Tau Oligomers: The Toxic Player at Synapses in Alzheimer’s Disease

Guerrero-Muñoz, Marcos J.; Gerson, Julia; Castillo-Carranza, Diana L.

doi:10.3389/fncel.2015.00464

Cited by 169Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

Tau Oligomers: The Toxic Player at Synapses in Alzheimer’s Disease

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Guerrero-Muñoz, Marcos J., Gerson, Julia, Castillo-Carranza, Diana L.·2015·Frontiers in Cellular Neuroscience

DOI 10.3389/fncel.2015.00464PMC PMC4667007

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Abstract

Alzheimer's disease (AD) is a progressive disorder in which the most noticeable symptoms are cognitive impairment and memory loss. However, the precise mechanism by which those symptoms develop remains unknown. Of note, neuronal loss occurs at sites where synaptic dysfunction is observed earlier, suggesting that altered synaptic connections precede neuronal loss. The abnormal accumulation of amyloid-β (Aβ) and tau protein is the main histopathological feature of the disease. Several lines of evidence suggest that the small oligomeric forms of Aβ and tau may act synergistically to promote synaptic dysfunction in AD. Remarkably, tau pathology correlates better with the progression of the disease than Aβ. Recently, a growing number of studies have begun to suggest that missorting of tau protein from the axon to the dendrites is required to mediate the detrimental effects of Aβ. In this review we discuss the novel findings regarding the potential mechanisms by which tau oligomers contribute to synaptic dysfunction in AD.

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Pathogenic tau has been linked to synaptic dysfunction and loss.
“Pathogenic tau has been linked to synaptic dysfunction and loss (69).”
From Modeling late-onset Alzheimer’s disease neuropathology via direct neuronal reprogramming (2024) · cites this paper as [69]

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RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., & Ashe, K. H. (2006) · Nature · doi:10.1038/nature04533 · Cited by 2,769 · cited 1× · see citing works
“It seems likely that the increase in trimers in treated mice may be a consequence of Aβ∗56 disassembly which has been suggested to be comprised of four Aβ trimers (Lesne et al., 2006).”
Background
Retracted
RETRACTED: Soluble α-Synuclein Is a Novel Modulator of Alzheimer's Disease Pathophysiology
Larson, M. E., Sherman, M. A., Greimel, S., Kuskowski, M., Schneider, J. A., Bennett, D. A., & Lesné, S. E. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.0581-12.2012 · Cited by 128 · see citing works
Retracted
Neuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123 · see citing works
Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359 · see citing works
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744 · see citing works
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064 · see citing works
Hearing loss and cognitive decline in older adults
Lin, F. R., Yaffe, K., Xia, J., Xue, Q.-L., Harris, T. B., Purchase-Helzner, E., Satterfield, S., Ayonayon, H. N., Ferrucci, L., Simonsick, E. M., et al. (2013) · JAMA Internal Medicine · doi:10.1001/jamainternmed.2013.1868 · Cited by 4,017 · see citing works
Neuropathological alterations in Alzheimer disease
Serrano-Pozo, A., Frosch, M. P., Masliah, E., & Hyman, B. T. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006189 · Cited by 3,345 · see citing works
Amyloid deposition as the central event in the aetiology of Alzheimer’s disease
Hardy, J., & Allsop, D. (1991) · Trends in Pharmacological Sciences · doi:10.1016/0165-6147(91)90609-v · Cited by 2,538 · see citing works
Synapse Loss and Microglial Activation Precede Tangles in a P301S Tauopathy Mouse Model
Yoshiyama, Y., Higuchi, M., Zhang, B., Huang, S.-M., Iwata, N., Saido, T. C., Maeda, J., Suhara, T., Trojanowski, J. Q., & Lee, V. M.-Y. (2007) · Neuron · doi:10.1016/j.neuron.2007.01.010 · Cited by 2,208 · see citing works
Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function
SantaCruz, K., Lewis, J., Spires, T., Paulson, J., Kotilinek, L., Ingelsson, M., Guimaraes, A., DeTure, M., Ramsden, M., McGowan, E., et al. (2005) · Science · doi:10.1126/science.1113694 · Cited by 2,014 · see citing works
Aβ Oligomers – a decade of discovery
Walsh, D. M., & Selkoe, D. J. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04426.x · Cited by 1,938 · 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
α-Synuclein Promotes SNARE-Complex Assembly in Vivo and in Vitro
Burré, J., Sharma, M., Tsetsenis, T., Buchman, V. L., Etherton, M. R., & Südhof, T. C. (2010) · Science · doi:10.1126/science.1195227 · Cited by 1,817 · see citing works
Natural Oligomers of the Alzheimer Amyloid-β Protein Induce Reversible Synapse Loss by Modulating an NMDA-Type Glutamate Receptor-Dependent Signaling Pathway
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
Soluble Amyloid β Peptide Concentration as a Predictor of Synaptic Change in Alzheimer's Disease
Lue, L.-F., Kuo, Y.-M., Roher, A. E., Brachova, L., Shen, Y., Sue, L., Beach, T., Kurth, J. H., Rydel, R. E., & Rogers, J. (1999) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)65184-x · Cited by 1,530 · see citing works
Formation of Neurofibrillary Tangles in P301L Tau Transgenic Mice Induced by Aβ42 Fibrils
Götz, J., Chen, F., van Dorpe, J., & Nitsch, R. M. (2001) · Science · doi:10.1126/science.1062097 · Cited by 1,526 · see citing works
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
Alzheimer disease: Epidemiology, diagnostic criteria, risk factors and biomarkers
Reitz, C., & Mayeux, R. P. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.12.024 · Cited by 1,180 · see citing works
Tau pathology and neurodegeneration
Spillantini, M. G., & Goedert, M. (2013) · The Lancet Neurology · doi:10.1016/s1474-4422(13)70090-5 · Cited by 1,133 · see citing works
Tangle and neuron numbers, but not amyloid load, predict cognitive status in Alzheimer’s disease
Giannakopoulos, P., Herrmann, F. R., Bussière, T., Bouras, C., Kövari, E., Perl, D. P., Morrison, J. H., Gold, G., & Hof, P. R. (2003) · Neurology · doi:10.1212/01.wnl.0000063311.58879.01 · Cited by 1,118 · see citing works
Tau Mislocalization to Dendritic Spines Mediates Synaptic Dysfunction Independently of Neurodegeneration
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
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
Rapid appearance and local toxicity of amyloid-β plaques in a mouse model of Alzheimer’s disease
Meyer-Luehmann, M., Spires-Jones, T. L., Prada, C., Garcia-Alloza, M., de Calignon, A., Rozkalne, A., Koenigsknecht-Talboo, J., Holtzman, D. M., Bacskai, B. J., & Hyman, B. T. (2008) · Nature · doi:10.1038/nature06616 · Cited by 987 · see citing works
Amyloid deposition precedes tangle formation in a triple transgenic model of Alzheimer's disease
Oddo, S. (2003) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2003.08.012 · Cited by 980 · see citing works
Tauopathy in Drosophila : Neurodegeneration Without Neurofibrillary Tangles
Wittmann, C. W., Wszolek, M. F., Shulman, J. M., Salvaterra, P. M., Lewis, J., Hutton, M., & Feany, M. B. (2001) · Science · doi:10.1126/science.1062382 · Cited by 939 · see citing works
Soluble amyloid β-protein dimers isolated from Alzheimer cortex directly induce Tau hyperphosphorylation and neuritic degeneration
Jin, M., Shepardson, N., Yang, T., Chen, G., Walsh, D., & Selkoe, D. J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1017033108 · Cited by 876 · see citing works
The amyloid hypothesis for Alzheimer’s disease: A critical reappraisal
Hardy, J. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06181.x · Cited by 814 · see citing works
Lewy Bodies in Alzheimer's Disease: A Neuropathological Review of 145 Cases Using α‐Synuclein Immunohistochemistry
Hamilton, R. L. (2000) · Brain Pathology · doi:10.1111/j.1750-3639.2000.tb00269.x · Cited by 754 · see citing works
Hyperphosphorylation and aggregation of tau in mice expressing normal human tau isoforms
Andorfer, C., Kress, Y., Espinoza, M., De Silva, R., Tucker, K. L., Barde, Y., Duff, K., & Davies, P. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01879.x · Cited by 722 · see citing works
Evolution of the neuropathology of Alzheimer's disease
Braak, H., & Braak, E. (1996) · Acta Neurologica Scandinavica · doi:10.1111/j.1600-0404.1996.tb05866.x · Cited by 710 · see citing works
Aβ Oligomers Cause Localized Ca 2+ Elevation, Missorting of Endogenous Tau into Dendrites, Tau Phosphorylation, and Destruction of Microtubules and Spines
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
“…it is possible that a direct interaction between the two proteins may be involved in the induction of synaptic dysfunction as tau and Aβ coexist within synaptic compartments in AD brain (Hoover et al., 2010; Ittner et al., 2010; Zempel et al., 2010; Tai et al., 2012; Miller et al., 2014).”
Background
Early 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
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
Distribution of Alzheimer-type pathologic changes in nondemented elderly individuals matches the pattern in Alzheimer’s disease
Arriagada, P. V., Marzloff, K., & Hyman, B. T. (1992) · Neurology · doi:10.1212/wnl.42.9.1681 · Cited by 638 · see citing works
Tau oligomers impair memory and induce synaptic and mitochondrial dysfunction in wild-type mice
Lasagna-Reeves, C. A., Castillo-Carranza, D. L., Sengupta, U., Clos, A. L., Jackson, G. R., & Kayed, R. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-39 · Cited by 633 · see citing works
Self-citation
Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders
Jucker, M., & Walker, L. C. (2011) · Annals of Neurology · doi:10.1002/ana.22615 · Cited by 622 · cited 1× · see citing works
“In the prion field, the acquisition of β-sheet conformation by a prion protein allows it to seed the misfolding and aggregation of other prion molecules, reviewed by Jucker and Walker (2011).”
Background
Demonstration of amyloid deposits and neurofibrillary changes in whole brain sections
Braak, H., & Braak, E. (1991) · Brain Pathology · doi:10.1111/j.1750-3639.1991.tb00661.x · Cited by 598 · see citing works
The Levels of Soluble versus Insoluble Brain Aβ Distinguish Alzheimer's Disease from Normal and Pathologic Aging
Wang, J., Dickson, D. W., Trojanowski, J. Q., & Lee, V. M.-Y. (1999) · Experimental Neurology · doi:10.1006/exnr.1999.7085 · Cited by 567 · see citing works
Linking Aβ and Tau in Late-Onset Alzheimer's Disease: A Dual Pathway Hypothesis
Small, S. A., & Duff, K. (2008) · Neuron · doi:10.1016/j.neuron.2008.11.007 · Cited by 546 · see citing works
Small Misfolded Tau Species Are Internalized via Bulk Endocytosis and Anterogradely and Retrogradely Transported in Neurons
Wu, 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
Identification of oligomers at early stages of tau aggregation in Alzheimer's disease
Lasagna‐Reeves, C. A., Castillo‐Carranza, D. L., Sengupta, U., Sarmiento, J., Troncoso, J., Jackson, G. R., & Kayed, R. (2012) · The FASEB Journal · doi:10.1096/fj.11-199851 · Cited by 527 · see citing works
Self-citation
Environmental Enrichment Mitigates Cognitive Deficits in a Mouse Model of Alzheimer's Disease
Jankowsky, J. L., Melnikova, T., Fadale, D. J., Xu, G. M., Slunt, H. H., Gonzales, V., Younkin, L. H., Younkin, S. G., Borchelt, D. R., & Savonenko, A. V. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.5080-04.2005 · Cited by 517 · 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
Self-citation
Reactive Glia not only Associates with Plaques but also Parallels Tangles in Alzheimer’s Disease
Serrano-Pozo, A., Mielke, M. L., Gómez-Isla, T., Betensky, R. A., Growdon, J. H., Frosch, M. P., & Hyman, B. T. (2011) · The American Journal of Pathology · doi:10.1016/j.ajpath.2011.05.047 · Cited by 488 · see citing works
Accumulation of Pathological Tau Species and Memory Loss in a Conditional Model of Tauopathy
Berger, Z., Roder, H. M., Hanna, A., Carlson, A. M., Rangachari, V., Yue, M., Wszołek, Z. K., Ashe, K. H., Knight, J. A., Dickson, D. W., et al. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.0587-07.2007 · Cited by 485 · see citing works
A novel in vivo model of tau propagation with rapid and progressive neurofibrillary tangle pathology: the pattern of spread is determined by connectivity, not proximity
Ahmed, Z., Cooper, J., Murray, T. K., Garn, K., McNaughton, E., Clarke, H., Parhizkar, S., Ward, M. A., Cavallini, A., Jackson, S., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1254-6 · Cited by 460 · see citing works
The Synaptic Accumulation of Hyperphosphorylated Tau Oligomers in Alzheimer Disease Is Associated With Dysfunction of the Ubiquitin-Proteasome System
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
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
Alzheimer's disease-type neuronal tau hyperphosphorylation induced by Aβ oligomers
De Felice, F. G., Wu, D., Lambert, M. P., Fernandez, S. J., Velasco, P. T., Lacor, P. N., Bigio, E. H., Jerecic, J., Acton, P. J., Shughrue, P. J., et al. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.02.029 · Cited by 432 · see citing works
Accelerating Amyloid-β Fibrillization Reduces Oligomer Levels and Functional Deficits in Alzheimer Disease Mouse Models
Cheng, I. H.-J., Scearce-Levie, K. A., Legleiter, J. A., Palop, J. J., Gerstein, H., Bien‐Ly, N., Puolivaöli, J., Lesné, S., Ashe, K. H., Muchowski, P. J., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701078200 · Cited by 403 · see citing works
Region-specific Dissociation of Neuronal Loss and Neurofibrillary Pathology in a Mouse Model of Tauopathy
Spires, T. L., Orne, J. D., SantaCruz, K., Pitstick, R., Carlson, G. A., Ashe, K. H., & Hyman, B. T. (2006) · The American Journal of Pathology · doi:10.2353/ajpath.2006.050840 · Cited by 401 · see citing works
Dissecting phenotypic traits linked to human resilience to Alzheimer’s pathology
Perez-Nievas, B. G., Stein, T. D., Tai, H.-C., Dols-Icardo, O., Scotton, T. C., Barroeta-Espar, I., Fernandez-Carballo, L., de Munain, E. L., Perez, J., Marquie, M., et al. (2013) · Brain · doi:10.1093/brain/awt171 · Cited by 387 · see citing works
Amyloid-β forms fibrils by nucleated conformational conversion of oligomers
Lee, J., Culyba, E. K., Powers, E. T., & Kelly, J. W. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.624 · Cited by 383 · see citing works
Tau aggregation is driven by a transition from random coil to beta sheet structure.
von Bergen, M., Barghorn, S., Biernat, J., Mandelkow, E., & Mandelkow, E. (2005) · Biochimica et Biophysica Acta · doi:10.1016/j.bbadis.2004.09.010 · Cited by 376 · see citing works
Preparation and Characterization of Neurotoxic Tau Oligomers
Lasagna-Reeves, C. A., Castillo-Carranza, D. L., Guerrero-Muñoz, M. J., Jackson, G. R., & Kayed, R. (2010) · Biochemistry · doi:10.1021/bi1016233 · Cited by 359 · see citing works
Self-citation
Reversible paired helical filament-like phosphorylation of tau is an adaptive process associated with neuronal plasticity in hibernating animals
Arendt, T., Stieler, J., Strijkstra, A. M., Hut, R. A., Rüdiger, J., Van der Zee, E. A., Harkany, T., Holzer, M., & Härtig, W. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-18-06972.2003 · Cited by 357 · see citing works
Characterization of Prefibrillar Tau Oligomers in Vitro and in Alzheimer Disease
Patterson, K. R., Remmers, C. L., Fu, Y., Brooker, S. M., Kanaan, N. M., Vana, L., Ward, S., Reyes, J. F., Philibert, K., Glucksman, M., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.237974 · Cited by 354 · see citing works
In Vivo Microdialysis Reveals Age-Dependent Decrease of Brain Interstitial Fluid Tau Levels in P301S Human Tau Transgenic Mice
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
Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments
Barghorn, S., & Mandelkow, E. (2002) · Biochemistry · doi:10.1021/bi026469j · Cited by 341 · 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
Clinicopathologic and11C-Pittsburgh compound B implications of Thal amyloid phase across the Alzheimer’s disease spectrum
Murray, M. E., Lowe, V. J., Graff-Radford, N. R., Liesinger, A. M., Cannon, A., Przybelski, S. A., Rawal, B., Parisi, J. E., Petersen, R. C., Kantarci, K., et al. (2015) · Brain · doi:10.1093/brain/awv050 · Cited by 324 · see citing works
<scp>F</scp>yn inhibition rescues established memory and synapse loss in <scp>A</scp>lzheimer mice
Kaufman, A. C., Salazar, S. V., Haas, L. T., Yang, J., Kostylev, M. A., Jeng, A. T., Robinson, S. A., Gunther, E. C., van Dyck, C. H., Nygaard, H. B., et al. (2015) · Annals of Neurology · doi:10.1002/ana.24394 · Cited by 314 · see citing works
Fyn kinase induces synaptic and cognitive impairments in a transgenic mouse model of Alzheimer’s disease
Chin, J., Palop, J. J., Puoliväli, J., Massaro, C., Bien-Ly, N., Gerstein, H., Scearce-Levie, K., Masliah, E., & Mucke, L. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.2980-05.2005 · Cited by 312 · see citing works
Granular Tau Oligomers as Intermediates of Tau Filaments
Maeda, S., Sahara, N., Saito, Y., Murayama, M., Yoshiike, Y., Kim, H., Miyasaka, T., Murayama, S., Ikai, A., & Takashima, A. (2007) · Biochemistry · doi:10.1021/bi061359o · Cited by 309 · see citing works
Microtubule-associated protein tau is essential for long-term depression in the hippocampus
Kimura, T., Whitcomb, D. J., Jo, J., Regan, P., Piers, T., Heo, S., Brown, C., Hashikawa, T., Murayama, M., Seok, H., et al. (2014) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2013.0144 · Cited by 307 · see citing works
Tau-induced defects in synaptic plasticity, learning, and memory are reversible in transgenic mice after switching off the toxic Tau mutant
Sydow, A., Van der Jeugd, A., Zheng, F., Ahmed, T., Balschun, D., Petrova, O., Drexler, D., Zhou, L., Rune, G., Mandelkow, E., et al. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.5245-10.2011 · Cited by 302 · see citing works
Increased levels of granular tau oligomers: An early sign of brain aging and Alzheimer's disease
Maeda, S., Sahara, N., Saito, Y., Murayama, S., Ikai, A., & Takashima, A. (2006) · Neuroscience Research · doi:10.1016/j.neures.2005.11.009 · Cited by 301 · see citing works
Reduction of Soluble Aβ and Tau, but Not Soluble Aβ Alone, Ameliorates Cognitive Decline in Transgenic Mice with Plaques and Tangles
Oddo, S., Vasilevko, V., Caccamo, A., Kitazawa, M., Cribbs, D. H., & LaFerla, F. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m608485200 · Cited by 282 · see citing works
Induction of Tau Pathology by Intracerebral Infusion of Amyloid-β-Containing Brain Extract and by Amyloid-β Deposition in APP × Tau Transgenic Mice
Bolmont, T., Clavaguera, F., Meyer-Luehmann, M., Herzig, M. C., Radde, R., Staufenbiel, M., Lewis, J., Hutton, M., Tolnay, M., & Jucker, M. (2007) · The American Journal of Pathology · doi:10.2353/ajpath.2007.070403 · Cited by 281 · see citing works
Activity-Dependent Tau Protein Translocation to Excitatory Synapse Is Disrupted by Exposure to Amyloid-Beta Oligomers
Frandemiche, M. L., De Seranno, S., Rush, T., Borel, E., Elie, A., Arnal, I., Lanté, F., & Buisson, A. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.4261-13.2014 · Cited by 272 · see citing works
Tau Accumulation Causes Mitochondrial Distribution Deficits in Neurons in a Mouse Model of Tauopathy and in Human Alzheimer's Disease Brain
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
Interaction of Endogenous Tau Protein with Synaptic Proteins Is Regulated by N-Methyl-d-aspartate Receptor-dependent Tau Phosphorylation*
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
Effects of frontotemporal dementia FTDP‐17 mutations on heparin‐induced assembly of tau filaments
Goedert, M., Jakes, R., & Crowther, R. A. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00508-6 · Cited by 260 · see citing works
Synaptic Contacts Enhance Cell-to-Cell Tau Pathology Propagation
Calafate, S., Buist, A., Miśkiewicz, K., Vijayan, V. A., Daneels, G., Strooper, B. D., de Wit, J., Verstreken, P., & Moechars, D. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.04.043 · Cited by 257 · see citing works
Prefibrillar Amyloid Aggregates Could Be Generic Toxins in Higher Organisms
Baglioni, S., Casamenti, F., Bucciantini, M., Luheshi, L. M., Taddei, N., Chiti, F., Dobson, C. M., & Stefani, M. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.4809-05.2006 · Cited by 245 · see citing works
Anionic Micelles and Vesicles Induce Tau Fibrillization in Vitro
Chirita, C. N., Necula, M., & Kuret, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301663200 · Cited by 244 · see citing works
Environmental Enrichment Exacerbates Amyloid Plaque Formation in a Transgenic Mouse Model of Alzheimer Disease
Jankowsky, J. L., Xu, G. M., Fromholt, D., Gonzales, V., & Borchelt, D. (2003) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/62.12.1220 · Cited by 240 · see citing works
Extracellular tau promotes intracellular calcium increase through M1 and M3 muscarinic receptors in neuronal cells
Gómez‐Ramos, A., Dı́az-Hernández, M., Rubio, A., Miras‐Portugal, M. T., & Ávila, J. (2008) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2007.12.010 · Cited by 233 · see citing works
Phosphorylation Regulates Tau Interactions with Src Homology 3 Domains of Phosphatidylinositol 3-Kinase, Phospholipase Cγ1, Grb2, and Src Family Kinases
Reynolds, C. H., Garwood, C. J., Wray, S., Price, C., Kellie, S., Perera, T. P. S., Zvelebil, M., Yang, A., Sheppard, P. W., Varndell, I. M., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709715200 · Cited by 226 · see citing works
Disease-related Modifications in Tau Affect the Interaction between Fyn and Tau
Bhaskar, K., Yen, S.-H. C., & Lee, G. S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505895200 · Cited by 223 · see citing works
Adult-derived neural precursors transplanted into multiple regions in the adult brain
Herrera, D. G., García‐Verdugo, J. M., & Álvarez-Buylla, A. (1999) · Annals of Neurology · doi:10.1002/1531-8249(199912)46:6 · Cited by 204 · see citing works
Tau Phosphorylation at Serine 396 Residue Is Required for Hippocampal LTD
Regan, P., Piers, T., Yi, J.-H., Kim, D.-H., Huh, S., Park, S. J., Ryu, J. H., Whitcomb, D. J., & Cho, K. (2015) · The Journal of Neuroscience · doi:10.1523/jneurosci.2842-14.2015 · Cited by 202 · see citing works
Neurofibrillary tangle-bearing neurons are functionally integrated in cortical circuits in vivo
Kuchibhotla, K. V., Wegmann, S., Kopeikina, K. J., Hawkes, J., Rudinskiy, N., Andermann, M. L., Spires-Jones, T. L., Bacskai, B. J., & Hyman, B. T. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1318807111 · Cited by 193 · see citing works
Assembly of two distinct dimers and higher‐order oligomers from full‐length tau
Sahara, N., Maeda, S., Murayama, M., Suzuki, T., Dohmae, N., Yen, S.-H. C., & Takashima, A. (2007) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2007.05555.x · Cited by 192 · 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
β-Amyloid Induces Paired Helical Filament-like Tau Filaments in Tissue Culture
Ferrari, A., Hoerndli, F. J., Baechi, T., Nitsch, R. M., & Götz, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308243200 · Cited by 182 · see citing works
Pathological Interface Between Oligomeric Alpha-Synuclein and Tau in Synucleinopathies
Sengupta, U., Guerrero‐Munoz, M. J., Castillo‐Carranza, D. L., Lasagna‐Reeves, C. A., Gerson, J. E., Paulucci-Holthauzen, A. A., Krishnamurthy, S., Farhed, M., Jackson, G. R., & Kayed, R. (2015) · Biological Psychiatry · doi:10.1016/j.biopsych.2014.12.019 · Cited by 181 · see citing works
Self-citation
Differential Assembly of Human Tau Isoforms in the Presence of Arachidonic Acid
King, M. E., Gamblin, T. C., Kuret, J., & Binder, L. I. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0741749.x · Cited by 179 · see citing works
In VivoImaging of Reactive Oxygen Species Specifically Associated with Thioflavine S-Positive Amyloid Plaques by Multiphoton Microscopy
McLellan, M. E., Kajdasz, S. T., Hyman, B. T., & Bacskai, B. J. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-06-02212.2003 · Cited by 174 · see citing works
Triggers of Full-Length Tau Aggregation: A Role for Partially Folded Intermediates
Chirita, C. N., Congdon, E. E., Yin, H., & Kuret, J. (2005) · Biochemistry · doi:10.1021/bi0500123 · Cited by 166 · see citing works
Fyn Kinase Modulates Synaptotoxicity, But Not Aberrant Sprouting, in Human Amyloid Precursor Protein Transgenic Mice
Chin, J., Palop, J. J., Yu, G.-Q., Kojima, N., Masliah, E., & Mucke, L. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.0277-04.2004 · Cited by 161 · see citing works
The intersection of amyloid beta and tau in glutamatergic synaptic dysfunction and collapse in Alzheimer's disease
Crimins, J. L., Pooler, A. M., Polydoro, M., Luebke, J. I., & Spires‐Jones, T. L. (2013) · Ageing Research Reviews · doi:10.1016/j.arr.2013.03.002 · Cited by 161 · see citing works
Plaque-bearing mice with reduced levels of oligomeric amyloid-β assemblies have intact memory function
Lesné, S., Kotilinek, L., & Ashe, K. H. (2007) · Neuroscience · doi:10.1016/j.neuroscience.2007.10.054 · Cited by 159 · see citing works
Soluble hyper-phosphorylated tau causes microtubule breakdown and functionally compromises normal tau in vivo
Cowan, C. M., Bossing, T., Page, A., Shepherd, D., & Mudher, A. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0716-8 · Cited by 156 · see citing works
Tissue-nonspecific Alkaline Phosphatase Promotes the Neurotoxicity Effect of Extracellular Tau
Dı́az-Hernández, M., Gómez‐Ramos, A., Rubio, A., Gómez‐Villafuertes, R., Naranjo, J. R., Miras‐Portugal, M. T., & Ávila, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.145003 · Cited by 154 · see citing works
Tau Immunotherapy Modulates Both Pathological Tau and Upstream Amyloid Pathology in an Alzheimer's Disease Mouse Model
Castillo-Carranza, D. L., Guerrero-Muñoz, M. J., Sengupta, U., Hernandez, C., Barrett, A. D. T., Dineley, K., & Kayed, R. (2015) · The Journal of Neuroscience · doi:10.1523/jneurosci.4989-14.2015 · Cited by 149 · see citing works
Self-citation
Frequent and symmetric deposition of misfolded tau oligomers within presynaptic and postsynaptic terminals in Alzheimer¿s disease
Tai, H., Wang, B. Y., Serrano‐Pozo, A., Frosch, M. P., Spires‐Jones, T. L., & Hyman, B. T. (2014) · Acta Neuropathologica Communications · doi:10.1186/s40478-014-0146-2 · Cited by 142 · see citing works
Distribution of the phosphorylated microtubule-associated protein tau in developing cortical neurons
Brion, J., Octave, J., & Couck, A. M. (1994) · Neuroscience · doi:10.1016/0306-4522(94)90533-9 · Cited by 141 · see citing works
The role of tau in the pathological process and clinical expression of Huntington’s disease
Vuono, R., Winder‐Rhodes, S., de Silva, R., Cisbani, G., Drouin‐Ouellet, J., REGISTRY Investigators of the European Huntington’s Disease Network, Spillantini, M. G., Cicchetti, F., & Barker, R. A. (2015) · Brain · doi:10.1093/brain/awv107 · Cited by 139 · see citing works
Progression of tau pathology in cholinergic Basal forebrain neurons in mild cognitive impairment and Alzheimer's disease
Vana, L., Kanaan, N. M., Ugwu, I. C., Wuu, J., Mufson, E. J., & Binder, L. I. (2011) · The American Journal of Pathology · doi:10.1016/j.ajpath.2011.07.044 · Cited by 138 · see citing works
Electrophysiological changes precede morphological changes to frontal cortical pyramidal neurons in the rTg4510 mouse model of progressive tauopathy
Crimins, J. L., Rocher, A. B., & Luebke, J. I. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-1038-9 · Cited by 137 · see citing works
Formation and Propagation of Tau Oligomeric Seeds
Gerson, J. E., & Kayed, R. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00093 · Cited by 137 · see citing works
Self-citation
Human P301L-Mutant Tau Expression in Mouse Entorhinal-Hippocampal Network Causes Tau Aggregation and Presynaptic Pathology but No Cognitive Deficits
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
Tau phosphorylation and tau mislocalization mediate soluble Aβ oligomer‐induced <scp>AMPA</scp> glutamate receptor signaling deficits
Miller, E. C., Teravskis, P. J., Dummer, B. W., Zhao, X., Huganir, R. L., & Liao, D. (2014) · European Journal of Neuroscience · doi:10.1111/ejn.12507 · Cited by 131 · see citing works
NMDA receptor subunit composition determines beta-amyloid-induced neurodegeneration and synaptic loss
Tackenberg, C., Grinschgl, S., Trutzel, A., Santuccione, A. C., Frey, M. C., Konietzko, U., Grimm, J., Brandt, R., & Nitsch, R. M. (2013) · Cell Death & Disease · doi:10.1038/cddis.2013.129 · Cited by 130 · see citing works
Divergent Pathways Mediate Spine Alterations and Cell Death Induced by Amyloid-β, Wild-Type Tau, and R406W Tau
Tackenberg, C., & Brandt, R. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.3590-09.2009 · Cited by 127 · see citing works
Soluble Aβ Promotes Wild-Type Tau PathologyIn Vivo
Chabrier, M. A., Blurton-Jones, M., Agazaryan, A. A., Nerhus, J. L., Martinez-Coria, H., & LaFerla, F. M. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.0172-12.2012 · Cited by 123 · see citing works
nNOS Expressing Neurons in the Entorhinal Cortex and Hippocampus Are Affected in Patients with Alzheimer's Disease
Thorns, V., Hansen, L., & Masliah, E. (1998) · Experimental Neurology · doi:10.1006/exnr.1997.6751 · Cited by 119 · see citing works
Tau as a therapeutic target in neurodegenerative disease
Himmelstein, D. S., Ward, S., Lancia, J. K., Patterson, K. R., & Binder, L. I. (2012) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2012.07.001 · Cited by 113 · see citing works
mTor mediates tau localization and secretion: implication for Alzheimer’s disease
Tang, Z., Ioja, E., Bereczki, E., Hultenby, K., Li, C., Guan, Z., Winblad, B., & Pei, J.-J. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.03.003 · Cited by 112 · see citing works
Delineating the Mechanism of Alzheimer’s Disease Aβ Peptide Neurotoxicity
Cappai, R., & Barnham, K. J. (2008) · Neurochemical Research · doi:10.1007/s11064-007-9469-8 · Cited by 108 · see citing works
Tau oligomerization: a role for tau aggregation intermediates linked to neurodegeneration
Sahara, N., Maeda, S., & Takashima, A. (2008) · Current Alzheimer Research · doi:10.2174/156720508786898442 · Cited by 99 · see citing works
Absence of amyloid β oligomers at the postsynapse and regulated synaptic Zn2+ in cognitively intact aged individuals with Alzheimer’s disease neuropathology
Bjorklund, N. L., Reese, L. C., Sadagoparamanujam, V.-M., Ghirardi, V., Woltjer, R. L., & Taglialatela, G. (2012) · Molecular Neurodegeneration · doi:10.1186/1750-1326-7-23 · Cited by 98 · see citing works
Synergistic effects of amyloid-beta and wild-type human tau on dendritic spine loss in a floxed double transgenic model of Alzheimer's disease
Chabrier, M. A., Cheng, D., Castello, N. A., Green, K. N., & LaFerla, F. M. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.01.007 · Cited by 97 · see citing works
Characteristics and consequences of muscarinic receptor activation by tau protein
Gómez‐Ramos, A., Dı́az-Hernández, M., Rubio, A., Díaz‐Hernandéz, J. I., Miras‐Portugal, M. T., & Ávila, J. (2009) · European Neuropsychopharmacology · doi:10.1016/j.euroneuro.2009.04.006 · Cited by 95 · see citing works
Characterization of tau oligomeric seeds in progressive supranuclear palsy
Gerson, J. E., Sengupta, U., Lasagna‐Reeves, C. A., Guerrero‐Munoz, M. J., Troncoso, J. C., & Kayed, R. (2014) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-2-73 · Cited by 95 · see citing works
Self-citation
Changes in dendritic complexity and spine morphology in transgenic mice expressing human wild-type tau
Dickstein, D. L., Brautigam, H., Stockton, S. D., Schmeidler, J., & Hof, P. R. (2010) · Brain Structure and Function · doi:10.1007/s00429-010-0245-1 · Cited by 94 · see citing works
Linking Amyloid-β and Tau: Amyloid-β Induced Synaptic Dysfunction via Local Wreckage of the Neuronal Cytoskeleton
Zempel, H., & Mandelkow, E. (2011) · Neurodegenerative Diseases · doi:10.1159/000332816 · Cited by 90 · see citing works
Tyrosine phosphorylation of tau regulates its interactions with Fyn SH2 domains, but not SH3 domains, altering the cellular localization of tau
Usardi, A., Pooler, A. M., Seereeram, A., Reynolds, C. H., Derkinderen, P., Anderton, B. H., Hanger, D. P., Noble, W. J., & Williamson, R. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08218.x · Cited by 89 · see citing works
P301L tau expression affects glutamate release and clearance in the hippocampal trisynaptic pathway
Hunsberger, H. C., Rudy, C. C., Batten, S. R., Gerhardt, G. A., & Reed, M. N. (2014) · Journal of Neurochemistry · doi:10.1111/jnc.12967 · Cited by 83 · see citing works
Tau aggregation and progressive neuronal degeneration in the absence of changes in spine density and morphology after targeted expression of Alzheimer's disease-relevant tau constructs in organotypic hippocampal slices
Shahani, N., Subramaniam, S., Wolf, T., Tackenberg, C., & Brandt, R. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.4245-05.2006 · Cited by 81 · see citing works
Pro-aggregant Tau impairs mossy fiber plasticity due to structural changes and Ca++ dysregulation
Decker, J., Krüger, L., Sydow, A., Zhao, S., Frotscher, M., Mandelkow, E., & Mandelkow, E. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0193-3 · Cited by 77 · see citing works
Homeostatic responses by surviving cortical pyramidal cells in neurodegenerative tauopathy
Crimins, J. L., Rocher, A. B., Peters, A., Shultz, P. L., Lewis, J. M., & Luebke, J. I. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0877-0 · Cited by 71 · see citing works
Human tau expression reduces adult neurogenesis in a mouse model of tauopathy
Komuro, Y., Xu, G., Bhaskar, K., & Lamb, B. T. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.03.002 · Cited by 61 · see citing works
Correlation of Specific Amyloid-β Oligomers With Tau in Cerebrospinal Fluid From Cognitively Normal Older Adults
Handoko, M., Grant, M. K. O., Kuskowski, M. A., Zahs, K. R., Wallin, A., Blennow, K., & Ashe, K. H. (2013) · JAMA Neurology · doi:10.1001/jamaneurol.2013.48 · Cited by 61 · see citing works
Microarray analysis of CA1 pyramidal neurons in a mouse model of tauopathy reveals progressive synaptic dysfunction
Alldred, M. J., Duff, K., & Ginsberg, S. D. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.10.022 · Cited by 58 · see citing works
AD synapses contain abundant Aβ monomer and multiple soluble oligomers, including a 56-kDa assembly
Sokolow, S., Henkins, K. M., Bilousova, T. V., Miller, C. A., Vinters, H. V., Poon, W. W., Cole, G. M., & Gylys, K. H. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.05.011 · Cited by 57 · see citing works
Prefibrillar Tau Oligomers in Mild Cognitive Impairment and Alzheimer's Disease
Mufson, E. J., Ward, S., & Binder, L. I. (2013) · Neurodegenerative Diseases · doi:10.1159/000353687 · Cited by 54 · see citing works
Do neuronal inclusions kill the cell?
Terry, R. (2000) · Springer eBooks · doi:10.1007/978-3-7091-6781-6_12 · Cited by 48 · see citing works
Tau Causes Synapse Loss without Disrupting Calcium Homeostasis in the rTg4510 Model of Tauopathy
Kopeikina, K. J., Wegmann, S., Pitstick, R., Carlson, G. A., Bacskai, B. J., Betensky, R. A., Hyman, B. T., & Spires‐Jones, T. L. (2013) · PLoS ONE · doi:10.1371/journal.pone.0080834 · Cited by 48 · see citing works
Early Structural and Functional Defects in Synapses and Myelinated Axons in Stratum Lacunosum Moleculare in Two Preclinical Models for Tauopathy
Maurin, H., Chong, S., Kraev, I., Davies, H. A., Kremer, A., Seymour, C. M., Lechat, B., Jaworski, T., Borghgraef, P., Devijver, H., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0087605 · Cited by 42 · see citing works
Non-tau based neuronal degeneration in Alzheimer's disease — an immunocytochemical and quantitative study in the supragranular layers of the middle temporal neocortex
van de Nes, J. A. P., Nafe, R., & Schlote, W. (2008) · Brain Research · doi:10.1016/j.brainres.2008.03.043 · Cited by 40 · see citing works
Blocking Effects of Human Tau on Squid Giant Synapse Transmission and Its Prevention by T-817 MA
Moreno, H., Choi, S., Yu, E., Brusco, J., Ávila, J., Moreira, J. E., Sugimori, M., & Llinás, R. R. (2011) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2011.00003 · Cited by 39 · see citing works
Tauopathy Differentially Affects Cell Adhesion Molecules in Mouse Brain: Early Down-Regulation of Nectin-3 in Stratum Lacunosum Moleculare
Maurin, H., Seymour, C. M., Lechat, B., Borghgraef, P., Devijver, H., Jaworski, T., Schmidt, M. V., Kügler, S., & LEUVEN, F. V. (2013) · PLoS ONE · doi:10.1371/journal.pone.0063589 · Cited by 36 · see citing works
Does β-amyloid plaque formation cause structural injury to neuronal processes?
Woodhouse, A., West, A. K., Chuckowree, J. A., Vickers, J. C., & Dickson, T. C. (2005) · Neurotoxicity Research · doi:10.1007/bf03033772 · Cited by 29 · see citing works
Breaking the Code of Amyloid- β Oligomers
Lesné, S. (2013) · International Journal of Cell Biology · doi:10.1155/2013/950783 · Cited by 29 · see citing works
Developmental expression of tau proteins in the chicken and rat brain: Rapid down‐regulation of a paired helical filament epitope in the rat cerebral cortex coincides with the transition from immature to adult tau isoforms
Rösner, H., Rebhan, M., Vacun, G., & Vanmechelen, E. (1995) · International Journal of Developmental Neuroscience · doi:10.1016/0736-5748(95)00042-f · Cited by 27 · see citing works
The Role of Prefibrillar Structures in the Assembly of a Peptide Amyloid
Ruschak, A. M., & Miranker, A. D. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.06.026 · Cited by 23 · see citing works
Differential phosphorylation of tau proteins during kitten brain development and Alzheimer's disease
Riederer, B. M., Mourton-Gilles, C., Frey, P., Delacourte, A., & Probst, A. (2001) · Journal of Neurocytology · doi:10.1023/a:1011991207942 · Cited by 22 · see citing works

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Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade
Chiti, F., & Dobson, C. M. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045115 · Cited by 2,629 · 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
Tau and tauopathies
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
Development of Multifunctional Molecules as Potential Therapeutic Candidates for Alzheimer’s Disease, Parkinson’s Disease, and Amyotrophic Lateral Sclerosis in the Last Decade
Savelieff, M. G., Nam, G., Kang, J., Lee, H. J., Lee, M., & Lim, M. H. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00138 · Cited by 603 · see citing works
Phosphorylated Tau in Alzheimer’s Disease and Other Tauopathies
Rawat, P., Sehar, U., Bisht, J., Selman, A., Culberson, J., & Reddy, P. H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232112841 · Cited by 509 · see citing works
Synaptic Impairment in Alzheimer’s Disease: A Dysregulated Symphony
Forner, S., Baglietto-Vargas, D., Martini, A. C., Trujillo-Estrada, L., & LaFerla, F. M. (2017) · Trends in Neurosciences · doi:10.1016/j.tins.2017.04.002 · Cited by 430 · see citing works
Amyloid Beta in Aging and Alzheimer’s Disease
Sehar, U., Rawat, P., Reddy, A. P., Kopel, J. J., & Reddy, P. H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232112924 · Cited by 385 · see citing works
Tau-targeting therapies for Alzheimer disease: Current status and future directions
Congdon, E. E., Ji, C., Tetlow, A. M., Jiang, Y., & Sigurdsson, E. M. (2023) · Nature Reviews Neurology · doi:10.1038/s41582-023-00883-2 · Cited by 371 · 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
Alzheimer's disease and type 2 diabetes: a critical assessment of the shared pathological traits
Chatterjee, S., & Mudher, A. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00383 · Cited by 270 · see citing works
The diabetes drug liraglutide reverses cognitive impairment in mice and attenuates insulin receptor and synaptic pathology in a non‐human primate model of Alzheimer's disease
Batista, A. F., Forny‐Germano, L., Clarke, J. R., Silva, N. M. L. E., Brito‐Moreira, J., Boehnke, S. E., Winterborn, A., Coe, B. C., Lablans, A., Vital, J. F. S., et al. (2018) · The Journal of Pathology · doi:10.1002/path.5056 · Cited by 246 · see citing works
Memantine for the Treatment of Dementia: A Review on its Current and Future Applications
Folch, J., Busquets, O., Ettcheto, M., Sánchez-López, E., Castro-Torres, R. D., Verdaguer, E., Garcia, M. L., Olloquequi, J., Casadesús, G., Beas-Zarate, C., et al. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-170672 · 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
Anesthesiology and cognitive impairment: a narrative review of current clinical literature
Belrose, J. C., & Noppens, R. R. (2019) · BMC Anesthesiology · doi:10.1186/s12871-019-0903-7 · Cited by 211 · see citing works
Intersection of pathological tau and microglia at the synapse
Vogels, T., Murgoci, A.-N., & Hromádka, T. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0754-y · Cited by 197 · see citing works
Fluid Biomarkers for Synaptic Dysfunction and Loss
Camporesi, E., Nilsson, J., Brinkmalm, A., Becker, B., Ashton, N. J., Blennow, K., & Zetterberg, H. (2020) · Biomarker Insights · doi:10.1177/1177271920950319 · Cited by 165 · see citing works
Toxic tau: structural origins of tau aggregation in Alzheimer's disease
Mamun, A. A., Uddin, M. S., Mathew, B., & Ashraf, G. M. (2020) · Neural Regeneration Research · doi:10.4103/1673-5374.274329 · Cited by 156 · see citing works
Tau-mediated synaptic and neuronal dysfunction in neurodegenerative disease
Tracy, T. E., & Gan, L. (2018) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2018.04.027 · Cited by 147 · see citing works
Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases
Rinauro, D. J., Chiti, F., Vendruscolo, M., & Limbocker, R. (2024) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00651-2 · Cited by 132 · see citing works
P53 aggregation, interactions with tau, and impaired DNA damage response in Alzheimer’s disease
Farmer, K. M., Ghag, G., Puangmalai, N., Montalbano, M., Bhatt, N. N., & Kayed, R. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-01012-6 · Cited by 126 · see citing works
Reduced gliotransmitter release from astrocytes mediates tau‐induced synaptic dysfunction in cultured hippocampal neurons
Piacentini, R., Puma, D. D. L., Mainardi, M., Lazzarino, G., Tavazzi, B., Arancio, O., & Grassi, C. (2017) · Glia · doi:10.1002/glia.23163 · Cited by 116 · see citing works
Tau Oligomer–Containing Synapse Elimination by Microglia and Astrocytes in Alzheimer Disease
Taddei, R. N., Perbet, R., Mate de Gerando, A., Wiedmer, A. E., Sanchez-Mico, M., Connors Stewart, T., Gaona, A., Melloni, A., Amaral, A. C., Duff, K., et al. (2023) · JAMA Neurology · doi:10.1001/jamaneurol.2023.3530 · Cited by 110 · see citing works
Advances and considerations in AD tau-targeted immunotherapy
Bittar, A., Bhatt, N. N., & Kayed, R. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.104707 · Cited by 105 · see citing works
Pathological Changes of Tau Related to Alzheimer’s Disease
Chu, D., & Liu, F. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00457 · Cited by 103 · see citing works
Cellular Prion Protein Mediates the Disruption of Hippocampal Synaptic Plasticity by Soluble TauIn Vivo
Ondrejčák, T., Klyubin, I. V., Corbett, G. T., Fraser, G. M., Hong, W., Mably, A. J., Gardener, M. J., Hammersley, J., Perkinton, M. S., Billinton, A., et al. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.1700-18.2018 · Cited by 102 · see citing works
Propagation of Tau Pathology: Integrating Insights From Postmortem and In Vivo Studies
Vogels, T., Leuzy, A., Cicognola, C., Ashton, N. J., Smolek, T., Novák, M., Blennow, K., Zetterberg, H., Hromádka, T., Žilka, N., et al. (2019) · Biological Psychiatry · doi:10.1016/j.biopsych.2019.09.019 · Cited by 94 · see citing works
Detection of Alzheimer Disease (AD)-Specific Tau Pathology in AD and NonAD Tauopathies by Immunohistochemistry With Novel Conformation-Selective Tau Antibodies
Gibbons, G. S., Banks, R. A., Kim, B., Changolkar, L., Riddle, D. M., Leight, S. N., Irwin, D. J., Trojanowski, J. Q., & Lee, V. M. Y. (2018) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nly010 · Cited by 94 · see citing works
SFPQ and Tau: critical factors contributing to rapid progression of Alzheimer’s disease
Younas, N., Zafar, S., Shafiq, M., Noor, A., Siegert, A., Arora, A. S., Galkin, A. P., Zafar, A., Schmitz, M., Stadelmann, C., et al. (2020) · Acta Neuropathologica · doi:10.1007/s00401-020-02178-y · Cited by 94 · see citing works
Human iPSC 4R tauopathy model uncovers modifiers of tau propagation
Bravo, C., Giani, A. M., Madero‐Pérez, J., Zhao, Z., Wan, Y., Samelson, A. J., Wong, M. Y., Evangelisti, A., Cordes, E., Fan, L., et al. (2024) · Cell · doi:10.1016/j.cell.2024.03.015 · Cited by 81 · see citing works
Liraglutide and a lipidized analog of prolactin-releasing peptide show neuroprotective effects in a mouse model of β-amyloid pathology
Holubová, M., Hrubá, L., Popelová, A., Bencze, M., Pražienková, V., Gengler, S., Kratochvílová, H., Haluzı́k, M., Železná, B., Kuneš, J., et al. (2018) · Neuropharmacology · doi:10.1016/j.neuropharm.2018.11.002 · Cited by 80 · see citing works
Persistent repression of tau in the brain using engineered zinc finger protein transcription factors
Wegmann, S., DeVos, S. L., Zeitler, B., Marlen, K., Bennett, R. E., Perez-Rando, M., MacKenzie, D., Yu, Q., Commins, C., Bannon, R. N., et al. (2021) · Science Advances · doi:10.1126/sciadv.abe1611 · Cited by 77 · see citing works
Modeling late-onset Alzheimer’s disease neuropathology via direct neuronal reprogramming
Sun, Z., Kwon, J.-S., Ren, Y., Chen, S., Walker, C. K., Lu, X., Cates, K., Karahan, H., Sviben, S., Fitzpatrick, J. A. J., et al. (2024) · Science · doi:10.1126/science.adl2992 · Cited by 77 · see citing works
“Pathogenic tau has been linked to synaptic dysfunction and loss (69).”
Toxic Tau Oligomers Modulated by Novel Curcumin Derivatives
Cascio, F. L., Puangmalai, N., Ellsworth, A., Bucchieri, F., Pace, A., Piccionello, A. P., & Kayed, R. (2019) · Scientific Reports · doi:10.1038/s41598-019-55419-w · Cited by 71 · 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
A state of delirium: Deciphering the effect of inflammation on tau pathology in Alzheimer's disease
Barron, M., Gartlon, J. E., Dawson, L. A., Atkinson, P. J., & Pardon, M. (2016) · Experimental Gerontology · doi:10.1016/j.exger.2016.12.006 · Cited by 70 · see citing works
Exosomal tau with seeding activity is released from Alzheimer's disease synapses, and seeding potential is associated with amyloid beta
Miyoshi, E., Bilousova, T. V., Melnik, M., Fakhrutdinov, D., Poon, W. W., Vinters, H. V., Miller, C. A., Corrada, M. M., Kawas, C. H., Bohannan, R. C., et al. (2021) · Laboratory Investigation · doi:10.1038/s41374-021-00644-z · Cited by 67 · see citing works
Sensitive and reproducible MEG resting-state metrics of functional connectivity in Alzheimer’s disease
Schoonhoven, D. N., Briels, C. T., Hillebrand, A., Scheltens, P., Stam, C. J., & Gouw, A. A. (2022) · Alzheimer s Research & Therapy · doi:10.1186/s13195-022-00970-4 · Cited by 65 · see citing works
Impaired AMPA signaling and cytoskeletal alterations induce early synaptic dysfunction in a mouse model of Alzheimer's disease
Baglietto‐Vargas, D., Prieto, G. A., Limón, A., Forner, S., Rodríguez‐Ortiz, C. J., Ikemura, K., Ager, R. R., Medeiros, R., Trujillo‐Estrada, L., Martini, A. C., et al. (2018) · Aging Cell · doi:10.1111/acel.12791 · Cited by 63 · see citing works
Mechanistic insights into remodeled Tau-derived PHF6 peptide fibrils by Naphthoquinone-Tryptophan hybrids
KrishnaKumar, V. G., Paul, A., Gazit, E., & Segal, D. (2018) · Scientific Reports · doi:10.1038/s41598-017-18443-2 · Cited by 57 · see citing works
S-nitrosylation of E3 ubiquitin-protein ligase RNF213 alters non-canonical Wnt/Ca+2 signaling in the P301S mouse model of tauopathy
Amal, H., Gong, G., Gjoneska, E., Lewis, S. M., Wishnok, J. S., Tsai, L., & Tannenbaum, S. R. (2019) · Translational Psychiatry · doi:10.1038/s41398-019-0388-7 · Cited by 55 · see citing works
Diagnóstico da doença de Alzheimer: recomendações do Departamento Científico de Neurologia Cognitiva e do Envelhecimento da Academia Brasileira de Neurologia
Schilling, L. P., Balthazar, M. L. F., Radanovic, M., Forlenza, O. V., Silagi, M. L., Smid, J., Barbosa, B. J. A. P., Frota, N. A. F., de Souza, L. C., Vale, F. A. C., et al. (2022) · Dementia & Neuropsychologia · doi:10.1590/1980-5764-dn-2022-s102pt · Cited by 54 · see citing works
Chemicals used for the induction of Alzheimer’s disease-like cognitive dysfunctions in rodents
Mahdi, O., Baharuldin, M. T. H., Nor, N. H. M., Chiroma, S. M., Jagadeesan, S., & Moklas, M. A. M. (2019) · Biomedical Research and Therapy · doi:10.15419/bmrat.v6i11.575 · Cited by 51 · see citing works
Hippocampal tau oligomerization early in tau pathology coincides with a transient alteration of mitochondrial homeostasis and DNA repair in a mouse model of tauopathy
Zheng, J., Akbari, M., Schirmer, C., Reynaert, M., Loyens, A., Lefebvre, B., Buée, L., Croteau, D. L., Galas, M., & Bohr, V. A. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-00896-8 · Cited by 51 · see citing works
Prospects for strain-specific immunotherapy in Alzheimer’s disease and tauopathies
Bittar, A., Sengupta, U., & Kayed, R. (2018) · npj Vaccines · doi:10.1038/s41541-018-0046-8 · Cited by 50 · see citing works
Generation of a human induced pluripotent stem cell–based model for tauopathies combining three microtubule‐associated protein TAU mutations which displays several phenotypes linked to neurodegeneration
García‐León, J. A., Cabrera‐Socorro, A., Eggermont, K., Swijsen, A., Terryn, J., Fazal, R., Nami, F., Ordovás, L., Quiles‐Jiménez, A., Lluı́s, F., et al. (2018) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2018.05.007 · Cited by 50 · see citing works
A Clinical Trial of Transcranial Electromagnetic Treatment in Alzheimer’s Disease: Cognitive Enhancement and Associated Changes in Cerebrospinal Fluid, Blood, and Brain Imaging
Arendash, G. W., Cao, C., Abulaban, H., Baranowski, R., Wisniewski, G., Becerra, L. R., Andel, R., Lin, X., Zhang, X., Wittwer, D., et al. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190367 · Cited by 49 · see citing works
Stress-Induced Synaptic Dysfunction and Neurotransmitter Release in Alzheimer’s Disease: Can Neurotransmitters and Neuromodulators be Potential Therapeutic Targets?
Jha, S. K., Jha, N. K., Kumar, D., Sharma, R., Shrivastava, A., Ambasta, R. K., & Kumar, P. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160623 · Cited by 46 · see citing works
Exploring the power of yeast to model aging and age-related neurodegenerative disorders
Oliveira, A. V., Vilaça, R., dos Santos, C. N., Costa, V., & Menezes, R. (2016) · Biogerontology · doi:10.1007/s10522-016-9666-4 · Cited by 46 · see citing works
Does Impairment of Adult Neurogenesis Contribute to Pathophysiology of Alzheimer's Disease? A Still Open Question
Puma, D. D. L., Piacentini, R., & Grassi, C. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.578211 · Cited by 45 · see citing works
Long Non-coding RNA: Insight Into Mechanisms of Alzheimer's Disease
Lan, Z., Chen, Y., Jin, J., Xu, Y., & Zhu, X. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.821002 · Cited by 45 · see citing works
Postsynaptic Proteome of Non-Demented Individuals with Alzheimer’s Disease Neuropathology
Zolochevska, O., Bjorklund, N., Woltjer, R., Wiktorowicz, J. E., & Taglialatela, G. (2018) · Journal of Alzheimer’s Disease · doi:10.3233/jad-180179 · Cited by 42 · see citing works
Recent Development in the Understanding of Molecular and Cellular Mechanisms Underlying the Etiopathogenesis of Alzheimer’s Disease
Afsar, A., Castro, M. D. C. C., Soladogun, A. S., & Li, Z. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24087258 · Cited by 42 · see citing works
Monitoring synaptic pathology in Alzheimer’s disease through fluid and PET imaging biomarkers: a comprehensive review and future perspectives
Lista, S., Santos‐Lozano, A., Emanuele, E., Mercuri, N. B., Gabelle, A., López‐Ortiz, S., Martín-Hernández, J., Maisto, N., Imbimbo, C., Caraci, F., et al. (2024) · Molecular Psychiatry · doi:10.1038/s41380-023-02376-6 · Cited by 42 · see citing works
Extra virgin olive oil improves synaptic activity, short‐term plasticity, memory, and neuropathology in a tauopathy model
Lauretti, E., Nenov, M. N., Dincer, O., Iuliano, L., & Praticò, D. (2019) · Aging Cell · doi:10.1111/acel.13076 · Cited by 42 · see citing works
Integrating in vitro and in silico approaches to evaluate the “dual functionality” of palmatine chloride in inhibiting and disassembling Tau-derived VQIVYK peptide fibrils
Haj, E., Losev, Y., KrishnaKumar, V. G., Pichinuk, E., Engel, H., Raveh, A., Gazit, E., & Segal, D. (2018) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2018.04.001 · Cited by 41 · see citing works
Tau Protein and Tauopathies: Exploring Tau Protein–Protein and Microtubule Interactions, Cross‐Interactions and Therapeutic Strategies
Lorenzo, D. D. (2024) · ChemMedChem · doi:10.1002/cmdc.202400180 · Cited by 40 · see citing works
The Potential Role of Herpes Simplex Virus Type 1 and Neuroinflammation in the Pathogenesis of Alzheimer's Disease
Laval, K., & Enquist, L. W. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2021.658695 · Cited by 40 · see citing works
Distinct Conformations, Aggregation and Cellular Internalization of Different Tau Strains
Karikari, T. K., Nagel, D. A., Grainger, A. I., Clarke-Bland, C., Crowe, J. A., Hill, E. J., & Moffat, K. G. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00296 · Cited by 39 · see citing works
Advances in protein misfolding, amyloidosis and its correlation with human diseases
Kundu, D., Prerna, K., Chaurasia, R., Bharty, M. K., & Dubey, V. K. (2020) · 3 Biotech · doi:10.1007/s13205-020-2166-x · Cited by 39 · see citing works
Tau in Alzheimer’s Disease: Pathological Alterations and an Attractive Therapeutic Target
Gu, J., & Liu, F. (2020) · Current Medical Science · doi:10.1007/s11596-020-2282-1 · Cited by 38 · see citing works
A quantitative biology approach correlates neuronal toxicity with the largest inclusions of TDP-43
Cascella, R., Bigi, A., Riffert, D. G., Gagliani, M. C., Ermini, E., Moretti, M., Cortese, K., Cecchi, C., & Chiti, F. (2022) · Science Advances · doi:10.1126/sciadv.abm6376 · Cited by 37 · see citing works
Tau Abnormalities and the Potential Therapy in Alzheimer’s Disease
Almansoub, H. A. M. M., Tang, H. R., Wu, Y., Wang, D., Mahaman, Y. A. R., Wei, N., Almansob, Y. A. M., He, W., & Liu, D. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180868 · Cited by 37 · see citing works
A prolyl oligopeptidase inhibitor reduces tau pathology in cellular models and in mice with tauopathy
Eteläinen, T. S., Silva, M. C., Uhari-Väänänen, J. K., Lorenzo, F. D., Jäntti, M. H., Cui, H., Chavero‐Pieres, M., Kilpeläinen, T. P., Mechtler, C., Svarcbahs, R., et al. (2023) · Science Translational Medicine · doi:10.1126/scitranslmed.abq2915 · Cited by 36 · see citing works
Alkaloids as Potential Multi-Target Drugs to Treat Alzheimer's Disease
Lima, J. A., & Hamerski, L. (2018) · Studies in natural products chemistry · doi:10.1016/b978-0-444-64183-0.00008-7 · Cited by 34 · see citing works
Intrinsically disordered proteins in the formation of functional amyloids from bacteria to humans
Avni, A., Swasthi, H. M., Majumdar, A., & Mukhopadhyay, S. (2019) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2019.05.005 · Cited by 34 · 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
Confocal Spectroscopy to Study Dimerization, Oligomerization and Aggregation of Proteins: A Practical Guide
Gambin, Y., Polinkovsky, M. E., François, B., Giles, N., Bhumkar, A., & Sierecki, E. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17050655 · Cited by 34 · see citing works
Targeting gut-brain axis by dietary flavonoids ameliorate aging-related cognition decline: Evidences and mechanisms
Chu, Z., Han, S., Luo, Y., Zhou, Y., Zhu, L., & Luo, F. (2023) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2023.2222404 · Cited by 32 · see citing works
Alzheimer’s disease: phenotypic approaches using disease models and the targeting of tau protein
Lauretti, E., & Praticò, D. (2020) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2020.1737012 · Cited by 32 · see citing works
Recent advances of small molecule JNK3 inhibitors for Alzheimer’s disease
Qin, P., Ran, Y., Liu, Y., Wei, C., Luan, X., Niu, H., Peng, J., Sun, J., & Wu, J. (2022) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2022.106090 · Cited by 31 · see citing works
Acetylation of Aβ42 at Lysine 16 Disrupts Amyloid Formation
Adhikari, R., Yang, M., Saikia, N., Dutta, C., Alharbi, W. F. A., Shan, Z. J., Pandey, R., & Tiwari, A. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00069 · Cited by 29 · see citing works
Vascular and Nonvascular Mechanisms of Cognitive Impairment and Dementia
Kara, B., Gordon, M. N., Gifani, M., Dorrance, A. M., & Counts, S. (2022) · Clinics in Geriatric Medicine · doi:10.1016/j.cger.2022.07.006 · Cited by 29 · see citing works
Diagnosis of Alzheimer’s disease: recommendations of the Scientific Department of Cognitive Neurology and Aging of the Brazilian Academy of Neurology
Schilling, L. P., Balthazar, M. L. F., Radanovic, M., Forlenza, O. V., Silagi, M. L., Smid, J., Barbosa, B. J. A. P., Frota, N. A. F., de Souza, L. C., Vale, F. A. C., et al. (2022) · Dementia & Neuropsychologia · doi:10.1590/1980-5764-dn-2022-s102en · Cited by 29 · see citing works
APOE ε4 is associated with decreased synaptic density in cognitively impaired participants
He, K., Li, B., Wang, J., Wang, Y., You, Z., Chen, X., Chen, H., Li, J., Huang, Q., Guo, Q., et al. (2024) · Alzheimer's & Dementia · doi:10.1002/alz.13775 · Cited by 29 · see citing works
Extracellular tau oligomers affect extracellular glutamate handling by astrocytes through downregulation of GLT‐1 expression and impairment of NKA1A2 function
Puma, D. D. L., Ripoli, C., Puliatti, G., Pastore, F., Lazzarino, G., Tavazzi, B., Arancio, O., Piacentini, R., & Grassi, C. (2022) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12811 · Cited by 28 · see citing works
Animal models of Alzheimer’s disease: preclinical insights and challenges
Xu, Q., Yang, W., Zhong, M., Lin, Z., Gray, N. E., & Xian, Y. (2023) · Acta Materia Medica · doi:10.15212/amm-2023-0001 · Cited by 28 · see citing works
Dysregulation of Microtubule Stability Impairs Morphofunctional Connectivity in Primary Neuronal Networks
Verstraelen, P., Detrez, J. R., Verschuuren, M., Kuijlaars, J., Nuydens, R., Timmermans, J., & Vos, W. H. D. (2017) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2017.00173 · Cited by 28 · see citing works
The Role of Chronic Inflammatory Bone and Joint Disorders in the Pathogenesis and Progression of Alzheimer's Disease
Culibrk, R. A., & Hahn, M. S. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.583884 · Cited by 27 · see citing works
On the role of the cellular prion protein in the uptake and signaling of pathological aggregates in neurodegenerative diseases
Legname, G., & Scialò, C. (2020) · Prion · doi:10.1080/19336896.2020.1854034 · Cited by 27 · see citing works
NK1 antagonists attenuate tau phosphorylation after blast and repeated concussive injury
Corrigan, F., Černak, I., McAteer, K. M., Hellewell, S. C., Rosenfeld, J. V., Turner, R. J., & Vink, R. (2021) · Scientific Reports · doi:10.1038/s41598-021-88237-0 · Cited by 27 · see citing works
All roads lead to Rome — a review of the potential mechanisms by which exerkines exhibit neuroprotective effects in Alzheimer’s disease
So, K., Li, A., Liang, Y., Zhang, L., Luo, X., Wu, L.-L., Chen, Z.-W., Wei, G.-H., Zhang, K., Du, Z.-A., et al. (2021) · Neural Regeneration Research · doi:10.4103/1673-5374.325012 · Cited by 26 · see citing works
Unveiling the Potential of Polyphenols as Anti-Amyloid Molecules in Alzheimer’s Disease
Kabir, E. R., Chowdhury, N. M., Yasmin, H., Kabir, M. T., Akter, R., Perveen, A., Ashraf, G. M., Akter, S., Rahman, M. H., & Sweilam, S. H. (2022) · Current Neuropharmacology · doi:10.2174/1570159x20666221010113812 · Cited by 26 · see citing works
A MultiTEP platform-based epitope vaccine targeting the phosphatase activating domain (PAD) of tau: therapeutic efficacy in PS19 mice
Hovakimyan, A., Antonyan, T., Shabestari, S. K., Svystun, O., Chailyan, G., Coburn, M., Carlen-Jones, W., Petrushina, I., Chadarevian, J. P., Zagorski, K., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-51809-2 · Cited by 26 · see citing works
Dual Targeting of Monomeric Tau and α-Synuclein Aggregation: A New Multitarget Therapeutic Strategy for Neurodegeneration
Gabr, M. T., & Peccati, F. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00281 · Cited by 24 · see citing works
Heterogeneous Tau Oligomers as Molecular Targets for Alzheimer’s Disease and Related Tauopathies
Lo, C. H. (2022) · Biophysica · doi:10.3390/biophysica2040039 · Cited by 24 · see citing works
Binding and neurotoxicity mitigation of toxic tau oligomers by synthetic heparin like oligosaccharides
Wang, P., Cascio, F. L., Gao, J., Kayed, R., & Huang, X. (2018) · Chemical Communications · doi:10.1039/c8cc05072d · Cited by 23 · see citing works
Advanced analytical methodologies in Alzheimer’s disease drug discovery
Simone, A. D., Naldi, M., Tedesco, D., Bartolini, M., Davani, L., & Andrisano, V. (2019) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2019.112899 · Cited by 22 · see citing works
Novel 6-hydroxybenzothiazol-2-carboxamides as potent and selective monoamine oxidase B inhibitors endowed with neuroprotective activity
Al-Saad, O. M., Gabr, M. T., Darwish, S. S., Rullo, M., Pisani, L., Miniero, D. V., Liuzzi, G. M., Kany, A. M., Hirsch, A. K. H., Abadi, A., et al. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116266 · Cited by 21 · see citing works
Monitoring plasma protein aggregation during aging using conformation-specific antibodies and FTIR spectroscopy
Magalhães, S., Trindade, D., Martins, T. S., Rosa, I. M., Delgadillo, I., Goodfellow, B. J., Silva, O. A. B. D. C. E., Henriques, A. G., & Nunes, A. (2019) · Clinica Chimica Acta · doi:10.1016/j.cca.2019.11.025 · Cited by 21 · see citing works
Transcranial Electromagnetic Treatment Stops Alzheimer’s Disease Cognitive Decline over a 2½-Year Period: A Pilot Study
Arendash, G. W., Abulaban, H., Steen, S., Andel, R., Wang, Y., Bai, Y., Baranowski, R., McGarity, J., Scritsmier, L., Lin, X., et al. (2022) · Medicines · doi:10.3390/medicines9080042 · Cited by 19 · see citing works
Role of NFE2L1 in the Regulation of Proteostasis: Implications for Aging and Neurodegenerative Diseases
Chandran, A., Oliver, H., & Rochet, J. (2023) · Biology · doi:10.3390/biology12091169 · Cited by 18 · see citing works
Intrathecal amyloid‐beta oligomer administration increases tau phosphorylation in the medial temporal lobe in the African green monkey: A nonhuman primate model of Alzheimer's disease
Wakeman, D. R., Weed, M. R., Perez, S. E., Cline, E. N., Viola, K. L., Wilcox, K. C., Moddrelle, D. S., Nisbett, E. Z., Kurian, A., Bell, A., et al. (2022) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12800 · Cited by 18 · see citing works
Tau-Reactive Endogenous Antibodies: Origin, Functionality, and Implications for the Pathophysiology of Alzheimer’s Disease
Hromádková, L., & Ovsepian, S. V. (2019) · Journal of Immunology Research · doi:10.1155/2019/7406810 · Cited by 17 · see citing works
In Vivo Validation of a Small Molecule Inhibitor of Tau Self-Association in htau Mice
Davidowitz, E. J., Krishnamurthy, P., Lopez, P. L. D. C., Jimenez, H. T., Adrien, L. R., Davies, P., & Moe, J. G. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190465 · Cited by 17 · see citing works
Both Amyloid-β Peptide and Tau Protein Are Affected by an Anti-Amyloid-β Antibody Fragment in Elderly 3xTg-AD Mice
Roda, A. R., Montoliu‐Gaya, L., Serra-Mir, G., & Villegas, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186630 · Cited by 17 · see citing works
Tau oligomers impair memory and synaptic plasticity through the cellular prion protein
Balducci, C., Orsini, F., Cerovic, M., Beeg, M., Rocutto, B., Dacomo, L., Masone, A., Busani, E., Raimondi, I., Lavigna, G., et al. (2025) · Acta Neuropathologica Communications · doi:10.1186/s40478-025-01930-3 · Cited by 16 · see citing works
Clinical Features and Potential Mechanisms Relating Neuropathological Biomarkers and Blood-Brain Barrier in Patients With Alzheimer’s Disease and Hearing Loss
Zhang, W., Lian, T., Lian, T.-H., Guo, P. F., Zhang, Y., Li, J., Guan, H., He, M., Zhang, W., Zhang, W., et al. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.911028 · Cited by 16 · see citing works
Regulation of Tau Homeostasis and Toxicity by Acetylation
Tracy, T. E., Claiborn, K. C., & Gan, L. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_4 · Cited by 16 · see citing works
Spreading of Pathology in Alzheimer’s Disease
Lv, Z., Tan, C., Yu, J., & Tan, L. (2017) · Neurotoxicity Research · doi:10.1007/s12640-017-9765-2 · Cited by 15 · see citing works
Absence of microglia or presence of peripherally‐derived macrophages does not affect tau pathology in young or old hTau mice
Zhu, K., Pieber, M., Han, J., Blomgren, K., Zhang, X., Harris, R. A., & Lund, H. (2020) · Glia · doi:10.1002/glia.23794 · Cited by 15 · see citing works

Dendritic/Post-synaptic Tau and Early Pathology of Alzheimer’s Disease
Yin, X., Zhao, C., Qiu, Y., Zhou, Z., Bao, J., & Qian, W. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.671779 · Cited by 39 · 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
Role of prion protein in mediating the synaptotoxic effects of tau oligomers: Implications for Alzheimer’s disease and related tauopathies
Chiesa, R., Fioriti, L., Forloni, G., & Balducci, C. (2025) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-25-00516 · Cited by 2 · see citing works
The synaptic interplay of Tau and Aβ oligomeric species in Alzheimer’s disease and related tauopathies.
Marcatti, M., Fracassi, A., Montalbano, M., Puangmalai, N., Bhatt, N. N., Natarajan, C., Guptarak, J., Krishnan, B., Kayed, R., & Taglialatela, G. (2022) · Alzheimer s & Dementia · doi:10.1002/alz.062586 · Cited by 1 · see citing works
A role for tau at the synapse in Alzheimer’s disease pathogenesis
Pooler, A. M., Noble, W., & Hanger, D. P. (2014) · Neuropharmacology · doi:10.1016/j.neuropharm.2013.09.018 · Cited by 203 · see citing works

Authors: Guerrero-Muñoz, M. J., Gerson, J., & Castillo-Carranza, D. L.
Affiliations: The University of Texas Medical Branch at Galveston (US)
ORCID: Gerson, Julia
Venue: Frontiers in Cellular Neuroscience
Publisher: Frontiers Media SA
Published: 2015-12-02
Volume: 9
Pages: 464-464
ISSN: 1662-5102 (ISSN-L)
DOI: 10.3389/fncel.2015.00464
PMC: PMC4667007
OpenAlex: W2228598504
Cited by: 168
References: 142
Citations by year: 2026: 9 · 2025: 14 · 2024: 13 · 2023: 13 · 2022: 23 · 2021: 12 · 2020: 23 · 2019: 20 · 2018: 25 · 2017: 9 · 2016: 7
FWCI: 1.68
Type: journal article
Language: en
Open access: gold
doi.org
Licence: cc-by
Locations: Frontiers in Cellular Neuroscience (publishedVersion, cc-by)
Europe PMC (PubMed Central) (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders: Mitchell Center for Neurodegenerative Diseases, University of Texas Medical Branch
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: tau oligomers, Alzheimer's disease, synaptic dysfunction, amyloid-beta, tau protein, neurotoxicity, cognitive impairment, memory loss, neuronal loss

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Tau Oligomers: The Toxic Player at Synapses in Alzheimer’s Disease

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