Like prions: the propagation of aggregated tau and α-synuclein in neurodegeneration
Open accessAbstract
The abnormal aggregation of a small number of known proteins underlies the most common human neurodegenerative diseases. In tauopathies and synucleinopathies, the normally soluble intracellular proteins tau and α-synuclein become insoluble and filamentous. In recent years, non-cell autonomous mechanisms of aggregate formation have come to the fore, suggesting that nucleation-dependent aggregation may occur in a localized fashion in human tauopathies and synucleinopathies, followed by seed-dependent propagation. There is a long prodromal phase between the formation of protein aggregates and the appearance of the first clinical symptoms, which manifest only after extensive propagation, opening novel therapeutic avenues.
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An earlier event in Alzheimer's disease is pronounced neuron loss in the locus coeruleus, a site of neuromelanin accumulation and the first site to develop tau neurofibrillary tangles.
“But an earlier event is pronounced neuron loss in the locus coeruleus, a site of neuromelanin accumulation and the first site to develop the intracellular inclusions of tau protein termed neurofibrillary tangles (250, 251).”
From Chemiexcitation: Mammalian Photochemistry in the Dark<sup>†</sup> (2023) · cites this paper as [250]
The Introduction (page unavailable) places tau inclusions in the locus coeruleus at early stages of Alzheimer’s disease. It does not report pronounced neuron loss or neuromelanin accumulation there, and it names the transentorhinal cortex—not the locus coeruleus—as the proposed single starting site for Alzheimer’s tau inclusions. (LLM, conf=0.86)
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Cites
Neuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123 · cited 2× · see citing works
“motor nucleus of the vagus nerve, as well as olfactory bulb, for the a-synuclein inclusions of Parkinson’s disease) (Braak and Braak, 1991; Braak et al., 2003; Saito et al., 2004; McKee et al., 2013).”
Staging of brain pathology related to sporadic Parkinson’s disease
Braak, H., Tredici, K. D., Rüb, U., de Vos, R. A. I., Jansen Steur, E. N. H., & Braak, E. (2003) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00065-9 · Cited by 10,777 · see citing works
Novel Proteinaceous Infectious Particles Cause Scrapie
Prusiner, S. B. (1982) · Science · doi:10.1126/science.6801762 · Cited by 5,121 · see citing works
Luk, K. C., Kehm, V., Carroll, J., Zhang, B., O’Brien, P., Trojanowski, J. Q., & Lee, V. M.-Y. (2012) · Science · doi:10.1126/science.1227157 · Cited by 2,563 · see citing works
Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D., & Crowther, R. A. (1989) · Neuron · doi:10.1016/0896-6273(89)90210-9 · Cited by 2,492 · see citing works
Self-citationThe spectrum of disease in chronic traumatic encephalopathy
McKee, A. C., Stein, T. D., Nowinski, C. J., Stern, R. A., Daneshvar, D. H., Alvarez, V. E., Lee, H.-S., Hall, G., Wojtowicz, S. M., Baugh, C. M., et al. (2013) · Brain · doi:10.1093/brain/aws307 · Cited by 2,098 · see citing works
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 · 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
Self-citationLewy 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 · 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
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 · see citing works
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 · see citing works
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 · 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
Goedert, M., Spillantini, M. G., Del Tredici, K., & Braak, H. (2013) · Nature Reviews Neurology · doi:10.1038/nrneurol.2012.242 · Cited by 1,190 · see citing works
Self-citationAn Analytical Solution to the Kinetics of Breakable Filament Assembly
Knowles, T. P. J., Waudby, C. A., Devlin, G. L., Cohen, S. I. A., Aguzzi, A., Vendruscolo, M., Terentjev, E. M., Welland, M. E., & Dobson, C. M. (2009) · Science · doi:10.1126/science.1178250 · Cited by 1,141 · see citing works
α-Synuclein strains cause distinct synucleinopathies after local and systemic administration
Peelaerts, W., Bousset, L., Van der Perren, A., Moskalyuk, A., Pulizzi, R., Giugliano, M., Van den Haute, C., Melki, R., & Baekelandt, V. (2015) · Nature · doi:10.1038/nature14547 · Cited by 1,130 · see citing works
Emmanouilidou, E., Melachroinou, K., Roumeliotis, T., Garbis, S. D., Ntzouni, M., Margaritis, L. H., Stefanis, L., & Vekrellis, K. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.5699-09.2010 · Cited by 1,115 · see citing works
Luk, K. C., Kehm, V. M., Zhang, B., O’Brien, P., Trojanowski, J. Q., & Lee, V. M. ‐. (2012) · The Journal of Experimental Medicine · doi:10.1084/jem.20112457 · Cited by 1,087 · see citing works
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 · see citing works
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 · see citing works
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
Goedert, M. (2015) · Science · doi:10.1126/science.1255555 · Cited by 977 · see citing works
Self-citationExogenous 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 · see citing works
Luk, K. C., Song, C., O’Brien, P., Stieber, A., Branch, J. R., Brunden, K. R., Trojanowski, J. Q., & Lee, V. M. ‐. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908005106 · Cited by 958 · see citing works
Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein
Tuttle, M. D., Comellas, G., Nieuwkoop, A. J., Covell, D. J., Berthold, D. A., Kloepper, K. D., Courtney, J. M., Kim, J. K., Barclay, A. M., Kendall, A. K., et al. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3194 · Cited by 951 · see citing works
Direct Observation of the Interconversion of Normal and Toxic Forms of α-Synuclein
Cremades, N., Cohen, S. I. A., Deas, E., Abramov, A. Y., Chen, A. Y., Orte, Á., Sandal, M., Clarke, R. W., Dunne, P., Aprile, F. A., et al. (2012) · Cell · doi:10.1016/j.cell.2012.03.037 · Cited by 901 · see citing works
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 890 · see citing works
Prion-like spreading of pathological α-synuclein in brain
Masuda-Suzukake, M., Nonaka, T., Hosokawa, M., Oikawa, T., Arai, T., Akiyama, H., Mann, D. M. A., & Hasegawa, M. (2013) · Brain · doi:10.1093/brain/awt037 · Cited by 867 · see citing works
Self-citationHeparan 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
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 · see citing works
Vagotomy and subsequent risk of <scp>P</scp> arkinson's disease
Svensson, E., Horváth‐Puhó, E., Thomsen, R. W., Djurhuus, J. C., Pedersen, L., Borghammer, P., & Sørensen, H. T. (2015) · Annals of Neurology · doi:10.1002/ana.24448 · Cited by 806 · see citing works
Intravesicular Localization and Exocytosis of α-Synuclein and its Aggregates
Lee, H.-J., Patel, S. S., & Lee, S. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.0692-05.2005 · Cited by 798 · see citing works
TFEB-mediated autophagy rescues midbrain dopamine neurons from α-synuclein toxicity
Decressac, M., Mattsson, B., Weikop, P., Lundblad, M., Jakobsson, J., & Björklund, A. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1305623110 · Cited by 753 · see citing works
Brain homogenates from human tauopathies induce tau inclusions in mouse brain
Clavaguera, F., Akatsu, H., Fraser, G. M., Crowther, R. A., Frank, S., Hench, J., Probst, A., Winkler, D. T., Reichwald, J., Staufenbiel, M., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1301175110 · Cited by 750 · see citing works
Self-citationLysosomal dysfunction increases exosome-mediated alpha-synuclein release and transmission
Alvarez‐Erviti, L., Seow, Y., Schapira, A. H. V., Gardiner, C., Sargent, I. L., Wood, M. J. A., & Cooper, J. A. D. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.01.029 · Cited by 741 · see citing works
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 · see citing works
The role of protein clearance mechanisms in organismal ageing and age-related diseases
Vı́lchez, D., Sáez, I., & Dillin, A. G. (2014) · Nature Communications · doi:10.1038/ncomms6659 · Cited by 684 · see citing works
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 · see citing works
Evidence for α-synuclein prions causing multiple system atrophy in humans with parkinsonism
Prusiner, S. B., Woerman, A. L., Mordes, D. A., Watts, J. C., Rampersaud, R., Berry, D. B., Patel, S. S., Oehler, A., Lowe, J. K., Kravitz, S. N., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1514475112 · Cited by 679 · see citing works
Iba, M., Guo, J. L., McBride, J. D., Zhang, B., Trojanowski, J. Q., & Lee, V. M.-Y. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.2642-12.2013 · Cited by 664 · see citing works
Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases
Guo, J. L., & Lee, V. M. Y. (2014) · Nature Medicine · doi:10.1038/nm.3457 · Cited by 641 · see citing works
Recasens, A., Dehay, B., Bové, J., Carballo‐Carbajal, I., Doveró, S., Pérez‐Villalba, A., Fernagut, P., Blesa, J., Parent, A., Perier, C., et al. (2013) · Annals of Neurology · doi:10.1002/ana.24066 · Cited by 629 · see citing works
Structure of the toxic core of α-synuclein from invisible crystals
Rodríguez, J. A., Ivanova, M. I., Sawaya, M. R., Cascio, D., Reyes, F. E., Shi, D., Sangwan, S., Guenther, E. L., Johnson, L. M., Zhang, M., et al. (2015) · Nature · doi:10.1038/nature15368 · Cited by 629 · see citing works
α-Synuclein binds to TOM20 and inhibits mitochondrial protein import in Parkinson’s disease
Di Maio, R., Barrett, P. J., Hoffman, E. K., Barrett, C. W., Zharikov, A., Borah, A., Hu, X., McCoy, J., Chu, C. T., Burton, E. A., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aaf3634 · Cited by 619 · see citing works
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
Peripherally Applied Aβ-Containing Inoculates Induce Cerebral β-Amyloidosis
Eisele, Y. S., Obermüller, U., Heilbronner, G., Baumann, F., Kaeser, S. A., Wolburg, H., Walker, L. C., Staufenbiel, M., Heikenwalder, M., & Jucker, M. (2010) · Science · doi:10.1126/science.1194516 · Cited by 568 · 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
Wu, J. W., Herman, M., Liu, L., Simoes, S., Acker, C. M., Figueroa, H., Steinberg, J. I., Margittai, M., Kayed, R., Zurzolo, C., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.394528 · Cited by 537 · see citing works
Pasanen, P., Myllykangas, L., Siitonen, M., Raunio, A., Kaakkola, S., Lyytinen, J., Tienari, P. J., Pöyhönen, M., & Paetau, A. E. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.03.024 · Cited by 535 · see citing works
Evidence for human transmission of amyloid-β pathology and cerebral amyloid angiopathy
Jaunmuktane, Z., Mead, S., Ellis, M., Wadsworth, J. D. F., Nicoll, A. J., Kenny, J., Launchbury, F., Linehan, J., Richard-Loendt, A., Walker, A. S., et al. (2015) · Nature · doi:10.1038/nature15369 · Cited by 518 · see citing works
Assembly-dependent endocytosis and clearance of extracellular a-synuclein
Lee, H.-J., Suk, J.-E., Bae, E.-J., Lee, J.-H., Paik, S. R., & Lee, S.-J. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.01.017 · Cited by 470 · see citing works
Ahmed, Z., Cooper, J., Murray, T. K., Garn, K., McNaughton, E., Clarke, H., Parhizkar, S., Ward, M. A., Cavallini, A., Jackson, S., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1254-6 · Cited by 460 · see citing works
Self-citationBiology and Genetics of Prions Causing Neurodegeneration
Prusiner, S. B. (2013) · Annual Review of Genetics · doi:10.1146/annurev-genet-110711-155524 · Cited by 455 · see citing works
Kiely, A. P., Asi, Y. T., Kara, E., Limousin, P. D., Ling, H., Lewis, P. A., Proukakis, C., Quinn, N. P., Lees, A. J., Hardy, J., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1096-7 · Cited by 450 · see citing works
Staging of Argyrophilic Grains: An Age-Associated Tauopathy
Saito, Y., Ruberu, N. N., Sawabe, M., Arai, T., Tanaka, N., Kakuta, Y., Yamanouchi, H., & Murayama, S. (2004) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/63.9.911 · Cited by 432 · see citing works
Stuendl, A., Kunadt, M., Kruse, N., Bartels, C., Moebius, W., Danzer, K. M., Mollenhauer, B., & Schneider, A. (2016) · Brain · doi:10.1093/brain/awv346 · Cited by 428 · see citing works
Stokholm, M. G., Danielsen, E. H., Hamilton‐Dutoit, S. J., & Borghammer, P. (2016) · Annals of Neurology · doi:10.1002/ana.24648 · Cited by 415 · see citing works
Human Hsp70 Disaggregase Reverses Parkinson’s-Linked α-Synuclein Amyloid Fibrils
Gao, X., Carroni, M., Nussbaum-Krammer, C. I., Mogk, A., Nillegoda, N. B., Szlachcic, A., Guilbride, D. L., Saibil, H. R., Mayer, M. P., & Bukau, B. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.07.012 · Cited by 404 · see citing works
Chu, Y., & Kordower, J. H. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.08.021 · Cited by 396 · see citing works
Paumier, K. L., Luk, K. C., Manfredsson, F. P., Kanaan, N. M., Lipton, J. W., Collier, T. J., Steece‐Collier, K., Kemp, C. J., Celano, S. L., Schulz, E., et al. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.06.003 · Cited by 386 · see citing works
Prion-like acceleration of a synucleinopathy in a transgenic mouse model
Mougenot, A.-L. J., Nicot, S., Bencsik, A. A., Morignat, E., Verchère, J., Lakhdar, L., Legastelois, S., & Baron, T. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.06.022 · Cited by 375 · see citing works
Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation
Nillegoda, N. B., Kirstein, J., Szlachcic, A., Berynskyy, M., Stank, A., Stengel, F., Arnsburg, K., Gao, X., Scior, A., Aebersold, R. H., et al. (2015) · Nature · doi:10.1038/nature14884 · Cited by 367 · see citing works
Neurodegenerative Diseases: Expanding the Prion Concept
Walker, L. C., & Jucker, M. (2015) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-071714-033828 · Cited by 361 · see citing works
Iatrogenic Creutzfeldt-Jakob Disease, Final Assessment
Brown, P., Brandel, J., SATO, T. A., Nakamura, Y., MacKenzie, J. M., Will, R. G., Ladogana, A., Pocchiari, M., Leschek, E., & Schonberger, L. B. (2012) · Emerging infectious diseases · doi:10.3201/eid1806.120116 · Cited by 360 · see citing works
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 359 · see citing works
Stimulation of autophagy reduces neurodegeneration in a mouse model of human tauopathy
Schaeffer, V., Lavenir, I., Ozcelik, S., Tolnay, M., Winkler, D. T., & Goedert, M. (2012) · Brain · doi:10.1093/brain/aws143 · Cited by 343 · see citing works
Self-citationAntibody-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 · see citing works
Seeded Aggregation and Toxicity of α-Synuclein and Tau
Nonaka, T., Watanabe, S., Iwatsubo, T., & Hasegawa, M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.148460 · Cited by 330 · see citing works
Sacino, A. N., Brooks, M., Thomas, M. A., McKinney, A. B., Lee, S., Regenhardt, R. W., McGarvey, N. H., Ayers, J. I., Notterpek, L. M., Borchelt, D., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1321785111 · Cited by 328 · see citing works
Lewy Body-like α-Synuclein Aggregates Resist Degradation and Impair Macroautophagy
Tanik, S. A., Schultheiss, C. E., Volpicelli-Daley, L. A., Brunden, K. R., & Lee, V. M. Y. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.457408 · Cited by 326 · see citing works
Tran, H., Chung, C. H.-Y., Iba, M., Zhang, B., Trojanowski, J. Q., Luk, K. C., & Lee, V. M. ‐. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.05.033 · Cited by 324 · see citing works
Prion propagation and toxicity in vivo occur in two distinct mechanistic phases
Sandberg, M. K., Al-Doujaily, H., Sharps, B., Clarke, A. R., & Collinge, J. (2011) · Nature · doi:10.1038/nature09768 · Cited by 318 · see citing works
Li, W., Englund, E., Widner, H., Mattsson, B., van Westen, D., Lätt, J., Rehncrona, S., Brundin, P., Björklund, A., Lindvall, O., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1605245113 · Cited by 313 · see citing works
Seeding induced by α‐synuclein oligomers provides evidence for spreading of α‐synuclein pathology
Danzer, K. M., Krebs, S. K., Wolff, M., Birk, G., & Hengerer, B. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06324.x · Cited by 303 · see citing works
A critical appraisal of the pathogenic protein spread hypothesis of neurodegeneration
Walsh, D. M., & Selkoe, D. J. (2016) · Nature reviews. Neuroscience · doi:10.1038/nrn.2016.13 · Cited by 290 · see citing works
Alpha‐synuclein transfers from neurons to oligodendrocytes
Reyes, J. F., Rey, N. L., Bousset, L., Melki, R., Brundin, P., & Angot, É. (2013) · Glia · doi:10.1002/glia.22611 · Cited by 278 · see citing works
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
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 · see citing works
Boluda, S., Iba, M., Zhang, B., Raible, K. M., Lee, V. M. ‐., & Trojanowski, J. Q. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1373-0 · Cited by 259 · see citing works
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
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
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
Self-citationPathological alpha-synuclein propagates through neural networks
Masuda‐Suzukake, M., Nonaka, T., Hosokawa, M., Kubo, M., Shimozawa, A., Akiyama, H., & Hasegawa, M. (2014) · Acta Neuropathologica Communications · doi:10.1186/s40478-014-0088-8 · Cited by 249 · see citing works
Self-citationUsenovic, 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
Expanding the spectrum of neuronal pathology in multiple system atrophy
Cykowski, M. D., Coon, E. A., Powell, S. Z., Jenkins, S. M., Benarroch, E. E., Low, P. A., Schmeichel, A. M., & Parisi, J. E. (2015) · Brain · doi:10.1093/brain/awv114 · Cited by 241 · 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
Osterberg, V. R., Spinelli, K. J., Weston, L. J., Luk, K. C., Woltjer, R. L., & Unni, V. K. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.01.060 · Cited by 240 · see citing works
Saper, C., Wainer, B. H., & German, D. C. (1987) · Neuroscience · doi:10.1016/0306-4522(87)90063-7 · Cited by 239 · see citing works
Amyloid accelerates tau propagation and toxicity in a model of early Alzheimer’s disease
Pooler, A. M., Polydoro, M., Maury, E. A., Nicholls, S. B., Reddy, S. M., Wegmann, S., William, C., Saqran, L., Cagsal-Getkin, O., Pitstick, R., et al. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0199-x · Cited by 236 · see citing works
Iba, M., McBride, J. D., Guo, J. L., Zhang, B., Trojanowski, J. Q., & Lee, V. M.-Y. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1458-4 · Cited by 223 · see citing works
Kinetic model of the aggregation of alpha-synuclein provides insights into prion-like spreading
Iljina, M., Garcia, G. A., Horrocks, M. H., Tosatto, L., Choi, M. L., Ganzinger, K. A., Abramov, A. Y., Gandhi, S., Wood, N. W., Cremades, N., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1524128113 · Cited by 219 · see citing works
Lee, J., Takahama, S., Zhang, G., Tomarev, S. I., & Ye, Y. (2016) · Nature Cell Biology · doi:10.1038/ncb3372 · Cited by 217 · see citing works
Dryanovski, D. I., Guzmán, J. N., Xie, Z., Galteri, D. J., Volpicelli‐Daley, L. A., Lee, V. M. Y., Miller, R. J., Schumacker, P. T., & Surmeier, D. J. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.5311-12.2013 · Cited by 213 · see citing works
Fontaine, S. N., Zheng, D., Sabbagh, J. J., Martin, M. D., Chaput, D., Darling, A. L., Trotter, J. H., Stothert, A. R., Nordhues, B. A., Lussier, A. L., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201593489 · Cited by 203 · see citing works
Mutant huntingtin is present in neuronal grafts in huntington disease patients
Cicchetti, F., Lacroix, S., Cisbani, G., Vallières, N., Saint‐Pierre, M., St‐Amour, I., Tolouei, R., Skepper, J. N., Hauser, R. A., Mantovani, D., et al. (2014) · Annals of Neurology · doi:10.1002/ana.24174 · Cited by 193 · see citing works
Growth hormone, IGF‐I and insulin and their abuse in sport
Holt, R. I. G., & Sönksen, P. H. (2008) · British Journal of Pharmacology · doi:10.1038/bjp.2008.99 · Cited by 188 · see citing works
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 186 · see citing works
Pecho‐Vrieseling, E., Rieker, C., Fuchs, S., Bleckmann, D., Esposito, M. S., Botta, P., Goldstein, C., Bernhard, M., Galimberti, I., Müller, M. M., et al. (2014) · Nature Neuroscience · doi:10.1038/nn.3761 · Cited by 185 · see citing works
Transfer of host-derived alpha synuclein to grafted dopaminergic neurons in rat
Kordower, J. H., Dodiya, H. B., Kordower, A. M., Terpstra, B. T., Paumier, K. L., Madhavan, L., Sortwell, C. E., Steece‐Collier, K., & Collier, T. J. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.05.001 · Cited by 170 · see citing works
Bernis, M. E., Babila, J. T., Breid, S., Wüsten, K. A., Wüllner, U., & Tamgüney, G. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0254-7 · Cited by 163 · see citing works
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
Self-citationSchwab, M. E., & Thoenen, H. (1976) · Brain Research · doi:10.1016/0006-8993(76)90422-4 · Cited by 145 · see citing works
Peripheral administration of tau aggregates triggers intracerebral tauopathy in transgenic mice
Clavaguera, F., Hench, J., Lavenir, I., Schweighauser, G., Frank, S., Goedert, M., & Tolnay, M. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1231-5 · Cited by 143 · see citing works
Self-citationSankaranarayanan, S., Barten, D. M., Vana, L., Devidze, N., Yang, L., Cadelina, G. W., Hoque, N., DeCarr, L. B., Keenan, S., Lin, A., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0125614 · Cited by 143 · see citing works
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 140 · see citing works
Djelloul, M., Holmqvist, S., Boza-Serrano, A., Azevedo, C., Yeung, M. S., Goldwurm, S., Frisén, J., Deierborg, T., & Roybon, L. (2015) · Stem Cell Reports · doi:10.1016/j.stemcr.2015.07.002 · Cited by 138 · see citing works
Harris, J. A., Koyama, A., Maeda, S., Ho, K., Devidze, N., Dubal, D. B., Yu, G.-Q., Masliah, E., & Mucke, L. (2012) · PLoS ONE · doi:10.1371/journal.pone.0045881 · Cited by 135 · see citing works
Removing endogenous tau does not prevent tau propagation yet reduces its neurotoxicity
Wegmann, S., Maury, E. A., Kirk, M. J., Saqran, L., Roe, A., DeVos, S. L., Nicholls, S., Fan, Z., Takeda, S., Cagsal‐Getkin, O., et al. (2015) · The EMBO Journal · doi:10.15252/embj.201592748 · Cited by 132 · see citing works
“Prion‐Like” Templated Misfolding in Tauopathies
Clavaguera, F., Lavenir, I., Falcon, B., Frank, S., Goedert, M., & Tolnay, M. (2013) · Brain Pathology · doi:10.1111/bpa.12044 · Cited by 129 · see citing works
Self-citationKovács, G. G., Majtényi, K., Spina, S., Murrell, J. R., Gelpí, E., Höftberger, R., Fraser, G. M., Crowther, R. A., Goedert, M., Budka, H., et al. (2008) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e318187a80f · Cited by 125 · see citing works
Self-citationFecal transmission of AA amyloidosis in the cheetah contributes to high incidence of disease
Zhang, B., Une, Y., Fu, X., Yan, J., Ge, F., Yao, J., Sawashita, J., Mori, M., Tomozawa, H., Kametani, F., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800367105 · Cited by 121 · see citing works
Frontzek, K., Lutz, M. I., Aguzzi, A., Kovács, G. G., & Budka, H. (2016) · Swiss Medical Weekly · doi:10.4414/smw.2016.14287 · Cited by 121 · see citing works
Yonetani, M., Nonaka, T., Masuda, M., Inukai, Y., Oikawa, T., Hisanaga, S., & Hasegawa, M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m807482200 · Cited by 107 · see citing works
Lewy body pathology in fetal grafts
Chu, Y., & Kordower, J. H. (2009) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2009.05229.x · Cited by 100 · see citing works
Morozova, O. A., March, Z. M., Robinson, A. S., & Colby, D. W. (2013) · Biochemistry · doi:10.1021/bi400866w · Cited by 87 · see citing works
Using Human iPSC-Derived Neurons to Model TAU Aggregation
Verheyen, A., Diels, A., Dijkmans, J., Oyelami, T., Meneghello, G., Mertens, L., Versweyveld, S., Borgers, M., Buist, A., Peeters, P., et al. (2015) · PLOS ONE · doi:10.1371/journal.pone.0146127 · Cited by 86 · see citing works
A cell culture model for monitoring α-synuclein cell-to-cell transfer
Reyes, J. F., Olsson, T. T., Lamberts, J. T., Devine, M. J., Kunath, T., & Brundin, P. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.07.003 · Cited by 84 · see citing works
Dissociation of Alzheimer type pathology in a disconnected piece of cortex
Duyckaerts, C. J., Uchihara, T., Seilhean, D., He, Y., & Hauw, J. (1997) · Acta Neuropathologica · doi:10.1007/s004010050645 · Cited by 71 · see citing works
Nakamura, K., Mori, F., Kon, T., Tanji, K., Miki, Y., Tomiyama, M., Kurotaki, H., Toyoshima, Y., Kakita, A., Takahashi, H., et al. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0208-0 · Cited by 60 · see citing works
Preusser, M. (2005) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.2005.070805 · Cited by 51 · see citing works
Deciphering the scaling of single-molecule interactions using Jarzynski’s equality
Raman, S., Utzig, T., Baimpos, T., et al. (2014) · Nature Communications · doi:10.1038/ncomms6539 · Cited by 51 · see citing works
Lam, H. T., Graber, M. C., Gentry, K. A., & Bieschke, J. (2016) · Biochemistry · doi:10.1021/acs.biochem.5b01168 · Cited by 40 · see citing works
A Rapid Gene Delivery-Based Mouse Model for Early-Stage Alzheimer Disease-Type Tauopathy
Siman, R., Lin, Y., Malthankar‐Phatak, G. H., & Dong, Y. (2013) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0000000000000006 · Cited by 27 · see citing works
Flagged first, then by citations
Research works printed but not linked: 3
- Kfoury N, Holmes BB, Jiang H, Holtzman DM, Diamond M. Transcellular propagation of tau aggregation by fibrillar species. J Biol Chem 2012; 287: 19440-51.
- Sto ¨hr J, Watts JC, Mensinger ZL, Oehler A, Grillo SK, DeArmond SJ, et al. Purified and synthetic Alzheimer's amyloidb (Ab) prions. Proc Natl Acad Sci USA 2012; 109: 11025-30.
- Stokholm MS, Danielsen EH, Hamilton-Dutoit SJ, Borghammer P. Pathological alpha-synuclein in gastrointestinal tissues from pro- dromal Parkinson's disease patients. Ann Neurol 2016; 79: 940-9.
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Cryo-EM structures of tau filaments from Alzheimer’s disease
Fitzpatrick, A. W. P., Falcon, B., He, S., Murzin, A. G., Murshudov, G., Garringer, H. J., Crowther, R. A., Ghetti, B., Goedert, M., & Scheres, S. H. W. (2017) · Nature · doi:10.1038/nature23002 · Cited by 2,061 · see citing works
Self-citationRoles 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
Innate Immunity and Neurodegeneration
Labzin, L. I., Heneka, M. T., & Latz, E. (2018) · Annual Review of Medicine · doi:10.1146/annurev-med-050715-104343 · Cited by 319 · see citing works
The olfactory bulb as the entry site for prion-like propagation in neurodegenerative diseases
Rey, N. L., Wesson, D. W., & Brundin, P. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.12.013 · Cited by 257 · see citing works
Parkinson’s Disease and the Gastrointestinal Microbiome
Lubomski, M., Tan, A. H., Lim, S.-Y., Holmes, A. J., Davis, R. L., & Sue, C. M. (2020) · Journal of Neurology · doi:10.1007/s00415-019-09320-1 · Cited by 172 · see citing works
Astroglia and Tau: New Perspectives
Kovacs, G. G. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00096 · Cited by 115 · see citing works
Mihaila, D., Donegan, J., Barns, S., LaRocca, D., Du, Q., Zheng, D., Vidal, M., Neville, C., Uhlig, R., & Middleton, F. A. (2019) · PLOS ONE · doi:10.1371/journal.pone.0218252 · Cited by 94 · see citing works
Oligodendroglial α‐synucleinopathy‐driven neuroinflammation in multiple system atrophy
Hoffmann, A., Ettle, B., Battis, K., Reiprich, S., Schlachetzki, J. C. M., Masliah, E., Wegner, M., Kuhlmann, T., Riemenschneider, M. J., & Winkler, J. (2019) · Brain Pathology · doi:10.1111/bpa.12678 · Cited by 83 · see citing works
Seizures are a druggable mechanistic link between TBI and subsequent tauopathy.
Alyenbaawi, H., Kanyo, R., Locskai, L. F., Kamali-Jamil, R., DuVal, M. G., Bai, Q., Wille, H., Burton, E. A., & Allison, W. T. (2021) · eLife · doi:10.7554/elife.58744 · Cited by 40 · see citing works
Manecka, D.-L., Vanderperre, B., Fon, E. A., & Durcan, T. M. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00311 · Cited by 21 · see citing works
Chemiexcitation: Mammalian Photochemistry in the Dark<sup>†</sup>
Brash, D. E., & Goncalves, L. C. P. (2023) · Photochemistry and Photobiology · doi:10.1111/php.13781 · Cited by 16 · see citing works
- Authors
- Goedert, M., Masuda-Suzukake, M., & Falcon, B.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- Corresponding author
- Goedert, Michel
- Venue
- Brain
- Publisher
- Oxford University Press (OUP)
- Published
- 2016-09-21
- Volume
- 140
- Issue
- 2
- Pages
- 266-278
- ISSN
- 0006-8950 (ISSN-L)
- 1460-2156
- OpenAlex
- W2521817318
- Cited by
- 323
- References
- 124
- Citations by year
- 2026: 27 · 2025: 30 · 2024: 27 · 2023: 15 · 2022: 29 · 2021: 38 · 2020: 45 · 2019: 35 · 2018: 36 · 2017: 39 · 2016: 1
- FWCI
- 4.34
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Brain (publishedVersion)
- PubMed (publishedVersion)
- HighWire Press Open Archive (submittedVersion)
- Funders
- Medical Research Council (MC-U105184291, MC_EX_MR/N027892/1)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
- Keywords
- tau protein, alpha-synuclein, protein aggregation, neurodegeneration, tauopathy, synucleinopathies, prion-like propagation, prodromal symptoms, therapeutic target
- MeSH terms
- Prion Proteins, Animals, Humans, tau Proteins, Neurodegenerative Diseases, alpha-Synuclein, Protein Aggregation, Pathological
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