021/bi400209z · Cited by 59
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Goedert, M., Falcon, B., Zhang, W., Ghetti, B. F., & Scheres, S. H. W. (2018) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2018.83.037580 · Cited by 59
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Hara, M., Hirokawa, K., Kamei, S., & Uchihara, T. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1097-6 · Cited by 55
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Gallardo, G., Wong, C. H. Y., Hernandez, S. M. R., Mann, C. N., Lin, K., Leyns, C. E. G., Jiang, H., & Holtzman, D. M. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0340-6 · Cited by 61
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Therriault, J., Pascoal, T. A., Savard, M., Mathotaarachchi, S. S., Benedet, A. L., Chamoun, M., Tissot, C., Lussier, F. Z., Rahmouni, N., Stevenson, J., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abc8693 · Cited by 58
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Malpetti, M., Jones, P. S., Cope, T. E., Holland, N., Naessens, M., Rouse, M. A., Rittman, T., Savulich, G., Whiteside, D. J., Street, D., et al. (2023) · Annals of Neurology · doi:10.1002/ana.26543 · Cited by 53
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Melis, V., Zabke, C., Stamer, K., Magbagbeolu, M., Schwab, K., Marschall, P., Veh, R. W., Bachmann, S., Deiana, S., Moreau, P., et al. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1804-z · Cited by 53
Magen, I., & Gozes, I. (2013) · Neuropeptides · doi:10.1016/j.npep.2013.10.011 · Cited by 52
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Carlson, G. A., & Prusiner, S. B. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094861 · Cited by 51
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Braak, H., & Tredici, K. D. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129029 · Cited by 54
Virgone‐Carlotta, A., Uhlrich, J., Akram, M. N., Ressnikoff, D., Chrétien, F., Domenget, C., Gherardi, R. K., Despars, G., Jurdic, P., Honnorat, J., et al. (2013) · Glia · doi:10.1002/glia.22546 · Cited by 52
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Wısnıewskı, T., & Boutajangout, A. (2010) · Mount Sinai Journal of Medicine A Journal of Translational and Personalized Medicine · doi:10.1002/msj.20156 · Cited by 53
Prion‐like propagation as a pathogenic principle in frontotemporal dementia
Hock, E., & Polymenidou, M. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13668 · Cited by 58
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Shu, S., Zhu, H., Tang, N., Chen, W., Li, X., Li, H., Pei, L., Liu, D., Mu, Y., Tian, Q., et al. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.2258-16.2016 · Cited by 51
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Bourré, G., Cantrelle, F., Kamah, A., Chambraud, B., Landrieu, I., & Smet‐Nocca, C. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00595 · Cited by 57
Chemicals used for the induction of Alzheimer’s disease-like cognitive dysfunctions in rodents
Mahdi, O., Baharuldin, M. T. H., Nor, N. H. M., Chiroma, S. M., Jagadeesan, S., & Moklas, M. A. M. (2019) · Biomedical Research and Therapy · doi:10.15419/bmrat.v6i11.575 · Cited by 53
Takeda, S. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.01274 · Cited by 53
Cecco, E. D., Celauro, L., Vanni, S., Grandolfo, M., Bistaffa, E., Moda, F., Aguzzi, A., & Legname, G. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15040 · Cited by 55
Long Non-coding RNAs in Pathogenesis of Neurodegenerative Diseases
Zhou, S., Xiao, Y., Wang, M., Meng, Y., Song, D., Yang, H., Wang, D., Bi, J., & Xu, S. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.719247 · Cited by 56
Metadata
- Authors
- Clavaguera, F., Bolmont, T., Crowther, R. A., Abramowski, D., Frank, S., Probst, A., Fraser, G., Stalder, A. K., Beibel, M., Staufenbiel, M., Jucker, M., Goedert, M., & Tolnay, M.
- Affiliations
- University of Basel (CH)
- Hertie Institute for Clinical Brain Research (DE)
- MRC Laboratory of Molecular Biology (GB)
- University Hospital of Basel (CH)
- Novartis (Switzerland) (CH)
- Corresponding author
- Goedert, Michel
- Tolnay, Markus
- ORCID
- Venue
- Nature Cell Biology
- Published
- 2009-06-07
- Volume
- 11
- Issue
- 7
- Pages
- 909-913
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- PMC
- PMC2726961
- OpenAlex
- W2099340107
- Cited by
- 1,803
- References
- 36
- Citations by year
- 2026: 76 · 2025: 85 · 2024: 96 · 2023: 94 · 2022: 114 · 2021: 130 · 2020: 135 · 2019: 128 · 2018: 115 · 2017: 105 · 2016: 113 · 2015: 121 · 2014: 107 · 2013: 122 · 2012: 98
- FWCI
- 56.34
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion, cc-by-nc-nd)
- Funders
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (120261)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Keywords
- tauopathy, tau protein, hyperphosphorylated tau, transgenic mice, Alzheimer's disease, Pick's disease, progressive supranuclear palsy, corticobasal degeneration, frontotemporal dementia, neurodegeneration, transentorhinal cortex, hippocampus
- MeSH terms
- Animals, Brain, Humans, Immunohistochemistry, Mice, Transgenic, Blotting, Western, tau Proteins, Tauopathies, Mice
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