Soluble pathological tau in the entorhinal cortex leads to presynaptic deficits in an early Alzheimer’s disease model
Open accessAbstract
Neurofibrillary tangles (NFTs), a hallmark of Alzheimer's disease, are intracellular silver and thioflavin S-staining aggregates that emerge from earlier accumulation of phospho-tau in the soma. Whether soluble misfolded but nonfibrillar tau disrupts neuronal function is unclear. Here we investigate if soluble pathological tau, specifically directed to the entorhinal cortex (EC), can cause behavioral or synaptic deficits. We studied rTgTauEC transgenic mice, in which P301L mutant human tau overexpressed primarily in the EC leads to the development of tau pathology, but only rare NFT at 16 months of age. We show that the early tau lesions are associated with nearly normal performance in contextual fear conditioning, a hippocampal-related behavior task, but more robust changes in neuronal system activation as marked by Arc induction and clear electrophysiological defects in perforant pathway synaptic plasticity. Electrophysiological changes were likely due to a presynaptic deficit and changes in probability of neurotransmitter release. The data presented here support the hypothesis that misfolded and hyperphosphorylated tau can impair neuronal function within the entorhinal-hippocampal network, even prior to frank NFT formation and overt neurodegeneration.
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?
Soluble oligomeric tau may play a more essential role in neurodegeneration than insoluble fibrillar tau, including NFTs.
“These findings indicate that soluble oligomeric tau may play a more essential role in neurodegeneration than insoluble fibrillar tau (including NFT), the “tau we can see”.”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [28]
Soluble tau, rather than fibrillar tau, impacts responsiveness of neurons to environmental stimuli in hippocampus after memory formation.
“From assessments of immediate early gene expression in the hippocampus after memory formation, it again appears that soluble tau, rather than fibrillar tau, seems to impact the responsiveness of neurons to environmental stimuli.”
From All the Tau We Cannot See (2023) · cites this paper as [20]
Mitochondrial abnormalities, synaptic loss and dysfunction, altered axonal transport, and activation of cell death pathways have been implicated as consequences of tau mislocalization or oligomerization.
“Mitochondrial abnormalities, synaptic loss and dysfunction, altered axonal transport, and activation of cell death pathways (including caspase activation and inflammatory responses) have all been directly or indirectly implicated as consequences of tau mislocalization or oligomerization (20, 40, 43–52).”
From All the Tau We Cannot See (2023) · cites this paper as [20]
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
Alzheimer's disease: cell-specific pathology isolates the hippocampal formation.
Hyman, B. T., Van Hoesen, G. W., Damasio, A. R., & Barnes, C. L. (1984) · Science · doi:10.1126/science.6474172 · Cited by 2,268 · see citing works
Self-citationTau Suppression in a Neurodegenerative Mouse Model Improves Memory Function
SantaCruz, K., Lewis, J., Spires, T., Paulson, J., Kotilinek, L., Ingelsson, M., Guimaraes, A., DeTure, M., Ramsden, M., McGowan, E., et al. (2005) · Science · doi:10.1126/science.1113694 · Cited by 2,014 · see citing works
Self-citationPropagation of Tau Pathology in a Model of Early Alzheimer's Disease
de Calignon, A., Polydoro, M., Suárez-Calvet, M., William, C., Adamowicz, D. H., Kopeikina, K. J., Pitstick, R., Sahara, N., Ashe, K. H., Carlson, G. A., et al. (2012) · Neuron · doi:10.1016/j.neuron.2011.11.033 · Cited by 1,427 · see citing works
Self-citationThe role of calcium in neuromuscular facilitation
Katz, B., & Miledi, R. (1968) · The Journal of Physiology · doi:10.1113/jphysiol.1968.sp008469 · Cited by 1,347 · see citing works
Trans-Synaptic Spread of Tau Pathology In Vivo
Liu, L., Drouet, V., Wu, J., Witter, M. P., Small, S. A., Clelland, C. L. T., & Duff, K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031302 · Cited by 994 · see citing works
Arc/Arg3.1 Is Essential for the Consolidation of Synaptic Plasticity and Memories
Plath, N., Ohana, O., Dammermann, B., Errington, M. L., Schmitz, D., Gross, C., Mao, X., Engelsberg, A., Mahlke, C., Welzl, H., et al. (2006) · Neuron · doi:10.1016/j.neuron.2006.08.024 · Cited by 827 · see citing works
Zempel, H., Thies, E., Mandelkow, E., & Mandelkow, E.-M. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.2357-10.2010 · Cited by 686 · cited 2× · see citing works
“Indeed, recent studies suggest that more soluble forms of tau, rather than fibrillar tangles, may be involved in neuronal dysfunction [28, 29, 44, 45, 50, 63].”
BackgroundResultEarly Aβ accumulation and progressive synaptic loss, gliosis, and tangle formation in AD brain
Ingelsson, M., Fukumoto, H., Newell, K. L., Growdon, J. H., Hedley–Whyte, E. T., Frosch, M. P., Albert, M. S., Hyman, B. T., & Irizarry, M. C. (2004) · Neurology · doi:10.1212/01.wnl.0000115115.98960.37 · Cited by 666 · see citing works
Self-citationActivity-dependent neuronal signalling and autism spectrum disorder
Ebert, D. H., & Greenberg, M. E. (2013) · Nature · doi:10.1038/nature11860 · Cited by 666 · see citing works
Manabe, T., Wyllie, D. J., Perkel, D. J., & Nicoll, R. A. (1993) · Journal of Neurophysiology · doi:10.1152/jn.1993.70.4.1451 · Cited by 666 · see citing works
Physiological release of endogenous tau is stimulated by neuronal activity
Pooler, A. M., Phillips, E. C., Lau, D. H. W., Noble, W., & Hanger, D. P. (2013) · The EMBO Reports · doi:10.1038/embor.2013.15 · Cited by 642 · see citing works
Self-citationHigh-frequency firing helps replenish the readily releasable pool of synaptic vesicles
Wang, L., & Kaczmarek, L. K. (1998) · Nature · doi:10.1038/28645 · Cited by 614 · see citing works
Debanne, D., Guérineau, N. C., Gähwiler, B. H., & Thompson, S. M. (1996) · The Journal of Physiology · doi:10.1113/jphysiol.1996.sp021204 · Cited by 613 · see citing works
A quantitative study of end‐plate potentials in isolated human muscle.
Elmqvist, D., & Quastel, D. M. J. (1965) · The Journal of Physiology · doi:10.1113/jphysiol.1965.sp007639 · Cited by 579 · see citing works
The Alzheimer’s Disease Mitochondrial Cascade Hypothesis
Swerdlow, R. H., Burns, J. M., & Khan, S. M. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100339 · Cited by 562 · cited 1× · see citing works
“Indeed, recent studies suggest that more soluble forms of tau, rather than fibrillar tangles, may be involved in neuronal dysfunction [28, 29, 44, 45, 50, 63].”
BackgroundReinforcing and locomotor stimulant effects of cocaine are absent in mGluR5 null mutant mice
Chiamulera, C., Epping-Jordan, M. P., Zocchi, A., Marcon, C., Cottiny, C., Tacconi, S., Corsi, M., Orzi, F., & Conquet, F. (2001) · Nature Neuroscience · doi:10.1038/nn0901-873 · Cited by 554 · see citing works
Hydrofluoric acid-treated tau PHF proteins display the same biochemical properties as normal tau.
Greenberg, S. G., Davies, P., Schein, J., & Binder, L. I. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48531-6 · Cited by 542 · see citing works
Monoclonal antibody PHF‐1 recognizes tau protein phosphorylated at serine residues 396 and 404
Otvos, L., Feiner, L., Lang, E., Szendrei, G. I., Goedert, M., & Lee, V. M. (1994) · Journal of Neuroscience Research · doi:10.1002/jnr.490390607 · Cited by 488 · cited 1× · see citing works
“The antibody Tau13 which recognizes the amino acid residues 20–35 on the longest isoform of human tau [2, 25] (Covance; 1:1,000) was used to detect human tau; the conformation-specific Alz50 and MC1 antibodies (courtesy Peter Davies, Albert einstein College of Medicine; 1:50) [3, 5, 30] used to detect misfolded tau, a…”
MethodTau, tangles, and Alzheimer's disease.
Binder, L., Guillozet-Bongaarts, A. L., García-Sierra, F., & Berry, R. (2005) · Biochimica et Biophysica Acta · doi:10.1016/j.bbadis.2004.08.014 · Cited by 443 · see citing works
Double-knockout mice for α- and β-synucleins: Effect on synaptic functions
Chandra, S., Fornai, F., Kwon, H.-B., Yazdani, U., Atasoy, D., Liu, X., Hammer, R. E., Battaglia, G., German, D. C., Castillo, P. E., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0406283101 · Cited by 438 · see citing works
Cortical Afferents to the Entorhinal Cortex of the Rhesus Monkey
Hoesen, G. W. V., Pandya, D. Ν., & Butters, N. (1972) · Science · doi:10.1126/science.175.4029.1471 · Cited by 412 · see citing works
Silver staining of Alzheimer's neurofibrillary changes by means of physical development.
Gallyas, F. (1971) · PubMed · Cited by 411 · see citing works
Dittman, J. S., & Regehr, W. G. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-16-06147.1998 · Cited by 410 · see citing works
The Structural Basis of Monoclonal Antibody Alz50's Selectivity for Alzheimer's Disease Pathology
Carmel, G., Mager, E. M., Binder, L. I., & Kuret, J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.51.32789 · Cited by 402 · see citing works
Facilitation, augmentation and potentiation at central synapses
Thomson, A. M. (2000) · Trends in Neurosciences · doi:10.1016/s0166-2236(00)01580-0 · Cited by 387 · see citing works
Stevens, C. F., & Tsujimoto, T. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.3.846 · Cited by 371 · see citing works
Yamada, K., Cirrito, J. R., Stewart, F. R., Jiang, H., Finn, M. B., Holmes, B. B., Binder, L. I., Mandelkow, E.-M., Diamond, M. I., Lee, V. M.-Y., et al. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.2569-11.2011 · Cited by 351 · see citing works
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
Self-citationStevens, C., & Wesseling, J. F. (1998) · Neuron · doi:10.1016/s0896-6273(00)80550-4 · Cited by 327 · see citing works
Conformational change as one of the earliest alterations of tau in Alzheimer's disease
Weaver, C. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00157-3 · Cited by 310 · see citing works
Kopeikina, K. J., Carlson, G. A., Pitstick, R., Ludvigson, A. E., Peters, A., Luebke, J. I., Koffie, R. M., Frosch, M. P., Hyman, B. T., & Spires‐Jones, T. L. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2011.07.004 · Cited by 272 · see citing works
Self-citationTDP-43 is deposited in the Guam parkinsonism-dementia complex brains
Hasegawa, M., Arai, T., Akiyama, H., Nonaka, T., Mori, H., Hashimoto, T., Yamazaki, M., & Oyanagi, K. (2007) · Brain · doi:10.1093/brain/awm065 · Cited by 242 · see citing works
Multiple periods of functional ocular dominance plasticity in mouse visual cortex
Tagawa, Y., Kanold, P. O., Majdan, M., & Shatz, C. J. (2005) · Nature Neuroscience · doi:10.1038/nn1410 · Cited by 235 · see citing works
Soluble forms of tau are toxic in Alzheimer's disease
Kopeikina, K., Hyman, B., & Spires-Jones, T. (2012) · Translational Neuroscience · doi:10.2478/s13380-012-0032-y · Cited by 232 · see citing works
Self-citationSakaba, T., & Neher, E. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-02-00462.2001 · Cited by 216 · see citing works
Wang, Y. P., Biernat, J., Pickhardt, M., Mandelkow�, E., & Mandelkow�, E. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0703676104 · Cited by 205 · see citing works
Structural and functional changes in tau mutant mice neurons are not linked to the presence of NFTs
Rocher, A. B., Crimins, J. L., Amatrudo, J. M., Kinson, M. S., Todd-Brown, M. A., Lewis, J., & Luebke, J. I. (2010) · Experimental Neurology · doi:10.1016/j.expneurol.2009.07.029 · Cited by 187 · see citing works
Caspase-cleaved Tau Expression Induces Mitochondrial Dysfunction in Immortalized Cortical Neurons
Quintanilla, R. A., Matthews-Roberson, T. A., Dolan, P. J., & Johnson, G. V. W. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808908200 · Cited by 170 · see citing works
Bi, M., Ittner, A., Ke, Y. D., Götz, J., & Ittner, L. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0026860 · Cited by 153 · see citing works
Long-Term Potentiation Selectively Expressed by NMDA Receptors at Hippocampal Mossy Fiber Synapses
Kwon, H., & Castillo, P. E. (2008) · Neuron · doi:10.1016/j.neuron.2007.11.024 · Cited by 147 · see citing works
Wilcox, K. S., & Dichter, M. (1994) · Journal of Neuroscience · doi:10.1523/jneurosci.14-03-01775.1994 · Cited by 136 · see citing works
Harris, J. A., Koyama, A., Maeda, S., Ho, K., Devidze, N., Dubal, D. B., Yu, G.-Q., Masliah, E., & Mucke, L. (2012) · PLoS ONE · doi:10.1371/journal.pone.0045881 · Cited by 135 · see citing works
Bellone, C., & Lüscher, C. (2005) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2005.03979.x · Cited by 129 · see citing works
Synaptic depression: a dynamic regulator of synaptic communication with varied functional roles
O'Donovan, M. J. (1997) · Trends in Neurosciences · doi:10.1016/s0166-2236(97)01124-7 · Cited by 115 · see citing works
Ksiȩżak-Reding, H., Davies, P., & Yen, S. H. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68425-x · Cited by 109 · see citing works
Ke, Y. D., Dramiga, J., Schütz, U., Kril, J. J., Ittner, L. M., Schröder, H., & Götz, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0035678 · Cited by 104 · see citing works
CaMKII Activation in the Entorhinal Cortex Disrupts Previously Encoded Spatial Memory
Yasuda, M., & Mayford, M. R. (2006) · Neuron · doi:10.1016/j.neuron.2006.03.035 · Cited by 100 · see citing works
Homer1 proteins and AMPA receptors modulate cocaine‐induced behavioural plasticity
Ghasemzadeh, M. B., Permenter, L. K., LAKE, R. W., Worley, P. F., & Kalivas, P. W. (2003) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.2003.02880.x · Cited by 93 · see citing works
Mennerick, S. J., & Zorumski, C. F. (1995) · Journal of Neuroscience · doi:10.1523/jneurosci.15-04-03178.1995 · Cited by 91 · see citing works
Czerniawski, J. L., Ree, F., Chia, C., Ramamoorthi, K., Kumata, Y., & Otto, T. A. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.2211-11.2011 · Cited by 91 · see citing works
Fox, 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
Self-citationKirischuk, S., Clements, J. D., & Grantyn, R. (2002) · The Journal of Physiology · doi:10.1113/jphysiol.2002.021576 · Cited by 86 · see citing works
Role of Ca2+ channels in short-term synaptic plasticity
Xu, J., He, L., & Wu, L. (2007) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2007.04.005 · Cited by 84 · see citing works
Lee, D., Lee, K.-H., Ho, W., & Lee, S. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.3985-07.2007 · Cited by 81 · see citing works
Lee, J. S., Kim, M., Ho, W., & Lee, S. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.2165-08.2008 · Cited by 80 · see citing works
Prescott, S. A. (1998) · Learning & Memory · doi:10.1101/lm.5.6.446 · Cited by 73 · see citing works
Paired‐pulse modulation at individual GABAergic synapses in rat hippocampus
Jiang, L., Sun, S., Nedergaard, M., & Kang, J. (2000) · The Journal of Physiology · doi:10.1111/j.1469-7793.2000.t01-1-00425.x · Cited by 63 · see citing works
Metabotropic glutamate receptors are necessary for sensitization by amphetamine
Kim, J., & Vezina, P. (1998) · Neuroreport · doi:10.1097/00001756-199802160-00008 · Cited by 54 · see citing works
Xiong, Z., & Stringer, J. L. (1997) · Epilepsy Research · doi:10.1016/s0920-1211(97)00022-3 · Cited by 39 · see citing works
Szumlinski, K. K., Toda, S., Middaugh, L. D., Worley, P. F., & Kalivas, P. W. (2003) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1300.055 · Cited by 27 · see citing works
Na+/Ca2+ Exchange and Ca2+ Homeostasis in Axon Terminals of Mammalian Central Neurons
Lee, S., LEE, S., Kim, M., et al. (2007) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1387.011 · Cited by 11 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
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
Tau association with synaptic vesicles causes presynaptic dysfunction
Zhou, L., McInnes, J., Wierda, K., Holt, M., Herrmann, A. G., Jackson, R. J., Wang, Y.-C., Swerts, J., Beyens, J., Miskiewicz, K., et al. (2017) · Nature Communications · doi:10.1038/ncomms15295 · Cited by 434 · see citing works
Self-citationSynaptic 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
Self-citationDe Chiara, G., Piacentini, R., Fabiani, M., Mastrodonato, A., Marcocci, M. E., Limongi, D., Napoletani, G., Protto, V., Coluccio, P., Celestino, I., et al. (2019) · PLOS Pathogens · doi:10.1371/journal.ppat.1007617 · Cited by 266 · see citing works
Synaptogyrin-3 Mediates Presynaptic Dysfunction Induced by Tau
McInnes, J., Wierda, K., Snellinx, A., Bounti, L., Wang, Y.-C., Stancu, I.-C., Apóstolo, N., Gevaert, K., Dewachter, I., Spires-Jones, T. L., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.01.022 · Cited by 242 · see citing works
Self-citationAmyloid accelerates tau propagation and toxicity in a model of early Alzheimer’s disease
Pooler, A. M., Polydoro, M., Maury, E. A., Nicholls, S. B., Reddy, S. M., Wegmann, S., William, C., Saqran, L., Cagsal-Getkin, O., Pitstick, R., et al. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0199-x · Cited by 236 · see citing works
Self-citationAnalyzing dendritic spine pathology in Alzheimer’s disease: Problems and opportunities
Dorostkar, M. M., Zou, C., Blazquez-Llorca, L., & Herms, J. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1449-5 · Cited by 235 · see citing works
Dendritic Spine Pathology in Neurodegenerative Diseases
Herms, J., & Dorostkar, M. M. (2016) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-012615-044216 · Cited by 201 · see citing works
Stancu, I.-C., Vasconcelos, B., Ris, L., Wang, P., Villers, A., Peeraer, E., Buist, A., Terwel, D., Baatsen, P., Oyelami, T., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1413-4 · Cited by 143 · see citing works
Corsetti, V., Florenzano, F., Atlante, A., Bobba, A., Ciotti, M. T., Natale, F., Della Valle, F., Borreca, A., Manca, A., Meli, G., et al. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv059 · Cited by 129 · see citing works
Hyman, B. (2023) · Annual Review of Medicine · doi:10.1146/annurev-med-042921-023749 · Cited by 39 · see citing works
Self-citationDendritic Spine Remodeling and Synaptic Tau Levels in PS19 Tauopathy Mice
Walker, C. K., Greathouse, K. M., Boros, B. D., Poovey, E. H., Clearman, K. R., Ramdas, R., Muhammad, H. M., & Herskowitz, J. H. (2021) · Neuroscience · doi:10.1016/j.neuroscience.2020.12.006 · Cited by 27 · see citing works
- Authors
- 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., & Hyman, B. T.
- Affiliations
- Harvard University (US)
- McLaughlin Research Institute (US)
- Corresponding author
- Hyman, Bradley T.
- ORCID
- Venue
- Acta Neuropathologica
- Published
- 2013-11-24
- Volume
- 127
- Issue
- 2
- Pages
- 257-270
- ISSN
- 0001-6322 (ISSN-L)
- 1432-0533
- PMC
- PMC3946978
- OpenAlex
- W2059127030
- Cited by
- 117
- References
- 63
- Citations by year
- 2026: 7 · 2025: 10 · 2024: 11 · 2023: 4 · 2022: 10 · 2021: 7 · 2020: 12 · 2019: 11 · 2018: 12 · 2017: 10 · 2016: 8 · 2015: 11 · 2014: 3 · 2013: 1
- FWCI
- 5.32
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Acta Neuropathologica (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Research Portal (King's College London) (submittedVersion)
- Funders
- National Institutes of Health
- National Institute on Aging (R01AG026249, 5T32AG00022222, R00AG033670, R21AG038835, P50AG005134, R21AG03885, T32AG000222, P30AG062421)
- 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 › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Keywords
- entorhinal cortex, Alzheimer's disease, neurofibrillary tangles, hyperphosphorylated tau, contextual fear conditioning, neurotransmitter release probability
- MeSH terms
- Alzheimer Disease, Animals, Cytoskeletal Proteins, Disease Models, Animal, Hippocampus, Humans, Mice, Inbred C57BL, Mice, Transgenic, Nerve Tissue Proteins, Neuronal Plasticity, tau Proteins, Presynaptic Terminals, Entorhinal Cortex, Mice, Electrophysiological Phenomena
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
