Intracerebral injection of preformed synthetic tau fibrils initiates widespread tauopathy and neuronal loss in the brains of tau transgenic mice
Open accessAbstract
Neurofibrillary tangles composed of hyperphosphorylated fibrillized tau are found in numerous tauopathies including Alzheimer's disease. Increasing evidence suggests that tau pathology can be transmitted from cell-to-cell; however the mechanisms involved in the initiation of tau fibrillization and spreading of disease linked to progression of tau pathology are poorly understood. We show here that intracerebral injections of preformed synthetic tau fibrils into the hippocampus or frontal cortex of young tau transgenic mice expressing mutant human P301L tau induces tau hyperphosphorylation and aggregation around the site of injection, as well as a time-dependent propagation of tau pathology to interconnected brain areas distant from the injection site. Furthermore, we show that the tau pathology as a consequence of injection of tau preformed fibrils into the hippocampus induces selective loss of CA1 neurons. Together, our data confirm previous studies on the seeded induction and the spreading of tau pathology in a different tau transgenic mouse model and reveals neuronal loss associated with seeded tau pathology in tau transgenic mouse brain. These results further validate the utility of the tau seeding model in studying disease transmission, and provide a more complete in vivo tauopathy model with associated neurodegeneration which can be used to investigate the mechanisms involved in tau aggregation and spreading, as well as aid in the search for disease modifying treatments for Alzheimer's disease and related tauopathies.
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?
Injection in tauP301L transgenic mice results in elevated p-tau levels close to the injection site.
“Injection in tauP301L transgenic mice resulted in elevated p-tau levels close to the site of injection [143].”
From Alzheimer's Disease: Treatment Strategies and Their Limitations. (2022) · cites this paper as [143]
The spread of tau pathology is time-dependent from the injection site to distant interconnected brain regions.
“In addition, the spread of tau pathology is time-dependent from the injection site to distant interconnected brain regions [58].”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [58]
Intracerebral injection of synthetic tau fibrils into the hippocampus or frontal cortex of tau-P301L transgenic mice at 3 months increases tau hyperphosphorylation and accumulation around the injection site.
“An in vivo study has demonstrated that the intracerebral injection of synthetic tau fibrils into the hippocampus or frontal cortex of tau-P301L transgenic mice at 3 months increases tau hyperphosphorylation and accumulation around the injection site.”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [58]
Tau pathology as a consequence of injection with tau-preformed fibrils into the hippocampus of tau-P301L transgenic mice induced selective neuron loss of the CA1 region.
“Peeraer and colleagues found that the tau pathology as a consequence of injection with tau-preformed fibrils into the hippocampus of tau-P301L transgenic mice induced selective neuron loss of the CA1 region [58].”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [58]
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
Neuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123 · see citing works
Inflammation and Alzheimer’s disease
Akiyama, H. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00124-x · Cited by 4,514 · see citing works
Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease
Arriagada, P. V., Growdon, J. H., Hedley-Whyte, E. T., & Hyman, B. T. (1992) · Neurology · doi:10.1212/wnl.42.3.631 · Cited by 2,668 · see citing works
Luk, K. C., Kehm, V., Carroll, J., Zhang, B., O’Brien, P., Trojanowski, J. Q., & Lee, V. M.-Y. (2012) · Science · doi:10.1126/science.1227157 · Cited by 2,563 · see citing works
Self-citationSynapse 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
Self-citationStages of the Pathologic Process in Alzheimer Disease: Age Categories From 1 to 100 Years
Braak, H., Thal, D. R., Ghebremedhin, E., & Del Tredici, K. (2011) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e318232a379 · Cited by 2,194 · see citing works
Tau-mediated neurodegeneration in Alzheimer’s disease and related disorders
Ballatore, C., Lee, V. M.-Y., & Trojanowski, J. Q. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2194 · Cited by 2,174 · see citing works
Self-citationReducing Endogenous Tau Ameliorates Amyloid ß-Induced Deficits in an Alzheimer's Disease Mouse Model
Roberson, E. D., Scearce-Levie, K., Palop, J. J., Yan, F., Cheng, I. H., Wu, T., Gerstein, H., Yu, G.-Q., & Mucke, L. (2007) · Science · doi:10.1126/science.1141736 · Cited by 1,892 · see citing works
Dendritic Function of Tau Mediates Amyloid-β Toxicity in Alzheimer's Disease Mouse Models
Ittner, L. M., Ke, Y. D., Delerue, F., Bi, M., Gladbach, A., van Eersel, J., Wölfing, H., Chieng, B. C., Christie, M. J., Napier, I. A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.06.036 · Cited by 1,821 · see citing works
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
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
Luk, K. C., Kehm, V. M., Zhang, B., O’Brien, P., Trojanowski, J. Q., & Lee, V. M. ‐. (2012) · The Journal of Experimental Medicine · doi:10.1084/jem.20112457 · Cited by 1,087 · see citing works
Self-citationTrans-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
Saman, S., Kim, W., Raya, M., Visnick, Y., Miro, S., Saman, S., Jackson, B., McKee, A. C., Alvarez, V. E., Lee, N. C. Y., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.277061 · Cited by 985 · see citing works
Exogenous Induction of Cerebral ß-Amyloidogenesis Is Governed by Agent and Host
Meyer-Luehmann, M., Coomaraswamy, J., Bolmont, T., Kaeser, S., Schaefer, C., Kilger, E., Neuenschwander, A., Abramowski, D., Frey, P., Jaton, A. L., et al. (2006) · Science · doi:10.1126/science.1131864 · Cited by 971 · see citing works
Prion-like spreading of pathological α-synuclein in brain
Masuda-Suzukake, M., Nonaka, T., Hosokawa, M., Oikawa, T., Arai, T., Akiyama, H., Mann, D. M. A., & Hasegawa, M. (2013) · Brain · doi:10.1093/brain/awt037 · Cited by 867 · 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
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
Self-citationRoberson, E. D., Halabisky, B., Yoo, J. W., Yao, J., Chin, J., Yan, F., Wu, T., Hamto, P., Devidze, N., Yu, G.-Q., et al. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.4152-10.2011 · Cited by 654 · see citing works
Seeding 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
Self-citationWu, J. W., Herman, M., Liu, L., Simoes, S., Acker, C. M., Figueroa, H., Steinberg, J. I., Margittai, M., Kayed, R., Zurzolo, C., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.394528 · Cited by 537 · see citing works
Schauwecker, P. E., & Steward, O. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.8.4103 · Cited by 510 · see citing works
Alzheimer brain-derived tau oligomers propagate pathology from endogenous tau
Lasagna-Reeves, C. A., Castillo-Carranza, D. L., Sengupta, U., Guerrero-Munoz, M. J., Kiritoshi, T., Neugebauer, V., Jackson, G. R., & Kayed, R. (2012) · Scientific Reports · doi:10.1038/srep00700 · Cited by 502 · 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
Mutations causing neurodegenerative tauopathies
Goedert, M., & Jakes, R. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.08.007 · Cited by 438 · see citing works
Spittaels, 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
Self-citationInflammation and Alzheimer’s disease
Lee, Y.-J., Han, S. B., Nam, S.-Y., Oh, K.-W., & Hong, J. T. (2010) · Archives of Pharmacal Research · doi:10.1007/s12272-010-1006-7 · Cited by 396 · see citing works
The Seeds of Neurodegeneration: Prion-like Spreading in ALS
Polymenidou, M., & Cleveland, D. W. (2011) · Cell · doi:10.1016/j.cell.2011.10.011 · Cited by 370 · see citing works
A nucleated assembly mechanism of Alzheimer paired helical filaments
Friedhoff, P., von Bergen�, M., Mandelkow�, E., Davies, P., & Mandelkow�, E. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.26.15712 · Cited by 340 · see citing works
Seeded Aggregation and Toxicity of α-Synuclein and Tau
Nonaka, T., Watanabe, S., Iwatsubo, T., & Hasegawa, M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.148460 · Cited by 330 · see citing works
Induction of cerebral β-amyloidosis: Intracerebral versus systemic Aβ inoculation
Eisele, Y. S., Bolmont, T., Heikenwalder, M., Langer, F., Jacobson, L. H., Yan, Z.-X., Roth, K., Aguzzi, A., Staufenbiel, M., Walker, L. C., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903200106 · Cited by 279 · see citing works
Terwel, 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
Holth, J. K., Bomben, V. C., Reed, J. G., Inoue, T., Younkin, L., Younkin, S. G., Pautler, R. G., Botas, J., & Noebels, J. L. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.3191-12.2013 · Cited by 238 · see citing works
Constitutive secretion of tau protein by an unconventional mechanism
Chai, X., Dage, J. L., & Citron, M. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.05.021 · Cited by 224 · see citing works
Bellucci, A., Westwood, A. J., Ingram, E., Casamenti, F., Goedert, M., & Spillantini, M. G. (2004) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63421-9 · Cited by 215 · see citing works
McKhann, G. M., Wenzel, H. J., Robbins, C. A., Sosunov, A. A., & Schwartzkroin, P. A. (2003) · Neuroscience · doi:10.1016/s0306-4522(03)00562-1 · Cited by 189 · see citing works
Proteostasis 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
Vandermeeren, M., Mercken, M., Vanmechelen, E., Six, J., Voorde, A., Martin, J.-J., & Cras, P. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb09823.x · Cited by 145 · see citing works
Self-citationTau gene mutations and their effects
Goedert, M. (2005) · Movement Disorders · doi:10.1002/mds.20539 · Cited by 134 · see citing works
Exogenous induction of cerebral β-amyloidosis in βAPP-transgenic mice
Walker, L. C., Callahan, M. J., Bian, F., Durham, R. A., Roher, A. E., & Lipinski, W. J. (2002) · Peptides · doi:10.1016/s0196-9781(02)00059-1 · Cited by 96 · see citing works
Huyghe, S., Schmalbruch, H., Gendt, K. D., Verhoeven, G., Guillou, F., Veldhoven, P. P. V., & Baes, M. I. (2006) · Endocrinology · doi:10.1210/en.2005-1571 · Cited by 76 · see citing works
Characterization of tau fibrillization in vitro
Xu, S., Brunden, K. R., Trojanowski, J. Q., & Lee, V. M. ‐. (2010) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2009.06.002 · Cited by 73 · see citing works
Self-citationBottelbergs, A., Verheijden, S., Van Veldhoven, P. P., Just, W., Devos, R., & Baes, M. (2012) · Journal of Neuroinflammation · doi:10.1186/1742-2094-9-61 · Cited by 66 · see citing works
Self-citationLiu, L., Hamre, K. M., & Goldowitz, D. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.6478-11.2012 · Cited by 16 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Tau in physiology and pathology
Wang, Y., & Mandelkow, E. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2015.1 · Cited by 2,251 · 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
Roles of tau protein in health and disease
Guo, T., Noble, W., & Hanger, D. P. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1707-9 · Cited by 1,003 · see citing works
Protein transmission in neurodegenerative disease
Peng, C., Trojanowski, J. Q., & Lee, V. M.-Y. (2020) · Nature Reviews Neurology · doi:10.1038/s41582-020-0333-7 · Cited by 625 · 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
Alzheimer's Disease: Treatment Strategies and Their Limitations.
Passeri, E., Elkhoury, K., Morsink, M., Broersen, K., Linder, M., Tamayol, A., Malaplate, C., Yen, F. T., & Arab-Tehrany, E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232213954 · Cited by 592 · see citing works
“Injection in tauP301L transgenic mice resulted in elevated p-tau levels close to the site of injection [143].”
BackgroundUpdate on Alzheimer’s Disease Therapy and Prevention Strategies
Graham, W. V., Bonito-Oliva, A., & Sakmar, T. P. (2017) · Annual Review of Medicine · doi:10.1146/annurev-med-042915-103753 · Cited by 506 · 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
“Peeraer and colleagues found that the tau pathology as a consequence of injection with tau-preformed fibrils into the hippocampus of tau-P301L transgenic mice induced selective neuron loss of the CA1 region [58].”
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-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
Self-citationMAPT 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
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-citationNeurodegenerative Diseases: Expanding the Prion Concept
Walker, L. C., & Jucker, M. (2015) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-071714-033828 · Cited by 361 · see citing works
Monoaminergic neuropathology in Alzheimer’s disease
Šimić, G., Leko, M. B., Wray, S., Harrington, C. R., Delalle, I., Milošević, N. J., Bažadona, D., Buée, L., de Silva, R., Giovanni, G. D., et al. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.04.001 · Cited by 289 · see citing works
Babiloni, C., Blinowska, K. J., Bonanni, L., Cichocki, A. S., de Haan, W., Percio, C. D., Dubois, B., Escudero, J., Fernández, A., Frisoni, G. B., et al. (2019) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2019.09.008 · Cited by 282 · see citing works
Boluda, 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
Self-citationCellular and pathological heterogeneity of primary tauopathies
Chung, D. C., Roemer, S. F., Petrucelli, L., & Dickson, D. W. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00476-x · Cited by 219 · 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
Self-citationLewis, J. M., & Dickson, D. W. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1507-z · Cited by 221 · see citing works
Xia, Y., Prokop, S., & Giasson, B. I. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00460-5 · Cited by 218 · see citing works
Dural lymphatics regulate clearance of extracellular tau from the CNS
Patel, T. K., Habimana-Griffin, L., Gao, X., Xu, B. J., Achilefu, S., Alitalo, K. K., McKee, C. A., Sheehan, P. W., Musiek, E. S., Xiong, C., et al. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0312-x · Cited by 215 · 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 concept of alpha-synuclein as a prion-like protein: ten years after
Steiner, J. A., Quansah, E., & Brundin, P. (2018) · Cell and Tissue Research · doi:10.1007/s00441-018-2814-1 · Cited by 183 · see citing works
Prevention of tau seeding and propagation by immunotherapy with a central tau epitope antibody
Albert, M., Mairet‐Coello, G., Danis, C., Lieger, S., Caillierez, R., Carrier, S., Skrobala, E., Landrieu, I., Michel, A., Schmitt, M., et al. (2019) · Brain · doi:10.1093/brain/awz100 · Cited by 177 · see citing works
Jin, M., Xu, R., Wang, L., Alam, M. M., Ma, Z., Zhu, S., Martini, A. C., Jadali, A., Bernabucci, M., Xie, P., et al. (2022) · Cell Stem Cell · doi:10.1016/j.stem.2022.06.007 · Cited by 174 · see citing works
Amyloidogenesis of Tau protein
Niżyński, B., Dzwolak, W., & Nieznański, K. (2017) · Protein Science · doi:10.1002/pro.3275 · Cited by 157 · 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
Sankaranarayanan, 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
Self-citationWidespread 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
Avila, J., Jiménez, J. S., Sayas, C. L., Bolós, M., Zabala, J. C., Rivas, G., & Hernández, F. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00262 · Cited by 140 · 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
Neuronal APOE4 removal protects against tau-mediated gliosis, neurodegeneration and myelin deficits
Koutsodendris, N., Blumenfeld, J., Agrawal, A., Traglia, M., Grone, B., Zilberter, M., Yip, O., Rao, A., Nelson, M. R., Hao, Y., et al. (2023) · Nature Aging · doi:10.1038/s43587-023-00368-3 · 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
(2022) · doi:10.1038/s41467-022-34129-4 · Cited by 128 · see citing works
Self-citationMiao, J., Shi, R., Li, L., Chen, F., Zhou, Y., Tung, Y. C., Hu, W. H., Gong, C., Iqbal, K., & Liu, F. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00034 · Cited by 125 · see citing works
Spreading 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
Progressive supranuclear palsy: Advances in diagnosis and management
Coughlin, D. G., & Litvan, I. (2020) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2020.04.014 · Cited by 113 · see citing works
Tau Positron Emission Tomography (PET) Imaging: Past, Present, and Future.
Ariza, M., Kolb, H., Moechars, D., Rombouts, F., & Andrés, J. (2015) · Journal of Medicinal Chemistry · doi:10.1021/jm5017544 · Cited by 97 · see citing works
Self-citationOssenkoppele, R., Iaccarino, L., Schonhaut, D. R., Brown, J. A., Joie, R. L., O’Neil, J. P., Janabi, M., Baker, S. L., Kramer, J. H., Gorno‐Tempini, M., et al. (2019) · NeuroImage Clinical · doi:10.1016/j.nicl.2019.101848 · Cited by 103 · see citing works
Dai, C.-L., Hu, W., Tung, Y. C., Liu, F., Gong, C.-X., & Iqbal, K. (2018) · Alzheimer's Research & Therapy · doi:10.1186/s13195-018-0341-7 · Cited by 99 · see citing works
Possible Mechanisms of Tau Spread and Toxicity in Alzheimer’s Disease
Zhang, H., Cao, Y., Ma, L., Wei, Y., & Li, H. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.707268 · Cited by 104 · see citing works
Prion-like Spreading in Tauopathies
Ayers, J. I., Giasson, B. I., & Borchelt, D. (2017) · Biological Psychiatry · doi:10.1016/j.biopsych.2017.04.003 · Cited by 100 · see citing works
Ahnaou, A., Moechars, D., Raeymaekers, L., Biermans, R., Manyakov, N. V., Bottelbergs, A., Wintmolders, C., Van Kolen, K., Van De Casteele, T., Kemp, J. A., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-13839-6 · Cited by 98 · see citing works
Self-citationShulman, 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
Prions 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
Hyperphosphorylation Renders Tau Prone to Aggregate and to Cause Cell Death
Liu, M., Sui, D., Dexheimer, T. S., Hovde, S., Deng, X., Wang, K., Lin, H. L., Hagar, H. C., Kweon, H. K., Kuo, N. S., et al. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-02034-w · Cited by 97 · see citing works
Wiersma, V. I., van Ziel, A. M., Vazquez‐Sanchez, S., Nölle, A., Berenjeno‐Correa, E., Bonaterra‐Pastra, A., Clavaguera, F., Tolnay, M., Musters, R. J. P., van Weering, J. R. T., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02046-4 · Cited by 88 · see citing works
Using Human iPSC-Derived Neurons to Model TAU Aggregation
Verheyen, A., Diels, A., Dijkmans, J., Oyelami, T., Meneghello, G., Mertens, L., Versweyveld, S., Borgers, M., Buist, A., Peeters, P., et al. (2015) · PLOS ONE · doi:10.1371/journal.pone.0146127 · Cited by 86 · see citing works
Edavettal, S. C., Cejudo–Martín, P., Dasgupta, B., Yang, D., Buschman, M. D., Domingo, D. L., Kolen, K. V., Jaiprasart, P., Gordon, R. E., Schutsky, K., et al. (2022) · Med · doi:10.1016/j.medj.2022.09.007 · Cited by 83 · 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
The Neurotoxic Role of Extracellular Tau Protein
Sebastián‐Serrano, Á., de Diego-García, L., & Dı́az-Hernández, M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19040998 · Cited by 81 · 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
Bae, E.-J., Yang, N. Y., Lee, C., Kim, S., Lee, H.-J., & Lee, S. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.283 · Cited by 77 · see citing works
Medda, X., Mertens, L., Versweyveld, S., Diels, A., Barnham, L., Bretteville, A., Buist, A., Verheyen, A., Royaux, I. E., Ebneth, A., et al. (2016) · SLAS DISCOVERY · doi:10.1177/1087057116638029 · Cited by 73 · 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
Scialò, C., Cecco, E. D., Manganotti, P., & Legname, G. (2019) · Viruses · doi:10.3390/v11030261 · Cited by 67 · see citing works
Degradation or aggregation: the ramifications of post-translational modifications on tau
Park, S., Lee, J. H., Jeon, J. H., & Lee, M. J. (2018) · BMB Reports · doi:10.5483/bmbrep.2018.51.6.077 · Cited by 69 · 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
Tau Filament Self-Assembly and Structure: Tau as a Therapeutic Target
Oakley, S. S., Maina, M. B., Marshall, K. E., Al‐Hilaly, Y. K., Harrington, C., Wischik, C. M., & Serpell, L. C. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.590754 · Cited by 57 · see citing works
Tau and Membranes: Interactions That Promote Folding and Condensation
Sallaberry, C. A., Voss, B. J., Majewski, J. P., Biernat, J., Mandelkow�, E., Chi, E. Y., & Zanden, C. M. V. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.725241 · Cited by 60 · see citing works
Alzheimer’s disease brain contains tau fractions with differential prion-like activities
Li, L., Shi, R., Gu, J., Tung, Y. C., Zhou, Y., Zhou, D., Wu, R., Chu, D., Jin, N., Deng, K., et al. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01127-4 · Cited by 59 · see citing works
Liu, M., Dexheimer, T. S., Sui, D., Hovde, S., Deng, X., Kwok, R. P. S., Bochar, D. A., & Kuo, M. (2020) · Scientific Reports · doi:10.1038/s41598-020-73680-2 · Cited by 56 · see citing works
Tau seeding and spreading in vivo is supported by both AD-derived fibrillar and oligomeric tau
de Gérando, A. M., Welikovitch, L. A., Khasnavis, A., Commins, C., Glynn, C. A., Chun, J. E., Perbet, R., & Hyman, B. T. (2023) · Acta Neuropathologica · doi:10.1007/s00401-023-02600-1 · Cited by 52 · see citing works
Highly specific and selective anti‐pS396‐tau antibody C10.2 targets seeding‐competent tau
Rosenqvist, N., Asuni, A. A., Andersson, C. R., Christensen, S., Daechsel, J. C. A., Egebjerg, J., Falsig, J., Helboe, L., Jul, P., Kartberg, F., et al. (2018) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1016/j.trci.2018.09.005 · Cited by 51 · see citing works
Prion‐like propagation as a pathogenic principle in frontotemporal dementia
Hock, E., & Polymenidou, M. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13668 · Cited by 51 · see citing works
McAllister, 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
Walker, L., & Attems, J. (2023) · Journal of Parkinson s Disease · doi:10.3233/jpd-230154 · Cited by 46 · see citing works
Immunological memory to hyperphosphorylated tau in asymptomatic individuals
Pascual, G., Wadia, J. S., Zhu, X., Keogh, E. A., Kaletaş, B. K., van Ameijde, J., Inganäs, H., Siregar, B., Perdok, G. J., Diefenbach, O., et al. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1705-y · Cited by 44 · 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
Annadurai, N., Sanctis, J. B. D., Hajdúch, M., & Das, V. (2021) · Experimental Neurology · doi:10.1016/j.expneurol.2021.113756 · Cited by 41 · 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
Vandermeeren, M., Borgers, M., Kolen, K. V., Theunis, C., Vasconcelos, B., Bottelbergs, A., Wintmolders, C., Daneels, G., Willems, R., Dockx, K., et al. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180404 · Cited by 39 · see citing works
Self-citationRegional vulnerability and spreading of hyperphosphorylated tau in seeded mouse brain
Detrez, J. R., Maurin, H., Van Kolen, K., Willems, R., Colombelli, J., Lechat, B., Roucourt, B., Van Leuven, F., Baatout, S., Larsen, P., et al. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.03.010 · Cited by 39 · see citing works
Walsh, C., Drinkenburg, W. H. I. M., & Ahnaou, A. (2016) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2016.12.020 · Cited by 35 · 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
Hu, J., Sha, W., Yuan, S., Wu, J., & Huang, Y. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241915023 · Cited by 35 · see citing works
Retinal ganglion cell vulnerability to pathogenic tau in Alzheimer’s disease
Davis, M. R., Robinson, E., Koronyo, Y., Salobrar‐García, E., Rentsendorj, A., Gaire, B. P., Mirzaei, N., Kayed, R., Sadun, A. A., Ljubimov, A. V., et al. (2025) · Acta Neuropathologica Communications · doi:10.1186/s40478-025-01935-y · Cited by 33 · see citing works
Tau Seeding Mouse Models with Patient Brain-Derived Aggregates
Robert, A., Schöll, M., & Vogels, T. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22116132 · Cited by 35 · see citing works
Pharmacological Modulators of Tau Aggregation and Spreading
Dominguez‐Meijide, A., Vasili, E., & Outeiro, T. F. (2020) · Brain Sciences · doi:10.3390/brainsci10110858 · Cited by 34 · see citing works
Jin, J. W., Fan, X., del Cid‐Pellitero, E., Liu, X., Zhou, L., Dai, C., Gibbs, E., He, W., Li, H., Wu, X., et al. (2021) · Communications Biology · doi:10.1038/s42003-021-01746-6 · Cited by 34 · see citing works
Park, H., Lee, Y., & Chang, K. (2022) · International Journal of Biological Sciences · doi:10.7150/ijbs.66604 · Cited by 33 · see citing works
Transcellular Spreading of Tau in Tauopathies
Demaegd, K. C., Schymkowitz, J. W. H., & Rousseau, F. (2018) · ChemBioChem · doi:10.1002/cbic.201800288 · Cited by 30 · 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).”
Post-Translational Modifications in Tau and Their Roles in Alzheimer's Pathology
Kalyaanamoorthy, S., Opare, S. K. A., Xu, X., Ganesan, A., & Rao, P. P. N. (2024) · Current Alzheimer Research · doi:10.2174/0115672050301407240408033046 · Cited by 31 · see citing works
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
Leighton, P. L. A., & Allison, W. T. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160361 · Cited by 29 · see citing works
Giong, H.-K., Subramanian, M., Yu, K., & Lee, J.-S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22168465 · Cited by 29 · see citing works
PET Imaging in Animal Models of Alzheimer’s Disease
Chen, B., Marquez-Nostra, B. V., Belitzky, E., Toyonaga, T., Tong, J., Huang, Y. H., & Cai, Z. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.872509 · Cited by 27 · see citing works
Eraña, H., Venegas, V., Charco, J. M., & Castilla, J. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.08.166 · Cited by 26 · see citing works
First-in-Rat Study of Human Alzheimer’s Disease Tau Propagation
Smolek, T., Jadhav, S., Brezováková, V., Cubinkova, V., Valachova, B., Novák, P., & Žilka, N. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1102-0 · Cited by 25 · see citing works
Weber, M. A., Kerr, G., Thangavel, R., Conlon, M. M., Gumusoglu, S. B., Gupta, K., Abdelmotilib, H., Halhouli, O., Zhang, Q., Geerling, J. C., et al. (2023) · Journal of Parkinson s Disease · doi:10.3233/jpd-230129 · Cited by 25 · see citing works
S100A8 ‐enriched microglia populate the brain of tau‐seeded and accelerated aging mice
Gruel, R., Bijnens, B., Daele, J. V. D., Thys, S., Willems, R., Wuyts, D., Dam, D. V., Verstraelen, P., Verboven, R., Roels, J., et al. (2024) · Aging Cell · doi:10.1111/acel.14120 · Cited by 23 · see citing works
Ahnaou, A., Walsh, C., Manyakov, N. V., Youssef, S. A., & Drinkenburg, W. H. I. M. (2019) · Neural Plasticity · doi:10.1155/2019/6981268 · Cited by 24 · see citing works
van Ameijde, J., Crespo, R., Janson, R., Juraszek, J., Siregar, B., Verveen, H., Sprengers, I., Nahar, T., Hoozemans, J. J. M., Steinbacher, S., et al. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0562-9 · Cited by 21 · see citing works
Self-citationEskandari-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
Neuron-derived extracellular vesicle-based diagnostics for Tau and Alzheimer’s disease
Chinnathambi, S., Kumarappan, M., Malik, S., Velmurugan, G., & Chandrashekar, M. (2025) · Brain Network Disorders · doi:10.1016/j.bnd.2024.12.006 · Cited by 21 · see citing works
- Authors
- Peeraer, E., Bottelbergs, A., Van Kolen, K., Stancu, I.-C., Vasconcelos, B., Mahieu, M., Duytschaever, H., Ver Donck, L., Torremans, A., Sluydts, E., Van Acker, N., Kemp, J. A., Mercken, M., Brunden, K. R., Trojanowski, J. Q., Dewachter, I., Lee, V. M. Y., & Moechars, D.
- Affiliations
- Janssen (Belgium) (BE)
- UCLouvain (BE)
- HistoGeneX (Belgium) (BE)
- University of Pennsylvania (US)
- Corresponding author
- Moechars, Diederik
- Venue
- Neurobiology of Disease
- Publisher
- Elsevier BV
- Published
- 2015-01
- Volume
- 73
- Pages
- 83-95
- ISSN
- 0969-9961 (ISSN-L)
- PMC
- PMC4303592
- OpenAlex
- W1979363343
- Cited by
- 214
- References
- 46
- Citations by year
- 2026: 4 · 2025: 15 · 2024: 18 · 2023: 18 · 2022: 21 · 2021: 28 · 2020: 19 · 2019: 25 · 2018: 19 · 2017: 15 · 2016: 18 · 2015: 12 · 2014: 2
- FWCI
- 10.42
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Neurobiology of Disease (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Digital Access to Libraries (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Document Server@UHasselt (UHasselt) (submittedVersion)
- Funders
- Institute for the Promotion of Innovation by Science and Technology (IWT120492)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- tauopathy, tau fibrils, tau seeding, tau hyperphosphorylation, tau aggregation, neurofibrillary tangles, P301L tau, tau transgenic mice, Alzheimer's disease, disease transmission, neuronal loss, CA1 neurons, hippocampus, frontal cortex
- MeSH terms
- Age Factors, Analysis of Variance, Animals, Disease Models, Animal, Gene Expression Regulation, Hippocampus, Humans, Functional Laterality, Mice, Transgenic, Mutation, Neurofibrillary Tangles, tau Proteins, Disease Progression, Tauopathies, Mice
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