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

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 2,410

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

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

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

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

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

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

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

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

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

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

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

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

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 766

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

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

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 663

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

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

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 606

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

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

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

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

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 443

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

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

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

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

Corrado, C., Raimondo, S., Chiesi, A., Ciccia, F., Leo, G. D., & Alessandro, R. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms14035338 · Cited by 402

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 386

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

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 363

In Vivo Microdialysis Reveals Age-Dependent Decrease of Brain Interstitial Fluid Tau Levels in P301S Human Tau Transgenic Mice

Yamada, K., Cirrito, J. R., Stewart, F. R., Jiang, H., Finn, M. B., Holmes, B. B., Binder, L. I., Mandelkow, E.-M., Diamond, M. I., Lee, V. M.-Y., et al. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.2569-11.2011 · Cited by 351

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

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 336

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

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

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

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 280

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 274

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

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

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 245

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 242

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

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

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

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 221

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

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

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 & Dementia · doi:10.1016/j.jalz.2016.04.003 · Cited by 206

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

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 186

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 185

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×

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 169

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 166

Tissue-nonspecific Alkaline Phosphatase Promotes the Neurotoxicity Effect of Extracellular Tau

Díaz-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 163

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 159

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 130

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 118

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

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

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

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

Vaz‐Silva, J., Gomes, P., Jin, Q., Zhu, M., Zhuravleva, V., Quintremil, S., Meira, T., Silva, J., Dioli, C., Soares‐Cunha, C., et al. (2018) · The EMBO Journal · doi:10.15252/embj.201899084 · Cited by 104

New Features about Tau Function and Dysfunction

Medina, M., Hernández, F., & Ávila, J. (2016) · Biomolecules · doi:10.3390/biom6020021 · Cited by 103

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

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 & Therapy · doi:10.1186/s13195-018-0341-7 · Cited by 99

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

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 86

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 80

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 57

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 55

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

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

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 52

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 45

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

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

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 27

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

eFAST for the diagnosis of a perioperative complication during percutaneous nephrolithotomy

Sharma, A., Bhattarai, P. R., & Sharma, A. (2018) · The Ultrasound Journal · doi:10.1186/s13089-018-0088-1 · Cited by 10

Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation

Chen, Y., & Yu, Y. (2023) · Journal of Neuroinflammation · doi:10.1186/s12974-023-02853-3 · Cited by 516

The different autophagy degradation pathways and neurodegeneration

Fleming, A., Bourdenx, M., Fujimaki, M., Karabiyik, C., Krause, G. J., Lopez, A., Martín‐Segura, A., Puri, C., Scrivo, A., Skidmore, J., et al. (2022) · Neuron · doi:10.1016/j.neuron.2022.01.017 · Cited by 500

Astrocyte-derived extracellular vesicles: Neuroreparative properties and role in the pathogenesis of neurodegenerative disorders

Upadhya, R., Zingg, W., Shetty, S., & Shetty, A. K. (2020) · Journal of Controlled Release · doi:10.1016/j.jconrel.2020.04.017 · Cited by 282

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

Caballero, B., Bourdenx, M., Luengo, E., Diaz, A., Sohn, P. D., Chen, X., Wang, C., Juste, Y. R., Wegmann, S., Patel, B., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-22501-9 · Cited by 223

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