What is the evidence that tau pathology spreads through prion-like propagation?
Open accessAbstract
Emerging experimental evidence suggests that the spread of tau pathology in the brain in Tauopathies reflects the propagation of abnormal tau species along neuroanatomically connected brain areas. This propagation could occur through a "prion-like" mechanism involving transfer of abnormal tau seeds from a "donor cell" to a "recipient cell" and recruitment of normal tau in the latter to generate new tau seeds. This review critically appraises the evidence that the spread of tau pathology occurs via such a "prion-like" mechanism and proposes a number of recommendations for directing future research. Recommendations for definitions of frequently used terms in the tau field are presented in an attempt to clarify and standardize interpretation of research findings. Molecular and cellular factors affecting tau aggregation are briefly reviewed, as are potential contributions of physiological and pathological post-translational modifications of tau. Additionally, the experimental evidence for tau seeding and "prion-like" propagation of tau aggregation that has emerged from cellular assays and in vivo models is discussed. Propagation of tau pathology using "prion-like" mechanisms is expected to incorporate several steps including cellular uptake, templated seeding, secretion and intercellular transfer through synaptic and non-synaptic pathways. The experimental findings supporting each of these steps are reviewed. The clinical validity of these experimental findings is then debated by considering the supportive or contradictory findings from patient samples. Further, the role of physiological tau release in this scenario is examined because emerging data shows that tau is secreted but the physiological function (if any) of this secretion in the context of propagation of pathological tau seeds is unclear. Bona fide prions exhibit specific properties, including transmission from cell to cell, tissue to tissue and organism to organism. The propagation of tau pathology has so far not been shown to exhibit all of these steps and how this influences the debate of whether or not abnormal tau species can propagate in a "prion-like" manner is discussed. The exact nature of tau seeds responsible for propagation of tau pathology in human tauopathies remains controversial; it might be tightly linked to the existence of tau strains stably propagating peculiar patterns of neuropathological lesions, corresponding to the different patterns seen in human tauopathies. That this is a property shared by all seed-competent tau conformers is not yet firmly established. Further investigation is also required to clarify the relationship between propagation of tau aggregates and tau-induced toxicity. Genetic variants identified as risks factors for tauopathies might play a role in propagation of tau pathology, but many more studies are needed to document this. The contribution of selective vulnerability of neuronal populations, as an alternative to prion-like mechanisms to explain spreading of tau pathology needs to be clarified. Learning from the prion field will be helpful to enhance our understanding of propagation of tau pathology. Finally, development of better models is expected to answer some of these key questions and allow for the testing of propagation-centred therapies.
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?
Pathogenic tau can be released from diseased neurons, taken up by previously unaffected normal neurons, and induce pathogenic tau production in normal neurons.
“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 [41]
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
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
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 · see citing works
Phases of Aβ-deposition in the human brain and its relevance for the development of AD
Thal, D. R., Rüb, U., Orantes, M., & Braak, H. (2002) · Neurology · doi:10.1212/wnl.58.12.1791 · Cited by 3,490 · see citing works
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 · see citing works
Self-citationCryo-EM structures of tau filaments from Alzheimer’s disease
Fitzpatrick, A. W. P., Falcon, B., He, S., Murzin, A. G., Murshudov, G., Garringer, H. J., Crowther, R. A., Ghetti, B., Goedert, M., & Scheres, S. H. W. (2017) · Nature · doi:10.1038/nature23002 · Cited by 2,061 · see citing works
Self-citationTau Suppression in a Neurodegenerative Mouse Model Improves Memory Function
SantaCruz, K., Lewis, J., Spires, T., Paulson, J., Kotilinek, L., Ingelsson, M., Guimaraes, A., DeTure, M., Ramsden, M., McGowan, E., et al. (2005) · Science · doi:10.1126/science.1113694 · Cited by 2,014 · see citing works
Buée, L., Bussière, T., Buée‐Scherrer, V., Delacourte, A., & Hof, P. R. (2000) · Brain Research Reviews · doi:10.1016/s0165-0173(00)00019-9 · Cited by 2,007 · see citing works
Self-citationTransmission and spreading of tauopathy in transgenic mouse brain
Clavaguera, F., Bolmont, T., Crowther, R. A., Abramowski, D., Frank, S., Probst, A., Fraser, G., Stalder, A. K., Beibel, M., Staufenbiel, M., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1901 · Cited by 1,803 · see citing works
Self-citationEnhanced 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
Depletion of microglia and inhibition of exosome synthesis halt tau propagation
Asai, H., Ikezu, S., Tsunoda, S., Medalla, M., Luebke, J., Haydar, T., Wolozin, B., Butovsky, O., Kügler, S., & Ikezu, T. (2015) · Nature Neuroscience · doi:10.1038/nn.4132 · Cited by 1,591 · 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
Mutation in the tau gene in familial multiple system tauopathy with presenile dementia
Spillantini, M. G., Murrell, J. R., Goedert, M., Farlow, M. R., Klug, A., & Ghetti, B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.13.7737 · Cited by 1,474 · see citing works
Self-citationPropagation of Tau Pathology in a Model of Early Alzheimer's Disease
de Calignon, A., Polydoro, M., Suárez-Calvet, M., William, C., Adamowicz, D. H., Kopeikina, K. J., Pitstick, R., Sahara, N., Ashe, K. H., Carlson, G. A., et al. (2012) · Neuron · doi:10.1016/j.neuron.2011.11.033 · Cited by 1,427 · see citing works
ApoE4 markedly exacerbates tau-mediated neurodegeneration in a mouse model of tauopathy
Initiative, A. D. N., Shi, Y., Yamada, K., Liddelow, S. A., Smith, S. T., Zhao, L., Luo, W., Tsai, R. M., Spina, S., Grinberg, L. T., et al. (2017) · Nature · doi:10.1038/nature24016 · Cited by 1,220 · see citing works
Goedert, M., Wischik, C. M., Crowther, R. A., Walker, J. E., & Klug, A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.11.4051 · Cited by 1,134 · see citing works
Self-citationGoedert, M., Jakes, R., Spillantini, M. G., Hasegawa, M., Smith, M. J., & Crowther, R. A. (1996) · Nature · doi:10.1038/383550a0 · Cited by 1,036 · see citing works
Self-citationvon Bergen, M., Friedhoff, P., Biernat, J., Heberle, J., Mandelkow, E.-M., & Mandelkow, E. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.10.5129 · Cited by 1,021 · see citing works
Self-citationRoles 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
Trans-Synaptic Spread of Tau Pathology In Vivo
Liu, L., Drouet, V., Wu, J., Witter, M. P., Small, S. A., Clelland, C. L. T., & Duff, K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031302 · Cited by 994 · see citing works
Distinct Tau Prion Strains Propagate in Cells and Mice and Define Different Tauopathies
Sanders, D. W., Kaufman, S. K., DeVos, S. L., Sharma, A. M., Mirbaha, H., Li, A., Barker, S. J., Foley, A. C., Thorpe, J. R., Serpell, L. C., et al. (2014) · Neuron · doi:10.1016/j.neuron.2014.04.047 · Cited by 986 · see citing works
Tauopathy in <i>Drosophila</i> : Neurodegeneration Without Neurofibrillary Tangles
Wittmann, C. W., Wszolek, M. F., Shulman, J. M., Salvaterra, P. M., Lewis, J., Hutton, M., & Feany, M. B. (2001) · Science · doi:10.1126/science.1062382 · Cited by 939 · see citing works
The genetic landscape of Alzheimer disease: clinical implications and perspectives
Van Cauwenberghe, C., Van Broeckhoven, C., & Sleegers, K. (2016) · Genetics in Medicine · doi:10.1038/gim.2015.117 · Cited by 863 · see citing works
Heparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds
Holmes, B. B., DeVos, S. L., Kfoury, N., Li, M., Jacks, R., Yanamandra, K., Ouidja, M. O., Brodsky, F. M., Marasa, J., Bagchi, D. P., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1301440110 · Cited by 859 · see citing works
Caspase cleavage of tau: Linking amyloid and neurofibrillary tangles in Alzheimer's disease
Gamblin, T. C., Chen, F., Zambrano, A., Abraha, A., Lagalwar, S., Guillozet, A. L., Lu, M., Fu, Y., Garcia-Sierra, F., LaPointe, N., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1630428100 · Cited by 831 · see citing works
Neuronal activity enhances tau propagation and tau pathology in vivo
Wu, J. W., Hussaini, S. A., Bastille, I. M., Rodriguez, G. A., Mrejeru, A., Rilett, K., Sanders, D. W., Cook, C., Fu, H., Boonen, R. A. C. M., et al. (2016) · Nature Neuroscience · doi:10.1038/nn.4328 · Cited by 820 · see citing works
Ambadipudi, S., Biernat, J., Riedel, D., Mandelkow, E., & Zweckstetter, M. (2017) · Nature Communications · doi:10.1038/s41467-017-00480-0 · Cited by 782 · see citing works
Self-citationBrain homogenates from human tauopathies induce tau inclusions in mouse brain
Clavaguera, F., Akatsu, H., Fraser, G. M., Crowther, R. A., Frank, S., Hench, J., Probst, A., Winkler, D. T., Reichwald, J., Staufenbiel, M., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1301175110 · Cited by 750 · see citing works
Self-citationHyperphosphorylation and aggregation of tau in mice expressing normal human tau isoforms
Andorfer, C., Kress, Y., Espinoza, M., De Silva, R., Tucker, K. L., Barde, Y., Duff, K., & Davies, P. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01879.x · Cited by 722 · see citing works
Proteopathic tau seeding predicts tauopathy in vivo
Holmes, B. B., Furman, J. L., Mahan, T. E., Yamasaki, T. R., Mirbaha, H., Eades, W. C., Belaygorod, L., Cairns, N. J., Holtzman, D. M., & Diamond, M. I. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1411649111 · Cited by 696 · see citing works
Distinct α-Synuclein Strains Differentially Promote Tau Inclusions in Neurons
Guo, J. L., Covell, D. J., Daniels, J. P., Iba, M., Stieber, A., Zhang, B., Riddle, D. M., Kwong, L. K., Xu, Y., Trojanowski, J. Q., et al. (2013) · Cell · doi:10.1016/j.cell.2013.05.057 · Cited by 680 · see citing works
The release and trans-synaptic transmission of Tau via exosomes
Wang, Y., Balaji, V., Kaniyappan, S., Krüger, L., Irsen, S., Tepper, K., Chandupatla, R., Maetzler, W., Schneider, A., Mandelkow, E., et al. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0143-y · Cited by 674 · see citing works
Self-citationIba, M., Guo, J. L., McBride, J. D., Zhang, B., Trojanowski, J. Q., & Lee, V. M.-Y. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.2642-12.2013 · Cited by 664 · see citing works
Physiological release of endogenous tau is stimulated by neuronal activity
Pooler, A. M., Phillips, E. C., Lau, D. H. W., Noble, W., & Hanger, D. P. (2013) · The EMBO Reports · doi:10.1038/embor.2013.15 · Cited by 642 · see citing works
Tau oligomers impair memory and induce synaptic and mitochondrial dysfunction in wild-type mice
Lasagna-Reeves, C. A., Castillo-Carranza, D. L., Sengupta, U., Clos, A. L., Jackson, G. R., & Kayed, R. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-39 · Cited by 633 · see citing works
Propagation of Tau aggregates and neurodegeneration
Goedert, M., Eisenberg, D. S., & Crowther, R. A. (2017) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-072116-031153 · Cited by 632 · see citing works
Self-citationArendt, T., Stieler, J. T., & Holzer, M. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.08.018 · Cited by 609 · see citing works
Identification of common variants influencing risk of the tauopathy progressive supranuclear palsy
PSP Genetics Study Group, Höglinger, G. U., Melhem, N. M., Dickson, D. W., Sleiman, P. M. A., Wang, L.-S., Klei, L., Rademakers, R., de Silva, R., Litvan, I., et al. (2011) · Nature Genetics · doi:10.1038/ng.859 · Cited by 603 · see citing works
Structural characterization of the core of the paired helical filament of Alzheimer disease.
Wischik, C. M., Novák, M., Edwards, P. C., Klug, A., Tichelaar, W., & Crowther, R. A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.13.4884 · Cited by 597 · see citing works
Matsuo, E. S., Shin, R., Billingsley, M., de Voorde, A. V., O'Connor, M., Trojanowski, J., & Lee, V. (1994) · Neuron · doi:10.1016/0896-6273(94)90264-x · Cited by 588 · see citing works
Yanamandra, K., Kfoury, N., Jiang, H., Mahan, T. E., Ma, S., Maloney, S. E., Wozniak, D. F., Diamond, M. I., & Holtzman, D. M. (2013) · Neuron · doi:10.1016/j.neuron.2013.07.046 · Cited by 574 · see citing works
Neuronal activity regulates extracellular tau in vivo
Yamada, K., Holth, J. K., Liao, F., Stewart, F. R., Mahan, T. E., Jiang, H., Cirrito, J. R., Patel, T. K., Hochgräfe, K., Mandelkow, E., et al. (2014) · The Journal of Experimental Medicine · doi:10.1084/jem.20131685 · Cited by 574 · see citing works
Self-citationSchneider, A., Biernat, J., von Bergen, M., Mandelkow, E., & Mandelkow, E.-M. (1999) · Biochemistry · doi:10.1021/bi981874p · Cited by 564 · see citing works
Self-citationKampers, T., Friedhoff, P., Biernat, J., Mandelkow, E.-M., & Mandelkow, E. (1996) · FEBS Letters · doi:10.1016/s0014-5793(96)01386-5 · Cited by 548 · see citing works
Self-citationIdentification of oligomers at early stages of tau aggregation in Alzheimer's disease
Lasagna‐Reeves, C. A., Castillo‐Carranza, D. L., Sengupta, U., Sarmiento, J., Troncoso, J., Jackson, G. R., & Kayed, R. (2012) · The FASEB Journal · doi:10.1096/fj.11-199851 · Cited by 527 · see citing works
Evidence for human transmission of amyloid-β pathology and cerebral amyloid angiopathy
Jaunmuktane, Z., Mead, S., Ellis, M., Wadsworth, J. D. F., Nicoll, A. J., Kenny, J., Launchbury, F., Linehan, J., Richard-Loendt, A., Walker, A. S., et al. (2015) · Nature · doi:10.1038/nature15369 · Cited by 518 · see citing works
Invited review: Neuropathology of tauopathies: principles and practice
Kovacs, G. G. (2015) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12208 · Cited by 492 · see citing works
Accumulation of Pathological Tau Species and Memory Loss in a Conditional Model of Tauopathy
Berger, Z., Roder, H. M., Hanna, A., Carlson, A. M., Rangachari, V., Yue, M., Wszołek, Z. K., Ashe, K. H., Knight, J. A., Dickson, D. W., et al. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.0587-07.2007 · Cited by 485 · see citing works
Morris, 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
Ahmed, Z., Cooper, J., Murray, T. K., Garn, K., McNaughton, E., Clarke, H., Parhizkar, S., Ward, M. A., Cavallini, A., Jackson, S., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1254-6 · Cited by 460 · see citing works
Self-citationKaufman, S. K., Sanders, D. W., Thomas, T. L., Ruchinskas, A. J., Vaquer-Alicea, J., Sharma, A. M., Miller, T. M., & Diamond, M. I. (2016) · Neuron · doi:10.1016/j.neuron.2016.09.055 · Cited by 450 · see citing works
Götz, J., Probst, A., Spillantini, M. G., Schäfer, T., Jakes, R., Bürki, K., & Goedert, M. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07116.x · Cited by 441 · see citing works
Self-citationGhetti, B. F., Oblak, A. L., Boeve, B. F., Johnson, K. A., Dickerson, B. C., & Goedert, M. (2014) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12213 · Cited by 440 · see citing works
Self-citationGuo, J. L., Narasimhan, S., Changolkar, L., He, Z., Stieber, A., Zhang, B., Gathagan, R. J., Iba, M., McBride, J. D., Trojanowski, J. Q., et al. (2016) · Journal of Experimental Medicine · doi:10.1084/jem.20160833 · Cited by 440 · see citing works
Braak, H., Braak, E., Grundke-Iqbal, I., & Iqbal, K. (1986) · Neuroscience Letters · doi:10.1016/0304-3940(86)90288-0 · Cited by 432 · see citing works
Interactions of pathological proteins in neurodegenerative diseases
Spires‐Jones, T. L., Attems, J., & Thal, D. R. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1709-7 · Cited by 424 · see citing works
Increased expression of BIN1 mediates Alzheimer genetic risk by modulating tau pathology
GERAD consortium, Chapuis, J., Hansmannel, F., Gistelinck, M., Mounier, A., Van Cauwenberghe, C., Kolen, K. V., Geller, F., Sottejeau, Y., Harold, D., et al. (2013) · Molecular Psychiatry · doi:10.1038/mp.2013.1 · Cited by 407 · see citing works
Self-citationSpittaels, K., den Haute, C. V., Dorpe, J. V., Bruynseels, K., Vandezande, K., Laenen, I., Geerts, H., Mercken, M., Sciot, R., Lommel, A. V. V., et al. (1999) · American Journal of Pathology · doi:10.1016/s0002-9440(10)65533-2 · Cited by 405 · see citing works
Planel, E., Richter, K. E. G., Nolan, C. E., Finley, J. E., Liu, L., Wen, Y., Krishnamurthy, P., Herman, M., Wang, L., Schachter, J. B., et al. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.4854-06.2007 · Cited by 386 · see citing works
Arendt, T., Stieler, J., Strijkstra, A. M., Hut, R. A., Rüdiger, J., Van der Zee, E. A., Harkany, T., Holzer, M., & Härtig, W. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-18-06972.2003 · Cited by 357 · see citing works
Pérez, M., Valpuesta, J., Medina, M., de Garcini, E. M., & Ávila, J. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.67031183.x · Cited by 355 · see citing works
Self-citation(1997) · Europe PMC (PubMed Central) · Cited by 354 · 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
Self-citationDetection of Phosphorylated Ser262 in Fetal Tau, Adult Tau, and Paired Helical Filament Tau
Seubert, P., Mawal-Dewan, M., Barbour, R., Jakes, R., Goedert, M., Johnson, G. V. W., Litersky, J. M., Schenk, D., Lieberburg, I., Trojanowski, J. Q., et al. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.32.18917 · Cited by 345 · see citing works
Self-citationKovács, G. G. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17020189 · Cited by 321 · see citing works
Cook, C. N., Carlomagno, Y., Gendron, T. F., Dunmore, J. H., Scheffel, K., Stetler, C. T., Davis, M., Dickson, D. W., Jarpe, M. B., Deture, M. A., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt402 · Cited by 309 · see citing works
RNA stores tau reversibly in complex coacervates
Zhang, X., Lin, Y., Eschmann, N. A., Zhou, H., Rauch, J. N., Hernández, I., Guzman, E., Kosik, K. S., & Han, S. (2017) · PLoS Biology · doi:10.1371/journal.pbio.2002183 · Cited by 308 · see citing works
Tunneling nanotube (TNT)-mediated neuron-to neuron transfer of pathological Tau protein assemblies
Tardivel, M., Bégard, S., Bousset, L., Dujardin, S., Coens, A., Melki, R., Buée, L., & Colin, M. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0386-4 · Cited by 305 · see citing works
Self-citationA critical appraisal of the pathogenic protein spread hypothesis of neurodegeneration
Walsh, D. M., & Selkoe, D. J. (2016) · Nature reviews. Neuroscience · doi:10.1038/nrn.2016.13 · Cited by 290 · see citing works
Apolipoprotein E4 Impairs Neuronal Insulin Signaling by Trapping Insulin Receptor in the Endosomes
Zhao, N., Liu, C.-C., Van Ingelgom, A. J., Martens, Y. A., Linares, C., Knight, J. A., Painter, M. M., Sullivan, P. M., & Bu, G. (2017) · Neuron · doi:10.1016/j.neuron.2017.09.003 · Cited by 289 · see citing works
Bolmont, T., Clavaguera, F., Meyer-Luehmann, M., Herzig, M. C., Radde, R., Staufenbiel, M., Lewis, J., Hutton, M., Tolnay, M., & Jucker, M. (2007) · The American Journal of Pathology · doi:10.2353/ajpath.2007.070403 · Cited by 281 · see citing works
PICALM modulates autophagy activity and tau accumulation
Moreau, K., Fleming, A., Imarisio, S., Lopez Ramirez, A., Mercer, J. L., Jimenez-Sanchez, M., Bento, C. F., Puri, C., Zavodszky, E., Siddiqi, F., et al. (2014) · Nature Communications · doi:10.1038/ncomms5998 · Cited by 281 · see citing works
Acetylated tau, a novel pathological signature in Alzheimer's disease and other tauopathies
Irwin, D. J., Cohen, T. J., Grossman, M., Arnold, S. E., Xie, S. X., Lee, V. M.-Y., & Trojanowski, J. Q. (2012) · Brain · doi:10.1093/brain/aws013 · Cited by 281 · see citing works
Polanco, J. C., Scicluna, B. J., Hill, A. F., & Götz, J. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.709485 · Cited by 271 · see citing works
GSK-3β inhibition reverses axonal transport defects and behavioural phenotypes in Drosophila
Mudher, A., Shepherd, D., Newman, T. A., Mildren, P., Jukes, J. P., Squire, A., Mears, A., Berg, S., MacKay, D., Asuni, A. A., et al. (2004) · Molecular Psychiatry · doi:10.1038/sj.mp.4001483 · Cited by 265 · see citing works
Self-citationDujardin, S., Lécolle, K., Caillierez, R., Bégard, S., Zommer, N., Lachaud, C., Carrier, S., Dufour, N., Aurégan, G., Winderickx, J., et al. (2014) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-2-14 · Cited by 259 · see citing works
Self-citationSynaptic Contacts Enhance Cell-to-Cell Tau Pathology Propagation
Calafate, S., Buist, A., Miśkiewicz, K., Vijayan, V. A., Daneels, G., Strooper, B. D., de Wit, J., Verstreken, P., & Moechars, D. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.04.043 · Cited by 257 · see citing works
Conformation Determines the Seeding Potencies of Native and Recombinant Tau Aggregates
Falcon, B., Cavallini, A., Angers, R. C., Glover, S. J., Murray, T. K., Barnham, L., Jackson, S., O'Neill, M. J., Isaacs, A. M., Hutton, M. L., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.589309 · Cited by 252 · see citing works
Self-citationIdentification of the Tau phosphorylation pattern that drives its aggregation
Despres, C., Byrne, C., Qi, H., Cantrelle, F., Huvent, I., Chambraud, B., Baulieu, É.-É., Jacquot, Y., Landrieu, I., Lippens, G. M., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1708448114 · Cited by 246 · see citing works
Hallmarks of Alzheimer’s Disease in Stem-Cell-Derived Human Neurons Transplanted into Mouse Brain
Espuny-Camacho, I., Arranz, A. M., Fiers, M., Snellinx, A., Ando, K., Munck, S., Bonnefont, J., Lambot, L., Corthout, N., Omodho, L., et al. (2017) · Neuron · doi:10.1016/j.neuron.2017.02.001 · Cited by 244 · see citing works
Self-citationAmyloid accelerates tau propagation and toxicity in a model of early Alzheimer’s disease
Pooler, A. M., Polydoro, M., Maury, E. A., Nicholls, S. B., Reddy, S. M., Wegmann, S., William, C., Saqran, L., Cagsal-Getkin, O., Pitstick, R., et al. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0199-x · Cited by 236 · see citing works
Gómez‐Ramos, A., Dı́az-Hernández, M., Rubio, A., Miras‐Portugal, M. T., & Ávila, J. (2008) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2007.12.010 · Cited by 233 · see citing works
Mammalian prions and their wider relevance in neurodegenerative diseases
Collinge, J. (2016) · Nature · doi:10.1038/nature20415 · Cited by 231 · see citing works
Iba, M., McBride, J. D., Guo, J. L., Zhang, B., Trojanowski, J. Q., & Lee, V. M.-Y. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1458-4 · Cited by 223 · see citing works
Lewis, J. M., & Dickson, D. W. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1507-z · Cited by 221 · see citing works
Ectosomes: A New Mechanism for Non-Exosomal Secretion of Tau Protein
Dujardin, S., Bégard, S., Caillierez, R., Lachaud, C., Delattre, L., Carrier, S., Loyens, A., Galas, M., Bousset, L., Melki, R., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0100760 · Cited by 215 · see citing works
Self-citationMirbaha, H., Holmes, B. B., Sanders, D. W., Bieschke, J., & Diamond, M. I. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.652693 · Cited by 215 · see citing works
Are tau aggregates toxic or protective in tauopathies?
Cowan, C. M., & Mudher, A. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00114 · Cited by 215 · see citing works
Self-citationPeeraer, 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
Self-citationGoedert, M., & Spillantini, M. G. (2017) · Molecular Brain · doi:10.1186/s13041-017-0298-7 · Cited by 213 · see citing works
Self-citationAbounit, S., Wu, J. W., Duff, K., Victoria, G. S., & Zurzolo, C. (2016) · Prion · doi:10.1080/19336896.2016.1223003 · Cited by 206 · see citing works
Alzheimer-like Changes in Microtubule-associated Protein Tau Induced by Sulfated Glycosaminoglycans
Hasegawa, M., Crowther, R. A., Jakes, R., & Goedert, M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.52.33118 · Cited by 205 · see citing works
Self-citationTaniguchi-Watanabe, S., Arai, T., Kametani, F., Nonaka, T., Masuda-Suzukake, M., Tarutani, A., Murayama, S., Saito, Y., Arima, K., Yoshida, M., et al. (2016) · Acta Neuropathologica · doi:10.1007/s00401-015-1503-3 · Cited by 200 · see citing works
Brion, J., Passareiro, H., Nunez, J., & Durand, J. F. (1985) · Dépôt institutionnel de l'Université libre de Bruxelles (Université Libre de Bruxelles) · Cited by 197 · see citing works
Self-citationBrion, J., Tremp, G. L., & Octave, J. (1999) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)65272-8 · Cited by 197 · see citing works
Self-citationSilver diagnosis in neuropathology: principles, practice and revised interpretation
Uchihara, T. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0200-2 · Cited by 197 · see citing works
Vasconcelos, B., Stancu, I.-C., Buist, A., Bird, M., Wang, P., Vanoosthuyse, A., Van Kolen, K., Verheyen, A., Kienlen-Campard, P., Octave, J.-N., et al. (2016) · Acta Neuropathologica · doi:10.1007/s00401-015-1525-x · Cited by 192 · see citing works
Self-citationAbnormal Tau-Containing Filaments in Neurodegenerative Diseases
Crowther, R. A., & Goedert, M. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4270 · Cited by 185 · see citing works
Self-citationCastillo‐Carranza, D. L., Gerson, J. E., Sengupta, U., Guerrero‐Munoz, M. J., Lasagna‐Reeves, C. A., & Kayed, R. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-132477 · Cited by 180 · see citing works
Extracellular Tau Levels Are Influenced by Variability in Tau That Is Associated with Tauopathies
Karch, C. M. M., Jeng, A. T., & Goate, A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.380642 · Cited by 171 · see citing works
Triggers of Full-Length Tau Aggregation: A Role for Partially Folded Intermediates
Chirita, C. N., Congdon, E. E., Yin, H., & Kuret, J. (2005) · Biochemistry · doi:10.1021/bi0500123 · Cited by 166 · see citing works
Prion-like transmission of neuronal huntingtin aggregates to phagocytic glia in the Drosophila brain
Pearce, M. M. P., Spartz, E. J., Hong, W., Luo, L., & Kopito, R. R. (2015) · Nature Communications · doi:10.1038/ncomms7768 · Cited by 159 · see citing works
Invited review: Prion‐like transmission and spreading of tau pathology
Clavaguera, F., Hench, J., Goedert, M., & Tolnay, M. (2015) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12197 · Cited by 156 · see citing works
Self-citationProteostasis of tau. Tau overexpression results in its secretion via membrane vesicles
Simón, D., García‐García, E., Royo, F., Falcón‐Pérez, J. M., & Ávila, J. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.11.022 · Cited by 156 · see citing works
Hasegawa, M., Jakes, R., Crowther, R. A., Lee, V. M.-Y., Ihara, Y., & Goedert, M. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00271-2 · Cited by 156 · see citing works
Self-citationCowan, C. M., Bossing, T., Page, A., Shepherd, D., & Mudher, A. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0716-8 · Cited by 156 · see citing works
Self-citationAccumulation of tau induced in neurites by microglial proinflammatory mediators
Gorlovoy, P., Larionov, S., Pham, T. T. H., & Neumann, H. (2009) · The FASEB Journal · doi:10.1096/fj.08-123877 · Cited by 156 · see citing works
Jackson, S. J., Kerridge, C., Cooper, J., Cavallini, A., Falcon, B., Cella, C. V., Landi, A., Szekeres, P. G., Murray, T. K., Ahmed, Z., et al. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.3542-15.2016 · Cited by 153 · see citing works
Self-citationHyperphosphorylation and Cleavage at D421 Enhance Tau Secretion
Plouffe, V., Mohamed, N., Rivest‐McGraw, J., Bertrand, J., Lauzon, M., & Leclerc, N. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0036873 · Cited by 146 · see citing works
Saijo, E., Ghetti, B. F., Zanusso, G., Oblak, A. L., Furman, J. L., Diamond, M. I., Kraus, A., & Caughey, B. W. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1692-z · Cited by 145 · see citing works
Peripheral administration of tau aggregates triggers intracerebral tauopathy in transgenic mice
Clavaguera, F., Hench, J., Lavenir, I., Schweighauser, G., Frank, S., Goedert, M., & Tolnay, M. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1231-5 · Cited by 143 · see citing works
Self-citationSankaranarayanan, S., Barten, D. M., Vana, L., Devidze, N., Yang, L., Cadelina, G. W., Hoque, N., DeCarr, L. B., Keenan, S., Lin, A., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0125614 · Cited by 143 · see citing works
Stancu, I.-C., Vasconcelos, B., Ris, L., Wang, P., Villers, A., Peeraer, E., Buist, A., Terwel, D., Baatsen, P., Oyelami, T., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1413-4 · Cited by 143 · see citing works
Self-citationFunk, K. E., Thomas, S. N., Schafer, K. N., Cooper, G. L., Liao, Z., Clark, D. J., Yang, A. J., & Kuret, J. (2014) · Biochemical Journal · doi:10.1042/bj20140372 · Cited by 142 · see citing works
Widespread tau seeding activity at early Braak stages
Furman, J. L., Vaquer‐Alicea, J., White, C. L., Cairns, N. J., Nelson, P. T., & Diamond, M. I. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1644-z · Cited by 142 · see citing works
Reynolds, M. R., Reyes, J. F., Fu, Y., Bigio, E. H., Guillozet-Bongaarts, A. L., Berry, R. W., & Binder, L. I. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.2143-06.2006 · Cited by 140 · see citing works
Ando, K., Brion, J.-P., Stygelbout, V., Suain, V., Authelet, M., Dedecker, R., Chanut, A., Lacor, P., Lavaur, J., Sazdovitch, V., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1111-z · Cited by 136 · see citing works
Self-citationRemoving endogenous tau does not prevent tau propagation yet reduces its neurotoxicity
Wegmann, S., Maury, E. A., Kirk, M. J., Saqran, L., Roe, A., DeVos, S. L., Nicholls, S., Fan, Z., Takeda, S., Cagsal‐Getkin, O., et al. (2015) · The EMBO Journal · doi:10.15252/embj.201592748 · Cited by 132 · see citing works
Hyperphosphorylation determines both the spread and the morphology of tau pathology
Hu, W. H., Zhang, X., Tung, Y. C., Xie, S.-T., Liu, F., & Iqbal, K. (2016) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2016.01.014 · Cited by 131 · see citing works
Acetylated Tau Neuropathology in Sporadic and Hereditary Tauopathies
Irwin, D. J., Cohen, T. J., Grossman, M., Arnold, S. E., McCarty-Wood, E., Van Deerlin, V. M., Lee, V. M.-Y., & Trojanowski, J. Q. (2013) · The American Journal of Pathology · doi:10.1016/j.ajpath.2013.04.025 · Cited by 125 · see citing works
Thomas, S. N., Funk, K. E., Wan, Y., Liao, Z., Davies, P., Kuret, J., & Yang, A. J. (2012) · Acta Neuropathologica · doi:10.1007/s00401-011-0893-0 · Cited by 123 · see citing works
Tau isoform composition influences rate and extent of filament formation
Zhong, Q., Congdon, E. E., Nagaraja, H. N., & Kuret, J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.364067 · Cited by 122 · see citing works
Nobuhara, C. K., DeVos, S. L., Commins, C., Wegmann, S., Moore, B. D., Roe, A. D., Costantino, I., Frosch, M. P., Pitstick, R., Carlson, G. A., et al. (2017) · The American Journal of Pathology · doi:10.1016/j.ajpath.2017.01.022 · Cited by 120 · see citing works
Dourlen, P., Fernandez-Gomez, F. J., Dupont, C., Grenier-Boley, B., Bellenguez, C., Obriot, H., Caillierez, R., Sottejeau, Y., Chapuis, J., Bretteville, A., et al. (2017) · Molecular Psychiatry · doi:10.1038/mp.2016.59 · Cited by 118 · see citing works
Self-citationTakeda, S., Commins, C., DeVos, S. L., Nobuhara, C. K., Wegmann, S., Roe, A. D., Costantino, I., Fan, Z., Nicholls, S. B., Sherman, A. E., et al. (2016) · Annals of Neurology · doi:10.1002/ana.24716 · Cited by 113 · see citing works
Are Tangles as Toxic as They Look?
Spires‐Jones, T. L., Kopeikina, K. J., Koffie, R. M., de Calignon, A., & Hyman, B. T. (2011) · Journal of Molecular Neuroscience · doi:10.1007/s12031-011-9566-7 · Cited by 110 · see citing works
Three Repeat Isoforms of Tau Inhibit Assembly of Four Repeat Tau Filaments
Adams, S. J., Deture, M. A., McBride, M., Dickson, D. W., & Petrucelli, L. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010810 · Cited by 104 · see citing works
Bussière, T., Hof, P. R., Vanbesien-Mailliot, C., Brown, C., Caillet‐Boudin, M., Perl, D. P., Buée, L., & Delacourte, A. (1999) · Acta Neuropathologica · doi:10.1007/s004010050978 · Cited by 102 · see citing works
Self-citationWray, S., Saxton, M., Anderton, B. H., & Hanger, D. P. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05321.x · Cited by 97 · see citing works
Characterization of tau prion seeding activity and strains from formaldehyde-fixed tissue
Kaufman, S. K., Thomas, T. L., Tredici, K. D., Braak, H., & Diamond, M. I. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0442-8 · Cited by 97 · see citing works
17q21.31 duplication causes prominent tau-related dementia with increased MAPT expression
Guennec, K. L., Quenez, O., Nicolas, G., Wallon, D., Rousseau, S., Richard, A.-C., Alexander, J., Paschou, P., Charbonnier, C., Bellenguez, C., et al. (2016) · Molecular Psychiatry · doi:10.1038/mp.2016.226 · Cited by 96 · see citing works
Characteristics and consequences of muscarinic receptor activation by tau protein
Gómez‐Ramos, A., Dı́az-Hernández, M., Rubio, A., Díaz‐Hernandéz, J. I., Miras‐Portugal, M. T., & Ávila, J. (2009) · European Neuropsychopharmacology · doi:10.1016/j.euroneuro.2009.04.006 · Cited by 95 · see citing works
Gilley, J., Seereeram, A., Ando, K., Mosely, S. I. S., Andrews, S., Kerschensteiner, M., Misgeld, T., Brion, J., Anderton, B. H., Hanger, D. P., et al. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.02.014 · Cited by 92 · see citing works
Self-citationExtracellular association of APP and tau fibrils induces intracellular aggregate formation of tau
Takahashi, M., Miyata, H., Kametani, F., Nonaka, T., Akiyama, H., Hisanaga, S., & Hasegawa, M. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1415-2 · Cited by 90 · see citing works
Activated microglia proliferate at neurites of mutant huntingtin-expressing neurons
Kraft, A. D., Kaltenbach, L. S., Lo, D. C., & Harry, G. J. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.02.015 · Cited by 90 · see citing works
Dujardin, S., Colin, M., & Buée, L. (2014) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12200 · Cited by 88 · see citing works
Self-citationHéraud, C., Goufak, D., Ando, K., Leroy, K., Suain, V., Yilmaz, Z., De Decker, R., Authelet, M., Laporte, V., Octave, J.-N., et al. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.09.010 · Cited by 80 · see citing works
Self-citationEisele, Y. S., & Duyckaerts, C. J. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1516-y · Cited by 78 · see citing works
Dissociation of Alzheimer type pathology in a disconnected piece of cortex
Duyckaerts, C. J., Uchihara, T., Seilhean, D., He, Y., & Hauw, J. (1997) · Acta Neuropathologica · doi:10.1007/s004010050645 · Cited by 71 · see citing works
Audouard, E., Houben, S., Masaracchia, C., Yilmaz, Z., Suain, V., Authelet, M., Decker, R. D., Buée, L., Boom, A., Leroy, K., et al. (2016) · American Journal Of Pathology · doi:10.1016/j.ajpath.2016.06.008 · Cited by 68 · see citing works
Self-citationScott, J. R., Davies, D., & Fraser, H. (1992) · Journal of General Virology · doi:10.1099/0022-1317-73-7-1637 · Cited by 67 · see citing works
Ando, K., Tomimura, K., Sazdovitch, V., Suain, V., Yilmaz, Z., Authelet, M., Ndjim, M., Vergara, C., Belkouch, M., Potier, M., et al. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.05.017 · Cited by 67 · see citing works
Self-citationThe 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 62 · see citing works
Self-citationRodríguez, L. C. D. L. C., Mohamed, N., Desjardins, A., Lippé, R., Fon, E. A., & Leclerc, N. M. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.13994 · Cited by 61 · see citing works
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 59 · see citing works
Alibhai, J. D., Blanco, R. A., Barria, M. A., Piccardo, P., Caughey, B. W., Perry, V. H., Freeman, T. C., & Manson, J. C. (2016) · PLoS Biology · doi:10.1371/journal.pbio.1002579 · Cited by 56 · see citing works
Co-expression of truncated and full-length tau induces severe neurotoxicity
Özcelik, S., Sprenger, F., Skachokova, Z. K., Fraser, G., Abramowski, D., Clavaguera, F., Probst, A., Frank, S., Müller, M. M., Staufenbiel, M., et al. (2016) · Molecular Psychiatry · doi:10.1038/mp.2015.228 · Cited by 54 · see citing works
Self-citationThe self-perpetuating tau truncation circle
Žilka, N., Kováčech, B., Baráth, P., Kontseková, E., & Novák, M. (2012) · Biochemical Society Transactions · doi:10.1042/bst20120015 · Cited by 50 · see citing works
Tau secretion is correlated to an increase of Golgi dynamics
Mohamed, N., Desjardins, A., & Leclerc, N. M. (2017) · PLoS ONE · doi:10.1371/journal.pone.0178288 · Cited by 50 · see citing works
Rescue from tau-induced neuronal dysfunction produces insoluble tau oligomers
Cowan, C. M., Quraishe, S., Hands, S. L., Sealey, M. A., Mahajan, S., Allan, D. W., & Mudher, A. K. (2015) · Scientific Reports · doi:10.1038/srep17191 · Cited by 39 · see citing works
Self-citationYetman, M. J., Lillehaug, S., Bjaalie, J. G., Leergaard, T. B., & Jankowsky, J. L. (2015) · Brain Structure and Function · doi:10.1007/s00429-015-1040-9 · Cited by 34 · see citing works
Mislocalization of neuronal tau in the absence of tangle pathology in phosphomutant tau knockin mice
Gilley, J., Ando, K., Seereeram, A., Rodríguez-Martín, T., Pooler, A. M., Sturdee, L., Anderton, B. H., Brion, J., Hanger, D. P., & Coleman, M. P. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.11.028 · Cited by 25 · see citing works
Self-citationAD genetic risk factors and tau spreading
Ávila, J., Gómez‐Ramos, A., & Bolós, M. (2015) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2015.00099 · Cited by 19 · see citing works
Mudher, A. K., WOOLLEY, S. T., Perry, V. H., & Greene, J. R. T. (1999) · Journal of Neuroscience Methods · doi:10.1016/s0165-0270(99)00006-0 · Cited by 8 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Tau PTM Profiles Identify Patient Heterogeneity and Stages of Alzheimer’s Disease
Wesseling, H., Mair, W., Kumar, M., Schlaffner, C. N., Tang, S., Beerepoot, P., Fatou, B., Guise, A. J., Cheng, L., Takeda, S., et al. (2020) · Cell · doi:10.1016/j.cell.2020.10.029 · Cited by 688 · see citing works
“…of Tau pathology with cognitive decline in AD (Arriagada et al., 1992; Bierer et al., 1995; Giannakopoulos et al., 2003; Gómez-Isla et al., 1997) have led to several mechanistic studies whose outcomes have underscored the importance of Tau in AD and other dementias (Mudher et al., 2017).”
ResultSelf-citationSelective vulnerability in neurodegenerative diseases
Fu, H., Hardy, J., & Duff, K. E. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0221-2 · Cited by 585 · see citing works
Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation
Chen, Y., & Yu, Y. (2023) · Journal of Neuroinflammation · doi:10.1186/s12974-023-02853-3 · Cited by 516 · see citing works
“This property of pathogenic tau leads to disease progression and broader clinical symptoms [41, 42].”
BackgroundStancu, I.-C., Cremers, N., Vanrusselt, H., Couturier, J., Vanoosthuyse, A., Kessels, S., Lodder, C., Brône, B., Huaux, F., Octave, J.-N., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-018-01957-y · Cited by 447 · see citing works
Self-citationHyperphosphorylation 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
The human connectome in Alzheimer disease — relationship to biomarkers and genetics
Yu, M., Sporns, O., & Saykin, A. J. (2021) · Nature Reviews Neurology · doi:10.1038/s41582-021-00529-1 · Cited by 265 · see citing works
Tau activates microglia via the PQBP1-cGAS-STING pathway to promote brain inflammation
Jin, M., Shiwaku, H., Tanaka, H., Obita, T., Ohuchi, S., Yoshioka, Y., Jin, X., Kondo, K., Fujita, K., Homma, H., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-26851-2 · Cited by 223 · see citing works
Intersection of pathological tau and microglia at the synapse
Vogels, T., Murgoci, A.-N., & Hromádka, T. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0754-y · Cited by 197 · see citing works
Tau Proteolysis in the Pathogenesis of Tauopathies: Neurotoxic Fragments and Novel Biomarkers
Quinn, J. P., Corbett, N. J., Kellett, K. A. B., & Hooper, N. M. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-170959 · Cited by 170 · see citing works
Braak, H., & Del Tredici, K. (2018) · Cerebral Cortex · doi:10.1093/cercor/bhy152 · Cited by 148 · see citing works
Astroglia and Tau: New Perspectives
Kovacs, G. G. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00096 · Cited by 115 · see citing works
Genetic determinants of survival in progressive supranuclear palsy: a genome-wide association study
Jabbari, E., Koga, S., Valentino, R. R., Reynolds, R. H., Ferrari, R., Tan, M. M. X., Rowe, J. B., Dalgard, C. L., Scholz, S. W., Dickson, D. W., et al. (2021) · The Lancet Neurology · doi:10.1016/s1474-4422(20)30394-x · Cited by 111 · see citing works
Filamentous recombinant human Tau activates primary astrocytes via an integrin receptor complex
Wang, P., & Ye, Y. (2021) · Nature Communications · doi:10.1038/s41467-020-20322-w · Cited by 93 · see citing works
Tau immunotherapies: Lessons learned, current status and future considerations
Sandusky-Beltran, L. A., & Sigurdsson, E. M. (2020) · Neuropharmacology · doi:10.1016/j.neuropharm.2020.108104 · Cited by 90 · see citing works
Ten Years of Tau-Targeted Immunotherapy: The Path Walked and the Roads Ahead
Novak, P., Kontsekova, E., Zilka, N., & Novak, M. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00798 · Cited by 87 · see citing works
“Seeding-capable tau molecules (“tauons”) convert healthy tau into pathological forms, and propagate tau pathology from cell to cell via multiple pathways (Novak et al., 2011; Mudher et al., 2017).”
BackgroundThe <scp>NLRP3</scp> inflammasome modulates tau pathology and neurodegeneration in a tauopathy model
Stancu, I. C., Lodder, C., Botella Lucena, P., Vanherle, S., Gutiérrez de Ravé, M., Terwel, D., Bottelbergs, A., & Dewachter, I. (2022) · Glia · doi:10.1002/glia.24160 · Cited by 72 · see citing works
Self-citationSeidler, P. M., Boyer, D. R., Murray, K. A., Yang, T. P., Bentzel, M., Sawaya, M. R., Rosenberg, G., Cascio, D., Williams, C. K., Newell, K. L., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.009688 · Cited by 70 · see citing works
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 · see citing works
Mallucci, G. R., Klenerman, D., & Rubinsztein, D. C. (2020) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-040320-120625 · Cited by 62 · see citing works
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 · see citing works
Seizures are a druggable mechanistic link between TBI and subsequent tauopathy.
Alyenbaawi, H., Kanyo, R., Locskai, L. F., Kamali-Jamil, R., DuVal, M. G., Bai, Q., Wille, H., Burton, E. A., & Allison, W. T. (2021) · eLife · doi:10.7554/elife.58744 · Cited by 40 · see citing works
The Effects of Amyloid and Tau on Functional Network Connectivity in Older Populations
Wales, R. M., & Leung, H.-C. (2021) · Brain Connectivity · doi:10.1089/brain.2020.0902 · Cited by 26 · see citing works
Maeda, S., & Takashima, A. (2019) · Advances in Experimental Medicine and Biology · doi:10.1007/978-981-32-9358-8_27 · Cited by 22 · see citing works
Continuous Monitoring of Tau-Induced Neurotoxicity in Patient-Derived iPSC-Neurons
Oakley, D. H., Klickstein, N., Commins, C., Chung, M., Dujardin, S., Bennett, R. E., Hyman, B. T., & Frosch, M. P. (2021) · The Journal of Neuroscience · doi:10.1523/jneurosci.2590-20.2021 · Cited by 18 · see citing works
Self-citationBittar, A., Al-Lahham, R., Bhatt, N., Moore, K., Montalbano, M., Jerez, C., Fung, L., McAllen, S., Ellsworth, A., & Kayed, R. (2022) · Journal of Alzheimer's Disease · doi:10.3233/jad-220518 · Cited by 18 · see citing works
Chongtham, A., Sharma, A., Nath, B., Murtha, K., Gorbachev, K., Ramakrishnan, A., Schmidt, E. F., Shen, L., & Pereira, A. C. (2024) · Experimental Neurology · doi:10.1016/j.expneurol.2024.114967 · Cited by 10 · see citing works
- Authors
- Mudher, A., Colin, M., Dujardin, S., Medina, M., Dewachter, I., Alavi Naini, S. M., Mandelkow, E.-M., Mandelkow, E., Buée, L., Goedert, M., & Brion, J.-P.
- Affiliations
- Inserm (FR)
- Harvard University (US)
- Biomedical Research Networking Center on Neurodegenerative Diseases (ES)
- Hasselt University (BE)
- Center of Advanced European Studies and Research (DE)
- MRC Laboratory of Molecular Biology (GB)
- Université Libre de Bruxelles (BE)
- Corresponding author
- Brion, Jean-Pierre
- ORCID
- Venue
- Acta Neuropathologica Communications
- Published
- 2017-12
- Volume
- 5
- Issue
- 1
- Pages
- 99-99
- ISSN
- 2051-5960 (ISSN-L)
- PMC
- PMC5735872
- OpenAlex
- W2779322228
- Cited by
- 384
- References
- 153
- Citations by year
- 2026: 33 · 2025: 38 · 2024: 48 · 2023: 38 · 2022: 48 · 2021: 51 · 2020: 48 · 2019: 48 · 2018: 32
- FWCI
- 4.30
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Acta Neuropathologica Communications (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Digital Access to Scholarship at Harvard (DASH) (Harvard University) (submittedVersion, cc-by)
- Dépôt institutionnel de l'Université libre de Bruxelles (Université Libre de Bruxelles) (submittedVersion, other-oa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Document Server@UHasselt (UHasselt) (submittedVersion, cc-by)
- Max Planck Digital Library (submittedVersion, other-oa)
- DZNE Pub (submittedVersion, cc-by)
- MPG.PuRe (Max Planck Society) (submittedVersion, other-oa)
- Funders
- University of Southampton
- Agence Nationale de la Recherche (ANR-11-LABX-0009)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- tauopathy, prion-like propagation, tau seeding, tau aggregation, tau secretion, intercellular transfer, genetic risk variants, selective neuronal vulnerability, prion transmission, terminology standardization
- MeSH terms
- Brain, Humans, Models, Molecular, Prions, Tauopathies, Protein Aggregation, Pathological
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
