Templated misfolding of Tau by prion-like seeding along neuronal connections impairs neuronal network function and associated behavioral outcomes in Tau transgenic mice
Open accessAbstract
Prion-like seeding and propagation of Tau-pathology have been demonstrated experimentally and may underlie the stereotyped progression of neurodegenerative Tauopathies. However, the involvement of templated misfolding of Tau in neuronal network dysfunction and behavioral outcomes remains to be explored in detail. Here we analyzed the repercussions of prion-like spreading of Tau-pathology via neuronal connections on neuronal network function in TauP301S transgenic mice. Spontaneous and GABA(A)R-antagonist-induced neuronal network activity were affected following templated Tau-misfolding using synthetic preformed Tau fibrils in cultured primary neurons. Electrophysiological analysis in organotypic hippocampal slices of Tau transgenic mice demonstrated impaired synaptic transmission and impaired long-term potentiation following Tau-seed induced Tau-aggregation. Intracerebral injection of Tau-seeds in TauP301S mice, caused prion-like spreading of Tau-pathology through functionally connected neuroanatomical pathways. Electrophysiological analysis revealed impaired synaptic plasticity in hippocampal CA1 region 6 months after Tau-seeding in entorhinal cortex (EC). Furthermore, templated Tau aggregation impaired cognitive function, measured in the object recognition test 6 months post-seeding. In contrast, Tau-seeding in basal ganglia and subsequent spreading through functionally connected neuronal networks involved in motor control, resulted in motoric deficits reflected in clasping and impaired inverted grid hanging, not significantly affected following Tau-seeding in EC. Immunostaining, biochemical and electron microscopic analysis in the different models suggested early pathological forms of Tau, including Tau-oligomers, rather than fully mature neurofibrillary tangles (NFTs) as culprits of neuronal dysfunction. We here demonstrate for the first time using in vitro, ex vivo and in vivo models, that prion-like spreading of Tau-misfolding by Tau seeds, along unique neuronal connections, causes neuronal network dysfunction and associated behavioral dysfunction. Our data highlight the potential relevance of this mechanism in the symptomatic progression in Tauopathies. We furthermore demonstrate that the initial site of Tau-seeding thereby determines the behavioral outcome, potentially underlying the observed heterogeneity in (familial) Tauopathies, including in TauP301 mutants.
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Degeneration could be initiated through synaptic or axonal mechanisms, independent of apoptosis.
“These observations raise the prospect that degeneration could be initiated through synaptic or axonal mechanisms, independent of apoptosis, a mechanism which has been widely studied in other model systems, such as spinal cord injury and Multiple Sclerosis 59–61.”
From Amyloid-beta induced retrograde axonal degeneration in a mouse tauopathy model (2019) · cites this paper as [60]
The Discussion (page unavailable) reports impaired synaptic plasticity and points to a postsynaptic mechanism for tau-seeding-induced neuronal dysfunction. It does not establish that degeneration is initiated through synaptic or axonal mechanisms, or that the process is independent of apoptosis. (LLM, conf=0.83)
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Cites
Neuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123 · see citing works
The Mouse Brain in Stereotaxic Coordinates
Paxinos, G. (2001) · Cited by 12,859 · see citing works
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
Neuropathological alterations in Alzheimer disease
Serrano-Pozo, A., Frosch, M. P., Masliah, E., & Hyman, B. T. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006189 · Cited by 3,345 · see citing works
A simple method for organotypic cultures of nervous tissue
Stoppini, L., Buchs, P., & Muller, D. (1991) · Journal of Neuroscience Methods · doi:10.1016/0165-0270(91)90128-m · Cited by 3,097 · see citing works
Lee, 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 · see citing works
Neurodegenerative Diseases Target Large-Scale Human Brain Networks
Seeley, W. W., Crawford, R. K., Zhou, J., Miller, B. L., & Greicius, M. D. (2009) · Neuron · doi:10.1016/j.neuron.2009.03.024 · Cited by 2,350 · see citing works
Synapse Loss and Microglial Activation Precede Tangles in a P301S Tauopathy Mouse Model
Yoshiyama, Y., Higuchi, M., Zhang, B., Huang, S.-M., Iwata, N., Saido, T. C., Maeda, J., Suhara, T., Trojanowski, J. Q., & Lee, V. M.-Y. (2007) · Neuron · doi:10.1016/j.neuron.2007.01.010 · Cited by 2,208 · see citing works
Tau 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
Learning induces long-term potentiation in the hippocampus
Whitlock, J. R., Heynen, A. J., Shuler, M. G., & Bear, M. F. (2006) · Science · doi:10.1126/science.1128134 · Cited by 1,913 · see citing works
Transmission 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
Profound Loss of Layer II Entorhinal Cortex Neurons Occurs in Very Mild Alzheimer’s Disease
Gómez-Isla, T., Price, J. L., McKeel Jr., D. W., Morris, J. C., Growdon, J. H., & Hyman, B. T. (1996) · The Journal of Neuroscience · doi:10.1523/jneurosci.16-14-04491.1996 · Cited by 1,796 · cited 1× · see citing works
“The first neurons to be affected are in entorhinal cortex (EC) (stage I), the neurons that give rise to the perforant pathway, the major projection connecting cerebral cortex with the hippocampus [23, 33].”
BackgroundHYMAN, B. T., & TROJANOWSKI, J. Q. (1997) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199710000-00002 · Cited by 1,542 · see citing works
Neuronal loss correlates with but exceeds neurofibrillary tangles in Alzheimer's disease
Gómez‐Isla, T., Hollister, R., West, H., Mui, S., Growdon, J. H., Petersen, R. C., Parisi, J. E., & Hyman, B. T. (1997) · Annals of Neurology · doi:10.1002/ana.410410106 · Cited by 1,489 · see citing works
Propagation 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
Propagation of Tau Misfolding from the Outside to the Inside of a Cell
Frost, B., Jacks, R. L., & Diamond, M. I. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808759200 · Cited by 1,252 · 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
Organotypic slice cultures: a technique has come of age
Gähwiler, B. H. (1997) · Trends in Neurosciences · doi:10.1016/s0166-2236(97)01122-3 · Cited by 884 · 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
The biochemical pathway of neurofibrillary degeneration in aging and Alzheimer's disease.
Delacourte, A., David, J. P., Sergeant, N., Buée, L., Wattez, A., Vermersch, P., Ghozali, F., Fallet-Bianco, C., Pasquier, F., Lebert, F., et al. (1999) · Neurology · doi:10.1212/wnl.52.6.1158 · Cited by 828 · see citing works
Prion-like mechanisms in neurodegenerative diseases
Frost, B., & Diamond, M. I. (2010) · Nature Reviews Neuroscience · doi:10.1038/nrn2786 · Cited by 776 · see citing works
Brain 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
Rampon, C., Tang, Y.-P., Goodhouse, J., Shimizu, E., Kyin, M., & Tsien, J. Z. (2000) · Nature Neuroscience · doi:10.1038/72945 · Cited by 737 · see citing works
A network diffusion model of disease progression in dementia
Raj, A., Kuceyeski, A., & Weiner, M. (2012) · Neuron · doi:10.1016/j.neuron.2011.12.040 · Cited by 723 · see citing works
Predicting Regional Neurodegeneration from the Healthy Brain Functional Connectome
Zhou, J., Gennatas, E. D., Kramer, J. H., Miller, B. L., & Seeley, W. W. (2012) · Neuron · doi:10.1016/j.neuron.2012.03.004 · Cited by 706 · 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
Iba, 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
Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases
Guo, J. L., & Lee, V. M. Y. (2014) · Nature Medicine · doi:10.1038/nm.3457 · Cited by 641 · see citing works
Postina, R., Schroeder, A., Dewachter, I., Bohl, J., Schmitt, U., Kojro, E., Prinzen, C., Endres, K., Hiemke, C., Blessing, M., et al. (2004) · Journal of Clinical Investigation · doi:10.1172/jci20864 · Cited by 638 · see citing works
Self-citationSeeding of Normal Tau by Pathological Tau Conformers Drives Pathogenesis of Alzheimer-like Tangles
Guo, J. L., & Lee, V. M.-Y. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.209296 · Cited by 636 · 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
Trans-cellular Propagation of Tau Aggregation by Fibrillar Species
Kfoury, N., Holmes, B. B., Jiang, H., Holtzman, D. M., & Diamond, M. I. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.346072 · Cited by 552 · see citing works
Identification 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
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
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
The propagation of prion-like protein inclusions in neurodegenerative diseases
Goedert, M., Clavaguera, F., & Tolnay, M. (2010) · Trends in Neurosciences · doi:10.1016/j.tins.2010.04.003 · Cited by 451 · see citing works
Spires, T. L., Orne, J. D., SantaCruz, K., Pitstick, R., Carlson, G. A., Ashe, K. H., & Hyman, B. T. (2006) · The American Journal of Pathology · doi:10.2353/ajpath.2006.050840 · Cited by 401 · see citing works
Schindowski, K., Bretteville, A., Leroy, K., Bégard, S., Brion, J., Hamdane, M., & Buée, L. (2006) · American Journal Of Pathology · doi:10.2353/ajpath.2006.060002 · Cited by 396 · see citing works
Preparation and Characterization of Neurotoxic Tau Oligomers
Lasagna-Reeves, C. A., Castillo-Carranza, D. L., Guerrero-Muñoz, M. J., Jackson, G. R., & Kayed, R. (2010) · Biochemistry · doi:10.1021/bi1016233 · Cited by 359 · see citing works
Age-Dependent Impairment of Cognitive and Synaptic Function in the htau Mouse Model of Tau Pathology
Polydoro, M., Acker, C. M., Duff, K., Castillo, P. E., & Davies, P. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.1065-09.2009 · Cited by 329 · see citing works
Tau pathophysiology in neurodegeneration: a tangled issue
Spires‐Jones, T. L., Stoothoff, W. H., de Calignon, A., Jones, P., & Hyman, B. T. (2009) · Trends in Neurosciences · doi:10.1016/j.tins.2008.11.007 · Cited by 316 · see citing works
Sydow, A., Van der Jeugd, A., Zheng, F., Ahmed, T., Balschun, D., Petrova, O., Drexler, D., Zhou, L., Rune, G., Mandelkow, E., et al. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.5245-10.2011 · Cited by 302 · see citing works
Amyloid Activates GSK-3β to Aggravate Neuronal Tauopathy in Bigenic Mice
Terwel, D., Muyllaert, D., Dewachter, I., Borghgraef, P., Croes, S., Devijver, H., & Van Leuven, F. (2008) · The American Journal of Pathology · doi:10.2353/ajpath.2008.070904 · Cited by 300 · see citing works
Self-citationCastillo-Carranza, D. L., Sengupta, U., Guerrero-Muñoz, M. J., Lasagna-Reeves, C. A., Gerson, J. E., Singh, G., Estes, D. M., Barrett, A. D. T., Dineley, K. T., Jackson, G. R., et al. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.3192-13.2014 · Cited by 278 · cited 1× · see citing works
“These data are in line with clear demonstration of detrimental effects of Tau-oligomers on neuronal function and behavior, as demonstrated following acute injection of oligomeric Tau and immunization with anti-Tau oligomeric antibodies [10, 11, 39, 40].”
ResultTerwel, D., Lasrado, R., Snauwaert, J., Vandeweert, E., Haesendonck, C. V., Borghgraef, P., & LEUVEN, F. V. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409876200 · Cited by 267 · see citing works
Self-citationBoluda, S., Iba, M., Zhang, B., Raible, K. M., Lee, V. M. ‐., & Trojanowski, J. Q. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1373-0 · Cited by 259 · see citing works
Dewachter, I., Reversé, D., Caluwaerts, N., Ris, L., Kuipéri, C., den Haute, C. V., Spittaels, K., Umans, L., Serneels, L., Thiry, E., et al. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-09-03445.2002 · Cited by 236 · see citing works
Self-citationBird, T. D., Nochlin, D., Poorkaj, P., Cherrier, M. M., Kaye, J. A., Payami, H., Peskind, E. R., Lampe, T. H., Nemens, E. J., Boyer, P. J., et al. (1999) · Brain · doi:10.1093/brain/122.4.741 · Cited by 222 · see citing works
Shao, C. Y., Mirra, S. S., Sait, H. B. R., Sacktor, T. C., & Sigurdsson, E. M. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0843-x · Cited by 219 · see citing works
Neurofibrillary tangle-bearing neurons are functionally integrated in cortical circuits in vivo
Kuchibhotla, K. V., Wegmann, S., Kopeikina, K. J., Hawkes, J., Rudinskiy, N., Andermann, M. L., Spires-Jones, T. L., Bacskai, B. J., & Hyman, B. T. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1318807111 · Cited by 193 · see citing works
Castillo‐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
Spontaneous synchronous synaptic calcium transients in cultured cortical neurons
Murphy, T. H., Blatter, L., Wier, W. G., & Baraban, J. M. (1992) · Journal of Neuroscience · doi:10.1523/jneurosci.12-12-04834.1992 · Cited by 177 · see citing works
Reinnervation of the hippocampal perforant pathway zone in Alzheimer's disease
Hyman, B. T., Kromer, L. J., & van Hoesen, G. W. (1987) · Annals of Neurology · doi:10.1002/ana.410210307 · Cited by 177 · see citing works
Cognitive defects are reversible in inducible mice expressing pro-aggregant full-length human Tau
Van der Jeugd, A., Hochgräfe, K., Ahmed, T., Decker, J. M., Sydow, A., Hofmann, A., Wu, D., Messing, L., Balschun, D., D’Hooge, R., et al. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-0987-3 · Cited by 135 · see citing works
Early axonopathy preceding neurofibrillary tangles in mutant tau transgenic mice
Leroy, K., Bretteville, A., Schindowski, K., Gilissen, E., Authelet, M., De Decker, R., Yilmaz, Z., Buée, L., & Brion, J.-P. (2007) · The American Journal of Pathology · doi:10.2353/ajpath.2007.070345 · Cited by 135 · see citing works
Increased regional cerebral glucose uptake in an APP/PS1 model of Alzheimer's disease
Poisnel, G., Hérard, A., Tayara, N. E. T. E., Bourrin, E., Volk, A., Kober, F., Delatour, B., Delzescaux, T., Debeir, T., Rooney, T., et al. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.09.026 · Cited by 120 · see citing works
Polydoro, M., Dzhala, V. I., Pooler, A. M., Nicholls, S. B., McKinney, A. P., Sanchez, L., Pitstick, R., Carlson, G. A., Staley, K. J., Spires-Jones, T. L., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-013-1215-5 · Cited by 117 · see citing works
Guo, J., & Lee, V. M. ‐. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.01.051 · Cited by 113 · see citing works
Deregulation of NMDA-receptor function and down-stream signaling in APP[V717I] transgenic mice
Dewachter, I., Filipkowski, R. K., Priller, C., Ris, L., Neyton, J., Croes, S., Terwel, D., Gysemans, M., Devijver, H., Borghgraef, P., et al. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.06.011 · Cited by 109 · see citing works
Self-citationFox, L. M., William, C. M., Adamowicz, D. H., Pitstick, R., Carlson, G. A., Spires-Jones, T. L., & Hyman, B. T. (2011) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e318220a658 · Cited by 88 · see citing works
Saul, A., Sprenger, F., Bayer, T. A., & Wirths, O. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.05.003 · Cited by 85 · see citing works
Warmus, B. A., Sekar, D., McCutchen, E., Schellenberg, G., Roberts, R., McMahon, L. L., & Roberson, E. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.3418-14.2014 · Cited by 84 · see citing works
Héraud, 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-citationBurnouf, S., Martire, A., Derisbourg, M. J., Laurent, C., Bélarbi, K., Leboucher, A., Fernández-Gómez, F.-J., Troquier, L., Eddarkaoui, S., Grosjean, M., et al. (2012) · Aging Cell · doi:10.1111/acel.12018 · Cited by 77 · see citing works
ALZHEIMER'S DISEASE AND TAU PROTEINS
Brion, J., Flament-Durand, J., & Dustin, P. (1986) · The Lancet · doi:10.1016/s0140-6736(86)90495-2 · Cited by 72 · see citing works
Hochgräfe, K., Sydow, A., & Mandelkow, E. (2013) · FEBS Journal · doi:10.1111/febs.12250 · Cited by 72 · see citing works
GSK-3α/β kinases and amyloid production in vivo
Jaworski, T., Dewachter, I., Lechat, B., Gees, M., Kremer, A., Demedts, D., Borghgraef, P., Devijver, H., Kügler, S., Patel, S., et al. (2011) · Nature · doi:10.1038/nature10615 · Cited by 69 · see citing works
Self-citationImpaired plasticity of cortical dendritic spines in P301S tau transgenic mice
Hoffmann, N. A., Dorostkar, M. M., Blumenstock, S., Goedert, M., & Herms, J. W. (2013) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-1-82 · Cited by 64 · see citing works
Arnold, S. E., Toledo, J. B., Appleby, D. H., Xie, S. X., Wang, W., Baek, Y., Wolk, D. A., Lee, E. B., Miller, B. L., Lee, V. M. ‐., et al. (2013) · The Journal of Comparative Neurology · doi:10.1002/cne.23430 · Cited by 61 · see citing works
Expression of Human Amyloid Precursor Protein in Rat Cortical Neurons Inhibits Calcium Oscillations
Santos, S. F., Pierrot, N., Morel, N., Gailly, P. L., Sindic, C., & Octave, J. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.4917-08.2009 · Cited by 55 · see citing works
Self-citationTauopathy 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
Self-citationReversibility of Tau-Related Cognitive Defects in a Regulatable FTD Mouse Model
Sydow, A., der Jeugd, A. V., Zheng, F., Ahmed, T., Balschun, D., Petrova, O. M., Drexler, D., Zhou, L., Rune, G. M., Mandelkow�, E., et al. (2011) · Journal of Molecular Neuroscience · doi:10.1007/s12031-011-9604-5 · Cited by 40 · see citing works
Luyten, L., Casteels, C., Vansteenwegen, D., van Kuyck, K., Koole, M., Van Laere, K., & Nuttin, B. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.3701-11.2012 · Cited by 39 · see citing works
Self-citationTau pathology does not affect experience-driven single-neuron and network-wide Arc/Arg3.1 responses
Rudinskiy, N., Hawkes, J. M., Wegmann, S., Kuchibhotla, K. V., Muzikansky, A., Betensky, R. A., Spires-Jones, T. L., & Hyman, B. T. (2014) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-2-63 · Cited by 32 · see citing works
Casteels, C., Vunckx, K., Aelvoet, S., Baekelandt, V., Bormans, G. M., Laere, K. V., & Koole, M. J. B. (2013) · PLoS ONE · doi:10.1371/journal.pone.0065286 · Cited by 20 · see citing works
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Stancu, 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-citationPropagation and spread of pathogenic protein assemblies in neurodegenerative diseases
Jucker, M., & Walker, L. C. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0238-6 · Cited by 450 · see citing works
Guo, 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
MAPT mutations, tauopathy, and mechanisms of neurodegeneration
Strang, K. H., Golde, T. E., & Giasson, B. I. (2019) · Laboratory Investigation · doi:10.1038/s41374-019-0197-x · Cited by 424 · see citing works
Rodent models for Alzheimer disease
Götz, J., Bodea, L., & Goedert, M. (2018) · Nature reviews. Neuroscience · doi:10.1038/s41583-018-0054-8 · Cited by 397 · see citing works
What is the evidence that tau pathology spreads through prion-like propagation?
Mudher, A., Colin, M., Dujardin, S., Medina, M., Dewachter, I., Alavi Naini, S. M., Mandelkow, E.-M., Mandelkow, E., Buée, L., Goedert, M., et al. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0488-7 · Cited by 384 · see citing works
Self-citationThe complexity of tau in Alzheimer’s disease
Naseri, N. N., Wang, H., Guo, J. D., Sharma, M., & Luo, W. (2019) · Neuroscience Letters · doi:10.1016/j.neulet.2019.04.022 · Cited by 374 · see citing works
Lewczuk, P., Riederer, P. F., O’Bryant, S. E., Verbeek, M. M., Dubois, B., Visser, P. J., Jellinger, K. A., Engelborghs, S., Ramı́rez, A., Parnetti, L., et al. (2017) · The World Journal of Biological Psychiatry · doi:10.1080/15622975.2017.1375556 · Cited by 308 · see citing works
Widespread brain tau and its association with ageing, Braak stage and Alzheimer’s dementia
Lowe, V. J., Wiste, H. J., Senjem, M. L., Weigand, S. D., Therneau, T. M., Boeve, B. F., Josephs, K. A., Fang, P., Pandey, M. K., Murray, M. E., et al. (2017) · Brain · doi:10.1093/brain/awx320 · Cited by 302 · see citing works
A 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
Synaptic Tau Seeding Precedes Tau Pathology in Human Alzheimer’s Disease Brain
DeVos, S. L., Corjuc, B. T., Oakley, D. H., Nobuhara, C. K., Bannon, R. N., Chase, A., Commins, C., Gonzalez, J. A., Dooley, P. M., Frosch, M. P., et al. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00267 · Cited by 285 · 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
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
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
Traumatic Brain Injury Induces Tau Aggregation and Spreading
Edwards, G., Zhao, J., Dash, P. K., Soto, C., & Moreno-Gonzalez, I. (2020) · Journal of Neurotrauma · doi:10.1089/neu.2018.6348 · Cited by 195 · see citing works
Tau Pathology in Parkinson's Disease
Zhang, X., Gao, F., Wang, D., Li, C., Fu, Y., He, W., & Zhang, J. (2018) · Frontiers in Neurology · doi:10.3389/fneur.2018.00809 · Cited by 199 · 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-citationThe basis of cellular and regional vulnerability in Alzheimer’s disease
Mrdjen, D., Fox, E. J., Bukhari, S. A., Montine, K. S., Bendall, S. C., & Montine, T. J. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02054-4 · Cited by 155 · see citing works
Sustained synchronized neuronal network activity in a human astrocyte co-culture system
Kuijlaars, J., Oyelami, T., Diels, A., Rohrbacher, J., Versweyveld, S., Meneghello, G., Tuefferd, M., Verstraelen, P., Detrez, J. R., Verschuuren, M., et al. (2016) · Scientific Reports · doi:10.1038/srep36529 · Cited by 133 · see citing works
Self-citationDiscovery and characterization of stable and toxic Tau/phospholipid oligomeric complexes
Ait‐Bouziad, N., Lv, G., Mahul‐Mellier, A., Xiao, S., Zorludemir, G., Eliezer, D., Walz, T., & Lashuel, H. A. (2017) · Nature Communications · doi:10.1038/s41467-017-01575-4 · Cited by 147 · 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
Strang, K. H., Croft, C. L., Sorrentino, Z. A., Chakrabarty, P., Golde, T. E., & Giasson, B. I. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.815357 · Cited by 144 · see citing works
Tau pathology in neurodegenerative disease: disease mechanisms and therapeutic avenues
Samudra, N. P., Lane‐Donovan, C., VandeVrede, L. A., & Boxer, A. L. (2023) · Journal of Clinical Investigation · doi:10.1172/jci168553 · Cited by 135 · see citing works
Valera, E., Spencer, B. J., & Masliah, E. (2015) · Neurotherapeutics · doi:10.1007/s13311-015-0397-z · Cited by 129 · 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
The role of exosomes in the pathogenesis of Alzheimer’ disease
Xiao, T., Zhang, W., Jiao, B., Pan, C., Liu, X., & Shen, L. H. (2017) · Translational Neurodegeneration · doi:10.1186/s40035-017-0072-x · Cited by 128 · see citing works
Wang, P., Joberty, G., Buist, A., Vanoosthuyse, A., Stancu, I., Vasconcelos, B., Pierrot, N., Faelth-Savitski, M., Kienlen‐Campard, P., Octave, J., et al. (2017) · Acta Neuropathologica · doi:10.1007/s00401-016-1663-9 · Cited by 118 · see citing works
Self-citationSpreading of α-Synuclein and Tau: A Systematic Comparison of the Mechanisms Involved
Vasili, E., Dominguez‐Meijide, A., & Outeiro, T. F. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00107 · Cited by 117 · see citing works
Tau biology, tauopathy, traumatic brain injury, and diagnostic challenges
Castellani, R. J., & Perry, G. (2019) · Journal of Alzheimer’s Disease · doi:10.3233/jad-180721 · Cited by 110 · see citing works
Different tau species lead to heterogeneous tau pathology propagation and misfolding
Dujardin, S., Bégard, S., Caillierez, R., Lachaud, C., Carrier, S., Lieger, S., Gonzalez, J. A., Deramecourt, V., Déglon, N., Maurage, C.-A., et al. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0637-7 · Cited by 109 · see citing works
In vivo tau pathology is associated with synaptic loss and altered synaptic function
Coomans, E. M., Schoonhoven, D. N., Tuncel, H., Verfaillie, S. C. J., Wolters, E. E., Boellaard, R., Ossenkoppele, R., den Braber, A., Scheper, W., Schober, P. R., et al. (2021) · Alzheimer s Research & Therapy · doi:10.1186/s13195-021-00772-0 · Cited by 101 · see citing works
Shulman, M. B., Kong, J., O'Gorman, J. T., Ratti, E., Rajagovindan, R., Viollet, L., Huang, E., Sharma, S., Racine, A. M., Czerkowicz, J., et al. (2023) · Nature Aging · doi:10.1038/s43587-023-00523-w · Cited by 100 · 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
Self-citationPrions and Protein Assemblies that Convey Biological Information in Health and Disease
Sanders, D. W., Kaufman, S. K., Holmes, B. B., & Diamond, M. I. (2016) · Neuron · doi:10.1016/j.neuron.2016.01.026 · Cited by 90 · see citing works
Dutta, D., Jana, M., Paidi, R. K., Majumder, M., Raha, S., Dasarathy, S., & Pahan, K. (2023) · Journal of Clinical Investigation · doi:10.1172/jci161987 · Cited by 87 · see citing works
Tau prion-like propagation: state of the art and current challenges
Dujardin, S., & Hyman, B. T. (2019) · Advances in Experimental Medicine and Biology · doi:10.1007/978-981-32-9358-8_23 · Cited by 84 · see citing works
Involvement of Oligodendrocytes in Tau Seeding and Spreading in Tauopathies
Ferrer, I., Aguiló, M., Carmona, M., Andrés‐Benito, P., Torrejón-Escribano, B., Garcia‐Esparcia, P., & del Rı́o, J. A. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00112 · Cited by 76 · see citing works
Wu, X., Piña-Crespo, J., Zhang, Y., Chen, X., & Xu, H. (2017) · Chinese Medical Journal · doi:10.4103/0366-6999.220313 · Cited by 79 · see citing works
Andersson, C. R., Falsig, J., Stavenhagen, J. B., Christensen, S., Kartberg, F., Rosenqvist, N., Finsen, B. R., & Pedersen, J. T. (2019) · Scientific Reports · doi:10.1038/s41598-019-41105-4 · Cited by 78 · see citing works
Neuronally derived extracellular vesicles: an emerging tool for understanding Alzheimer’s disease
Watson, L. S., Hamlett, E. D., Stone, T. D., & Sims‐Robinson, C. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0317-5 · Cited by 72 · see citing works
The <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-citationLodder, C., Scheyltjens, I., Stancu, I., Lucena, P. B., de Ravé, M. G., Vanherle, S., Vanmierlo, T., Cremers, N., Vanrusselt, H., Brône, B., et al. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01204-8 · Cited by 68 · see citing works
Self-citationAudouard, 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
Prion-like mechanisms in Alzheimer disease
Walker, L. C. (2018) · Handbook of clinical neurology · doi:10.1016/b978-0-444-63945-5.00016-7 · Cited by 65 · see citing works
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 · see citing works
Ferrer, I., Andrés‐Benito, P., Zelaya, M. V., Aguirre, M. E. E., Carmona, M., Ausín, K., Lachén‐Montes, M., Fernández‐Irigoyen, J., Santamaría, E., & del Rı́o, J. A. (2020) · Acta Neuropathologica · doi:10.1007/s00401-019-02122-9 · Cited by 57 · see citing works
Elevated matrix metalloproteinase‐9 levels in neuronal extracellular vesicles in Alzheimer’s disease
Gu, D., Liu, F., Meng, M., Zhang, L., Gordon, M. L., Wang, Y., Cai, L., & Zhang, N. (2020) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.51155 · Cited by 58 · see citing works
Tau-Cofactor Complexes as Building Blocks of Tau Fibrils
Fichou, Y., Oberholtzer, Z. R., Ngo, H., Cheng, C., Keller, T. J., Eschmann, N. A., & Han, S. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.01339 · Cited by 57 · see citing works
The evolutionary scope and neurological disease linkage of yeast-prion-like proteins in humans
An, L., & Harrison, P. M. (2016) · Biology Direct · doi:10.1186/s13062-016-0134-5 · Cited by 53 · see citing works
Effects of pharmacological modulators of α-synuclein and tau aggregation and internalization
Dominguez‐Meijide, A., Vasili, E., König, A., Cima‐Omori, M., de Opakua, A. I., Leonov, A., Ryazanov, S., Zweckstetter, M., Griesinger, C., & Outeiro, T. F. (2020) · Scientific Reports · doi:10.1038/s41598-020-69744-y · Cited by 51 · see citing works
Chai, A. B., Hartz, A. M. S., Gao, X., Yang, A., Callaghan, R., & Gelissen, I. C. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms22010246 · Cited by 50 · see citing works
The evolving landscape of Alzheimer’s disease therapy: From Aβ to tau
Courade, J., Zetterberg, H., Höglinger, G. U., & Dewachter, I. (2025) · Cell · doi:10.1016/j.cell.2025.11.033 · Cited by 52 · see citing works
Self-citationMcAllister, B. B., Lacoursiere, S. G., Sutherland, R. J., & Mohajerani, M. H. (2020) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2020.01.026 · Cited by 47 · see citing works
Neuropathology of the Alzheimer's continuum: an update
Jellinger, K. A. (2020) · Free Neuropathology · doi:10.17879/freeneuropathology-2020-3050 · Cited by 45 · see citing works
The Prion-Like Behavior of Assembled Tau in Transgenic MicePreprint
Clavaguera, F., Tolnay, M., & Goedert, M. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024372 · Cited by 42 · see citing works
Schultz, M. K., Gentzel, R. C., Usenovic, M., Gretzula, C. A., Ware, C., Parmentier‐Batteur, S., Schachter, J. B., & Zariwala, H. A. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.07.003 · Cited by 40 · see citing works
CSF biomarkers in neurodegenerative and vascular dementias
Llorens, F., Schmitz, M., Ferrer, I., & Zerr, I. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.03.003 · Cited by 39 · see citing works
Chronic Traumatic Encephalopathy: Is Latency in Symptom Onset Explained by Tau Propagation?Preprint
Kriegel, J., Papadopoulos, Z., & McKee, A. C. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024059 · Cited by 36 · see citing works
Relevance of host tau in tau seeding and spreading in tauopathies
Ferrer, I., Zelaya, M. V., Aguiló, M., Carmona, M., López‐González, I., Andrés‐Benito, P., Lidón, L., Gavı́n, R., Garcia‐Esparcia, P., & del Rı́o, J. A. (2019) · Brain Pathology · doi:10.1111/bpa.12778 · Cited by 35 · see citing works
Kim, Y. D., Jeong, E. I., Nah, J., Yoo, S., Lee, W. J., Kim, Y., Moon, S., Hong, S., & Jung, Y. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.14109 · Cited by 33 · see citing works
Amyloid-beta induced retrograde axonal degeneration in a mouse tauopathy model
Nishioka, C., Liang, H.-F., Barsamian, B., & Sun, S.-W. (2019) · NeuroImage · doi:10.1016/j.neuroimage.2019.01.007 · Cited by 30 · see citing works
“Although tau aggregates are hallmarks of AD, several studies have suggested that oligomeric tau in soluble forms may be the most potent neurotoxic form (Wu et al., 2013; Iba et al., 2013, 2015; Stancu et al., 2015; Peeraer et al., 2015; Kopeikina et al., 2012).”
Hosokawa, M., Masuda‐Suzukake, M., Shitara, H., Shimozawa, A., Suzuki, G., Kondo, H., Nonaka, T., Campbell, W. D., Arai, T., & Hasegawa, M. (2021) · Brain · doi:10.1093/brain/awab289 · Cited by 30 · see citing works
Elevated medial temporal lobe and pervasive brain tau‐PET signal in normal participants
Lowe, V. J., Bruinsma, T. J., Min, H.-K. P., Lundt, E. S., Fang, P., Senjem, M. L., Boeve, B. F., Josephs, K. A., Pandey, M. K., Murray, M. E., et al. (2018) · Alzheimer s & Dementia Diagnosis Assessment & Disease Monitoring · doi:10.1016/j.dadm.2018.01.005 · Cited by 30 · see citing works
Multicenter 18F-PI-2620 PET for In Vivo Braak Staging of Tau Pathology in Alzheimer’s Disease
Rullmann, M., Brendel, M., Schroeter, M. L., Saur, D., Levin, J., Perneczky, R. G., Tiepolt, S., Patt, M., Mueller, A., Villemagne, V. L., et al. (2022) · Biomolecules · doi:10.3390/biom12030458 · Cited by 29 · see citing works
Jiang, Z., Wang, J., Qin, Y., Liu, S., Luo, B., Bai, F., Wei, H., Zhang, S., Wei, J., Ding, G., et al. (2024) · Alzheimer s Research & Therapy · doi:10.1186/s13195-024-01392-0 · Cited by 31 · see citing works
Visualization of prion-like transfer in Huntington's disease models
Jansen, A. H. P., Batenburg, K. L., Pecho‐Vrieseling, E., & Reits, E. A. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.12.015 · Cited by 26 · see citing works
Amyloid-β oligomers increase the binding and internalization of tau oligomers in human synapses
Kadamangudi, S., Marcatti, M., Zhang, W.-R., Fracassi, A., Kayed, R., Limon, A., & Taglialatela, G. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02839-2 · Cited by 25 · see citing works
Interactions between Microtubule-Associated Protein Tau (MAPT) and Small MoleculesPreprint
Rauch, J. N., Olson, S. H., & Gestwicki, J. E. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024034 · Cited by 22 · see citing works
Quantitative proteomics of tau and Aβ in detergent fractions from Alzheimer's disease brains
Mukherjee, S., Dubois, C., Perez, K. A., Varghese, S., Birchall, I. E., Leckey, M., Davydova, N., McLean, C., Nisbet, R. M., Roberts, B. R., et al. (2022) · Journal of Neurochemistry · doi:10.1111/jnc.15713 · Cited by 21 · see citing works
Eskandari-Sedighi, G., Daude, N., Gapeshina, H., Sanders, D. W., Kamali-Jamil, R., Yang, J., Shi, B., Wille, H., Ghetti, B., Diamond, M. I., et al. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0215-7 · Cited by 22 · see citing works
Intraneuronal tau aggregation induces the integrated stress response in astrocytes
Batenburg, K. L., Kasri, N. N., Heine, V. M., & Scheper, W. (2022) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjac071 · Cited by 21 · see citing works
Koch, Y., Helferich, A. M., Steinacker, P., Oeckl, P., Walther, P., Weishaupt, J. H., Danzer, K. M., & Otto, M. (2016) · American Journal Of Pathology · doi:10.1016/j.ajpath.2016.04.008 · Cited by 21 · see citing works
Zhang, G., Shen, Y., Phipps, J., Sun, L., & Ma, S. (2024) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2024.216059 · Cited by 21 · see citing works
Candelise, N., Schmitz, M., Correia, S., Arora, A. S., Villar‐Piqué, A., Zafar, S., Llorens, F., Cramm, M., & Zerr, I. (2017) · Expert Review of Molecular Diagnostics · doi:10.1080/14737159.2017.1368389 · Cited by 20 · see citing works
Astrocytes in Neurodegenerative Diseases: A Perspective from Tauopathy and α-Synucleinopathy
Wang, P., & Ye, Y. (2021) · Life · doi:10.3390/life11090938 · Cited by 20 · see citing works
Self-citationLucena, P. B., Vanherle, S., Lodder, C., de Ravé, M. G., Stancu, I., Lambrichts, I., Vangheluwe, R., Bruffaerts, R., & Dewachter, I. (2022) · Acta Neuropathologica · doi:10.1007/s00401-022-02458-9 · Cited by 20 · see citing works
Self-citationHromádková, L., Siddiqi, M. K., Liu, H., & Safar, J. (2022) · Cells · doi:10.3390/cells11192997 · Cited by 19 · see citing works
Zhang, X., Zou, L., Tang, L., Xiong, M., Yan, X., Meng, L., Chen, G., Xiong, J., Nie, S., Zhang, Z., et al. (2024) · PLoS Biology · doi:10.1371/journal.pbio.3002470 · Cited by 19 · see citing works
Indication of retrograde tau spreading along Braak stages and functional connectivity pathways
Seemiller, J., Bischof, G. N., Hoenig, M. C., Tahmasian, M., van Eimeren, T., Drzezga, A. E., & Initiative, A. T. A. D. N. (2021) · European Journal of Nuclear Medicine and Molecular Imaging · doi:10.1007/s00259-020-05183-1 · Cited by 19 · see citing works
Inflammasome links traumatic brain injury, chronic traumatic encephalopathy, and Alzheimer’s disease
Seplovich, G., Bouchi, Y., Vaccari, J. P. D. R., Pareja, J. C. M., Reisner, A., Blackwell, L. S., Mechref, Y. S., Wang, K., Tyndall, J. A., Tharakan, B., et al. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-24-00107 · Cited by 20 · see citing works
Umeda, T., Uekado, R., Shigemori, K., Eguchi, H., & Tomiyama, T. (2022) · Biomedicines · doi:10.3390/biomedicines10020297 · Cited by 18 · see citing works
Tau: More than a microtubule‐binding protein in neurons
Alonso, A. D. C., Idrissi, A. E., Candia, R. F., Morozova, V., & Kleiman, F. E. (2023) · Cytoskeleton · doi:10.1002/cm.21795 · Cited by 17 · see citing works
Masuda‐Suzukake, M., Suzuki, G., Hosokawa, M., Nonaka, T., Goedert, M., & Hasegawa, M. (2020) · Brain Communications · doi:10.1093/braincomms/fcaa091 · Cited by 16 · see citing works
The use of mouse models to study cell-to-cell transmission of pathological tau
Narasimhan, S., & Lee, V. M. ‐. (2017) · Methods in cell biology · doi:10.1016/bs.mcb.2017.06.009 · Cited by 16 · see citing works
Spreading of Pathology in Alzheimer’s Disease
Lv, Z., Tan, C., Yu, J., & Tan, L. (2017) · Neurotoxicity Research · doi:10.1007/s12640-017-9765-2 · Cited by 15 · see citing works
Pineau, H., & Sim, V. L. (2020) · Biomolecules · doi:10.3390/biom10071079 · Cited by 15 · see citing works
Veys, L., houcke, J. V., Aerts, J., Pottelberge, S. V., Mahieu, M., Coens, A., Melki, R., Moechars, D., Muynck, L. D., & Groef, L. D. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.614587 · Cited by 14 · see citing works
Self-citationA seeding-based neuronal model of tau aggregation for use in drug discovery
Amorim, I. S., Challal, S., Cistarelli, L., Dorval, T., Abjean, L., Touzard, M., Arbez, N., François, A., Panayi, F., Jeggo, R., et al. (2023) · PLoS ONE · doi:10.1371/journal.pone.0283941 · Cited by 13 · see citing works
The role of wild-type tau in Alzheimer’s disease and related tauopathies
Lo, C. H., & Sachs, J. N. (2020) · JoLS Journal of Life Sciences · doi:10.36069/jols/20201201 · Cited by 14 · see citing works
Yang, X., Yao, K., Zhang, M., Zhang, W., & Zu, H. (2025) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2025.111321 · Cited by 12 · see citing works
Martins, D. R., Sha, F., der Elst, W. V., Shih, P., Devoght, J., Kolen, K. V., Mercken, M. H., Broeck, B. V., Declerck, P. J., & Theunis, C. (2023) · Molecular Therapy — Methods & Clinical Development · doi:10.1016/j.omtm.2023.101158 · Cited by 12 · see citing works
Unknown roles of tau pathology in neurological disorders. Challenges and new perspectives
Olesen, M. A., Villavicencio-Tejo, F., Cuevas-Espinoza, V., & Quintanilla, R. A. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102594 · Cited by 12 · see citing works
Cho, H., Baek, M., Lee, H. S., Lee, J., Ryu, Y., & Lyoo, C. (2020) · Alzheimer's Research & Therapy · doi:10.1186/s13195-020-00685-4 · Cited by 11 · see citing works
Apolipoprotein E isoform does not influence trans-synaptic spread of tau pathology in a mouse model
Davies, C., Tulloch, J., Yip, E., Currie, L., Colom‐Cadena, M., Wegmann, S., Hyman, B. T., Wilkins, L., Hooley, M., Tzioras, M., et al. (2023) · Brain and Neuroscience Advances · doi:10.1177/23982128231191046 · Cited by 11 · see citing works
Nam, W., & Choi, Y. P. (2018) · Prion · doi:10.1080/19336896.2018.1545524 · Cited by 12 · see citing works
Basheer, N., Buée, L., Brion, J., Smolek, T., Muhammadi, M. K., Hritz, J., Hromádka, T., Dewachter, I., Wegmann, S., Landrieu, I., et al. (2024) · Acta Neuropathologica Communications · doi:10.1186/s40478-024-01748-5 · Cited by 11 · see citing works
Self-citationDetrez, J. R., Ben-Nejma, I. R. H., Kolen, K. V., Dam, D. V., Deyn, P. P. D., Fransén, E., Verhoye, M., Timmermans, J., Nuydens, R., der Linden, A. V., et al. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.105011 · Cited by 10 · see citing works
Dynamics of microtubules and their associated proteins
Benarroch, E. E. (2016) · Neurology · doi:10.1212/wnl.0000000000002686 · Cited by 9 · see citing works
Cerebrospinal fluid in Creutzfeldt–Jakob disease
Zerr, I., Zafar, S., Schmitz, M., & Llorens, F. (2017) · Handbook of clinical neurology · doi:10.1016/b978-0-12-804279-3.00008-3 · Cited by 9 · see citing works
- Authors
- Stancu, I.-C., Vasconcelos, B., Ris, L., Wang, P., Villers, A., Peeraer, E., Buist, A., Terwel, D., Baatsen, P., Oyelami, T., Pierrot, N., Casteels, C., Bormans, G., Kienlen-Campard, P., Octave, J.-N., Moechars, D., & Dewachter, I.
- Affiliations
- UCLouvain (BE)
- University of Mons (BE)
- Janssen (Belgium) (BE)
- KU Leuven (BE)
- Corresponding author
- Dewachter, Ilse
- ORCID
- Venue
- Acta Neuropathologica
- Published
- 2015-04-11
- Volume
- 129
- Issue
- 6
- Pages
- 875-894
- ISSN
- 0001-6322 (ISSN-L)
- 1432-0533
- PMC
- PMC4436846
- OpenAlex
- W2109355761
- Cited by
- 143
- References
- 76
- Citations by year
- 2026: 4 · 2025: 6 · 2024: 12 · 2023: 10 · 2022: 12 · 2021: 15 · 2020: 16 · 2019: 15 · 2018: 14 · 2017: 18 · 2016: 18 · 2015: 3
- FWCI
- 13.01
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Acta Neuropathologica (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Lirias (submittedVersion, other-oa)
- Digital Access to Libraries (submittedVersion)
- Document Server@UHasselt (UHasselt) (submittedVersion, cc-by)
- ORBi UMONS (submittedVersion)
- Funders
- Fonds De La Recherche Scientifique - FNRS
- Vlaamse regering
- 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
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- tau protein, prion-like seeding, tauopathy, neuronal network dysfunction, synaptic transmission, long-term potentiation, synaptic plasticity, hippocampus, entorhinal cortex, basal ganglia, motor impairment, cognitive impairment, object recognition, tau oligomers, neurofibrillary tangles, GABA-A receptor antagonists, organotypic hippocampal slices
- MeSH terms
- Animals, Animals, Newborn, Calcium, Cognition Disorders, Disease Models, Animal, Exploratory Behavior, Hippocampus, Membrane Potentials, Mice, Inbred C57BL, Mice, Transgenic, Mutation, Nerve Net, Prions, Fura-2, Neurofibrillary Tangles, tau Proteins, Tauopathies, Mice, Proteostasis Deficiencies, In Vitro Techniques
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