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

Neuropathological stageing of Alzheimer-related changes.

Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123

2013 Alzheimer's disease facts and figures

Thies, W. H., & Bleiler, L. (2013) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2013.02.003 · Cited by 3,372

Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse

Schenk, D., Barbour, R., Dunn, W., Gordon, G., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., Khan, K., et al. (1999) · Nature · doi:10.1038/22124 · Cited by 3,160

TDP-43 Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis

Sreedharan, J., Blair, I. P., Tripathi, V. B., Hu, X., Vance, C., Rogelj, B., Ackerley, S., Durnall, J. C., Williams, K. L., Buratti, E., et al. (2008) · Science · doi:10.1126/science.1154584 · Cited by 2,630

Neurodegenerative Diseases Target Large-Scale Human Brain Networks

Seeley, W. W., Crawford, R. K., Zhou, J., Miller, B. L., & Greicius, M. D. (2009) · Neuron · doi:10.1016/j.neuron.2009.03.024 · Cited by 2,350

Reducing Endogenous Tau Ameliorates Amyloid ß-Induced Deficits in an Alzheimer's Disease Mouse Model

Roberson, E. D., Scearce-Levie, K., Palop, J. J., Yan, F., Cheng, I. H., Wu, T., Gerstein, H., Yu, G.-Q., & Mucke, L. (2007) · Science · doi:10.1126/science.1141736 · Cited by 1,892

Lewy bodies in grafted neurons in subjects with Parkinson's disease suggest host-to-graft disease propagation

Li, J.-Y., Englund, E., Holton, J. L., Soulet, D., Hagell, P., Lees, A. J., Lashley, T., Quinn, N. P., Rehncrona, S., Björklund, A., et al. (2008) · Nature Medicine · doi:10.1038/nm1746 · Cited by 1,845

Lewy body–like pathology in long-term embryonic nigral transplants in Parkinson's disease

Kordower, J. H., Chu, Y., Hauser, R. A., Freeman, T. B., & Olanow, C. W. (2008) · Nature Medicine · doi:10.1038/nm1747 · Cited by 1,722

Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils

Petkova, A. T., Leapman, R. D., Guo, Z., Yau, W.-M., Mattson, M. P., & Tycko, R. (2005) · Science · doi:10.1126/science.1105850 · Cited by 1,687

Exogenous α-Synuclein Fibrils Induce Lewy Body Pathology Leading to Synaptic Dysfunction and Neuron Death

Volpicelli-Daley, L. A., Luk, K. C., Patel, T. P., Tanik, S. A., Riddle, D. M., Stieber, A., Meaney, D. F., Trojanowski, J. Q., & Lee, V. M.-Y. (2011) · Neuron · doi:10.1016/j.neuron.2011.08.033 · Cited by 1,569

Inclusion formation and neuronal cell death through neuron-to-neuron transmission of α-synuclein

Desplats, P., Lee, H.-J., Bae, E.-J., Patrick, C., Rockenstein, E., Crews, L., Spencer, B., Masliah, E., & Lee, S.-J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903691106 · Cited by 1,485

Propagation of Tau Pathology in a Model of Early Alzheimer's Disease

de Calignon, A., Polydoro, M., Suárez-Calvet, M., William, C., Adamowicz, D. H., Kopeikina, K. J., Pitstick, R., Sahara, N., Ashe, K. H., Carlson, G. A., et al. (2012) · Neuron · doi:10.1016/j.neuron.2011.11.033 · Cited by 1,427

Clinical effects of Aβ immunization (AN1792) in patients with AD in an interrupted trial

Gilman, S., Koller, M., Black, R. S., Jenkins, L., Griffith, S. G., Fox, N. C., Eisner, L., Kirby, L., Rovira, M. B., Forette, F., et al. (2005) · Neurology · doi:10.1212/01.wnl.0000159740.16984.3c · Cited by 1,329

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

Eight prion strains have PrPSc molecules with different conformations

Safar, J., Wille, H., Itri, V., Groth, D., Serban, H., Torchia, M., Cohen, F. E., & Prusiner, S. B. (1998) · Nature Medicine · doi:10.1038/2654 · Cited by 1,244

Molecular Structure of β-Amyloid Fibrils in Alzheimer’s Disease Brain Tissue

Lu, J., Qiang, W., Yau, W., Schwieters, C. D., Meredith, S. C., & Tycko, R. (2013) · Cell · doi:10.1016/j.cell.2013.08.035 · Cited by 1,105

Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans

Goedert, M., Jakes, R., Spillantini, M. G., Hasegawa, M., Smith, M. J., & Crowther, R. A. (1996) · Nature · doi:10.1038/383550a0 · Cited by 1,036

Synthetic Mammalian Prions

Legname, G., Baskakov, I. V., Nguyen, H.-O. B., Riesner, D., Cohen, F. E., DeArmond, S. J., & Prusiner, S. B. (2004) · Science · doi:10.1126/science.1100195 · Cited by 1,022

Trans-Synaptic Spread of Tau Pathology In Vivo

Liu, L., Drouet, V., Wu, J., Witter, M. P., Small, S. A., Clelland, C. L. T., & Duff, K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031302 · Cited by 994

Distinct Tau Prion Strains Propagate in Cells and Mice and Define Different Tauopathies

Sanders, D. W., Kaufman, S. K., DeVos, S. L., Sharma, A. M., Mirbaha, H., Li, A., Barker, S. J., Foley, A. C., Thorpe, J. R., Serpell, L. C., et al. (2014) · Neuron · doi:10.1016/j.neuron.2014.04.047 · Cited by 986

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

Exogenous Induction of Cerebral ß-Amyloidogenesis Is Governed by Agent and Host

Meyer-Luehmann, M., Coomaraswamy, J., Bolmont, T., Kaeser, S., Schaefer, C., Kilger, E., Neuenschwander, A., Abramowski, D., Frey, P., Jaton, A. L., et al. (2006) · Science · doi:10.1126/science.1131864 · Cited by 971

Exogenous α-synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells

Luk, K. C., Song, C., O'Brien, P., Stieber, A., Branch, J. R., Brunden, K. R., Trojanowski, J. Q., & Lee, V. M.-Y. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908005106 · Cited by 938

Structural and functional characterization of two alpha-synuclein strains

Bousset, L., Pieri, L., Ruiz-Arlandis, G., Gath, J., Jensen, P. H., Habenstein, B., Madiona, K., Oliéric, V., Böckmann, A., Meier, B. H., et al. (2013) · Nature Communications · doi:10.1038/ncomms3575 · Cited by 925

Cancer cell exosomes depend on cell-surface heparan sulfate proteoglycans for their internalization and functional activity

Christianson, H. C., Svensson, K. J., van Kuppevelt, T. H., Li, J.-P., & Belting, M. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1304266110 · Cited by 903

Direct Transfer of α-Synuclein from Neuron to Astroglia Causes Inflammatory Responses in Synucleinopathies

Lee, H.-J., Suk, J.-E., Patrick, C., Bae, E.-J., Cho, J.-H., Rho, S., Hwang, D., Masliah, E., & Lee, S.-J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.081125 · Cited by 877

Evidence for the Conformation of the Pathologic Isoform of the Prion Protein Enciphering and Propagating Prion Diversity

Telling, G. C., Parchi, P., DeArmond, S. J., Cortelli, P., Montagna, P., Gabizon, R., Mastrianni, J. A., Lugaresi, E., Gambetti, P. L., & Prusiner, S. B. (1996) · Science · doi:10.1126/science.274.5295.2079 · Cited by 875

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

Virus entry by macropinocytosis

Mercer, J., & Helenius, A. (2009) · Nature Cell Biology · doi:10.1038/ncb0509-510 · Cited by 857

α-Synuclein propagates from mouse brain to grafted dopaminergic neurons and seeds aggregation in cultured human cells

Hansen, C., Angot, E., Bergström, A.-L., Steiner, J. A., Pieri, L., Paul, G., Outeiro, T. F., Melki, R., Kallunki, P., Fog, K., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci43366 · Cited by 842

The function of α-synuclein

Bendor, J. T., Logan, T. P., & Edwards, R. H. (2013) · Neuron · doi:10.1016/j.neuron.2013.09.004 · Cited by 825

A network diffusion model of disease progression in dementia

Raj, A., Kuceyeski, A., & Weiner, M. (2012) · Neuron · doi:10.1016/j.neuron.2011.12.040 · Cited by 723

Predicting Regional Neurodegeneration from the Healthy Brain Functional Connectome

Zhou, J., Gennatas, E. D., Kramer, J. H., Miller, B. L., & Seeley, W. W. (2012) · Neuron · doi:10.1016/j.neuron.2012.03.004 · Cited by 706

Distinct α-Synuclein Strains Differentially Promote Tau Inclusions in Neurons

Guo, J. L., Covell, D. J., Daniels, J. P., Iba, M., Stieber, A., Zhang, B., Riddle, D. M., Kwong, L. K., Xu, Y., Trojanowski, J. Q., et al. (2013) · Cell · doi:10.1016/j.cell.2013.05.057 · Cited by 680

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

Seeding of Normal Tau by Pathological Tau Conformers Drives Pathogenesis of Alzheimer-like Tangles

Guo, J. L., & Lee, V. M.-Y. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.209296 · Cited by 636

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

Effects of Aβ immunization (AN1792) on MRI measures of cerebral volume in Alzheimer disease

Fox, N. C., Black, R. S., Gilman, S., Rossor, M. N., Griffith, S. G., Jenkins, L., & Koller, M. (2005) · Neurology · doi:10.1212/01.wnl.0000159743.08996.99 · Cited by 550 · cited 1×

Effects of α-Synuclein Immunization in a Mouse Model of Parkinson’s Disease

Masliah, E., Rockenstein, E., Adame, A., Alford, M., Crews, L., Hashimoto, M., Seubert, P., Lee, M., Goldstein, J., Chilcote, T., et al. (2005) · Neuron · doi:10.1016/j.neuron.2005.05.010 · Cited by 542

Inhibition of neuronal maturation in primary hippocampal neurons from tau deficient mice

Dawson, H. N., Ferreira, A., Eyster, M. V., Ghoshal, N., Binder, L. I., & Vitek, M. P. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.6.1179 · Cited by 527

Immunotherapy Targeting Pathological Tau Conformers in a Tangle Mouse Model Reduces Brain Pathology with Associated Functional Improvements

Asuni, A. A., Boutajangout, A., Quartermain, D., & Sigurdsson, E. M. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.2361-07.2007 · Cited by 506

Heparin-Binding Proteins

(1998) · Elsevier eBooks · doi:10.1016/b978-0-12-186060-8.x5000-1 · Cited by 504

Protein Homeostasis and Aging: the importance of exquisite quality control

Koga, H., Kaushik, S., & Cuervo, A. M. (2011) · Ageing research reviews · doi:10.1016/j.arr.2010.02.001 · Cited by 476

Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells

Münch, C., O’Brien, J., & Bertolotti, A. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1017275108 · Cited by 475

Darwinian Evolution of Prions in Cell Culture

Li, J., Browning, S. R., Mahal, S. P., Oelschlegel, A. M., & Weissmann, C. (2009) · Science · doi:10.1126/science.1183218 · Cited by 442

Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates

Ren, P.-H., Lauckner, J. E., Kachirskaia, I., Heuser, J. E., Melki, R., & Kopito, R. R. (2009) · Nature Cell Biology · doi:10.1038/ncb1830 · Cited by 427

The presence of heparan sulfate proteoglycans in the neuritic plaques and congophilic angiopathy in Alzheimer's disease.

Snow, A. D., Mar, H., Nochlin, D., Kimata, K., Kato, M., Suzuki, S., Hassell, J., & Wight, T. N. (1988) · PubMed Central · Cited by 418

Intercellular propagated misfolding of wild-type Cu/Zn superoxide dismutase occurs via exosome-dependent and -independent mechanisms

Grad, L. I., Yerbury, J. J., Turner, B. J., Guest, W. C., Pokrishevsky, E., O’Neill, M. A., Yanai, A., Silverman, J. M., Zeineddine, R., Corcoran, L., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1312245111 · Cited by 414

Sulfated polyanion inhibition of scrapie-associated PrP accumulation in cultured cells

Caughey, B. W., & Raymond, G. J. (1993) · Journal of Virology · doi:10.1128/jvi.67.2.643-650.1993 · Cited by 395

Neuron‐to‐neuron transmission of α‐synuclein fibrils through axonal transport

Freundt, E. C., Maynard, N., Clancy, E. K., Roy, S., Bousset, L., Sourigues, Y., Covert, M. W., Melki, R., Kirkegaard, K., & Brahic, M. (2012) · Annals of Neurology · doi:10.1002/ana.23747 · Cited by 394

Evidence for Seeding of β-Amyloid by Intracerebral Infusion of Alzheimer Brain Extracts in β-Amyloid Precursor Protein-Transgenic Mice

Kane, M. D., Lipinski, W. J., Callahan, M. J., Bian, F., Durham, R. A., Schwarz, R. D., Roher, A. E., & Walker, L. C. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-10-03606.2000 · Cited by 394

Purified and synthetic Alzheimer’s amyloid beta (Aβ) prions

Stöhr, J., Watts, J. C., Mensinger, Z. L., Oehler, A., Grillo, S. K., DeArmond, S. J., Prusiner, S. B., & Giles, K. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1206555109 · Cited by 375

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

Polymerization of τ into Filaments in the Presence of Heparin: The Minimal Sequence Required for τ ‐ τ Interaction

Pérez, M., Valpuesta, J., Medina, M., de Garcini, E. M., & Ávila, J. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.67031183.x · Cited by 355

Antibody-Aided Clearance of Extracellular α-Synuclein Prevents Cell-to-Cell Aggregate Transmission

Bae, E.-J., Lee, H.-J., Rockenstein, E., Ho, D.-H., Park, E.-B., Yang, N.-Y., Desplats, P., Masliah, E., & Lee, S.-J. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.1292-12.2012 · Cited by 339

Focality of upper and lower motor neuron degeneration at the clinical onset of ALS

Ravits, J., Paul, P., & Jorg, C. (2007) · Neurology · doi:10.1212/01.wnl.0000260965.20021.47 · Cited by 317

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

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 284

Induction of cerebral β-amyloidosis: Intracerebral versus systemic Aβ inoculation

Eisele, Y. S., Bolmont, T., Heikenwalder, M., Langer, F., Jacobson, L. H., Yan, Z.-X., Roth, K., Aguzzi, A., Staufenbiel, M., Walker, L. C., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903200106 · Cited by 279

Immunotherapy Targeting Pathological Tau Prevents Cognitive Decline in a New Tangle Mouse Model

Boutajangout, A., Quartermain, D., & Sigurdsson, E. M. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.4363-10.2010 · Cited by 272

Alpha-synuclein cell-to-cell transfer and seeding in grafted dopaminergic neurons in vivo

Angot, E., Steiner, J. A., Lema Tomé, C. M., Ekström, P., Mattsson, B., Björklund, A., & Brundin, P. (2012) · PLoS ONE · doi:10.1371/journal.pone.0039465 · Cited by 270

A Seeding Reaction Recapitulates Intracellular Formation of Sarkosyl-insoluble Transactivation Response Element (TAR) DNA-binding Protein-43 Inclusions

Furukawa, Y., Kaneko, K., Watanabe, S., Yamanaka, K., & Nukina, N. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.231209 · Cited by 239

Constitutive secretion of tau protein by an unconventional mechanism

Chai, X., Dage, J. L., & Citron, M. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.05.021 · Cited by 238

Soluble Aβ Seeds Are Potent Inducers of Cerebral β-Amyloid Deposition

Langer, F., Eisele, Y. S., Fritschi, S. K., Staufenbiel, M., Walker, L. C., & Jucker, M. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.3088-11.2011 · Cited by 237

Binding of the protease-sensitive form of PrP (prion protein) to sulfated glycosaminoglycan and congo red [corrected]

Caughey, B. W., Brown, K., Raymond, G. J., Katzenstein, G., & Thresher, W. C. (1994) · Journal of Virology · doi:10.1128/jvi.68.4.2135-2141.1994 · Cited by 237

Treatment of Transmissible Spongiform Encephalopathy by Intraventricular Drug Infusion in Animal Models

Doh‐ura, K., Ishikawa, K., Murakami-Kubo, I., Sasaki, K., Mohri, S., Race, R., & Iwaki, T. (2004) · Journal of Virology · doi:10.1128/jvi.78.10.4999-5006.2004 · Cited by 229

Conformational Diversity of Wild-type Tau Fibrils Specified by Templated Conformation Change

Frost, B., Ollesch, J., Wille, H., & Diamond, M. I. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m805627200 · Cited by 224

Continuum of prion protein structures enciphers a multitude of prion isolate-specified phenotypes

Legname, G., Nguyen, H.-O. B., Peretz, D., Cohen, F. E., DeArmond, S. J., & Prusiner, S. B. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608970103 · Cited by 219

Heparan Sulphate Proteoglycan and the Low-Density Lipoprotein Receptor-Related Protein 1 Constitute Major Pathways for Neuronal Amyloid-β Uptake

Kanekiyo, T., Zhang, J., Liu, Q., Liu, C.-C., Zhang, L., & Bu, G. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.5491-10.2011 · Cited by 212

Targeting Phospho-Ser422 by Active Tau Immunotherapy in the THYTau22 Mouse Model: A Suitable Therapeutic Approach

Zommer, N., Sergeant, N., Schraen-Maschke, S., Blum, D., & Buee, L. (2012) · Current Alzheimer Research · doi:10.2174/156720512800492503 · Cited by 193

Very long term studies of the seeding of β-amyloidosis in primates

Ridley, R. M., Baker, H. F., Windle, C. P., & Cummings, R. M. (2005) · Journal of Neural Transmission · doi:10.1007/s00702-005-0385-2 · Cited by 190

Axonal Transport RatesIn VivoAre Unaffected by Tau Deletion or Overexpression in Mice

Yuan, A., Kumar, A. R., Peterhoff, C. M., Duff, K., & Nixon, R. A. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.5242-07.2008 · Cited by 187

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

Heparan Sulfate Is a Cellular Receptor for Purified Infectious Prions

Horonchik, L., Tzaban, S., Ben-Zaken, O., Yedidia, Y., Rouvinski, A., Papy-García, D., Barritault, D., Vlodavsky, I., & Taraboulos, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500122200 · Cited by 181

In vivo fragmentation of heparan sulfate by heparanase overexpression renders mice resistant to amyloid protein A amyloidosis

Li, J., Galvis, M. L. E., Gong, F., Zhang, X., Zcharia, E., Metzger, S., Vlodavsky, I., Kisilevsky, R., & Lindahl, U. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502287102 · Cited by 180

Heparan Sulfate Glycosaminoglycans as Primary Cell Surface Receptors for Herpes Simplex Virus

Spear, P. G., Shieh, M.-T., Herold, B. C., WuDunn, D., & Koshy, T. I. (1992) · Advances in experimental medicine and biology · doi:10.1007/978-1-4899-2444-5_33 · Cited by 176

Localization of heparan sulfate glycosaminoglycan and proteoglycan core protein in aged brain and Alzheimer's disease

Su, J., Cummings, B. J., & Cotman, C. W. (1992) · Neuroscience · doi:10.1016/0306-4522(92)90521-3 · Cited by 173

Tau Mutations in Neurodegenerative Diseases

Wolfe, M. S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800013200 · Cited by 172

Genetic and Infectious Prion Diseases

Prusiner, S. B. (1993) · Archives of Neurology · doi:10.1001/archneur.1993.00540110011002 · Cited by 167

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

Evidence for and against the transmissibility of Alzheimer disease

Goudsmit, J., Morrow, C. H., Asher, D. M., Yanagihara, R. T., Masters, C. L., Gibbs, C. J., & Gajdusek, D. C. (1980) · Neurology · doi:10.1212/wnl.30.9.945 · Cited by 165

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

Induction of β(A4)-amyloid in primates by injection of Alzheimer’s disease brain homogenate

Baker, H. F., Ridley, R. M., Duchen, L. W., Crow, T. J., & Bruton, C. J. (1994) · Molecular Neurobiology · doi:10.1007/bf02778005 · Cited by 153

Tau-Targeted Immunization Impedes Progression of Neurofibrillary Histopathology in Aged P301L Tau Transgenic Mice

Bi, M., Ittner, A., Ke, Y. D., Götz, J., & Ittner, L. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0026860 · Cited by 153

Protein Homeostasis and Aging: Taking Care of Proteins From the Cradle to the Grave

Morimoto, R. I., & Cuervo, A. M. (2009) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/gln071 · Cited by 151

Synaptotoxic Amyloid-β Oligomers: A Molecular Basis for the Cause, Diagnosis, and Treatment of Alzheimer's Disease?

Klein, W. L. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129039 · Cited by 145

Paired Helical Filaments from Alzheimer Disease Brain Induce Intracellular Accumulation of Tau Protein in Aggresomes

Santa‐María, I., Varghese, M., Ksiȩżak-Reding, H., Dzhun, A., Wang, J., & Pasinetti, G. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.323279 · Cited by 145

Seeded strain‐like transmission of β‐amyloid morphotypes in APP transgenic mice

Heilbronner, G., Eisele, Y. S., Langer, F., Kaeser, S. A., Novotny, R., Nagarathinam, A., Åslund, A., Hammarström, P., Nilsson, K. P. R., & Jucker, M. (2013) · EMBO Reports · doi:10.1038/embor.2013.137 · Cited by 143

Continuous intraventricular infusion of pentosan polysulfate: Clinical trial against prion diseases

Tsuboi, Y., Doh‐ura, K., & Yamada, T. (2009) · Neuropathology · doi:10.1111/j.1440-1789.2009.01058.x · Cited by 127

Heparan sulfate mediates amyloid-beta internalization and cytotoxicity

Sandwall, E., O'Callaghan, P. W., Zhang, X., Lindahl, U., Lannfelt, L., & Li, J. (2010) · Glycobiology · doi:10.1093/glycob/cwp205 · Cited by 116

Novel heparan mimetics potently inhibit the scrapie prion protein and its endocytosis

Schonberger, O., Horonchik, L., Gabizon, R., Papy-García, D., Barritault, D., & Taraboulos, A. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.10.150 · Cited by 82

Systemic vaccination with anti‐oligomeric monoclonal antibodies improves cognitive function by reducing Aβ deposition and tau pathology in 3xTg‐AD mice

Rasool, S., Martínez‐Coria, H., Wu, J., LaFerla, F. M., & Glabe, C. G. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12305 · Cited by 74

Scrapie in the central nervous system: neuroanatomical spread of infection and Sinc control of pathogenesis

Scott, J. R., Davies, D., & Fraser, H. (1992) · Journal of General Virology · doi:10.1099/0022-1317-73-7-1637 · Cited by 68

Accumulation of Vesicle-Associated Human Tau in Distal Dendrites Drives Degeneration and Tau Secretion in anIn SituCellular Tauopathy Model

Lee, S., Kim, W., Li, Z., & Hall, G. F. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/172837 · Cited by 67

Quantitative traits of prion strains are enciphered in the conformation of the prion protein

Safar, J., Cohen, F. E., & Prusiner, S. B. (2000) · Springer eBooks · doi:10.1007/978-3-7091-6308-5_22 · Cited by 53

Comparison of CR36, a new heparan mimetic, and pentosan polysulfate in the treatment of prion diseases

Larramendy-Gozalo, C., Barret, A., Daudigeos‐Dubus, E., Mathieu, E., Antonangeli, L., Riffet, C., Petit, E., Papy-García, D., Barritault, D., Brown, P., et al. (2007) · Journal of General Virology · doi:10.1099/vir.0.82286-0 · Cited by 48

Mutability of prions

Li, J., Mahal, S. P., Demczyk, C. A., & Weissmann, C. (2011) · EMBO Reports · doi:10.1038/embor.2011.191 · Cited by 36

The Adenovirus Type 3 Dodecahedron's RGD Loop Comprises an HSPG Binding Site That Influences Integrin Binding

Gout, E., Schoehn, G., Fenel, D., Lortat‐Jacob, H., & Fender, P. (2010) · BioMed Research International · doi:10.1155/2010/541939 · Cited by 19

Tau in physiology and pathology

Wang, Y., & Mandelkow, E. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2015.1 · Cited by 2,251

Proteopathic tau seeding predicts tauopathy in vivo

Holmes, B. B., Furman, J. L., Mahan, T. E., Yamasaki, T. R., Mirbaha, H., Eades, W. C., Belaygorod, L., Cairns, N. J., Holtzman, D. M., & Diamond, M. I. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1411649111 · Cited by 696

Aggregated Tau activates NLRP3–ASC inflammasome exacerbating exogenously seeded and non-exogenously seeded Tau pathology in vivo

Stancu, I.-C., Cremers, N., Vanrusselt, H., Couturier, J., Vanoosthuyse, A., Kessels, S., Lodder, C., Brône, B., Huaux, F., Octave, J.-N., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-018-01957-y · Cited by 447

Amyloid-β and tau complexity — towards improved biomarkers and targeted therapies

Polanco, J. C., Li, C., Bodea, L., Martínez‐Mármol, R., Meunier, F. A., & Götz, J. (2017) · Nature Reviews Neurology · doi:10.1038/nrneurol.2017.162 · Cited by 386

The complexity of tau in Alzheimer’s disease

Naseri, N. N., Wang, H., Guo, J. D., Sharma, M., & Luo, W. (2019) · Neuroscience Letters · doi:10.1016/j.neulet.2019.04.022 · Cited by 393

Is tau ready for admission to the prion club?

Hall, G. F., & Patuto, B. A. (2012) · Prion · doi:10.4161/pri.19912 · Cited by 43

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

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 152

Prion-like properties of assembled TDP-43

Nonaka, T., & Hasegawa, M. (2019) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2019.11.018 · Cited by 28

Neurodegeneration‐related amyloids interact with the prion protein

Cecco, E. D., Narkiewicz, J., Grandolfo, M., Parisse, P., & Legname, G. (2019) · The FASEB Journal · doi:10.1096/fasebj.2019.33.1_supplement.464.3