Propagation of Tau via Extracellular Vesicles

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

A protein factor essential for microtubule assembly

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Exosomes – vesicular carriers for intercellular communication

Simons, M., & Raposo, G. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.03.007 · Cited by 2,351 · 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

Transmission and spreading of tauopathy in transgenic mouse brain

Clavaguera, F., Bolmont, T., Crowther, R. A., Abramowski, D., Frank, S., Probst, A., Fraser, G., Stalder, A. K., Beibel, M., Staufenbiel, M., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1901 · Cited by 1,803 · see citing works

Depletion of microglia and inhibition of exosome synthesis halt tau propagation

Asai, H., Ikezu, S., Tsunoda, S., Medalla, M., Luebke, J., Haydar, T., Wolozin, B., Butovsky, O., Kügler, S., & Ikezu, T. (2015) · Nature Neuroscience · doi:10.1038/nn.4132 · Cited by 1,591 · see citing works

Alzheimer’s disease β-amyloid peptides are released in association with exosomes

Rajendran, L., Honsho, M., Zahn, T. R., Keller, P., Geiger, K. D., Verkade, P., & Simons, K. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603838103 · Cited by 1,343 · see citing works

Propagation of Tau Misfolding from the Outside to the Inside of a Cell

Frost, B., Jacks, R. L., & Diamond, M. I. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808759200 · Cited by 1,252 · see citing works

Microtubule Formation in vitro in Solutions Containing Low Calcium Concentrations

Weisenberg, R. C. (1972) · Science · doi:10.1126/science.177.4054.1104 · Cited by 1,216 · see citing works

Exfoliation of membrane ecto-enzymes in the form of micro-vesicles

Trams, E. G., Lauter, C. J., Salem, N., & Heine, U. (1981) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(81)90512-5 · Cited by 1,094 · see citing works

Role of tau protein in both physiological and pathological conditions

AVILA, J., LUCAS, J. J., PÉREZ, M., & HERNÁNDEZ, F. (2004) · Physiological Reviews · doi:10.1152/physrev.00024.2003 · Cited by 1,005 · see citing works

Roles of tau protein in health and disease

Guo, T., Noble, W., & Hanger, D. P. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1707-9 · Cited by 1,003 · see citing works

Exosome-associated tau is secreted in tauopathy models and is selectively phosphorylated in cerebrospinal fluid in early Alzheimer disease

Saman, S., Kim, W., Raya, M., Visnick, Y., Miro, S., Saman, S., Jackson, B., McKee, A. C., Alvarez, V. E., Lee, N. C. Y., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.277061 · Cited by 985 · see citing works

Identification of preclinical Alzheimer's disease by a profile of pathogenic proteins in neurally derived blood exosomes: A case‐control study

Fiandaca, M. S., Kapogiannis, D., Mapstone, M., Boxer, A., Eitan, E., Schwartz, J. B., Abner, E. L., Petersen, R. C., Federoff, H. J., Miller, B. L., et al. (2015) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2014.06.008 · Cited by 959 · see citing works

Heparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds

Holmes, B. B., DeVos, S. L., Kfoury, N., Li, M., Jacks, R., Yanamandra, K., Ouidja, M. O., Brodsky, F. M., Marasa, J., Bagchi, D. P., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1301440110 · Cited by 859 · see citing works

Tau protein function in living cells.

Drubin, D. G., & Kirschner, M. W. (1986) · The Journal of Cell Biology · doi:10.1083/jcb.103.6.2739 · Cited by 745 · see citing works

Astrocyte function from information processing to cognition and cognitive impairment

Santello, M., Toni, N., & Volterra, A. (2019) · Nature Neuroscience · doi:10.1038/s41593-018-0325-8 · Cited by 737 · see citing works

The release and trans-synaptic transmission of Tau via exosomes

Wang, Y., Balaji, V., Kaniyappan, S., Krüger, L., Irsen, S., Tepper, K., Chandupatla, R., Maetzler, W., Schneider, A., Mandelkow, E., et al. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0143-y · Cited by 674 · 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

Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain.

Brandt, R., Léger, J. G., & Lee, G. S. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.131.5.1327 · Cited by 624 · see citing works

Tau fragmentation, aggregation and clearance: the dual role of lysosomal processing

Wang, Y., Martinez-Vicente, M., Krüger, U., Kaushik, S., Wong, E., Mandelkow, E.-M., Cuervo, A. M., & Mandelkow, E. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp367 · Cited by 617 · see citing works

Anti-Tau Antibodies that Block Tau Aggregate Seeding In Vitro Markedly Decrease Pathology and Improve Cognition In Vivo

Yanamandra, K., Kfoury, N., Jiang, H., Mahan, T. E., Ma, S., Maloney, S. E., Wozniak, D. F., Diamond, M. I., & Holtzman, D. M. (2013) · Neuron · doi:10.1016/j.neuron.2013.07.046 · Cited by 574 · see citing works

Neuronal activity regulates extracellular tau in vivo

Yamada, K., Holth, J. K., Liao, F., Stewart, F. R., Mahan, T. E., Jiang, H., Cirrito, J. R., Patel, T. K., Hochgräfe, K., Mandelkow, E., et al. (2014) · The Journal of Experimental Medicine · doi:10.1084/jem.20131685 · Cited by 574 · see citing works

Trans-cellular Propagation of Tau Aggregation by Fibrillar Species

Kfoury, N., Holmes, B. B., Jiang, H., Holtzman, D. M., & Diamond, M. I. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.346072 · Cited by 552 · see citing works

Alzheimer’s disease pathology propagation by exosomes containing toxic amyloid-beta oligomers

Sardar Sinha, M., Ansell-Schultz, A., Civitelli, L., Hildesjö, C., Larsson, M., Lannfelt, L., Ingelsson, M., & Hallbeck, M. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1868-1 · Cited by 527 · see citing works

Quantification of tau phosphorylated at threonine 181 in human cerebrospinal fluid: a sandwich ELISA with a synthetic phosphopeptide for standardization

Vanmechelen, E., Vanderstichele, H., Davidsson, P., Kerschaver, E. V., Perre, B. V. D., Sjögren, M. J. C., Andreasen, N. C., & Blennow, K. (2000) · Neuroscience Letters · doi:10.1016/s0304-3940(00)01036-3 · Cited by 487 · see citing works

Tau association with synaptic vesicles causes presynaptic dysfunction

Zhou, L., McInnes, J., Wierda, K., Holt, M., Herrmann, A. G., Jackson, R. J., Wang, Y.-C., Swerts, J., Beyens, J., Miskiewicz, K., et al. (2017) · Nature Communications · doi:10.1038/ncomms15295 · Cited by 434 · see citing works

Heparan sulfate proteoglycan as a cell-surface endocytosis receptor

Christianson, H. C., & Belting, M. (2014) · Matrix Biology · doi:10.1016/j.matbio.2013.10.004 · Cited by 429 · see citing works

Exosomes: Mechanisms of Uptake

McKelvey, K. J., Powell, K., Ashton, A. W., Morris, J. M., & McCracken, S. A. (2015) · Journal of Circulating Biomarkers · doi:10.5772/61186 · Cited by 421 · see citing works

Nuclear Tau, a Key Player in Neuronal DNA Protection

Sultan, A., Nesslany, F., Violet, M., Bégard, S., Loyens, A., Talahari, S., Mansuroglu, Z., Marzin, D., Sergeant, N., Humez, S., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.199976 · Cited by 421 · see citing works

Exosomes as Intercellular Signaling Organelles Involved in Health and Disease: Basic Science and Clinical Applications

Corrado, C., Raimondo, S., Chiesi, A., Ciccia, F., de Leo, G., & Alessandro, R. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms14035338 · Cited by 395 · see citing works

The Exosome Secretory Pathway Transports Amyloid Precursor Protein Carboxyl-terminal Fragments from the Cell into the Brain Extracellular Space

Pérez‐González, R., Gauthier, S. A., Kumar, A. R., & Levy, E. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.404467 · Cited by 385 · see citing works

Reduced non–rapid eye movement sleep is associated with tau pathology in early Alzheimer’s disease

Lucey, B. P., McCullough, A. A., Landsness, E. C., Toedebusch, C. D., McLeland, J., Zaza, A., Fagan, A. M., McCue, L. M., Xiong, C., Morris, J. C., et al. (2019) · Science Translational Medicine · doi:10.1126/scitranslmed.aau6550 · Cited by 369 · see citing works

Tau degradation: The ubiquitin–proteasome system versus the autophagy-lysosome system

Lee, M. J., Lee, J. H., & Rubinsztein, D. C. (2013) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2013.03.001 · Cited by 364 · see citing works

<i>In Vivo</i> 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

Passive Immunization with Anti-Tau Antibodies in Two Transgenic Models

Chai, X., Wu, S., Murray, T. K., Kinley, R. D., Cella, C. V., Sims, H., Buckner, N., Hanmer, J. M., Davies, P., O’Neill, M. J., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.229633 · Cited by 346 · see citing works

Adhesion and signaling by B cell‐derived exosomes: the role of integrins

Clayton, A., Turkes, A., Dewitt, S., Steadman, R., Mason, M. D., & Hallett, M. B. (2004) · The FASEB Journal · doi:10.1096/fj.03-1094fje · Cited by 339 · see citing works

Tau Oligomers: Cytotoxicity, Propagation, and Mitochondrial Damage

Shafiei, S. S., Guerrero-Muñoz, M. J., & Castillo-Carranza, D. L. (2017) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00083 · Cited by 314 · see citing works

Passive immunization targeting pathological phospho‐tau protein in a mouse model reduces functional decline and clears tau aggregates from the brain

Boutajangout, A., Ingadottir, J., Davies, P., & Sigurdsson, E. M. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07337.x · Cited by 306 · see citing works

Value of CSF β-amyloid1–42 and tau as predictors of Alzheimer's disease in patients with mild cognitive impairment

Hampel, H., Teipel, S. J., Fuchsberger, T., Andreasen, N., Wiltfang, J., Otto, M., Shen, Y., Dodel, R., Du, Y., Farlow, M., et al. (2004) · Molecular Psychiatry · doi:10.1038/sj.mp.4001473 · Cited by 287 · see citing works

Extracellular Vesicles Isolated from the Brains of rTg4510 Mice Seed Tau Protein Aggregation in a Threshold-dependent Manner

Polanco, J. C., Scicluna, B. J., Hill, A. F., & Götz, J. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.709485 · Cited by 271 · see citing works

Loss of Bin1 Promotes the Propagation of Tau Pathology

Calafate, S., Flavin, W., Verstreken, P., & Moechars, D. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.09.063 · Cited by 265 · see citing works

Inhibition of γ‐secretase causes increased secretion of amyloid precursor protein C‐terminal fragments in association with exosomes

Sharples, R. A., Vella, L. J., Nisbet, R. M., Naylor, R., Perez, K. A., Barnham, K. J., Masters, C. L., & Hill, A. F. (2008) · The FASEB Journal · doi:10.1096/fj.07-9357com · Cited by 253 · see citing works

Unconventional Secretion Mediates the Trans-cellular Spreading of Tau

Katsinelos, T., Zeitler, M., Dimou, E., Karakatsani, A., Müller, H., Nachman, E., Steringer, J. P., de Almodóvar, C. R., Nickel, W., & Jahn, T. R. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.04.056 · Cited by 252 · see citing works

Synaptogyrin-3 Mediates Presynaptic Dysfunction Induced by Tau

McInnes, J., Wierda, K., Snellinx, A., Bounti, L., Wang, Y.-C., Stancu, I.-C., Apóstolo, N., Gevaert, K., Dewachter, I., Spires-Jones, T. L., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.01.022 · Cited by 242 · see citing works

Extracellular tau is toxic to neuronal cells

Gómez-Ramos, A., Díaz-Hernández, M., Cuadros, R., Hernández, F., & Avila, J. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.07.078 · Cited by 241 · 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

Absence of CX3CR1 impairs the internalization of Tau by microglia

Bolós, M., Llorens-Martín, M., Perea, J. R., Jurado-Arjona, J., Rábano, A., Hernández, F., & Avila, J. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0200-1 · Cited by 231 · see citing works

Tau clearance mechanisms and their possible role in the pathogenesis of Alzheimer disease.

Chesser, A. S., Pritchard, S. M., & Johnson, G. V. W. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00122 · Cited by 219 · see citing works

Declining levels of functionally specialized synaptic proteins in plasma neuronal exosomes with progression of Alzheimer's disease

Goetzl, E. J., Abner, E. L., Jicha, G. A., Kapogiannis, D., & Schwartz, J. B. (2018) · The FASEB Journal · doi:10.1096/fj.201700731r · Cited by 219 · see citing works

Ectosomes: A New Mechanism for Non-Exosomal Secretion of Tau Protein

Dujardin, S., Bégard, S., Caillierez, R., Lachaud, C., Delattre, L., Carrier, S., Loyens, A., Galas, M., Bousset, L., Melki, R., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0100760 · Cited by 215 · see citing works

Atypical, non-standard functions of the microtubule associated Tau protein

Sotiropoulos, I., Galas, M., Silva, J. M., Skoulakis, E. M. C., Wegmann, S., Maina, M. B., Blum, D. L., Sayas, C. L., Mandelkow, E., Mandelkow�, E., et al. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0489-6 · Cited by 211 · see citing works

CNS tau efflux via exosomes is likely increased in Parkinson's disease but not in Alzheimer's disease

Shi, M., Kovac, A., Korff, A., Cook, T. J., Ginghina, C., Bullock, K. M., Yang, L., Stewart, T., Zheng, D., Aro, P., et al. (2016) · Alzheimer's &amp; Dementia · doi:10.1016/j.jalz.2016.04.003 · Cited by 206 · see citing works

The expression and distribution of the microtubule-associated proteins tau and microtubule-associated protein 2 in hippocampal neurons in the rat in situ and in cell culture

Dotti, C. G., Banker, G., & Binder, L. (1987) · Neuroscience · doi:10.1016/0306-4522(87)90276-4 · Cited by 199 · see citing works

Detection of Aggregation-Competent Tau in Neuron-Derived Extracellular Vesicles

Guix, F. X., Corbett, G. T., Cha, D., Mustapić, M., Liu, W., Mengel, D., Chen, Z., Aïkawa, E., Young‐Pearse, T. L., Kapogiannis, D., et al. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19030663 · Cited by 182 · see citing works

Correlation of cerebrospinal fluid levels of Tau protein phosphorylated at threonine 231 with rates of hippocampal atrophy in Alzheimer disease

Hampel, H., Bürger, K., Pruessner, J. C., Zinkowski, R., DeBernardis, J., Kerkman, D., Leinsinger, G., Evans, A. C., Davies, P., Möller, H.-J., et al. (2005) · Archives of Neurology · doi:10.1001/archneur.62.5.770 · Cited by 175 · cited 2× · see citing works

Extracellular Tau Levels Are Influenced by Variability in Tau That Is Associated with Tauopathies

Karch, C. M. M., Jeng, A. T., & Goate, A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.380642 · Cited by 171 · see citing works

C-Terminally Truncated Forms of Tau, But Not Full-Length Tau or Its C-Terminal Fragments, Are Released from Neurons Independently of Cell Death

Kanmert, D., Cantlon, A., Muratore, C., Jin, M., O’Malley, T. T., Lee, G. S., Young‐Pearse, T. L., Selkoe, D. J., & Walsh, D. M. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.0387-15.2015 · Cited by 159 · see citing works

Proteostasis of tau. Tau overexpression results in its secretion via membrane vesicles

Simón, D., García‐García, E., Royo, F., Falcón‐Pérez, J. M., & Ávila, J. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.11.022 · 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

Hyperphosphorylation and Cleavage at D421 Enhance Tau Secretion

Plouffe, V., Mohamed, N., Rivest‐McGraw, J., Bertrand, J., Lauzon, M., & Leclerc, N. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0036873 · Cited by 146 · see citing works

Tau Dephosphorylation at Tau-1 Site Correlates with its Association to Cell Membrane

Arrasate, M., Pérez, M., & Ávila, J. (2000) · Neurochemical Research · doi:10.1023/a:1007583214722 · Cited by 116 · see citing works

Tau Accumulation in Clinically Normal Older Adults Is Associated with Hippocampal Hyperactivity

Huijbers, W., Schultz, A. P., Papp, K. V., LaPoint, M. R., Hanseeuw, B. J., Chhatwal, J. P., Hedden, T., Johnson, K. A., & Sperling, R. A. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.1397-18.2018 · Cited by 113 · see citing works

Interneuronal Transfer of Human Tau Between Lamprey Central Neurons in situ

Kim, W., Lee, S., Jung, C., Ahmed, A., Lee, G. S., & Hall, G. F. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1273 · Cited by 107 · see citing works

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 106 · see citing works

αB-Crystallin Is Found in Detergent-resistant Membrane Microdomains and Is Secreted via Exosomes from Human Retinal Pigment Epithelial Cells

Gangalum, R. K., Atanasov, I. C., Zhou, Z. H., & Bhat, S. P. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.160135 · Cited by 105 · see citing works

Tracking of Alzheimer's disease progression with cerebrospinal fluid tau protein phosphorylated at threonine 231

Hampel, H. J., Büerger, K., Kohnken, R. E., Teipel, S. J., Zinkowski, R. P., Moeller, H., Rapoport, S. I., & Davies, P. (2001) · Annals of Neurology · doi:10.1002/ana.111 · Cited by 102 · see citing works

Tau passive immunization blocks seeding and spread of Alzheimer hyperphosphorylated Tau-induced pathology in 3 × Tg-AD mice

Dai, C.-L., Hu, W., Tung, Y. C., Liu, F., Gong, C.-X., & Iqbal, K. (2018) · Alzheimer's Research &amp; Therapy · doi:10.1186/s13195-018-0341-7 · Cited by 99 · see citing works

Extracellular Vesicles Containing P301L Mutant Tau Accelerate Pathological Tau Phosphorylation and Oligomer Formation but Do Not Seed Mature Neurofibrillary Tangles in ALZ17 Mice

Baker, S., Polanco, J. C., & Götz, J. (2016) · Journal of Alzheimer's Disease · doi:10.3233/jad-160371 · Cited by 98 · see citing works

New Features about Tau Function and Dysfunction

Medina, M., Hernández, F., & Ávila, J. (2016) · Biomolecules · doi:10.3390/biom6020021 · Cited by 92 · see citing works

Endolysosomal degradation of Tau and its role in glucocorticoid-driven hippocampal malfunction

Vaz-Silva, J., Gomes, P. A., Jin, Q., Zhu, M., Zhuravleva, V., Quintremil, S., Meira, T., Silva, J., Dioli, C., Soares-Cunha, C., et al. (2018) · bioRxiv · doi:10.15252/embj.201899084 · Cited by 92 · see citing works

Extracellular Tau and Its Potential Role in the Propagation of Tau Pathology

Yamada, K. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00667 · Cited by 84 · see citing works

Exosomal biomarkers in Down syndrome and Alzheimer's disease

Hamlett, E. D., Ledreux, A., Potter, H., Chial, H. J., Patterson, D., Espinosa, J. M., Bettcher, B. M., & Granholm, A. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.08.028 · Cited by 78 · see citing works

Acellular approaches for regenerative medicine: on the verge of clinical trials with extracellular membrane vesicles?

Fuster-Matanzo, A., Gessler, F. A., Leonardi, T., Iraci, N., & Pluchino, S. (2015) · Stem Cell Research & Therapy · doi:10.1186/s13287-015-0232-9 · Cited by 56 · see citing works

Dephosphorylated rather than hyperphosphorylated Tau triggers a pro-inflammatory profile in microglia through the p38 MAPK pathway

Perea, J. R., Ávila, J., & Bolós, M. (2018) · Experimental Neurology · doi:10.1016/j.expneurol.2018.08.007 · Cited by 54 · see citing works

Growth Hormone-Releasing Hormone Modulation of Neuronal Exosome Biomarkers in Mild Cognitive Impairment

Winston, C. N., Goetzl, E. J., Baker, L. D., Vitiello, M. V., & Rissman, R. A. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180302 · Cited by 54 · see citing works

Tau secretion is correlated to an increase of Golgi dynamics

Mohamed, N., Desjardins, A., & Leclerc, N. M. (2017) · PLoS ONE · doi:10.1371/journal.pone.0178288 · Cited by 50 · see citing works

Tau Protein Role in Sleep-Wake Cycle

Cantero, J. L., Hita-Yáñez, E., Moreno‐López, B., Portillo, F., Rubio, A., & Ávila, J. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100285 · Cited by 48 · see citing works

Adenosine A 1 receptor antagonist rolofylline alleviates axonopathy caused by human Tau ΔK280

Dennissen, F. J. A., Anglada‐Huguet, M., Sydow, A., Mandelkow�, E., & Mandelkow, E. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1603119113 · Cited by 46 · see citing works

Binding of microtubule protein to DNA and chromatin: possibility of simultaneous linkage of microtubule to nucleic acid and assembly of the microtubule structure

Villasanté, A., Corces, V. G., Manso-Martínez, R., & Ávila, J. (1981) · Nucleic Acids Research · doi:10.1093/nar/9.4.895 · Cited by 40 · see citing works

Role of tau N-terminal motif in the secretion of human tau by End Binding proteins

Sayas, C. L., Medina, M., Cuadros, R., Ollà, I., García, E., Pérez, M., Ferrer, I., Hernández, F., & Ávila, J. (2019) · PLoS ONE · doi:10.1371/journal.pone.0210864 · Cited by 28 · see citing works

Secretion of full-length tau or tau fragments in a cell culture model

Pérez, M., Cuadros, R., Hernández, F., & Ávila, J. (2016) · Neuroscience Letters · doi:10.1016/j.neulet.2016.09.026 · Cited by 25 · see citing works

Tracking of Alzheimer's disease progression with cerebrospinal fluid tau protein phosphorylated at threonine 231

Hampel, H. J., Büerger, K., Kohnken, R. E., et al. (2001) · Annals of Neurology · doi:10.1002/ana.111.abs · Cited by 14 · see citing works

eFAST for the diagnosis of a perioperative complication during percutaneous nephrolithotomy

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Acetylated tau inhibits chaperone-mediated autophagy and promotes tau pathology propagation in mice

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Plasma extracellular vesicle tau and TDP-43 as diagnostic biomarkers in FTD and ALS

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From the prion-like propagation hypothesis to therapeutic strategies of anti-tau immunotherapy

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TNF Production and Release from Microglia via Extracellular Vesicles: Impact on Brain Functions

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Oligomerization and Conformational Change Turn Monomeric β-Amyloid and Tau Proteins Toxic: Their Role in Alzheimer’s Pathogenesis

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Exosomes: Their Role in Pathogenesis, Diagnosis and Treatment of Diseases

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Extracellular Vesicles in neural cell interaction and CNS homeostasis

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Extracellular vesicles and intercellular communication in the central nervous system

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Brain Derived Exosomes Are a Double-Edged Sword in Alzheimer’s Disease

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A new paradigm for diagnosis of neurodegenerative diseases: peripheral exosomes of brain origin

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The Roles of Exosomal Proteins: Classification, Function, and Applications

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Exosome Production Is Key to Neuronal Endosomal Pathway Integrity in Neurodegenerative Diseases

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A critical appraisal of tau‐targeting therapies for primary and secondary tauopathies

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Gut Microbiota Extracellular Vesicles as Signaling Molecules Mediating Host-Microbiota Communications

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α– Linolenic acid modulates phagocytosis and endosomal pathways of extracellular Tau in microglia

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Cell Type-Specific Extracellular Vesicles and Their Impact on Health and Disease

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Tau-targeting therapy in Alzheimer’s disease: Critical advances and future opportunities

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Function of exosomes in neurological disorders and brain tumors

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Extracellular microvesicles promote microglia‐mediated pro‐inflammatory responses to ethanol

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Emerging therapeutic role of gut microbial extracellular vesicles in neurological disorders

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Tetrandrine ameliorates cognitive deficits and mitigates tau aggregation in cell and animal models of tauopathies

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Early- and Late-Onset Alzheimer’s Disease: Two Sides of the Same Coin?

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Brain Exosomes: Friend or Foe in Alzheimer’s Disease?

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Dual role of brain-derived extracellular vesicles in dementia-related neurodegenerative disorders: cargo of disease spreading signals and diagnostic-therapeutic molecules

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Disentangling tau: One protein, many therapeutic approaches

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The Sulfation Code of Tauopathies: Heparan Sulfate Proteoglycans in the Prion Like Spread of Tau Pathology

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Extracellular vesicles: Major actors of heterogeneity in tau spreading among human tauopathies

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Mesenchymal and Neural Stem Cell-Derived Exosomes in Treating Alzheimer’s Disease

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RNA and Protein Delivery by Cell‐Secreted and Bioengineered Extracellular Vesicles

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Role of brain extracellular vesicles in air pollution-related cognitive impairment and neurodegeneration

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The propagation mechanisms of extracellular tau in Alzheimer’s disease

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Alzheimer's disease brain‐derived extracellular vesicles reveal altered synapse‐related proteome and induce cognitive impairment in mice

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Syntenin-knock out reduces exosome turnover and viral transduction

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Extracellular Vesicles From 3xTg-AD Mouse and Alzheimer’s Disease Patient Astrocytes Impair Neuroglial and Vascular Components

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Increased exosome secretion in neurons aging in vitro by NPC1-mediated endosomal cholesterol buildup

Guix, F. X., Marrero, A. D., Casadomé‐Perales, Á., Palomares-Pérez, I., Castillo, I. L. D., Miguel, V., Goedeke, L., Martín, M. G., Lamas, S., Peinado, H., et al. (2021) · Life Science Alliance · doi:10.26508/lsa.202101055 · Cited by 39 · see citing works

Dual Neutral Sphingomyelinase-2/Acetylcholinesterase Inhibitors for the Treatment of Alzheimer’s Disease

Bilousova, T. V., Simmons, B. J., Knapp, R. R., Elias, C. J., Campagna, J. J., Melnik, M., Chandra, S., Focht, S., Zhu, C., Vadivel, K., et al. (2020) · ACS Chemical Biology · doi:10.1021/acschembio.0c00311 · Cited by 32 · see citing works

The Impact of the Cellular Environment and Aging on Modeling Alzheimer's Disease in 3D Cell Culture Models

Hebisch, M., Klostermeier, S., Wolf, K., Boccaccini, A. R., Wolf, S. E., Tanzi, R. E., & Kim, D. Y. (2023) · Advanced Science · doi:10.1002/advs.202205037 · Cited by 29 · see citing works

Differential Profile of Systemic Extracellular Vesicles From Sporadic and Familial Alzheimer’s Disease Leads to Neuroglial and Endothelial Cell Degeneration

Villar-Vesga, J., Henao-Restrepo, J., Voshart, D. C., Aguillon, D., Villegas, A., Castaño, D., Arias-Londoño, J. D., Zuhorn, I. S., Ribovski, L., Barazzuol, L., et al. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.587989 · Cited by 29 · see citing works

Exosome nanovesicles: biomarkers and new strategies for treatment of human diseases

Xu, C. Y., Jiang, C., Li, Z., Gao, H., Xian, J., Guo, W., He, D., Peng, X., Zhou, D., & Li, D. (2024) · MedComm · doi:10.1002/mco2.660 · Cited by 28 · see citing works

LC3-associated endocytosis facilitates extracellular Tau aggregate internalization and degradation in microglia

Chidambaram, H., & Chinnathambi, S. (2025) · Brain Network Disorders · doi:10.1016/j.bnd.2024.12.005 · Cited by 25 · see citing works

The Chemokine-like Receptor 1 Deficiency Improves Cognitive Deficits of AD Mice and Attenuates Tau Hyperphosphorylation via Regulating Tau Seeding

Zhang, H., Lin, A., Gong, P., Chen, Y., Ye, R. D., Qian, F., Zhang, Y., & Yu, Y. (2020) · The Journal of Neuroscience · doi:10.1523/jneurosci.0455-20.2020 · Cited by 24 · see citing works

Heparan Sulfate Proteoglycans in Tauopathy

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Cerebrospinal Fluid EV Concentration and Size Are Altered in Alzheimer’s Disease and Dementia with Lewy Bodies

Longobardi, A., Nicsanu, R., Bellini, S., Squitti, R., Catania, M., Tiraboschi, P., Saraceno, C., Ferrari, C., Zanardini, R., Binetti, G. G., et al. (2022) · Cells · doi:10.3390/cells11030462 · Cited by 22 · see citing works

Biomarker Organization in Circulating Extracellular Vesicles: New Applications in Detecting Neurodegenerative Diseases

Lim, C. Z. J., Natalia, A., Sundah, N. R., & Shao, H. (2020) · Advanced Biosystems · doi:10.1002/adbi.201900309 · Cited by 22 · see citing works

Neuron-derived extracellular vesicle-based diagnostics for Tau and Alzheimer’s disease

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Alzheimer’s disease is an inherent, natural part of human brain aging: an integrated perspective

Ferrer, I. (2022) · Free Neuropathology · doi:10.17879/freeneuropathology-2022-3806 · Cited by 21 · see citing works

Nanomaterials-Based Exosomes for the Diagnostics and Drug Deliveries of Central Nervous System Diseases

Haizan, I., Park, D. H., Choi, M. Y., Lee, H.-R., & Choi, J. (2023) · BioChip Journal · doi:10.1007/s13206-023-00112-4 · Cited by 21 · see citing works

A noncanonical function of SKP1 regulates the switch between autophagy and unconventional secretion

Li, J., Krause, G. J., Gui, Q., Kaushik, S., Róna, G., Zhang, Q., Liang, F., Dhabaria, A., Anerillas, C., Martindale, J. L., et al. (2023) · Science Advances · doi:10.1126/sciadv.adh1134 · Cited by 21 · see citing works

Challenges associated with using extracellular vesicles as biomarkers in neurodegenerative disease

Couch, Y. (2023) · Expert Review of Molecular Diagnostics · doi:10.1080/14737159.2023.2277373 · Cited by 21 · see citing works

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 22 · see citing works

Switching Roles: Beneficial Effects of Adipose Tissue-Derived Mesenchymal Stem Cells on Microglia and Their Implication in Neurodegenerative Diseases

Sánchez-Castillo, A. I., Sepúlveda, M. R., Marín‐Teva, J. L., Cuadros, M. Á., Martín‐Oliva, D., González‐Rey, E., Delgado, M., & Neubrand, V. E. (2022) · Biomolecules · doi:10.3390/biom12020219 · Cited by 21 · see citing works

A Crucial Role for the Protein Quality Control System in Motor Neuron Diseases

Cristofani, R., Crippa, V., Cicardi, M. E., Tedesco, B., Ferrari, V., Chierichetti, M., Casarotto, E., Piccolella, M., Messi, E., Galbiati, M., et al. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00191 · Cited by 22 · see citing works

New progress on the role and mechanism of tau protein in Alzheimer's disease and depression

Wang, Y., Zhou, J., Zhou, Q., & Wang, H. (2025) · Frontiers in Neurology · doi:10.3389/fneur.2025.1551273 · Cited by 19 · see citing works

Numb regulates Tau levels and prevents neurodegeneration in tauopathy mouse models

Lacomme, M., Hales, S. C., Brown, T. W., Stevanovic, K., Jolicoeur, C., Cai, J., Bois, T., Desrosiers, M., Dalkara, D., & Cayouette, M. (2022) · Science Advances · doi:10.1126/sciadv.abm4295 · Cited by 18 · see citing works

A review on gut microbiota and miRNA crosstalk: implications for Alzheimer’s disease

Ayyanar, M. P., & Vijayan, M. (2024) · GeroScience · doi:10.1007/s11357-024-01432-5 · Cited by 23 · see citing works

Prion-Like Propagation Mechanisms in Tauopathies and Traumatic Brain Injury: Challenges and Prospects

Alyenbaawi, H., Allison, W. T., & Mok, S. (2020) · Biomolecules · doi:10.3390/biom10111487 · Cited by 18 · see citing works

Amyloid pathology reduces ELP3 expression and tRNA modifications leading to impaired proteostasis

Pereira, M., Ribeiro, D. R., Berg, M., Tsai, A. P., Dong, C., Nho, K. T., Kaiser, S., Moutinho, M., & Soares, A. R. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2023.166857 · Cited by 16 · see citing works

Arc mediates intercellular tau transmission via extracellular vesicles

Tyagi, M., de Hoog, E., Grega, M., Sullivan, K. R., Walker, A., Chadha, R., Northrop, A., Fábián, B., Hummer, G., Fuxreiter, M., et al. (2026) · Cell · doi:10.1016/j.cell.2026.06.008 · Cited by 19 · see citing works

Astrocytes and Microglia in Alzheimer's Disease: Friends, Foes, or Both?

Sharma, A., Parekh, B. K., Patil, V., Renuka Jyothi, S., Nayak, P. P., Janney, J. B., Singh, G., & Al-Hasnaawei, S. (2025) · Developmental Neurobiology · doi:10.1002/dneu.23015 · Cited by 17 · see citing works

Tau Protein Biosensors in the Diagnosis of Neurodegenerative Diseases

Sadeghzadeh, J., Shahabi, P., Farhoudi, M., Kalan, A. E., Mobed, A., & Shahpasand, K. (2022) · Advanced Pharmaceutical Bulletin · doi:10.34172/apb.2023.061 · Cited by 15 · see citing works

Resolution of MoS 2 Nanosheets‐Induced Pulmonary Inflammation Driven by Nanoscale Intracellular Transformation and Extracellular‐Vesicle Shuttles

Peña, N. O., Cherukula, K., Even, B., Ji, D., Razafindrakoto, S., Peng, S., Silva, A., Ménard‐Moyon, C., Hillaireau, H., Bianco, A., et al. (2023) · Advanced Materials · doi:10.1002/adma.202209615 · Cited by 15 · see citing works

Clonal mesenchymal stem cell-derived extracellular vesicles improve mouse model of weight drop-induced traumatic brain injury through reducing cistauosis and apoptosis

Amini, A., Shekari, F., Kashani, S. A., Eslami, N., Nazari, A., Tofigh, N., Shahpasand, K., Javar, H. A., & Baharvand, H. (2023) · Experimental Neurology · doi:10.1016/j.expneurol.2023.114467 · Cited by 15 · see citing works

Complications of COVID-19 on the Central Nervous System: Mechanisms and Potential Treatment for Easing Long COVID

Wei, Z. D., Liang, K., & Shetty, A. K. (2023) · Aging and Disease · doi:10.14336/ad.2023.0312 · Cited by 16 · see citing works

Extracellular Vesicles as Mediators of Intercellular Communication: Implications for Drug Discovery and Targeted Therapies

Mimi, M. A., Sohag, S. M., Toma, S. N., & Hasan, M. M. (2025) · Future Pharmacology · doi:10.3390/futurepharmacol5030048 · Cited by 14 · see citing works

CDK5 Targeting as a Therapy for Recovering Neurovascular Unit Integrity in Alzheimer’s Disease

Posada-Duque, R. A., & Cardona-Gómez, G. P. (2021) · Journal of Alzheimer's Disease · doi:10.3233/jad-200730 · Cited by 14 · see citing works

FGFR3 drives Aβ-induced tau uptake

Kim, D. K., Suh, K. Y., Park, J., Lee, S., Han, J., Chang, S., Kim, Y., & Mook‐Jung, I. (2024) · Experimental & Molecular Medicine · doi:10.1038/s12276-024-01274-3 · Cited by 13 · see citing works

Emerging evidence for dysregulated proteome cargoes of tau-propagating extracellular vesicles driven by familial mutations of tau and presenilin

HOOK, V. Y. H., Podvin, S., Mosier, C., Boyarko, B., Demsey, L. L., Stringer, H., & Rissman, R. A. (2023) · Extracellular Vesicles and Circulating Nucleic Acids · doi:10.20517/evcna.2023.44 · Cited by 12 · see citing works

α-Linolenic acid modulates phagocytosis of extracellular Tau and induces microglial migrationPreprint

Desale, S. E., & Chinnathambi, S. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.04.15.042143 · Cited by 12 · see citing works

Advancements in extracellular vesicle therapy for neurodegenerative diseases

Hu, N., Chen, L., Hu, G., & Ma, R. (2025) · Exploration of Neuroprotective Therapy · doi:10.37349/ent.2025.1004104 · Cited by 11 · see citing works

Potential of Microfluidics and Lab-on-Chip Platforms to Improve Understanding of “prion-like” Protein Assembly and Behavior

del Rı́o, J. A., & Ferrer, I. (2020) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2020.570692 · Cited by 8 · see citing works

Recent Progress in the Application of Tau Protein Biosensors for Diagnosis of Neurodegenerative Diseases

Nazir, S., & Iqbal, R. A. (2024) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-024-04960-0 · Cited by 8 · see citing works

Stratification of brain-derived extracellular vesicles of Alzheimer’s disease patients indicates a unique proteomic content and a higher seeding capacity of small extracellular vesicles

Oosterlynck, M., Leroux, É., Namasivayam, B., Bouillet, T., Caillierez, R., Loyens, A., Mazur, D., Perbet, R., Lefebvre, C., Aboulouard, S., et al. (2025) · Translational Neurodegeneration · doi:10.1186/s40035-025-00519-z · Cited by 10 · see citing works

The Adult Neurogenesis Theory of Alzheimer’s Disease

Abbate, C. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-221279 · Cited by 8 · see citing works

TMEM16F exacerbates tau pathology and mediates phosphatidylserine exposure in phospho-tau-burdened neurons

Zubia, M. V., Yong, A. J. H., Holtz, K. M., Huang, E. J., Jan, Y. N., & Jan, L. Y. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2311831121 · Cited by 6 · see citing works

Effect of Phosphorylated Tau on Cortical Pyramidal Neuron Morphology during Hibernation

Regalado-Reyes, M., Benavides‐Piccione, R., Fernaud-Espinosa, I., DeFelipe, J., & León‐Espinosa, G. (2020) · Cerebral Cortex Communications · doi:10.1093/texcom/tgaa018 · Cited by 5 · see citing works

A complete sojourn on exosomes: Potential diagnostic and therapeutic agents

Garg, S., Garg, G., Patel, P., Kumar, M., Thakur, S., Sharma, N., & Kurmi, B. D. (2024) · Pathology - Research and Practice · doi:10.1016/j.prp.2024.155674 · Cited by 5 · see citing works

Plasma extracellular vesicles from <i>APOE3</i> Christchurch carriers display a protective phenotype in early stages of autosomal dominant Alzheimer's disease

Pineda‐Lopez, L., Aguillon, D., Villar‐Vesga, J., Valderrama‐Carmona, P., Guerrero, A., Upreti, A., Arevalo‐Alquichire, S., Correa, L., Mendez‐Castellanos, K., Castaño, D., et al. (2026) · Alzheimer's &amp; Dementia · doi:10.1002/alz.71148 · Cited by 4 · see citing works

Mapping the current trends and hotspots of extracellular vesicles in Alzheimer's disease: a bibliometric analysis

Xing, X., Liu, H., Zhang, M., & Li, Y. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1485750 · Cited by 4 · see citing works

Tau Seeds in Extracellular Vesicles Induce Tau Accumulation in Degradative Organelles of Cells

Pedrioli, G., Barberis, M., Magrin, C., Morone, D., Piovesana, E., Senesi, G., Sola, M., Papin, S., & Paganetti, P. (2021) · DNA and Cell Biology · doi:10.1089/dna.2021.0485 · Cited by 4 · see citing works

Extracellular Vesicles Hijack the Autophagic Pathway to Induce Tau Accumulation in EndolysosomesPreprint

Pedrioli, G., Barberis, M., Molinari, M., Morone, D., Papin, S., & Paganetti, P. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.27.118323 · Cited by 4 · see citing works

Tau seeding activity in Alzheimer's disease: Characteristics, factors, and applications

Liu, Y., Chen, Y., Chen, Z., Wan, H., & Wu, C. (2025) · Journal of Alzheimer s Disease · doi:10.1177/13872877251378772 · Cited by 3 · see citing works

Les vésicules extracellulaires

Leroux, É., Perbet, R., Buée, L., & Colin, M. (2021) · médecine/sciences · doi:10.1051/medsci/2021205 · Cited by 3 · see citing works

Tau Pathology in Neurodegenerative Diseases

Vogels, T., & Hromádka, T. (2021) · Neuromethods · doi:10.1007/978-1-0716-1712-0_4 · Cited by 2 · see citing works

Phosphorylated Tau at T181 accumulates in the serum of hibernating Syrian hamsters and rapidly disappears after arousal

León‐Espinosa, G., Murillo, A. M., Turégano-López, M., DeFelipe, J., & Holgado, M. (2024) · Scientific Reports · doi:10.1038/s41598-024-71481-5 · Cited by 2 · see citing works

Inducing aggresome and stable tau aggregation in Neuro2a cells with an optogenetic tool

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Tau Pathology in Alzheimer's Disease: Bridging Molecular Mechanisms and Targeted Therapies

Dahiya, M., Yadav, M., Kumar, A., & Goyal, C. (2025) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/0118715273376581250626003322 · Cited by 1 · see citing works

Co‐localization of tau and TDP ‐43 after extracellular vesicle delivery to cells

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Outer Membrane Vesicles as Systems-Level Drivers of Neuroinflammation, Metabolic Dysfunction, and Proteinopathy in Alzheimer’s Disease

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Exosome Imaging

Hwang, D. W., Suh, M., & Lee, D. S. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-816386-3.00054-5 · Cited by 1 · see citing works

Wherefore Art Tau? Functional importance of site-specific tau phosphorylation in diverse subcellular domains

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Stratification of Brain-Derived Extracellular Vesicles of Alzheimer’s Disease Patients Indicates a Unique Proteomic Content and a Higher Seeding Capacity of Small Extracellular VesiclesPreprint

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Parkinson’s disease and exosomes: from pathogenesis to diagnosis and treatment

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Amyloid pathology reduces ELP3 expression and tRNA modifications leading to impaired proteostasis in Alzheimer’s disease modelsPreprint

Pereira, M., Ribeiro, D. R., Berg, M., Tsai, A. P., Nho, K. T., Kaiser, S., Moutinho, M., & Soares, A. R. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.05.02.538928

Exosomes and extracellular vesicles for neurodegenerative diseases

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Emerging evidence for dysregulated proteome cargoes of tau-propagating extracellular vesicles driven by familial mutations of tau and presenilin

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The role of exosomes in the pathogenesis of Alzheimer’ disease

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Tissue Science 2019: Neuronal exosome-derived human tau toxicity on recipient cells: Shauna H. Yuan- University of California, USA

Yuan, S. H. (2020)

The release and trans-synaptic transmission of Tau via exosomes

Wang, Y., Balaji, V., Kaniyappan, S., Krüger, L., Irsen, S., Tepper, K., Chandupatla, R., Maetzler, W., Schneider, A., Mandelkow, E., et al. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0143-y · Cited by 674 · see citing works

Tau Secretion

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