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Propagation of Tau Misfolding from the Outside to the Inside of a Cell
Open accessAbstract
Tauopathies are neurodegenerative diseases characterized by aggregation of the microtubule-associated protein Tau in neurons and glia. Although Tau is normally considered an intracellular protein, Tau aggregates are observed in the extracellular space, and Tau peptide is readily detected in the cerebrospinal fluid of patients. Tau aggregation occurs in many diseases, including Alzheimer disease and frontotemporal dementia. Tau pathology begins in discrete, disease-specific regions but eventually involves much larger areas of the brain. It is unknown how this propagation of Tau misfolding occurs. We hypothesize that extracellular Tau aggregates can transmit a misfolded state from the outside to the inside of a cell, similar to prions. Here we show that extracellular Tau aggregates, but not monomer, are taken up by cultured cells. Internalized Tau aggregates displace tubulin, co-localize with dextran, a marker of fluid-phase endocytosis, and induce fibrillization of intracellular full-length Tau. These intracellular fibrils are competent to seed fibril formation of recombinant Tau monomer in vitro. Finally, we observed that newly aggregated intracellular Tau transfers between co-cultured cells. Our data indicate that Tau aggregates can propagate a fibrillar, misfolded state from the outside to the inside of a cell. This may have important implications for understanding how protein misfolding spreads through the brains of tauopathy patients, and it is potentially relevant to myriad neurodegenerative diseases associated with protein misfolding.
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“Pathogenic forms of tau spread toxicity between cells through a prion-like mechanism involving seeded conformational change (Colin et al. 2020, Frost et al. 2009).”
From The Role of Retrotransposons and Endogenous Retroviruses in Age-Dependent Neurodegenerative Disorders (2024) · cites this paper as Frost et al. 2009
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“Several lines of evidence indicate tau propagates pathology among neurons.”
From Spontaneous pathology in PS19 tauopathy mice progresses via brain networks (2025) · cites this paper as Frost et al., 2009
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“Proteopathic tau seeds are capable of entering a cell and promoting aggregation in a prion-like manner (Clavaguera et al., 2009; Frost et al., 2009).”
From Network analysis identifies strain-dependent response to tau and tau seeding-associated genes (2023) · cites this paper as Frost et al., 2009
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“Tau assemblies enter cells to trigger intracellular aggregation (Frost et al., 2009; Holmes et al., 2014)”
From Spontaneous pathology in PS19 tauopathy mice progresses via brain networks (2025) · cites this paper as Frost et al., 2009
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“The aggregation of tau impairs the axons, leading to neurodegeneration [23].”
From The Multifaceted Role of Neuroprotective Plants in Alzheimer’s Disease Treatment (2022) · cites this paper as [23]
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“The current clinical trial literature is compatible with the idea that AβP-related substances kindle a self-propagating process related to neocortical NFTs, as has been hypothesized (266-269).”
From Correlation of Alzheimer Disease Neuropathologic Changes With Cognitive Status: A Review of the Literature (2012) · cites this paper as [267]
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Citations
Cites
Neuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123
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
Inflammation and Alzheimer’s disease
Akiyama, H. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00124-x · Cited by 4,514
Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17
Hutton, M., Lendon, C. L., Rizzu, P., Baker, M., Froelich, S., Houlden, H., Pickering-Brown, S., Chakraverty, S., Isaacs, A., Grover, A., et al. (1998) · Nature · doi:10.1038/31508 · Cited by 3,498
A protein factor essential for microtubule assembly
Weingarten, M. D., Lockwood, A. H., Hwo, S. Y., & Kirschner, M. W. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.5.1858 · Cited by 3,089
Lee, V. M.-Y., Goedert, M., & Trojanowski, J. Q. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1121 · Cited by 2,480
Frequency of Stages of Alzheimer-Related Lesions in Different Age Categories
Braak, H., & Braak, E. (1997) · Neurobiology of Aging · doi:10.1016/s0197-4580(97)00056-0 · Cited by 1,656
Mutation in the tau gene in familial multiple system tauopathy with presenile dementia
Spillantini, M. G., Murrell, J. R., Goedert, M., Farlow, M. R., Klug, A., & Ghetti, B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.13.7737 · Cited by 1,474
Arnold, S. E., Hyman, B. T., Flory, J., Damasio, A. R., & Van Hoesen, G. W. (1991) · Cerebral Cortex · doi:10.1093/cercor/1.1.103 · Cited by 1,380
Tau is a candidate gene for chromosome 17 frontotemporal dementia
Poorkaj, P., Bird, T. D., Wijsman, E., Nemens, E., Garruto, R. M., Anderson, L., Andreadis, A., Wiederholt, W. C., Raskind, M., & Schellenberg, G. D. (1998) · Annals of Neurology · doi:10.1002/ana.410430617 · Cited by 1,374
Research works printed but not linked: 2
- Delacourte, 2005, Polish Acad. Sci., 43, 244
- DePace, 2002, Nat. Struct. Biol., 9, 389
Cited by
Sorted by citations
Items 301–400 of 1,001
Harrington, C. R., Storey, J. M. D., Clunas, S., Harrington, K. A., Horsley, D., Ishaq, A., Kemp, S. J., Larch, C. P., Marshall, C., Nicoll, S. L., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.616029 · Cited by 107
Extracellular Vesicle Biology in Alzheimer’s Disease and Related Tauopathy
DeLeo, A. M., & Ikezu, T. (2017) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-017-9768-z · Cited by 109
Alzheimer's disease: Pathogenesis and prevention
Braak, H., & Tredici, K. D. (2012) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2012.01.011 · Cited by 110
Can Parkinson's disease pathology be propagated from one neuron to another?
Dunning, C. J. R., Reyes, J. F., Steiner, J. A., & Brundin, P. (2011) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2011.11.003 · Cited by 111
Prions and the Potential Transmissibility of Protein Misfolding Diseases
Kraus, A., Groveman, B. R., & Caughey, B. W. (2013) · Annual Review of Microbiology · doi:10.1146/annurev-micro-092412-155735 · Cited by 107
Ando, K., Maruko-Otake, A., Ohtake, Y., Hayashishita, M., Sekiya, M., & Iijima, K. M. (2016) · PLOS Genetics · doi:10.1371/journal.pgen.1005917 · Cited by 105
Variations in filament conformation dictate seeding barrier between three- and four-repeat Tau
Dinkel, P. D., Siddiqua, A., Huynh, H., Shah, M., & Margittai, M. (2011) · Biochemistry · doi:10.1021/bi2004685 · Cited by 104
Tau-Based Therapeutics for Alzheimer’s Disease: Active and Passive Immunotherapy
Panza, F., Solfrizzi, V., Seripa, D., Imbimbo, B. P., Lozupone, M., Santamato, A., Tortelli, R., Galizia, I., Prete, C., Daniele, A., et al. (2016) · Immunotherapy · doi:10.2217/imt-2016-0019 · Cited by 113
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 106
Li, H., Liu, C.-C., Zheng, H., & Huang, T. Y. (2018) · Translational Neurodegeneration · doi:10.1186/s40035-018-0139-3 · Cited by 103
Guerrero‐Munoz, M. J., Castillo‐Carranza, D. L., & Kayed, R. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.12.023 · Cited by 105
TIA1 regulates the generation and response to toxic tau oligomers
Jiang, L., Ash, P. E. A., Maziuk, B. F., Ballance, H. I., Boudeau, S., Abdullatif, A. A., Orlando, M., Petrucelli, L., Ikezu, T., & Wolozin, B. L. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1937-5 · Cited by 100
Possible Mechanisms of Tau Spread and Toxicity in Alzheimer’s Disease
Zhang, H., Cao, Y., Ma, L., Wei, Y., & Li, H. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.707268 · Cited by 109
Matrix Metalloproteinase in Blood-Brain Barrier Breakdown in Dementia
Weekman, E. M., & Wilcock, D. M. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-150759 · Cited by 106
Angot, É., & Brundin, P. (2009) · Parkinsonism & Related Disorders · doi:10.1016/s1353-8020(09)70802-8 · Cited by 107
Tau Overexpression Results in Its Secretion via Membrane Vesicles
Simón, D., García‐García, E., Gómez‐Ramos, A., Falcón‐Pérez, J. M., Dı́az-Hernández, M., Hernández, F., & Ávila, J. (2012) · Neurodegenerative Diseases · doi:10.1159/000334915 · Cited by 99
Ryan, P., Patel, B., Makwana, V., Jadhav, H. R., Kiefel, M. J., Davey, A. K., Reekie, T. A., Rudrawar, S., & Kassiou, M. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00185 · Cited by 101
Dai, C.-L., Hu, W., Tung, Y. C., Liu, F., Gong, C.-X., & Iqbal, K. (2018) · Alzheimer's Research & Therapy · doi:10.1186/s13195-018-0341-7 · Cited by 99
Tau as a Therapeutic Target for Alzheimers Disease
Boutajangout, A., Sigurdsson, E. M., & Krishnamurthy, P. K. (2011) · Current Alzheimer Research · doi:10.2174/156720511796717195 · Cited by 102
Tau in neurodegenerative diseases: molecular mechanisms, biomarkers, and therapeutic strategies
Zhang, X., Wang, J., Zhang, Z., & Ye, K. (2024) · Translational Neurodegeneration · doi:10.1186/s40035-024-00429-6 · Cited by 119
Mouse models of frontotemporal dementia
Roberson, E. D. (2012) · Annals of Neurology · doi:10.1002/ana.23722 · Cited by 103
TRIM11 protects against tauopathies and is down-regulated in Alzheimer’s disease
Zhang, Z., Harischandra, D. S., Wang, R., Ghaisas, S., Zhao, J. Y., McMonagle, T. P., Zhu, G., Lacuarta, K. D., Song, J., Trojanowski, J. Q., et al. (2023) · Science · doi:10.1126/science.add6696 · Cited by 95
Targeting tau: clinical trials and novel therapeutic approaches
VandeVrede, L., Boxer, A. L., & Polydoro, M. (2020) · Neuroscience Letters · doi:10.1016/j.neulet.2020.134919 · Cited by 90
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 99
The Role of Tau in Neurodegenerative Diseases and Its Potential as a Therapeutic Target
Wolfe, M. S. (2012) · Scientifica · doi:10.6064/2012/796024 · Cited by 105
Sensitive Detection of Proteopathic Seeding Activity with FRET Flow Cytometry
Furman, J. L., Holmes, B. B., & Diamond, M. I. (2015) · Journal of Visualized Experiments · doi:10.3791/53205 · Cited by 104
Self-citationSmethurst, P., Sidle, K. C. L., & Hardy, J. (2014) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12206 · Cited by 99
Filamentous recombinant human Tau activates primary astrocytes via an integrin receptor complex
Wang, P., & Ye, Y. (2021) · Nature Communications · doi:10.1038/s41467-020-20322-w · Cited by 93
Tau and TDP-43 proteinopathies: kindred pathologic cascades and genetic pleiotropy
Chornenkyy, Y., Fardo, D. W., & Nelson, P. T. (2019) · Laboratory Investigation · doi:10.1038/s41374-019-0196-y · Cited by 93
The Ubiquitin-Proteasome System and Molecular Chaperone Deregulation in Alzheimer’s Disease
Sulistio, Y. A., & Heese, K. (2015) · Molecular Neurobiology · doi:10.1007/s12035-014-9063-4 · Cited by 93
Prions and Protein Assemblies that Convey Biological Information in Health and Disease
Sanders, D. W., Kaufman, S. K., Holmes, B. B., & Diamond, M. I. (2016) · Neuron · doi:10.1016/j.neuron.2016.01.026 · Cited by 92
Self-citationHyperphosphorylation Renders Tau Prone to Aggregate and to Cause Cell Death
Liu, M., Sui, D., Dexheimer, T. S., Hovde, S., Deng, X., Wang, K., Lin, H. L., Hagar, H. C., Kweon, H. K., Kuo, N. S., et al. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-02034-w · Cited by 98
Alkaline Phosphatase Is Increased in both Brain and Plasma in Alzheimer’s Disease
Vardy, E. R. L. C., Kellett, K. A. B., Cocklin, S. L., & Hooper, N. M. (2011) · Neurodegenerative Diseases · doi:10.1159/000329722 · Cited by 93
Effects of oxidized and reduced forms of methylthioninium in two transgenic mouse tauopathy models
Melis, V., Magbagbeolu, M., Rickard, J. E., Horsley, D., Davidson, K., Harrington, K. A., Goatman, K. A., Goatman, E. A., Deiana, S., Close, S., et al. (2015) · Behavioural Pharmacology · doi:10.1097/fbp.0000000000000133 · Cited by 91
An astrocyte BMAL1-BAG3 axis protects against alpha-synuclein and tau pathology
Sheehan, P. W., Nadarajah, C. J., Kanan, M. F., Patterson, J. N., Novotny, B. C., Lawrence, J. H., King, M. W., Brase, L., Inman, C. E., Yuede, C. M., et al. (2023) · Neuron · doi:10.1016/j.neuron.2023.05.006 · Cited by 91
Dai, C., Chen, X., Kazim, S. F., Liu, F., Gong, C., Grundke, I., & Iqbal, K. (2014) · Journal of Neural Transmission · doi:10.1007/s00702-014-1315-y · Cited by 94
Shibuya, Y., Niu, Z., Bryleva, E. Y., Harris, B. T., Murphy, S. R., Kheirollah, A., Bowen, Z. D., Chang, C. C. Y., & Chang, T.-Y. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.04.002 · Cited by 87
Frontal Cortex Neuropathology in Dementia Pugilistica
Saing, T., Dick, M. B., Nelson, P. T., Kim, R. C., Cribbs, D. H., & Head, E. (2011) · Journal of Neurotrauma · doi:10.1089/neu.2011.1957 · Cited by 92
The toxicity of tau in Alzheimer disease: turnover, targets and potential therapeutics
Pritchard, S. M., Dolan, P. J., Vitkus, A., & Johnson, G. V. W. (2011) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2011.01273.x · Cited by 89
Alzheimer’s disease and its treatment–yesterday, today, and tomorrow
Kim, A. Y., Jerdi, S. A., MacDonald, R., & Triggle, C. R. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1399121 · Cited by 99
Pin1 dysregulation helps to explain the inverse association between cancer and Alzheimer's disease
Driver, J. A., Zhou, X. Z., & Lu, K. P. (2015) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.12.025 · Cited by 95
Emerging Therapeutics for Alzheimer's Disease
Chiang, K., & Koo, E. H. (2014) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-011613-135932 · Cited by 95
De novo generation of prion strains
Colby, D. W., & Prusiner, S. B. (2011) · Nature Reviews Microbiology · doi:10.1038/nrmicro2650 · Cited by 88
Morozova, O. A., March, Z. M., Robinson, A. S., & Colby, D. W. (2013) · Biochemistry · doi:10.1021/bi400866w · Cited by 92
Leroy, A., Landrieu, I., Huvent, I., Legrand, D., Codeville, B., Wieruszeski, J.-M., & Lippens, G. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.149419 · Cited by 86
Metabolic Dysfunction in Alzheimer’s Disease: From Basic Neurobiology to Clinical Approaches
Clarke, J. R., Ribeiro, F. C., Frozza, R. L., Felice, F. G. D., & Lourenco, M. V. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-179911 · Cited by 93
Predictive model of spread of Parkinson's pathology using network diffusion
Pandya, S., Zeighami, Y., Freeze, B. S., Dadar, M., Collins, D. L., Dagher, A., & Raj, A. (2019) · NeuroImage · doi:10.1016/j.neuroimage.2019.03.001 · Cited by 90
Review: Modulating the unfolded protein response to prevent neurodegeneration and enhance memory
Halliday, M., & Mallucci, G. R. (2014) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12211 · Cited by 85
Tauopathies: Deciphering Disease Mechanisms to Develop Effective Therapies
Silva, M. C., & Haggarty, S. J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21238948 · Cited by 89
Starvation and inhibition of lysosomal function increased tau secretion by primary cortical neurons
Mohamed, N., Plouffe, V., Rémillard‐Labrosse, G., Planel, E., & Leclerc, N. M. (2014) · Scientific Reports · doi:10.1038/srep05715 · Cited by 92
O-GlcNAc forces an α-synuclein amyloid strain with notably diminished seeding and pathology
Balana, A. T., Mahul-Mellier, A.-L., Nguyen, B. A., Horvath, M., Javed, A., Hard, E. R., Jasiqi, Y., Singh, P., Afrin, S., Pedretti, R., et al. (2024) · Nature Chemical Biology · doi:10.1038/s41589-024-01551-2 · Cited by 84
Ryan, P., Xu, M., Davey, A. K., Danon, J. J., Mellick, G. D., Kassiou, M., & Rudrawar, S. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00143 · Cited by 84
Tau prion-like propagation: state of the art and current challenges
Dujardin, S., & Hyman, B. T. (2019) · Advances in Experimental Medicine and Biology · doi:10.1007/978-981-32-9358-8_23 · Cited by 84
Moore, K. B. E., Hung, T.-J., & Fortin, J. S. (2023) · Drug Discovery Today · doi:10.1016/j.drudis.2023.103487 · Cited by 93
Signature of an aggregation-prone conformation of tau
Eschmann, N. A., Georgieva, E. R., Ganguly, P., Borbat, P. P., Rappaport, M. D., Akdoğan, Y., Freed, J. H., Shea, J., & Han, S. (2017) · Scientific Reports · doi:10.1038/srep44739 · Cited by 83
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Kundel, F., Hong, L., Falcon, B., McEwan, W. A., Michaels, T. C. T., Meisl, G., Esteras, N., Abramov, A. Y., Knowles, T. P. J., Goedert, M., et al. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00094 · Cited by 82
Sharma, A. M., Thomas, T. L., Woodard, D. R., Kashmer, O. M., & Diamond, M. I. (2018) · eLife · doi:10.7554/elife.37813 · Cited by 80
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Musiek, E. S., & Holtzman, D. M. (2012) · Current Opinion in Neurology · doi:10.1097/wco.0b013e32835a30f4 · Cited by 85
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Current Understanding of Neurodegenerative Diseases Associated With the Protein Tau
Josephs, K. A. (2017) · Mayo Clinic Proceedings · doi:10.1016/j.mayocp.2017.04.016 · Cited by 87
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Tetz, G. V., Pinho, M. A., Pritzkow, S., Méndez, N., Soto, C. A., & Tetz, V. (2020) · Scientific Reports · doi:10.1038/s41598-020-59364-x · Cited by 81
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Chastagner, P., Loría, F., Vargas, J., Tois, J., Diamond, M. I., Okafo, G. N., Brou, C., & Zurzolo, C. (2020) · EMBO Molecular Medicine · doi:10.15252/emmm.202012025 · Cited by 80
Self-citationCellular mechanisms of protein aggregate propagation
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Self-citationCurrent directions in tau research: Highlights from Tau 2020
Sexton, C. E., Snyder, H. M., Beher, D., Boxer, A. L., Brannelly, P., Brion, J., Buée, L., Cacace, A. M., Chételat, G., Citron, M., et al. (2021) · Alzheimer s & Dementia · doi:10.1002/alz.12452 · Cited by 89
Self-citationTau fibrils induce nanoscale membrane damage and nucleate cytosolic tau at lysosomes
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Barucker, C., Harmeier, A., Weiske, J., Fauler, B., Albring, K. F., Prokop, S., Hildebrand, P. W., Lurz, R., Heppner, F. L., Huber, O., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.564690 · Cited by 83
From molecule to molecule and cell to cell: Prion-like mechanisms in amyotrophic lateral sclerosis
Grad, L. I., Fernando, S. M., & Cashman, N. R. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.02.009 · Cited by 80
Amyloid cross-seeding raises new dimensions to understanding of amyloidogenesis mechanism
Chaudhuri, P., Prajapati, K. P., Anand, B. G., Dubey, K., & Kar, K. (2019) · Ageing Research Reviews · doi:10.1016/j.arr.2019.100937 · Cited by 80
Danis, C., Dupré, E., Zejneli, O., Caillierez, R., Arrial, A., Bégard, S., Mortelecque, J., Eddarkaoui, S., Loyens, A., Cantrelle, F., et al. (2022) · Molecular Therapy · doi:10.1016/j.ymthe.2022.01.009 · Cited by 75
Kim, W., Lee, S., & Hall, G. F. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.05.042 · Cited by 83
Bezafibrate administration improves behavioral deficits and tau pathology in P301S mice
Dumont, M., Stack, C., Elipenahli, C., Jainuddin, S., Gerges, M., Starkova, N. N., Calingasan, N. Y., Yang, L., Tampellini, D., Starkov, A. A., et al. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds355 · Cited by 78
Swanson, E., Breckenridge, L., McMahon, L. P., Som, S., McConnell, I., & Bloom, G. S. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170168 · Cited by 76
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BackgroundInfluentialWu, X., Piña-Crespo, J., Zhang, Y., Chen, X., & Xu, H. (2017) · Chinese Medical Journal · doi:10.4103/0366-6999.220313 · Cited by 82
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Giustiniani, J., Chambraud, B., Sardin, E., Dounane, O., Guillemeau, K., Nakatani, H., Paquet, D., Kamah, A., Landrieu, I., Lippens, G. M., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1402645111 · Cited by 72
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Metadata
- Authors
- Frost, B., Jacks, R. L., & Diamond, M. I.
- Affiliations
- University of California, San Francisco (US)
- Corresponding author
- Diamond, Marc I.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2009-05
- Volume
- 284
- Issue
- 19
- Pages
- 12845-12852
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC2676015
- OpenAlex
- W1989208474
- Cited by
- 1,252
- References
- 32
- Citations by year
- 2026: 34 · 2025: 71 · 2024: 76 · 2023: 78 · 2022: 72 · 2021: 96 · 2020: 97 · 2019: 70 · 2018: 67 · 2017: 76 · 2016: 67 · 2015: 83 · 2014: 78 · 2013: 89 · 2012: 81
- FWCI
- 43.07
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Muscular Dystrophy Association
- National Institutes of Health
- University of California, San Francisco
- National Institute of Neurological Disorders and Stroke (R01NS050284, R01 NS50284-03)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- tauopathy, prion-like propagation, fluid-phase endocytosis, Alzheimer's disease, frontotemporal dementia
- MeSH terms
- Animals, Animals, Newborn, Cell Line, Dextrans, Extracellular Space, Flow Cytometry, Fluorescent Antibody Technique, Humans, Kidney, Luminescent Proteins, Neurons, Stem Cells, Blotting, Western, tau Proteins, Protein Folding, Microscopy, Atomic Force, Coculture Techniques, Intracellular Space, Mice
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