Activity-Dependent Tau Protein Translocation to Excitatory Synapse Is Disrupted by Exposure to Amyloid-Beta Oligomers
Open accessAbstract
Tau is a microtubule-associated protein well known for its stabilization of microtubules in axons. Recently, it has emerged that tau participates in synaptic function as part of the molecular pathway leading to amyloid-beta (Aβ)-driven synaptotoxicity in the context of Alzheimer's disease. Here, we report the implication of tau in the profound functional synaptic modification associated with synaptic plasticity. By exposing murine cultured cortical neurons to a pharmacological synaptic activation, we induced translocation of endogenous tau from the dendritic to the postsynaptic compartment. We observed similar tau translocation to the postsynaptic fraction in acute hippocampal slices subjected to long-term potentiation. When we performed live confocal microscopy on cortical neurons transfected with human-tau-GFP, we visualized an activity-dependent accumulation of tau in the postsynaptic density. Coprecipitation using phalloidin revealed that tau interacts with the most predominant cytoskeletal component present, filamentous actin. Finally, when we exposed cortical cultures to 100 n m human synthetic Aβ oligomers (Aβo's) for 15 min, we induced mislocalization of tau into the spines under resting conditions and abrogated subsequent activity-dependent synaptic tau translocation. These changes in synaptic tau dynamics may rely on a difference between physiological and pathological phosphorylation of tau. Together, these results suggest that intense synaptic activity drives tau to the postsynaptic density of excitatory synapses and that Aβo-driven tau translocation to the spine deserves further investigation as a key event toward synaptotoxicity in neurodegenerative diseases.
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?
Aβ exposure modifies Tau's phosphorylation status and prevents it from relocalizing away from the post-synaptic domain following synaptic activation.
“Aβ exposure modifies Tau’s phosphorylation status and prevents it from relocalizing away from the post-synaptic domain following synaptic activation [29].”
From The new genetic landscape of Alzheimer’s disease: from amyloid cascade to genetically driven synaptic failure hypothesis? (2019) · cites this paper as [29]
The phosphorylation-results section reports that Aβ oligomers alter tau’s phosphorylation profile. But the Abstract and the section on synaptic activation describe tau moving into the postsynaptic compartment during activation; Aβ exposure induces its entry under resting conditions and abrogates subsequent activity-dependent translocation. They do not report that Aβ prevents tau from moving away from that compartment after activation. (LLM, conf=0.88)
Experimental — accuracy not yet measuredIn vivo, tau co-localizes with actin in differentiating PC12 cells and in the post-synaptic compartments of mature neurons.
“In vivo, tau co-localizes with actin in differentiating PC12 cells22 and in the post-synaptic compartments of mature neurons23.”
From Tau co-organizes dynamic microtubule and actin networks (2015) · cites this paper as [23]
Citation 23 attaches to the postsynaptic-neuron part of the sentence, not the PC12-cell part. Figure 4 shows tau and F-actin colocalizing in dendritic spines of cultured cortical neurons after synaptic activation, while Figure 1 reports only limited colocalization under resting conditions. These cell-culture observations do not establish the claim's in vivo setting. (LLM, conf=0.86)
Experimental — accuracy not yet measuredTau is also present in dendrites and postsynaptic compartments.
“Recent studies demonstrate that tau is also present in dendrites and postsynaptic compartments [128–130].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [129]
Dendritic tau may regulate synaptic plasticity; synaptic activity can recruit tau to postsynaptic densities, and tau deletion in various mouse models shows deficits in LTP or LTD.
“Dendritic tau may also play a role in regulating synaptic plasticity, as synaptic activity can recruit tau to the postsynaptic densities, where tau deletion in various mouse models show deficits either in LTP or LTD [129, 131, 132].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [129]
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
AMPA Receptor Trafficking and Synaptic Plasticity
Malinow, R., & Malenka, R. C. (2002) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.25.112701.142758 · Cited by 2,588 · see citing works
Lifeact: a versatile marker to visualize F-actin
Riedl, J., Crevenna, A. H., Kessenbrock, K., Yu, J. H., Neukirchen, D., Bista, M., Bradke, F., Jenne, D., Holak, T. A., Werb, Z., et al. (2008) · Nature Methods · doi:10.1038/nmeth.1220 · Cited by 2,189 · see citing works
Reducing Endogenous Tau Ameliorates Amyloid ß-Induced Deficits in an Alzheimer's Disease Mouse Model
Roberson, E. D., Scearce-Levie, K., Palop, J. J., Yan, F., Cheng, I. H., Wu, T., Gerstein, H., Yu, G.-Q., & Mucke, L. (2007) · Science · doi:10.1126/science.1141736 · Cited by 1,892 · see citing works
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
Shankar, G. M., Bloodgood, B. L., Townsend, M., Walsh, D. M., Selkoe, D. J., & Sabatini, B. L. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4970-06.2007 · Cited by 1,592 · see citing works
Amyloid-β and tau — a toxic pas de deux in Alzheimer's disease
Ittner, L. M., & Götz, J. (2010) · Nature reviews. Neuroscience · doi:10.1038/nrn2967 · Cited by 1,357 · see citing works
Impaired Long-Term Potentiation, Spatial Learning, and Hippocampal Development in fyn Mutant Mice
Grant, S. G. N., O’Dell, T. J., Karl, K. A., Stein, P. L., Soriano, P. M., & Kandel, E. R. (1992) · Science · doi:10.1126/science.1361685 · Cited by 1,154 · see citing works
Hoover, B. R., Reed, M. N., Su, J., Penrod, R. D., Kotilinek, L. A., Grant, M. K., Pitstick, R., Carlson, G. A., Lanier, L. M., Yuan, L.-L., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.11.030 · Cited by 1,118 · see citing works
Soluble oligomers of the amyloid β-protein impair synaptic plasticity and behavior
Selkoe, D. J. (2008) · Behavioural Brain Research · doi:10.1016/j.bbr.2008.02.016 · Cited by 1,038 · see citing works
In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis
Stine, W. B., Dahlgren, K. N., Krafft, G. A., & LaDu, M. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210207200 · Cited by 1,015 · see citing works
Synaptic AMPA receptor plasticity and behavior
Kessels, H. W., & Malinow, R. (2009) · Neuron · doi:10.1016/j.neuron.2009.01.015 · Cited by 993 · see citing works
Activity level controls postsynaptic composition and signaling via the ubiquitin-proteasome system
Ehlers, M. D. (2003) · Nature Neuroscience · doi:10.1038/nn1013 · Cited by 977 · see citing works
Morris, M., Maeda, S., Vossel, K., & Mucke, L. (2011) · Neuron · doi:10.1016/j.neuron.2011.04.009 · Cited by 899 · see citing works
Inhibition of actin polymerization by latrunculin A
Coué, M., Brenner, S. L., Spector, I., & Korn, E. D. (1987) · FEBS Letters · doi:10.1016/0014-5793(87)81513-2 · Cited by 824 · see citing works
Actin in dendritic spines: connecting dynamics to function
Hotulainen, P., & Hoogenraad, C. C. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201003008 · Cited by 815 · see citing works
Tau is essential to β-amyloid-induced neurotoxicity
Rapoport, M., Dawson, H. N., Binder, L. I., Vitek, M. P., & Ferreira, A. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.092136199 · Cited by 807 · see citing works
Li, S., Jin, M., Koeglsperger, T., Shepardson, N. E., Shankar, G. M., & Selkoe, D. J. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.0203-11.2011 · Cited by 664 · see citing works
Roberson, 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
Dynamic microtubules regulate dendritic spine morphology and synaptic plasticity
Jaworski, J., Kapitein, L. C., Gouveia, S. M., Dortland, B. R., Wulf, P. S., Grigoriev, I., Camera, P., Spangler, S. A., Di Stefano, P., Demmers, J., et al. (2009) · Neuron · doi:10.1016/j.neuron.2008.11.013 · Cited by 643 · see citing works
Hutchinson, E. (2011) · Nature reviews. Neuroscience · doi:10.1038/nrn2985 · Cited by 534 · see citing works
Rapid turnover of actin in dendritic spines and its regulation by activity
Star, E. N., Kwiatkowski, D. J., & Murthy, V. N. (2002) · Nature Neuroscience · doi:10.1038/nn811 · Cited by 465 · see citing works
Tai, H., Serrano‐Pozo, A., Hashimoto, T., Frosch, M. P., Spires‐Jones, T. L., & Hyman, B. T. (2012) · American Journal Of Pathology · doi:10.1016/j.ajpath.2012.06.033 · Cited by 456 · see citing works
Abnormal bundling and accumulation of F-actin mediates tau-induced neuronal degeneration in vivo
Fulga, T. A., Elson-Schwab, I., Khurana, V., Steinhilb, M. L., Spires, T. L., Hyman, B. T., & Feany, M. B. (2007) · Nature Cell Biology · doi:10.1038/ncb1528 · Cited by 452 · see citing works
Tau interacts with src-family non-receptor tyrosine kinases
Lee, G. S., Newman, S. T., Gard, D. L., Band, H., & Panchamoorthy, G. (1998) · Journal of Cell Science · doi:10.1242/jcs.111.21.3167 · Cited by 445 · see citing works
Nuclear Tau, a Key Player in Neuronal DNA Protection
Sultan, A., Nesslany, F., Violet, M., Bégard, S., Loyens, A., Talahari, S., Mansuroglu, Z., Marzin, D., Sergeant, N., Humez, S., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.199976 · Cited by 421 · cited 5× · see citing works
“Such a role is supported by previous observations that the silencing of tau expression using small hairpin RNA produced spine loss in cultured neurons (Chen et al., 2012).”
BackgroundMethodInfluentialDistribution of tau proteins in the normal human central and peripheral nervous system.
Trojanowski, J. Q., Schuck, T., Schmidt, M. L., & Lee, V. M. (1989) · Journal of Histochemistry & Cytochemistry · doi:10.1177/37.2.2492045 · Cited by 329 · see citing works
Tau protein as a differential biomarker of tauopathies
Sergeant, N., Delacourte, A., & Buée, L. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.06.020 · Cited by 312 · see citing works
Mondragón-Rodríguez, S., Trillaud-Doppia, E., Dudilot, A., Bourgeois, C., Lauzon, M., Leclerc, N., & Boehm, J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.401240 · Cited by 272 · see citing works
A Spatial Gradient of Tau Protein Phosphorylation in Nascent Axons
Mandell, J. W., & Banker, G. A. (1996) · Journal of Neuroscience · doi:10.1523/jneurosci.16-18-05727.1996 · Cited by 270 · see citing works
Steiner, P., Higley, M. J., Xu, W., Czervionke, B. L., Malenka, R. C., & Sabatini, B. L. (2008) · Neuron · doi:10.1016/j.neuron.2008.10.014 · Cited by 259 · see citing works
Léveillé, F., Gaamouch, F. E., Gouix, E., Lecocq, M., Lobner, D., Nicole, O., & Buisson, A. (2008) · The FASEB Journal · doi:10.1096/fj.08-107268 · Cited by 258 · see citing works
Self-citationIdentification of nuclear tau isoforms in human neuroblastoma cells.
Loomis, P. A., Howard, T. H., Castleberry, R. P., & Binder, L. I. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.21.8422 · Cited by 217 · see citing works
Myosin motors at neuronal synapses: drivers of membrane transport and actin dynamics
Kneussel, M., & Wagner, W. (2013) · Nature Reviews Neuroscience · doi:10.1038/nrn3445 · Cited by 191 · see citing works
Rescuing impairment of long-term potentiation in fyn-deficient mice by introducing Fyn transgene
Kojima, N., Wang, J., Mansuy, I. M., Grant, S. G. N., Mayford, M. R., & Kandel, E. R. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.9.4761 · Cited by 188 · see citing works
Synaptic Regulation of Microtubule Dynamics in Dendritic Spines by Calcium, F-Actin, and Drebrin
Merriam, E. B., Millette, M. M., Lumbard, D., Saengsawang, W., Fothergill, T., Hu, X., Ferhat, L., & Dent, E. W. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.0661-13.2013 · Cited by 177 · see citing works
Dynamic association of tau with neuronal membranes is regulated by phosphorylation
Pooler, A. M., Usardi, A., Evans, C. J., Philpott, K. L., Noble, W., & Hanger, D. P. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.01.005 · Cited by 148 · see citing works
The proline-rich domain of tau plays a role in interactions with actin
He, H. J., Wang, X. S., Pan, R., Wang, D. L., Liu, M. N., & He, R. Q. (2009) · BMC Cell Biology · doi:10.1186/1471-2121-10-81 · Cited by 142 · see citing works
Tau protein diffuses along the microtubule lattice
Hinrichs, M. H., Jalal, A., Brenner, B., Mandelkow, E., Kumar, S., & Scholz, T. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.369785 · Cited by 141 · see citing works
Merino-Serrais, P., Benavides-Piccione, R., Blazquez-Llorca, L., Kastanauskaite, A., Rábano, A., Avila, J., & DeFelipe, J. (2013) · Brain · doi:10.1093/brain/awt088 · Cited by 134 · see citing works
Cytoskeleton proteins are modulators of mutant tau-induced neurodegeneration in Drosophila
Blard, O., Feuillette, S., Bou, J., Chaumette, B., Frébourg, T., Campion, D., & Lecourtois, M. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm011 · Cited by 110 · see citing works
Somatodendritic localization of phosphorylated tau in neonatal and adult rat cerebral cortex
Tashiro, K., Hasegawa, M., Ihara, Y., & Iwatsubo, T. (1997) · Neuroreport · doi:10.1097/00001756-199708180-00029 · Cited by 109 · see citing works
Tau protein is involved in morphological plasticity in hippocampal neurons in response to BDNF
Chen, Q., Zhou, Z., Zhang, L., Wang, Y., Zhang, Y., Zhong, M., Xu, S., Chen, C., Li, L., & Yu, Z. (2011) · Neurochemistry International · doi:10.1016/j.neuint.2011.12.013 · Cited by 87 · see citing works
Götz, J., Xia, D., Leinenga, G., Chew, Y. L., & Nicholas, H. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00072 · Cited by 85 · see citing works
Dynamics of an F-actin aggresome generated by the actin-stabilizing toxin jasplakinolide
Lázaro‐Diéguez, F., Aguado, C., Mato, E., Sánchez-Ruíz, Y., Esteban, I., Alberch, J., Knecht, E., & Egea, G. (2008) · Journal of Cell Science · doi:10.1242/jcs.017665 · Cited by 79 · see citing works
Tau associates with actin in differentiating PC12 cells
Yu, J.-Z., & Rasenick, M. M. (2006) · The FASEB Journal · doi:10.1096/fj.05-5206com · Cited by 72 · see citing works
Modeling of Tau-Mediated Synaptic and Neuronal Degeneration in Alzheimer's Disease
Jaworski, T., Kügler, S., & LEUVEN, F. V. (2010) · International Journal of Alzheimer s Disease · doi:10.4061/2010/573138 · Cited by 42 · see citing works
Feuillette, S., Deramecourt, V., Laquerrière, A., Duyckaerts, C. J., Delisle, M., Maurage, C., Blum, D. L., Buée, L., Frébourg, T., Campion, D., et al. (2010) · Brain Research · doi:10.1016/j.brainres.2010.05.007 · Cited by 31 · see citing works
Blockade of NR2A-Containing NMDA Receptors Induces Tau Phosphorylation in Rat Hippocampal Slices
Allyson, J., Dontigny, E., Auberson, Y. P., Cyr, M., & Massicotte, G. (2010) · Neural Plasticity · doi:10.1155/2010/340168 · Cited by 21 · 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
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
Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease
Guo, T., Zhang, D., Zeng, Y., Huang, T. Y., Xu, H., & Zhao, Y. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00391-7 · Cited by 994 · see citing works
The Amyloid-β Oligomer Hypothesis: Beginning of the Third Decade
Cline, E. N., Bicca, M. A., Viola, K. L., & Klein, W. L. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-179941 · Cited by 870 · see citing works
Arendt, T., Stieler, J. T., & Holzer, M. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.08.018 · Cited by 609 · see citing works
Dejanovic, B., Huntley, M. A., De Mazière, A., Meilandt, W. J., Wu, T., Srinivasan, K., Jiang, Z., Gandham, V., Friedman, B. A., Ngu, H., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.10.014 · Cited by 575 · see citing works
Amyloid-β and tau complexity — towards improved biomarkers and targeted therapies
Polanco, J. C., Li, C., Bodea, L., Martínez‐Mármol, R., Meunier, F. A., & Götz, J. (2017) · Nature Reviews Neurology · doi:10.1038/nrneurol.2017.162 · Cited by 374 · see citing works
The 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
Ferreira, S. T., Lourenco, M. V., Oliveira, M. M., & De Felice, F. G. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00191 · Cited by 373 · see citing works
Tau and neuroinflammation: what impact for Alzheimer's disease and tauopathies?
Laurent, C., Buée, L., & Blum, D. (2018) · Biomedical Journal · doi:10.1016/j.bj.2018.01.003 · Cited by 348 · see citing works
Tau interactome maps synaptic and mitochondrial processes associated with neurodegeneration
Tracy, T. E., Madero‐Pérez, J., Swaney, D. L., Chang, T. S., Moritz, M., Konràd, C., Ward, M. E., Stevenson, E. J., Hüttenhain, R., Kauwe, G., et al. (2022) · Cell · doi:10.1016/j.cell.2021.12.041 · Cited by 347 · see citing works
Interaction of tau with the RNA-Binding Protein TIA1 Regulates tau Pathophysiology and Toxicity
Vanderweyde, T. E., Apicco, D. J., Youmans-Kidder, K., Ash, P. E. A., Cook, C. N., da Rocha, E. L., Jansen‐West, K. R., Frame, A. A., Citro, A., Leszyk, J., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.04.045 · Cited by 346 · see citing works
Role of Amyloid-β and Tau Proteins in Alzheimer’s Disease: Confuting the Amyloid Cascade
Gulisano, W., Maugeri, D., Baltrons, M. A., Fà, M., Amato, A., Palmeri, A., D’Adamio, L., Grassi, C., Devanand, D. P., Honig, L. S., et al. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-179935 · Cited by 313 · 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
A walk through tau therapeutic strategies
Jadhav, S., Ávila, J., Schöll, M., Kovács, G. G., Kövari, E., Škrabana, R., Evans, L., Kontseková, E., Malawska, B., de Silva, R., et al. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0664-z · Cited by 286 · 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
Tracy, T. E., Sohn, P. D., Minami, S. S., Wang, C., Min, S.-W., Li, Y., Zhou, Y., Le, D., Lo, I., Ponnusamy, R., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.03.005 · Cited by 277 · see citing works
Tau-based therapies in neurodegeneration: opportunities and challenges
Li, C., & Götz, J. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.155 · Cited by 272 · see citing works
Synaptic dysfunction in Alzheimer's disease: Mechanisms and therapeutic strategies
Chen, Y., Fu, A. K. Y., & Ip, N. Y. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2018.11.006 · Cited by 258 · see citing works
Modifiable Risk Factors for Alzheimer’s Disease
Edwards III, G. A., Gamez, N., Escobedo Jr., G., Calderon, O., & Moreno-Gonzalez, I. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00146 · Cited by 253 · see citing works
Cellular and pathological functions of tau
Bravo, C. P., Naguib, S. A., & Gan, L. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00753-9 · Cited by 245 · see citing works
The role of pathological tau in synaptic dysfunction in Alzheimer’s diseases
Wu, M., Zhang, M., Yin, X., Chen, K., Hu, Z., Zhou, Q., Cao, X., Chen, Z., & Liu, D. (2021) · Translational Neurodegeneration · doi:10.1186/s40035-021-00270-1 · Cited by 241 · see citing works
Alzheimer’s Disease: From Firing Instability to Homeostasis Network Collapse
Frère, S. G. A., & Slutsky, I. (2018) · Neuron · doi:10.1016/j.neuron.2017.11.028 · Cited by 230 · see citing works
A Brief Overview of Tauopathy: Causes, Consequences, and Therapeutic Strategies
Orr, M. E., Sullivan, A. C., & Frost, B. E. (2017) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2017.03.011 · Cited by 232 · see citing works
Rösler, T. W., Marvian, A. T., Brendel, M., Nykänen, N.-P., Höllerhage, M., Schwarz, S. C., Hopfner, F., Koeglsperger, T., Respondek, G., Schweyer, K., et al. (2019) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2019.101644 · Cited by 219 · see citing works
Atypical, non-standard functions of the microtubule associated Tau protein
Sotiropoulos, I., Galas, M., Silva, J. M., Skoulakis, E. M. C., Wegmann, S., Maina, M. B., Blum, D. L., Sayas, C. L., Mandelkow, E., Mandelkow�, E., et al. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0489-6 · Cited by 207 · see citing works
Tau co-organizes dynamic microtubule and actin networks
Elie, A., Prezel, E., Guérin, C., Denarier, E., Ramirez-Rios, S., Serre, L., Andrieux, A., Fourest-Lieuvin, A., Blanchoin, L., & Arnal, I. (2015) · Scientific Reports · doi:10.1038/srep09964 · Cited by 200 · see citing works
Self-citationNeurodegenerative Disease and the NLRP3 Inflammasome
Holbrook, J. A., Jarosz-Griffiths, H., Caseley, E. A., Reyna, S. J. L., Poulter, J. A., Williams‐Gray, C. H., Peckham, D. G., & McDermott, M. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.643254 · Cited by 197 · see citing works
Li, C., & Götz, J. (2017) · The EMBO Journal · doi:10.15252/embj.201797724 · Cited by 178 · see citing works
Metabolism: A Novel Shared Link between Diabetes Mellitus and Alzheimer’s Disease
Sun, Y., Ma, C., Sun, H. J., Wang, H., Wei, P., Zhou, Z., Wang, H., Pi, C., Shi, Y., & He, X. (2020) · Journal of Diabetes Research · doi:10.1155/2020/4981814 · Cited by 172 · see citing works
Dourlen, P., Kilinc, D., Malmanche, N., Chapuis, J., & Lambert, J.-C. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02004-0 · Cited by 168 · see citing works
Tau Oligomers: The Toxic Player at Synapses in Alzheimer’s Disease
Guerrero-Muñoz, M. J., Gerson, J., & Castillo-Carranza, D. L. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00464 · Cited by 168 · see citing works
TIA1 potentiates tau phase separation and promotes generation of toxic oligomeric tau
Ash, P. E. A., Lei, S., Shattuck, J., Boudeau, S., Carlomagno, Y., Medalla, M., Mashimo, B. L., Socorro, G., Al-Mohanna, L. F. A., Jiang, L., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2014188118 · Cited by 159 · see citing works
Hall, A. M., Throesch, B. T., Buckingham, S. C., Markwardt, S. J., Peng, Y., Wang, Q., Hoffman, D. A., & Roberson, E. D. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.2552-14.2015 · Cited by 152 · see citing works
TRIM28 regulates the nuclear accumulation and toxicity of both alpha-synuclein and tau
Rousseaux, M. W. C., de Haro, M., Lasagna‐Reeves, C. A., Maio, A. D., Park, J., Jafar‐Nejad, P., Al‐Ramahi, I., Sharma, A., See, L., Lü, N., et al. (2016) · eLife · doi:10.7554/elife.19809 · Cited by 150 · see citing works
Cabrales Fontela, Y., Kadavath, H., Biernat, J., Riedel, D., Mandelkow, E., & Zweckstetter, M. (2017) · Nature Communications · doi:10.1038/s41467-017-02230-8 · Cited by 148 · see citing works
Role of Aβ in Alzheimer’s-related synaptic dysfunction
Zhang, H., Jiang, X., Ma, L., Wei, W., Li, Z., Chang, S., Wen, J., Sun, J., & Li, H. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.964075 · Cited by 144 · see citing works
Pre‐synaptic C‐terminal truncated tau is released from cortical synapses in Alzheimer's disease
Sokolow, S., Henkins, K. M., Bilousova, T., Gonzalez, B., Vinters, H. V., Miller, C. A., Cornwell, L., Poon, W. W., & Gylys, K. H. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.12991 · Cited by 133 · see citing works
Synaptic dysfunction and septin protein family members in neurodegenerative diseases
Marttinen, M., Kurkinen, K. M. A., Soininen, H. S., Haapasalo, A., & Hiltunen, M. O. (2015) · Molecular Neurodegeneration · doi:10.1186/s13024-015-0013-z · Cited by 129 · see citing works
Connecting the dots between tau dysfunction and neurodegeneration
Frost, B., Götz, J., & Feany, M. B. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.07.005 · Cited by 124 · see citing works
Baas, P. W., & Qiang, L. (2019) · Trends in Cell Biology · doi:10.1016/j.tcb.2019.02.007 · Cited by 123 · see citing works
Tau: The Center of a Signaling Nexus in Alzheimer's Disease
Khan, S. S., & Bloom, G. S. (2016) · Frontiers in Neuroscience · doi:10.3389/fnins.2016.00031 · Cited by 121 · see citing works
Henderson, B. W., Gentry, E. G., Rush, T., Troncoso, J. C., Thambisetty, M., Montine, T. J., & Herskowitz, J. H. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13688 · Cited by 120 · see citing works
Self-citationBiswas, S., & Kalil, K. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.2281-17.2017 · Cited by 119 · see citing works
Calderón‐Garcidueñas, A. L., & Duyckaerts, C. J. (2017) · Handbook of clinical neurology · doi:10.1016/b978-0-12-802395-2.00023-7 · Cited by 120 · see citing works
Kabir, M. T., Sufian, M. A., Uddin, M. S., Begum, M. M., Akhter, S., Islam, A., Mathew, B., Islam, M. S., Amran, M. S., & Ashraf, G. M. (2019) · Current Pharmaceutical Design · doi:10.2174/1381612825666191011102444 · Cited by 120 · see citing works
Synaptic tau: A pathological or physiological phenomenon?
Robbins, M., Clayton, E. L., & Schierle, G. S. K. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01246-y · Cited by 117 · see citing works
Penke, B., Szűcs, M., & Bogár, F. (2020) · Molecules · doi:10.3390/molecules25071659 · Cited by 115 · see citing works
Amar, F., Sherman, M. A., Rush, T., Larson, M. E., Boyle, G. E., Liu, C., Götz, J., Buisson, A., & Lesné, S. (2017) · Science Signaling · doi:10.1126/scisignal.aal2021 · Cited by 109 · see citing works
Self-citationRetractedTau in the Pathophysiology of Parkinson’s Disease
Pan, L., Meng, L., He, M., & Zhang, Z. (2021) · Journal of Molecular Neuroscience · doi:10.1007/s12031-020-01776-5 · Cited by 110 · 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
Rush, T., Hernández, J. M., Dollmeyer, M., Frandemiche, M., Borel, E., Boisseau, S., Jacquier‐Sarlin, M. R., & Buisson, A. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.1409-18.2018 · Cited by 110 · see citing works
Self-citationEndolysosomal degradation of Tau and its role in glucocorticoid-driven hippocampal malfunction
Vaz-Silva, J., Gomes, P. A., Jin, Q., Zhu, M., Zhuravleva, V., Quintremil, S., Meira, T., Silva, J., Dioli, C., Soares-Cunha, C., et al. (2018) · bioRxiv · doi:10.15252/embj.201899084 · Cited by 92 · see citing works
Synaptic activity and Alzheimer's disease: a critical update
Tampellini, D. (2015) · Frontiers in Neuroscience · doi:10.3389/fnins.2015.00423 · Cited by 105 · see citing works
The cytoskeleton as a novel therapeutic target for old neurodegenerative disorders
Eira, J., Silva, C. S., Sousa, M. M., & Liz, M. A. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.04.007 · Cited by 103 · see citing works
Tau physiology and pathomechanisms in frontotemporal lobar degeneration
Bodea, L., Eckert, A., Ittner, L. M., Piguet, O., & Götz, J. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13600 · Cited by 104 · see citing works
The Role of Protein Misfolding and Tau Oligomers (TauOs) in Alzheimer′s Disease (AD)
Mroczko, B., Groblewska, M., & Litman‐Zawadzka, A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20194661 · Cited by 106 · see citing works
Pallas‐Bazarra, N., Jurado‐Arjona, J., Navarrete, M., Esteban, J. A., Hernández, F., Ávila, J., & Llorens‐Martín, M. (2016) · The EMBO Journal · doi:10.15252/embj.201593518 · Cited by 101 · see citing works
Acute tau knockdown in the hippocampus of adult mice causes learning and memory deficits
Velázquez, R., Ferreira, E., Tran, A., Turner, E. C., Belfiore, R., Branca, C., & Oddo, S. (2018) · Aging Cell · doi:10.1111/acel.12775 · Cited by 96 · see citing works
Tau-mediated synaptic damage in Alzheimer’s disease
Jadhav, S., Cubinkova, V., Zimova, I., Brezováková, V., Maďari, A., Cigánková, V., & Žilka, N. (2015) · Translational Neuroscience · doi:10.1515/tnsci-2015-0023 · Cited by 92 · see citing works
Xia, D., Li, C., & Götz, J. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.12.017 · Cited by 88 · see citing works
Liquid–liquid phase separation of Tau by self and complex coacervation
Najafi, S., Lin, Y., Longhini, A. P., Zhang, X., Delaney, K. T., Kosik, K. S., Fredrickson, G. H., Shea, J., & Han, S. (2021) · Protein Science · doi:10.1002/pro.4101 · Cited by 87 · see citing works
Molecular Mechanisms of Synaptotoxicity and Neuroinflammation in Alzheimer’s Disease
Marttinen, M., Takalo, M., Natunen, T., Wittrahm, R., Gabbouj, S., Kemppainen, S., Leinonen, V., Tanila, H., Haapasalo, A., & Hiltunen, M. O. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00963 · Cited by 86 · see citing works
Specialized roles of neurofilament proteins in synapses: Relevance to neuropsychiatric disorders
Yuan, A., & Nixon, R. A. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.09.002 · Cited by 84 · see citing works
Tauopathies: Deciphering Disease Mechanisms to Develop Effective Therapies
Silva, M. C., & Haggarty, S. J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21238948 · Cited by 87 · see citing works
Fyn Kinase Controls Tau Aggregation In Vivo
Briner, A., Götz, J., & Polanco, J. C. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108045 · Cited by 80 · see citing works
Domise, M., Sauvé, F., Didier, S., Caillerez, R., Bégard, S., Carrier, S., Colin, M., Marinangeli, C., Buée, L., & Vingtdeux, V. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1464-x · Cited by 81 · see citing works
Sanyal, C., Pietsch, N., Ramírez‐Ríos, S., Peris, L., Carrier, L., & Moutin, M. (2021) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2021.12.006 · Cited by 80 · see citing works
Mueller, R. L., Combs, B., Alhadidy, M. M., Brady, S. T., Morfini, G. A., & Kanaan, N. M. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.647054 · Cited by 78 · see citing works
Dendritic Spine and Synaptic Plasticity in Alzheimer’s Disease: A Focus on MicroRNA
Reza-Zaldívar, E. E., Hernández-Sapiéns, M. A., Minjarez, B. D., Gómez‐Pinedo, U., Sánchez-González, V., Márquez-Aguirre, A. L., & Canales-Aguirre, A. A. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00255 · Cited by 77 · see citing works
Kobayashi, S., Tanaka, T., Soeda, Y., Almeida, O. F. X., & Takashima, A. (2017) · EBioMedicine · doi:10.1016/j.ebiom.2017.05.012 · Cited by 74 · see citing works
Acetylated tau in Alzheimer's disease: An instigator of synaptic dysfunction underlying memory loss
Tracy, T. E., & Gan, L. (2017) · BioEssays · doi:10.1002/bies.201600224 · Cited by 72 · see citing works
Inhibiting BACE1 to reverse synaptic dysfunctions in Alzheimer’s disease
Yan, R., Fan, Q., Zhou, J., & Vassar, R. J. (2016) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2016.03.025 · Cited by 71 · see citing works
Sun, X., Tuo, Q., Liuyang, Z., Xie, A., Feng, X.-L., Yan, X., Qiu, M., Shen, L., Wang, X.-L., Cao, F.-Y., et al. (2016) · Cell Death and Disease · doi:10.1038/cddis.2016.329 · Cited by 71 · see citing works
Alzheimer’s disease risk gene BIN1 induces Tau-dependent network hyperexcitability
Voskobiynyk, Y., Roth, J. R., Cochran, J. N., Rush, T., Carullo, N. V. N., Mesina, J. S., Waqas, M., Vollmer, R. M., Day, J. J., McMahon, L. L., et al. (2020) · eLife · doi:10.7554/elife.57354 · Cited by 66 · see citing works
Self-citationAltered ribosomal function and protein synthesis caused by tau
Evans, H. T., Taylor, D. W., Kneynsberg, A., Bodea, L., & Götz, J. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01208-4 · Cited by 70 · see citing works
Physiological and Pathophysiological Implications of Synaptic Tau
Regan, P. L., Whitcomb, D. J., & Cho, K. (2016) · The Neuroscientist · doi:10.1177/1073858416633439 · Cited by 70 · see citing works
Drosophila Models of Alzheimer's Disease: Advances, Limits, and Perspectives
Bouleau, S., & Tricoire, H. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-142802 · Cited by 68 · see citing works
Lopes, S., Teplytska, L., Vaz-Silva, J., Dioli, C., Trindade, R., Morais, M., Webhofer, C., Maccarrone, G., Almeida, O. F. X., Turck, C. W., et al. (2016) · Cerebral Cortex · doi:10.1093/cercor/bhw057 · Cited by 66 · see citing works
Tau, microtubule dynamics, and axonal transport: New paradigms for neurodegenerative disease
Cario, A., & Berger, C. L. (2023) · BioEssays · doi:10.1002/bies.202200138 · Cited by 64 · see citing works
Engineering Cortical Neuron Polarity with Nanomagnets on a Chip
Kunze, A., Tseng, P., Godzich, C., Murray, C., Caputo, A., Schweizer, F. E., & Carlo, D. D. (2015) · ACS Nano · doi:10.1021/nn505330w · Cited by 62 · see citing works
Synaptic activity protects against AD and FTD-like pathology via autophagic-lysosomal degradation
Akwa, Y., Gondard, E., Mann, A., Capetillo‐Zarate, E., Alberdi, E. M., Matute, C., Marty, S., Vaccari, T., Lozano, A. M., Baulieu, E. E., et al. (2017) · Molecular Psychiatry · doi:10.1038/mp.2017.142 · Cited by 62 · see citing works
Tau neurotoxicity and rescue in animal models of human Tauopathies
Krüger, L., & Mandelkow, E. (2015) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2015.09.004 · Cited by 60 · see citing works
Actin dynamics shape microglia effector functions.
Uhlemann, R., Gertz, K., Boehmerle, W., Schwarz, T., Nolte, C., Freyer, D., Kettenmann, H., Endres, M., & Kronenberg, G. (2016) · Brain Structure and Function · doi:10.1007/s00429-015-1067-y · Cited by 61 · see citing works
Distribution of endogenous normal tau in the mouse brain
Kubo, A., Misonou, H., Matsuyama, M., Nomori, A., Wada‐Kakuda, S., Takashima, A., Kawata, M., Murayama, S., Ihara, Y., & Miyasaka, T. (2019) · Journal of Comparative Neurology · doi:10.1002/cne.24577 · Cited by 57 · see citing works
Eysert, F., Coulon, A., Boscher, E., Vreulx, A.-C., Flaig, A., Mendes, T., Hughes, S., Grenier-Boley, B., Hanoulle, X., Demiautte, F., et al. (2021) · Molecular Psychiatry · doi:10.1038/s41380-020-00926-w · Cited by 55 · see citing works
Alzheimer disease: modeling an Aβ-centered biological network
Campion, D., Pottier, C. P., Nicolas, G., Guennec, K. L., & Rovelet‐Lecrux, A. (2016) · Molecular Psychiatry · doi:10.1038/mp.2016.38 · Cited by 52 · see citing works
Soluble Tau has devastating effects on the structural plasticity of hippocampal granule neurons
Bolós, M., Pallas‐Bazarra, N., Terreros‐Roncal, J., Perea, J. R., Jurado‐Arjona, J., Ávila, J., & Llorens-Martı́n, M. (2017) · Translational Psychiatry · doi:10.1038/s41398-017-0013-6 · Cited by 51 · see citing works
Melone, M. A. B., Dato, C., Paladino, S., Coppola, C., Trebini, C., Giordana, M. T., & Perrone, L. (2018) · Pharmaceutical Research · doi:10.1007/s11095-017-2276-2 · Cited by 52 · see citing works
RetractedPhosphorylation of nuclear Tau is modulated by distinct cellular pathways
Ulrich, G., Salvadè, A., Boersema, P. J., Calí, T., Foglieni, C., Sola, M., Picotti, P., Papin, S., & Paganetti, P. (2018) · Scientific Reports · doi:10.1038/s41598-018-36374-4 · Cited by 52 · see citing works
VEGF counteracts amyloid-β-induced synaptic dysfunction
Martin, L., Bouvet, P., Chounlamountri, N., Watrin, C., Besançon, R., Pinatel, D., Meyronet, D., Honnorat, J., Buisson, A., Salin, P. A., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109121 · Cited by 49 · see citing works
Self-citationXia, D., Gutmann, J. M., & Götz, J. (2016) · Scientific Reports · doi:10.1038/srep29074 · Cited by 47 · see citing works
Tau Spreading Mechanisms; Implications for Dysfunctional Tauopathies
Fuster-Matanzo, A., Hernández, F., & Ávila, J. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19030645 · Cited by 48 · see citing works
Saranza, G., Whitwell, J. L., Kovács, G. G., & Lang, A. E. (2019) · International review of neurobiology · doi:10.1016/bs.irn.2019.10.014 · Cited by 48 · see citing works
Montalbano, M., McAllen, S., Sengupta, U., Puangmalai, N., Bhatt, N. N., Ellsworth, A., & Kayed, R. (2019) · Aging Cell · doi:10.1111/acel.13035 · Cited by 45 · see citing works
Neuronal and Glial Distribution of Tau Protein in the Adult Rat and Monkey
Kanaan, N. M., & Grabinski, T. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.607303 · Cited by 46 · see citing works
The multifaceted role of WNT signaling in Alzheimer’s disease onset and age-related progression.
Kostes, W. W., & Brafman, D. A. (2023) · Cells · doi:10.3390/cells12081204 · Cited by 43 · see citing works
Ribosome-Directed Therapies in Cancer
Temaj, G., Chichiarelli, S., Eufemi, M., Fabio Altieri, F., Hadžiselimović, R., Farooqı, A. A., Yaylım, İ., & Saso, L. (2022) · Biomedicines · doi:10.3390/biomedicines10092088 · Cited by 43 · see citing works
Tau Mislocation in Glucocorticoid-Triggered Hippocampal Pathology
Pinheiro, S., Silva, J. M., Mota, C., Vaz‐Silva, J., Veloso, A., Pinto, V., Sousa, N., Cerqueira, J., & Sotiropoulos, I. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9356-2 · Cited by 43 · see citing works
Hill, E., Wall, M. J., Moffat, K. G., & Karikari, T. K. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.00155 · Cited by 42 · see citing works
- Authors
- Frandemiche, M. L., De Seranno, S., Rush, T., Borel, E., Elie, A., Arnal, I., Lanté, F., & Buisson, A.
- Affiliations
- Inserm (FR)
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2014-04-23
- Volume
- 34
- Issue
- 17
- Pages
- 6084-6097
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC6608293
- OpenAlex
- W2006955217
- Cited by
- 272
- References
- 48
- Citations by year
- 2026: 11 · 2025: 21 · 2024: 27 · 2023: 9 · 2022: 18 · 2021: 30 · 2020: 29 · 2019: 26 · 2018: 32 · 2017: 23 · 2016: 25 · 2015: 18 · 2014: 3
- FWCI
- 15.34
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Fondation Neurodis
- Agence Nationale de la Recherche
- Institut National de la Santé et de la Recherche Médicale
- Centre National de la Recherche Scientifique
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- tau protein, amyloid-beta oligomers, synaptic plasticity, postsynaptic density, excitatory synapses, synaptotoxicity, Alzheimer's disease, long-term potentiation, actin, tau phosphorylation, dendritic spines, cortical neurons, hippocampus
- MeSH terms
- Animals, Cells, Cultured, Cerebral Cortex, Dendrites, Neurons, Peptide Fragments, Phosphorylation, Synapses, Amyloid beta-Peptides, tau Proteins, Protein Transport, 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
