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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
Flagged first, then by citations
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 701–800 of 1,001
Microglia internalize tau monomers and fibrils using distinct receptors but similar mechanisms
Falkon, K. F., Danford, L., Kuri, E. G., Esquinca‐Moreno, P., Señeriz, Y. L. P., Smith, S. A., Wickline, J. L., Louwrier, A., McPhail, J. A., Sayre, N. L., et al. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.14418 · Cited by 26
Church, T. R., & Margolis, S. S. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1531797 · Cited by 25
Martínez‐Viturro, C. M., Trabanco, A. A., Royes, J., Fernández, E., Tresadern, G., Vega, J. A., del Cerro, A., Delgado, F., Molina, A. G., Tovar, F., et al. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01479 · Cited by 23
Targeting Tau to Treat Clinical Features of Huntington's Disease
Masnata, M., Salem, S., Jacquet, A. D. R., Anwer, M., & Cicchetti, F. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.580732 · Cited by 25
Essential role of sulfide oxidation in brain health and neurological disorders
Kanemaru, E., & Ichinose, F. (2024) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2024.108787 · Cited by 22
Detecting tau in serum of transgenic animal models after tau immunotherapy treatment
d’Abramo, C., Acker, C. M., Schachter, J. B., Terracina, G., Wang, X., Forest, S. K., & Davies, P. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.09.017 · Cited by 22
Functional interplay between plasma membrane Ca2+-ATPase, amyloid β-peptide and tau
Mata, A. M. (2017) · Neuroscience Letters · doi:10.1016/j.neulet.2017.08.004 · Cited by 22
Tau assemblies do not behave like independently acting prion-like particles in mouse neural tissue
Mukadam, A. S., Miller, L. V. C., Durrant, C. S., Vaysburd, M. J., Katsinelos, T., Tuck, B. J., Sanford, S., Sheppard, O., Knox, C., Cheng, S., et al. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01141-6 · Cited by 23
Raj, A. (2021) · Brain Connectivity · doi:10.1089/brain.2020.0905 · Cited by 21
Ruan, Z., & Ikezu, T. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_11 · Cited by 23
Schnabel, J. (2010) · Nature · doi:10.1038/466s2b · Cited by 22
Cellular Models for the Study of PrionsPreprint
Holmes, B. B., & Diamond, M. I. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024026 · Cited by 23
Self-citationPathogenic Role of RAGE in Tau Transmission and Memory Deficits
Kim, Y., Park, H., Kim, Y., Kim, S., Lee, J., Yang, H., Kim, S. J., Li, C. M., Lee, H., Na, D.-H., et al. (2022) · Biological Psychiatry · doi:10.1016/j.biopsych.2022.10.015 · Cited by 23
Endocytic pathways of pathogenic protein aggregates in neurodegenerative diseases
Hivare, P., Mujmer, K., Swarup, G., Gupta, S. K., & Bhatia, D. D. (2023) · Traffic · doi:10.1111/tra.12906 · Cited by 24
Hyperphosphorylated Tau Inflicts Intracellular Stress Responses that Are Mitigated by Apomorphine
Song, Z., Wang, K., Hagar, H. C., Chen, H., Kuan, C.-Y., Zhang, K., & Kuo, M. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03689-x · Cited by 23
VCP regulates early tau seed amplification via specific cofactors
Batra, S., Vaquer‐Alicea, J., Valdez, C., Taylor, S. P., Manon, V. A., Vega, A. R., Kashmer, O. M., Kolay, S., Lemoff, A. S., Cairns, N. J., et al. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-024-00783-z · Cited by 25
Self-citationClavaguera, F., Goedert, M., & Tolnay, M. (2010) · médecine/sciences · doi:10.1051/medsci/2010262121 · Cited by 22
Cehlár, O., Njemoga, S., Horvath, M., Cizmazia, E., Bednáriková, Z., & Barrera, E. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252313049 · Cited by 23
Harnessing the Immune System for Treatment and Detection of Tau Pathology
Congdon, E. E., Krishnaswamy, S., & Sigurdsson, E. M. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-132435 · Cited by 20
Liu, L., Zou, Z., Yang, J., Li, X., Zhu, B., Zhang, H., Sun, Y., Zhang, Y., Zhang, Z., & Wang, W. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.645638 · Cited by 21
Non-Canonical Roles of Tau and Their Contribution to Synaptic Dysfunction
Siano, G., Falcicchia, C., Origlia, N., Cattaneo, A., & Primio, C. D. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221810145 · Cited by 22
Tau R2 and R3 are essential regions for tau aggregation, seeding and propagation
Annadurai, N., Malina, L., Malohlava, J., Hajdúch, M., & Das, V. (2022) · Biochimie · doi:10.1016/j.biochi.2022.05.013 · Cited by 18
Multiple Actions of H2S-Releasing Peptides in Human β-Amyloid Expressing C. elegans
Ali, R., Hameed, R., Chauhan, D., Sen, S., Wahajuddin, M., Nazir, A., & Verma, S. K. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00402 · Cited by 20
Gut Microbiota and Immunotherapy for Alzheimer’s Disease
Dai, C., Liu, F., Iqbal, K., & Gong, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232315230 · Cited by 22
Cofilin promotes tau pathology in Alzheimer’s disease
Yan, M., Tang, L., Dai, L., Lei, C., Xiong, M., Zhang, X., He, M., Tian, Y., Xiong, J., Ke, W., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112138 · Cited by 20
Countering amyloid polymorphism and drug resistance with minimal drug cocktails
Duennwald, M. L., & Shorter, J. (2010) · Prion · doi:10.4161/pri.4.4.13597 · Cited by 20
Unaltered prion protein expression in Alzheimer disease patients
Saijo, E., Scheff, S. W., & Telling, G. C. (2011) · Prion · doi:10.4161/pri.5.2.16355 · Cited by 19
Lasagna‐Reeves, C. A., Rousseaux, M. W. C., Guerrero‐Munoz, M. J., Vilanova-Velez, L., Park, J., See, L., Jafar‐Nejad, P., Richman, R., Orr, H. T., Kayed, R., et al. (2015) · eLife · doi:10.7554/elife.10891 · Cited by 20
Prion Peptides Are Extremely Sensitive to Copper Induced Oxidative Stress
Dell’Acqua, S., Bacchella, C., Monzani, E., Nicolis, S., Natale, G. D., Rizzarelli, E., & Casella, L. (2017) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.7b01757 · Cited by 21
Song, X., Zhou, H.-Y., Sun, Y.-Y., & Huang, H. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-210337 · Cited by 20
Moon, M. R., Castro, L. J., DeAnda, A., Daughters, G. T., Ingels, N. B., & Miller, D. C. (1994) · PubMed · Cited by 20
Co-Existence of tau and α-synuclein pathology in fetal graft tissue at autopsy: A case report
Ornelas, A. S., Adler, C. H., Serrano, G. E., Curry, J. R., Shill, H. A., Kopyov, O. V., & Beach, T. G. (2020) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2019.12.013 · Cited by 18
Identification of cis-acting determinants mediating the unconventional secretion of tau
Katsinelos, T., McEwan, W. A., Jahn, T. R., & Nickel, W. (2021) · Scientific Reports · doi:10.1038/s41598-021-92433-3 · Cited by 16
Site‐Specific Ubiquitination of Tau Amyloids Promoted by the E3 Ligase CHIP
Parolini, F., Kachoie, E. A., Leo, G., Civiero, L., Bubacco, L., Arrigoni, G., Munari, F., Assfalg, M., D’Onofrio, M., & Capaldi, S. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202310230 · Cited by 18
Ramsden, C. E., Zamora, D., Horowitz, M. S., Jahanipour, J., Calzada, E., Li, X., Keyes, G. S., Murray, H. C., Curtis, M. A., Faull, R. L. M., et al. (2023) · Acta Neuropathologica Communications · doi:10.1186/s40478-023-01693-9 · Cited by 21
Kabani, M., & Melki, R. (2011) · Prion · doi:10.4161/pri.18070 · Cited by 20
PrionsEx Vivo: What Cell Culture Models Tell Us about Infectious Proteins
Krauß, S., & Vorberg, I. M. (2013) · International Journal of Cell Biology · doi:10.1155/2013/704546 · Cited by 19
A note on testing hypotheses for stationary processes in the frequency domain
Holger Dette, A., & Hildebrandt, T. (2011) · Journal of Multivariate Analysis · doi:10.1016/j.jmva.2011.07.002 · Cited by 19
Ruiz-Arlandis, G., Pieri, L., Bousset, L., & Melki, R. (2015) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12258 · Cited by 21
Evans, L., Strano, A., Tuck, E. J., Campbell, A., Smith, J. C., Hung, C., Behr, T. S., Ghetti, B. F., Falcon, B., Karakoç, E., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.08.11.246363 · Cited by 19
Basurto‐Islas, G., Diaz, M. C., Zavala-Ocampo, L. M., Martínez‐Herrera, M., & López-Camacho, P. Y. (2025) · Archiv der Pharmazie · doi:10.1002/ardp.202400721 · Cited by 20
Zhang, X., Zou, L. B., Meng, L., Xiong, M., Pan, L., Chen, G., Zheng, Y., Xiong, J., Wang, Z., Duong, D. M., et al. (2021) · eLife · doi:10.7554/elife.65301 · Cited by 17
Mendsaikhan, A., Tooyama, I., Serrano, G. E., Beach, T. G., & Walker, D. G. (2021) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlab056 · Cited by 17
Navarro‐Hortal, M. D., Romero‐Márquez, J. M., Osta, S., Jiménez-Trigo, V., Muñoz-Ollero, P., & Varela‐López, A. (2022) · Diseases · doi:10.3390/diseases10020028 · Cited by 18
Li, L., Miao, J., Chu, D., Jin, N., Tung, Y. C., Dai, C., Hu, W. H., Gong, C., Iqbal, K., & Liu, F. (2022) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.13970 · Cited by 17
Aβ and Tau Prions Causing Alzheimer’s Disease
Condello, C., Merz, G. E., Aoyagi, A., DeGrado, W. F., & Prusiner, S. B. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2655-9_16 · Cited by 18
Vaccines for prion diseases: a realistic goal?
Napper, S., & Schätzl, H. M. (2023) · Cell and Tissue Research · doi:10.1007/s00441-023-03749-7 · Cited by 18
A 3D human co-culture to model neuron-astrocyte interactions in tauopathies
Batenburg, K. L., Sestito, C., Cornelissen‐Steijger, P., van Weering, J. R. T., Price, L., Heine, V. M., & Scheper, W. (2023) · Biological Procedures Online · doi:10.1186/s12575-023-00194-2 · Cited by 22
Tau: More than a microtubule‐binding protein in neurons
Alonso, A. D. C., Idrissi, A. E., Candia, R. F., Morozova, V., & Kleiman, F. E. (2023) · Cytoskeleton · doi:10.1002/cm.21795 · Cited by 17
Poduslo, J. F., Howell, K. G., Olson, N., Ramı́rez-Alvarado, M., & Kandimalla, K. K. (2012) · Biochemistry · doi:10.1021/bi300275g · Cited by 18
Pérez, M., Medina, M., Hernández, F., & Ávila, J. (2018) · BioMolecular Concepts · doi:10.1515/bmc-2018-0001 · Cited by 20
Intercellular Transmission of a Synthetic Bacterial Cytotoxic Prion-Like Protein in Mammalian Cells
Revilla-García, A., Fernández, C., Álamo, M. M., Rı́os, V. D. L., Vorberg, I. M., & Giraldo, R. (2020) · mBio · doi:10.1128/mbio.02937-19 · Cited by 18
Triaca, V., Ruberti, F., & Canu, N. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-74046-7_10 · Cited by 18
FKBP52 in Neuronal Signaling and Neurodegenerative Diseases: A Microtubule Story
Chambraud, B., Byrne, C., Méduri, G., Baulieu, E. E., & Giustiniani, J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031738 · Cited by 18
Amyotrophic lateral sclerosis and organ donation: Is there risk of disease transmission?
Holmes, B. B., & Diamond, M. I. (2012) · Annals of Neurology · doi:10.1002/ana.23684 · Cited by 18
Self-citationKey Points Concerning Amyloid Infectivity and Prion-Like Neuronal Invasion
Espargaró, A., Busquets, M. A., Estelrich, J., & Sabaté, R. (2016) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2016.00029 · Cited by 18
The release and transmission of amyloid precursor protein via exosomes
Zheng, T., Wu, X., Wei, X., Wang, M., & Zhang, B. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.12.009 · Cited by 18
Eisenbaum, M., Pearson, A., Ortiz, C., Koprivica, M., Cembran, A., MULLAN, M. J., Crawford, F., Ojo, J. O., & Bachmeier, C. J. (2024) · Experimental Neurology · doi:10.1016/j.expneurol.2024.114702 · Cited by 18
α-Synuclein aggregates inhibit ESCRT-III through sequestration and collateral degradation
Sitron, C. S., Trinkaus, V. A., Galesic, A., Garhammer, M., Yuste‐Checa, P., Dransfeld, U., Feigenbutz, D., Zhang, J., Ivashko, L., Dudanova, I., et al. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.08.022 · Cited by 19
Sol, O., Mermoud, J., Hallikainen, M., Kurl, S., Rinne, J. O., DAUTZENBERG, P. L. J., Vijverberg, E. G. B., Mummery, C. J., Börjesson‐Hanson, A., Jonsson, M. A. G., et al. (2025) · EBioMedicine · doi:10.1016/j.ebiom.2025.105940 · Cited by 25
Long COVID could become a widespread post-pandemic disease? A debate on the organs most affected
Ferrara, F., Zovi, A., Masi, M., Langella, R., Trama, U., Boccellino, M., & Vitiello, A. (2023) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-023-02417-5 · Cited by 22
Le, L., Lee, J., Im, D., Park, S., Hwang, K.-D., Lee, J., Jiang, Y., Lee, Y.-S., Suh, Y. H., Kim, H. I., et al. (2023) · Advancement of science · doi:10.1002/advs.202302035 · Cited by 13
Prions and Prion-Like Pathogens in Neurodegenerative Disorders
Peggion, C., Sorgato, M. C., & Bertoli, A. (2014) · Pathogens · doi:10.3390/pathogens3010149 · Cited by 17
Neurodegenerative disorders: Dysregulation of a carefully maintained balance?
Swart, C., Haylett, W. L., Kinnear, C. J., Johnson, G., Bardien, S., & Loos, B. (2014) · Experimental Gerontology · doi:10.1016/j.exger.2014.09.003 · Cited by 19
Looking for novel functions of tau
Ávila, J., de Barreda, E. G., Fuster-Matanzo, A., Simón, D., Llorens-Martı́n, M., Engel, T., Lucas, J. J., Dı́az-Hernández, M., & Hernández, F. (2012) · Biochemical Society Transactions · doi:10.1042/bst20120006 · Cited by 17
Tau Fibril Formation in Cultured Cells Compatible with a Mouse Model of Tauopathy
Matsumoto, G., Matsumoto, K., Kimura, T., Suhara, T., Higuchi, M., Sahara, N., & Mori, N. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19051497 · Cited by 17
Couly, S., Denus, M., Bouchet, M., Rubinstenn, G., & Maurice, T. (2020) · The International Journal of Neuropsychopharmacology · doi:10.1093/ijnp/pyaa075 · Cited by 19
Alyenbaawi, H., Allison, W. T., & Mok, S. (2020) · Biomolecules · doi:10.3390/biom10111487 · Cited by 20
History in perspective: How Alzheimer's Disease came to be where it is?
Ahmed, T. F., Ahmed, A., & Imtiaz, F. (2021) · Brain Research · doi:10.1016/j.brainres.2021.147342 · Cited by 21
Calvo-Rodríguez, M., Kharitonova, E. K., & Bacskai, B. J. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2021.118998 · Cited by 17
Synthetic prions and other human neurodegenerative proteinopathies
Le, N. T. T., Narkiewicz, J., Aulić, S., Salzano, G., Tran, T. H., Scaini, D., Moda, F., Giachin, G., & Legname, G. (2014) · Virus Research · doi:10.1016/j.virusres.2014.10.020 · Cited by 19
Endogenous Tau Aggregates in Oligodendrocytes of rTg4510 Mice Induced by Human P301L Tau
Ren, Y., Lin, W.-L., Sanchez, L., Ceballos, C., Polydoro, M., Spires‐Jones, T. L., Hyman, B. T., Dickson, D. W., & Sahara, N. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-130986 · Cited by 19
Anti-Tau Antibodies: Hitting the Target
Golde, T. E., Lewis, J. M., & McFarland, N. R. (2013) · Neuron · doi:10.1016/j.neuron.2013.10.009 · Cited by 17
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
Water-directed pinning is key to tau prion formation
Vigers, M. P., Lobo, S., Najafi, S., DuBose, A., Tsay, K., Ganguly, P., Longhini, A. P., Jin, Y., Buratto, S. K., Kosik, K. S., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2421391122 · Cited by 24
Direct Demonstration of Seed Size-Dependent α-Synuclein Amyloid Amplification
Sakunthala, A., Datta, D., Navalkar, A., Gadhe, L., Kadu, P., Patel, K., Mehra, S., Kumar, R., Chatterjee, D., Devi, J., et al. (2022) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.2c01650 · Cited by 16
Li, J., Chen, L., Liu, S., Sun, Y., Zhen, L., Zhu, Z., Wang, G., & Li, X. (2023) · Cells · doi:10.3390/cells12192348 · Cited by 18
Wallings, R. L., Mark, J. R., Staley, H. A., Gillett, D. A., Neighbarger, N. K., Kordasiewicz, H. B., Hirst, W. D., & Tansey, M. G. (2023) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2023.102064 · Cited by 18
Davidson, R., Krider, R. I., Borsellino, P., Noorda, K., Alhwayek, G., & Vida, T. A. (2023) · Current Issues in Molecular Biology · doi:10.3390/cimb45110553 · Cited by 17
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Iturria‐Medina, Y., Hachinski, V., & Evans, A. C. (2017) · Current Opinion in Neurology · doi:10.1097/wco.0000000000000497 · Cited by 18
Wang, X., Liu, E.-J., Liu, Q. R., Li, S., Li, T., Zhou, Q., Liu, Y., Zhang, H., & Wang, J. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200529 · Cited by 16
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Arc mediates intercellular tau transmission via extracellular vesicles
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Chiarini, A., Gardenal, E., Whitfield, J., Chakravarthy, B., Armato, U., & Prà, I. D. (2015) · Current Pharmaceutical Biotechnology · doi:10.2174/1389201016666150505123813 · Cited by 14
Nieznańska, H., Boyko, S., Dec, R., Rędowicz, M. J., Dzwolak, W., & Nieznański, K. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2021.166209 · Cited by 16
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Ávila, J., de Barreda, E. G., Pallas‐Bazarra, N., & Hernández, F. (2013) · Europe PMC (PubMed Central) · doi:10.13039/501100006373 · Cited by 15
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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