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Untitled work

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Advances in developing novel therapeutic strategies for Alzheimer’s disease

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Passive Immunization with Tau Oligomer Monoclonal Antibody Reverses Tauopathy Phenotypes without Affecting Hyperphosphorylated Neurofibrillary Tangles

Castillo-Carranza, D. L., Sengupta, U., Guerrero-Muñoz, M. J., Lasagna-Reeves, C. A., Gerson, J. E., Singh, G., Estes, D. M., Barrett, A. D. T., Dineley, K. T., Jackson, G. R., et al. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.3192-13.2014 · Cited by 278 · see citing works

Extracellular Tau Oligomers Produce An Immediate Impairment of LTP and Memory

Fà, M., Puzzo, D., Piacentini, R., Staniszewski, A., Zhang, H., Baltrons, M. A., Puma, D. D. L., Chatterjee, I., Li, J., Saeed, F., et al. (2016) · Scientific Reports · doi:10.1038/srep19393 · Cited by 274 · 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

The Emerging Link between O-GlcNAc and Alzheimer Disease

Zhu, Y., Shan, X., Yuzwa, S. A., & Vocadlo, D. J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.r114.601351 · Cited by 267 · 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

Neuron-to-neuron wild-type Tau protein transfer through a trans-synaptic mechanism: relevance to sporadic tauopathies

Dujardin, S., Lécolle, K., Caillierez, R., Bégard, S., Zommer, N., Lachaud, C., Carrier, S., Dufour, N., Aurégan, G., Winderickx, J., et al. (2014) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-2-14 · Cited by 259 · see citing works

Mechanisms of Cell-to-Cell Transmission of Pathological Tau: A Review

Gibbons, G. S., Lee, V. M. Y., & Trojanowski, J. Q. (2019) · JAMA Neurology · doi:10.1001/jamaneurol.2018.2505 · Cited by 257 · see citing works

Synaptic Contacts Enhance Cell-to-Cell Tau Pathology Propagation

Calafate, S., Buist, A., Miśkiewicz, K., Vijayan, V. A., Daneels, G., Strooper, B. D., de Wit, J., Verstreken, P., & Moechars, D. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.04.043 · Cited by 257 · see citing works

TFEB enhances astroglial uptake of extracellular tau species and reduces tau spreading

Martini-Stoica, H., Cole, A. L., Swartzlander, D. B., Chen, F., Wan, Y.-W., Bajaj, L., Bader, D. A., Lee, V. M. Y., Trojanowski, J. Q., Liu, Z., et al. (2018) · Journal of Experimental Medicine · doi:10.1084/jem.20172158 · Cited by 253 · see citing works

Conformation Determines the Seeding Potencies of Native and Recombinant Tau Aggregates

Falcon, B., Cavallini, A., Angers, R. C., Glover, S. J., Murray, T. K., Barnham, L., Jackson, S., O'Neill, M. J., Isaacs, A. M., Hutton, M. L., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.589309 · Cited by 252 · see citing works

Tau immunotherapy for Alzheimer's disease

Pedersen, J. T., & Sigurdsson, E. M. (2015) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2015.03.003 · Cited by 247 · see citing works

O-GlcNAc and neurodegeneration: biochemical mechanisms and potential roles in Alzheimer's disease and beyond

Yuzwa, S. A., & Vocadlo, D. J. (2014) · Chemical Society Reviews · doi:10.1039/c4cs00038b · Cited by 247 · see citing works

Internalized Tau Oligomers Cause Neurodegeneration by Inducing Accumulation of Pathogenic Tau in Human Neurons Derived from Induced Pluripotent Stem Cells

Usenovic, M., Niroomand, S., Drolet, R. E., Yao, L., Gaspar, R. C., Hatcher, N. G., Schachter, J., Renger, J. J., & Parmentier-Batteur, S. (2015) · The Journal of Neuroscience · doi:10.1523/jneurosci.1523-15.2015 · Cited by 245 · see citing works

Enhanced tau aggregation in the presence of Amyloid β

Bennett, R. E., DeVos, S. L., Dujardin, S., Corjuc, B., Gor, R., Gonzalez, J., Roe, A. D., Frosch, M. P., Pitstick, R., Carlson, G. A., et al. (2017) · The American Journal of Pathology · doi:10.1016/j.ajpath.2017.03.011 · Cited by 245 · see citing works

Propagation of prions causing synucleinopathies in cultured cells

Woerman, A. L., Stöhr, J., Aoyagi, A., Rampersaud, R., Krejciova, Z., Watts, J. C., Ohyama, T., Patel, S. S., Widjaja, K., Oehler, A., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1513426112 · Cited by 241 · see citing works

Direct Evidence of Internalization of Tau by Microglia In Vitro and In Vivo

Bolós, M., Llorens-Martín, M., Jurado-Arjona, J., Hernández, F., Rábano, A., & Avila, J. (2016) · Journal of Alzheimer's Disease · doi:10.3233/jad-150704 · Cited by 234 · see citing works

Next-generation active immunization approach for synucleinopathies: implications for Parkinson’s disease clinical trials

Mandler, M., Valera, E., Rockenstein, E. M., Weninger, H., Patrick, C., Adame, A., Santic, R., Meindl, S., Vigl, B., Smrzka, O. W., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1256-4 · Cited by 228 · see citing works

Developing Therapeutic Antibodies for Neurodegenerative Disease

Yu, Y. J., & Watts, R. J. (2013) · Neurotherapeutics · doi:10.1007/s13311-013-0187-4 · Cited by 227 · see citing works

Mechanisms of Protein Seeding in Neurodegenerative Diseases

Walker, L. C., Diamond, M. I., Duff, K. E., & Hyman, B. T. (2013) · JAMA Neurology · doi:10.1001/jamaneurol.2013.1453 · Cited by 226 · see citing works

Tau in neurodegenerative disease

Gao, Y.-L., Wang, N., Sun, F.-R., Cao, X.-P., Zhang, W., & Yu, J.-T. (2018) · Annals of Translational Medicine · doi:10.21037/atm.2018.04.23 · Cited by 222 · see citing works

Neuronal Aggregates: Formation, Clearance, and Spreading

Lim, J., & Yue, Z. (2015) · Developmental Cell · doi:10.1016/j.devcel.2015.02.002 · Cited by 221 · see citing works

Propagation of tau pathology: hypotheses, discoveries, and yet unresolved questions from experimental and human brain studies

Lewis, J. M., & Dickson, D. W. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1507-z · Cited by 221 · see citing works

Four-repeat tauopathies

Rösler, T. W., Marvian, A. T., Brendel, M., Nykänen, N.-P., Höllerhage, M., Schwarz, S. C., Hopfner, F., Koeglsperger, T., Respondek, G., Schweyer, K., et al. (2019) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2019.101644 · 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

Are tau aggregates toxic or protective in tauopathies?

Cowan, C. M., & Mudher, A. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00114 · Cited by 215 · see citing works

Dural lymphatics regulate clearance of extracellular tau from the CNS

Patel, T. K., Habimana-Griffin, L., Gao, X., Xu, B. J., Achilefu, S., Alitalo, K. K., McKee, C. A., Sheehan, P. W., Musiek, E. S., Xiong, C., et al. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0312-x · Cited by 215 · see citing works

Transfer of polyglutamine aggregates in neuronal cells occurs in tunneling nanotubes

Costanzo, M., Abounit, S., Marzo, L., Danckaert, A., Chamoun, Z., Roux, P., & Zurzolo, C. (2013) · Journal of Cell Science · doi:10.1242/jcs.126086 · Cited by 210 · see citing works

Tunneling nanotubes: A possible highway in the spreading of tau and other prion-like proteins in neurodegenerative diseases

Abounit, S., Wu, J. W., Duff, K., Victoria, G. S., & Zurzolo, C. (2016) · Prion · doi:10.1080/19336896.2016.1223003 · Cited by 206 · see citing works

Prion-like Properties of Tau Protein: The Importance of Extracellular Tau as a Therapeutic Target

Holmes, B. B., & Diamond, M. I. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.r114.549295 · Cited by 202 · see citing works

Intersection of pathological tau and microglia at the synapse

Vogels, T., Murgoci, A.-N., & Hromádka, T. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0754-y · Cited by 197 · see citing works

Alzheimer’s pathology targets distinct memory networks in the ageing brain

Maaß, A., Berron, D., Harrison, T. M., Adams, J. N., Joie, R. L., Baker, S. L., Mellinger, T. J., Bell, R. K., Swinnerton, K. N., Inglis, B. A., et al. (2019) · Brain · doi:10.1093/brain/awz154 · Cited by 197 · see citing works

Antibody Uptake into Neurons Occurs Primarily via Clathrin-dependent Fcγ Receptor Endocytosis and Is a Prerequisite for Acute Tau Protein Clearance

Congdon, E. E., Gu, J., Sait, H. B. R., & Sigurdsson, E. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.491001 · Cited by 195 · see citing works

Heterotypic seeding of Tau fibrillization by pre-aggregated Abeta provides potent seeds for prion-like seeding and propagation of Tau-pathology in vivo

Vasconcelos, B., Stancu, I.-C., Buist, A., Bird, M., Wang, P., Vanoosthuyse, A., Van Kolen, K., Verheyen, A., Kienlen-Campard, P., Octave, J.-N., et al. (2016) · Acta Neuropathologica · doi:10.1007/s00401-015-1525-x · Cited by 192 · see citing works

Tau Assembly: The Dominant Role of PHF6 (VQIVYK) in Microtubule Binding Region Repeat R3

Ganguly, P., Do, T. D., Larini, L., LaPointe, N. E., Sercel, A. J., Shade, M. F., Feinstein, S. C., Bowers, M. T., & Shea, J. (2015) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5b00175 · Cited by 191 · see citing works

Extracellular Monomeric and Aggregated Tau Efficiently Enter Human Neurons through Overlapping but Distinct Pathways

Evans, L., Wassmer, T., Fraser, G. M., Smith, J. C., Perkinton, M. S., Billinton, A., & Livesey, F. J. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.03.021 · Cited by 187 · see citing works

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

Colin, M., Dujardin, S., Schraen-Maschke, S., Meno-Tetang, G., Duyckaerts, C., Courade, J.-P., & Buée, L. (2020) · Acta Neuropathologica · doi:10.1007/s00401-019-02087-9 · Cited by 187 · see citing works

Tau prions from Alzheimer’s disease and chronic traumatic encephalopathy patients propagate in cultured cells

Woerman, A. L., Aoyagi, A., Patel, S. S., Kazmi, S. A., Lobach, I. V., Grinberg, L. T., McKee, A. C., Seeley, W. W., Olson, S. H., & Prusiner, S. B. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1616344113 · Cited by 174 · see citing works

Compromised function of the ESCRT pathway promotes endolysosomal escape of tau seeds and propagation of tau aggregation

Chen, J. J., Nathaniel, D. L., Raghavan, P., Nelson, M., Tian, R., Tse, E., Hong, J. Y., See, S. K., Mok, S.-A., Hein, M. Y., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.009432 · Cited by 170 · see citing works

Extracellular Monomeric Tau Protein Is Sufficient to Initiate the Spread of Tau Protein Pathology

Michel, C. H., Kumar, S., Pinotsi, D., Tunnacliffe, A., St. George-Hyslop, P., Mandelkow, E., Mandelkow, E.-M., Kaminski, C. F., & Kaminski Schierle, G. S. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.515445 · Cited by 165 · see citing works

Two Novel Tau Antibodies Targeting the 396/404 Region Are Primarily Taken Up by Neurons and Reduce Tau Protein Pathology

Gu, J., Congdon, E. E., & Sigurdsson, E. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.494922 · Cited by 163 · see citing works

Axonal transport and secretion of fibrillar forms of α-synuclein, Aβ42 peptide and HTTExon 1

Brahic, M., Bousset, L., Bieri, G., Melki, R., & Gitler, A. D. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1538-0 · Cited by 162 · see citing works

The role of extracellular Tau in the spreading of neurofibrillary pathology

Medina, M., & Avila, J. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00113 · Cited by 161 · 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

Prolonged tau clearance and stress vulnerability rescue by pharmacological activation of autophagy in tauopathy neurons

Silva, M. C., Nandi, G. A., Tentarelli, S., Gurrell, I. K., Jamier, T., Lucente, D., Dickerson, B. C., Brown, D. G., Brandon, N. J., & Haggarty, S. J. (2020) · Nature Communications · doi:10.1038/s41467-020-16984-1 · Cited by 157 · see citing works

Amyloidogenesis of Tau protein

Niżyński, B., Dzwolak, W., & Nieznański, K. (2017) · Protein Science · doi:10.1002/pro.3275 · Cited by 157 · see citing works

Review: Manipulating the extracellular matrix and its role in brain and spinal cord plasticity and repair

Burnside, E. R., & Bradbury, E. J. (2013) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12114 · Cited by 153 · see citing works

Short Fibrils Constitute the Major Species of Seed-Competent Tau in the Brains of Mice Transgenic for Human P301S Tau

Jackson, S. J., Kerridge, C., Cooper, J., Cavallini, A., Falcon, B., Cella, C. V., Landi, A., Szekeres, P. G., Murray, T. K., Ahmed, Z., et al. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.3542-15.2016 · Cited by 153 · see citing works

The spread of prion-like proteins by lysosomes and tunneling nanotubes: Implications for neurodegenerative diseases

Victoria, G. S., & Zurzolo, C. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201701047 · Cited by 150 · see citing works

Role of Different Alpha-Synuclein Strains in Synucleinopathies, Similarities with other Neurodegenerative Diseases

Melki, R. (2015) · Journal of Parkinson s Disease · doi:10.3233/jpd-150543 · Cited by 147 · see citing works

Prion-like Mechanisms in the Pathogenesis of Tauopathies and Synucleinopathies

Goedert, M., Falcon, B., Clavaguera, F., & Tolnay, M. (2014) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-014-0495-z · Cited by 145 · see citing works

Mapping interactions with the chaperone network reveals factors that protect against tau aggregation

Mok, S., Condello, C., Freilich, R., Gillies, A. T., Arhar, T., Oroz, J., Kadavath, H., Julien, O., Assimon, V. A., Rauch, J. N., et al. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0057-1 · Cited by 145 · see citing works

Distinct differences in prion-like seeding and aggregation between Tau protein variants provide mechanistic insights into tauopathies

Strang, K. H., Croft, C. L., Sorrentino, Z. A., Chakrabarty, P., Golde, T. E., & Giasson, B. I. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.815357 · Cited by 144 · see citing works

Templated misfolding of Tau by prion-like seeding along neuronal connections impairs neuronal network function and associated behavioral outcomes in Tau transgenic mice

Stancu, I.-C., Vasconcelos, B., Ris, L., Wang, P., Villers, A., Peeraer, E., Buist, A., Terwel, D., Baatsen, P., Oyelami, T., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1413-4 · Cited by 143 · see citing works

Frequent and symmetric deposition of misfolded tau oligomers within presynaptic and postsynaptic terminals in Alzheimer¿s disease

Tai, H., Wang, B. Y., Serrano‐Pozo, A., Frosch, M. P., Spires‐Jones, T. L., & Hyman, B. T. (2014) · Acta Neuropathologica Communications · doi:10.1186/s40478-014-0146-2 · Cited by 142 · see citing works

Widespread tau seeding activity at early Braak stages

Furman, J. L., Vaquer‐Alicea, J., White, C. L., Cairns, N. J., Nelson, P. T., & Diamond, M. I. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1644-z · Cited by 142 · see citing works

Sports-Related Concussions in Youth

Institute of Medicine and National Research Council (2014) · National Academies Press eBooks · doi:10.17226/18377 · Cited by 141 · see citing works

The Neurovascular Unit Dysfunction in Alzheimer’s Disease

Soto-Rojas, L. O., Pacheco‐Herrero, M., Martínez-Gómez, P. A., Campa-Córdoba, B. B., Apátiga-Pérez, R., Villegas-Rojas, M. M., Harrington, C. R., de la Cruz, F., Garcés‐Ramírez, L., & Luna‐Muñoz, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22042022 · Cited by 140 · see citing works

Tau: From research to clinical development

Holtzman, D. M., Carrillo, M. C., Hendrix, J. A., Bain, L. J., Catafau, A. M., Gault, L. M., Goedert, M., Mandelkow, E., Mandelkow, E., Miller, D. S., et al. (2016) · Alzheimer's &amp; Dementia · doi:10.1016/j.jalz.2016.03.018 · Cited by 139 · 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

S4‐02‐04: Propagation of tau misfolding: A new mechanism for Alzheimer's disease?

Diamond, M. I. (2010) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2010.05.461

Mechanisms of Cell-to-Cell Transmission of Pathological Tau: A Review

Gibbons, G. S., Lee, V. M. Y., & Trojanowski, J. Q. (2019) · JAMA Neurology · doi:10.1001/jamaneurol.2018.2505 · Cited by 257 · see citing works

Mechanisms of secretion and spreading of pathological tau protein

Brunello, C. A., Merezhko, M., Uronen, R.-L., & Huttunen, H. J. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03349-1 · Cited by 304 · see citing works

O1‐07‐03: Aggregation and size‐dependent uptake and transport of tau aggregates in neurons

Wu, J., Herman, M., & Duff, K. (2012) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2012.05.241