Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases

Neuropathological stageing of Alzheimer-related changes.

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

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

Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis

Neumann, M., Sampathu, D. M., Kwong, L. K., Truax, A. C., Micsenyi, M. C., Chou, T. T., Bruce, J., Schuck, T., Grossman, M., Clark, C. M., et al. (2006) · Science · doi:10.1126/science.1134108 · Cited by 6,576 · see citing works

Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein

Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404 · 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

Protein folding and misfolding

Dobson, C. M. (2003) · Nature · doi:10.1038/nature02261 · Cited by 4,791 · see citing works

Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide

Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744 · see citing works

Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo

Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291 · see citing works

Mechanisms underlying inflammation in neurodegeneration

Glass, C. K., Saijo, K., Winner, B., Marchetto, M. C., & Gage, F. H. (2010) · Cell · doi:10.1016/j.cell.2010.02.016 · Cited by 3,580 · see citing works

Diffusible, nonfibrillar ligands derived from Aβ _1–42 are potent central nervous system neurotoxins

Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506 · see citing works

Phases of Aβ-deposition in the human brain and its relevance for the development of AD

Thal, D. R., Rüb, U., Orantes, M., & Braak, H. (2002) · Neurology · doi:10.1212/wnl.58.12.1791 · Cited by 3,490 · see citing works

Protein aggregation and neurodegenerative disease

Ross, C. A., & Poirier, M. A. (2004) · Nature Medicine · doi:10.1038/nm1066 · Cited by 3,454 · see citing works

α-Synuclein in filamentous inclusions of Lewy bodies from Parkinson’s disease and dementia with Lewy bodies

Spillantini, M. G., Crowther, R. A., Jakes, R., Hasegawa, M., & Goedert, M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6469 · Cited by 3,151 · see citing works

Aggregation of Huntingtin in Neuronal Intranuclear Inclusions and Dystrophic Neurites in Brain

DiFiglia, M., Sapp, E., Chase, K. O., Davies, S. W., Bates, G. P., Vonsattel, J., & D, N. A. M. (1997) · Science · doi:10.1126/science.277.5334.1990 · Cited by 2,849 · see citing works

Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease

Arriagada, P. V., Growdon, J. H., Hedley-Whyte, E. T., & Hyman, B. T. (1992) · Neurology · doi:10.1212/wnl.42.3.631 · Cited by 2,668 · see citing works

Pathological α-Synuclein Transmission Initiates Parkinson-like Neurodegeneration in Nontransgenic Mice

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

Synapse Loss and Microglial Activation Precede Tangles in a P301S Tauopathy Mouse Model

Yoshiyama, Y., Higuchi, M., Zhang, B., Huang, S.-M., Iwata, N., Saido, T. C., Maeda, J., Suhara, T., Trojanowski, J. Q., & Lee, V. M.-Y. (2007) · Neuron · doi:10.1016/j.neuron.2007.01.010 · Cited by 2,208 · see citing works

Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function

SantaCruz, K., Lewis, J., Spires, T., Paulson, J., Kotilinek, L., Ingelsson, M., Guimaraes, A., DeTure, M., Ramsden, M., McGowan, E., et al. (2005) · Science · doi:10.1126/science.1113694 · Cited by 2,014 · see citing works

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 · see citing works

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 · see citing works

Dendritic Function of Tau Mediates Amyloid-β Toxicity in Alzheimer's Disease Mouse Models

Ittner, L. M., Ke, Y. D., Delerue, F., Bi, M., Gladbach, A., van Eersel, J., Wölfing, H., Chieng, B. C., Christie, M. J., Napier, I. A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.06.036 · Cited by 1,821 · see citing works

Transmission and spreading of tauopathy in transgenic mouse brain

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

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 · see citing works

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 · see citing works

P <scp>ROTOFIBRILS</scp> , P <scp>ORES</scp> , F <scp>IBRILS, AND</scp> N <scp>EURODEGENERATION</scp> : Separating the Responsible Protein Aggregates from The Innocent Bystanders

Caughey, B., & Lansbury, P. T. (2003) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.010302.081142 · Cited by 1,650 · see citing works

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 · see citing works

In vivo demonstration that α-synuclein oligomers are toxic

Winner, B., Jappelli, R., Maji, S. K., Desplats, P., Boyer, L. F., Aigner, S., Hetzer, C., Loher, T., Vilar, M., Campioni, S., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1100976108 · Cited by 1,487 · 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

Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease.

Kosik, K. S., Joachim, C. L., & Selkoe, D. J. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.11.4044 · Cited by 1,462 · see citing works

Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability

Dahlgren, K. N., Manelli, A. M., Stine, W. B., Baker, L. K., Krafft, G. A., & LaDu, M. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201750200 · Cited by 1,452 · 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

Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism

Cohen, S. I. A., Linse, S. S., Luheshi, L. M., Hellstrand, E., White, D. A., Rajah, L., Otzen, D. E., Vendruscolo, M., Dobson, C. M., & Knowles, T. P. J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1218402110 · Cited by 1,410 · see citing works

Membrane-Associated Heparan Sulfate Proteoglycan Is a Receptor for Adeno-Associated Virus Type 2 Virions

Summerford, C., & Samulski, R. J. (1998) · Journal of Virology · doi:10.1128/jvi.72.2.1438-1445.1998 · Cited by 1,409 · see citing works

The precursor protein of non-Aβ component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system

Iwai, A., Masliah, E., Yoshimoto, M., Ge, N., Flanagan, L., Rohan de Silva, H. A., Kittel, A., & Saitoh, T. (1995) · Neuron · doi:10.1016/0896-6273(95)90302-x · Cited by 1,316 · see citing works

Identification of a Protein That Purifies with the Scrapie Prion

Bolton, D. C., McKinley, M. P., & Prusiner, S. B. (1982) · Science · doi:10.1126/science.6815801 · Cited by 1,281 · 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

Cell-produced α-synuclein is secreted in a calcium-dependent manner by exosomes and impacts neuronal survival

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

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 1,087 · see citing works

Intracerebral inoculation of pathological α-synuclein initiates a rapidly progressive neurodegenerative α-synucleinopathy in mice

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

Navigating the folding routes

Wolynes, P., Onuchic, J., & Thirumalai, D. (1995) · Science · doi:10.1126/science.7886447 · Cited by 1,080 · see citing works

Stages of pTDP‐43 pathology in amyotrophic lateral sclerosis

Brettschneider, J., Del Tredici, K., Toledo, J. B., Robinson, J. L., Irwin, D. J., Grossman, M., Suh, E., Van Deerlin, V. M., Wood, E. M., Baek, Y., et al. (2013) · Annals of Neurology · doi:10.1002/ana.23937 · Cited by 1,065 · see citing works

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 · 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

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

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

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 · see citing works

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. ‐. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908005106 · Cited by 958 · see citing works

Tauopathy in <i>Drosophila</i> : Neurodegeneration Without Neurofibrillary Tangles

Wittmann, C. W., Wszolek, M. F., Shulman, J. M., Salvaterra, P. M., Lewis, J., Hutton, M., & Feany, M. B. (2001) · Science · doi:10.1126/science.1062382 · Cited by 939 · see citing works

The most infectious prion protein particles

Silveira, J. R., Raymond, G. J., Hughson, A. G., Race, R. E., Sim, V. L., Hayes, S. F., & Caughey, B. (2005) · Nature · doi:10.1038/nature03989 · Cited by 899 · see citing works

Cerebrospinal Fluid β-Amyloid 42 and Tau Proteins as Biomarkers of Alzheimer-Type Pathologic Changes in the Brain

Tapiola, T., Alafuzoff, I., Herukka, S.-K., Parkkinen, L., Hartikainen, P., Soininen, H., & Pirttilä, T. (2009) · Archives of Neurology · doi:10.1001/archneurol.2008.596 · Cited by 896 · 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

Heparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds

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

Exosomal cell-to-cell transmission of alpha synuclein oligomers

Danzer, K. M., Kranich, L. R., Ruf, W. P., Cagsal‐Getkin, O., Winslow, A. R., Zhu, L., Vanderburg, C. R., & McLean, P. J. (2012) · Molecular Neurodegeneration · doi:10.1186/1750-1326-7-42 · Cited by 852 · see citing works

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 · see citing works

Normal host prion protein necessary for scrapie-induced neurotoxicity

Brandner, S., Isenmann, S., Raeber, A. J., Fischer, M., Sailer, A. W., Kobayashi, Y., Marino, S., Weissmann, C., & Aguzzi, A. (1996) · Nature · doi:10.1038/379339a0 · Cited by 813 · see citing works

α-Synuclein, Especially the Parkinson's Disease-associated Mutants, Forms Pore-like Annular and Tubular Protofibrils

Lashuel, H. A., Petre, B. M., Wall, J. S., Simon, M. N., Nowak, R. J., Walz, T., & Lansbury, P. T. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00735-0 · Cited by 802 · see citing works

Prion-like transmission of protein aggregates in neurodegenerative diseases

Brundin, P., Melki, R., & Kopito, R. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2873 · Cited by 778 · 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

α-Synuclein Fibrillogenesis Is Nucleation-dependent

Wood, S. J., Wypych, J., Steavenson, S., Louis, J., Citron, M., & Biere, A. L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.28.19509 · Cited by 719 · see citing works

Staging of the intracerebral inclusion body pathology associated with idiopathic Parkinson's disease (preclinical and clinical stages)

Braak, H., Tredici, K. D., Bratzke, H., Hamm-Clement, J., Sandmann-Keil, D., & Rüb, U. (2002) · Journal of Neurology · doi:10.1007/s00415-002-1301-4 · Cited by 710 · 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

Synthetic Tau Fibrils Mediate Transmission of Neurofibrillary Tangles in a Transgenic Mouse Model of Alzheimer's-Like Tauopathy

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

Generating a Prion with Bacterially Expressed Recombinant Prion Protein

Wang, F., Wang, X., Yuan, C., & Ma, J. (2010) · Science · doi:10.1126/science.1183748 · Cited by 659 · see citing works

Progressive disruption of cellular protein folding in models of polyglutamine diseases

Gidalevitz, T., Ben-Zvi, A., Ho, K. H., Brignull, H. R., & Morimoto, R. I. (2006) · Science · doi:10.1126/science.1124514 · Cited by 643 · see citing works

Physiological release of endogenous tau is stimulated by neuronal activity

Pooler, A. M., Phillips, E. C., Lau, D. H. W., Noble, W., & Hanger, D. P. (2013) · The EMBO Reports · doi:10.1038/embor.2013.15 · Cited by 642 · see citing works

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 · see citing works

Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders

Jucker, M., & Walker, L. C. (2011) · Annals of Neurology · doi:10.1002/ana.22615 · Cited by 622 · see citing works

Prions hijack tunnelling nanotubes for intercellular spread

Gousset, K., Schiff, E., Langevin, C., Marijanovic, Z., Caputo, A., Browman, D., Chenouard, N., de Chaumont, F., Martino, A., Enninga, J., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1841 · Cited by 616 · 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

Small Misfolded Tau Species Are Internalized via Bulk Endocytosis and Anterogradely and Retrogradely Transported in Neurons

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

Soluble oligomers of β amyloid (1-42) inhibit long-term potentiation but not long-term depression in rat dentate gyrus

Wang, H.-W., Pasternak, J. F., Kuo, H., Ristic, H., Lambert, M. P., Chromy, B., Viola, K. L., Klein, W. L., Stine, W. B., Krafft, G. A., et al. (2002) · Brain Research · doi:10.1016/s0006-8993(01)03058-x · Cited by 527 · see citing works

Prion-like Properties of Pathological TDP-43 Aggregates from Diseased Brains

Nonaka, T., Masuda‐Suzukake, M., Arai, T., Hasegawa, Y., Akatsu, H., Obi, T., Yoshida, M., Murayama, S., Mann, D. M. A., Akiyama, H., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.06.007 · Cited by 520 · see citing works

Alzheimer brain-derived tau oligomers propagate pathology from endogenous tau

Lasagna-Reeves, C. A., Castillo-Carranza, D. L., Sengupta, U., Guerrero-Munoz, M. J., Kiritoshi, T., Neugebauer, V., Jackson, G. R., & Kayed, R. (2012) · Scientific Reports · doi:10.1038/srep00700 · Cited by 502 · see citing works

Prions: Protein Aggregation and Infectious Diseases

Aguzzi, A., & Calella, A. M. (2009) · Physiological Reviews · doi:10.1152/physrev.00006.2009 · Cited by 502 · see citing works

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 · see citing works

Pre‐fibrillar α‐synuclein variants with impaired β‐structure increase neurotoxicity in Parkinson's disease models

Karpinar, D. P., Balija, M. B. G., Kügler, S., Opazo, F., Rezaei‐Ghaleh, N., Wender, N., Kim, H., Taschenberger, G., Falkenburger, B. H., Heise, H., et al. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.257 · Cited by 443 · see citing works

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 434 · see citing works

Packaging of prions into exosomes is associated with a novel pathway of PrP processing

Vella, L. J., Sharples, R., Lawson, V., Masters, C. L., Cappai, R., & Hill, A. F. (2007) · The Journal of Pathology · doi:10.1002/path.2145 · Cited by 426 · see citing works

Neuropathologic differentiation of progressive supranuclear palsy and corticobasal degeneration

Dickson, D. W. (1999) · Journal of Neurology · doi:10.1007/bf03161076 · Cited by 424 · see citing works

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 410 · see citing works

Rapid Assembly of Alzheimer-like Paired Helical Filaments from Microtubule-Associated Protein Tau Monitored by Fluorescence in Solution

Friedhoff, P., Schneider, A., Mandelkow, E., & Mandelkow�, E. (1998) · Biochemistry · doi:10.1021/bi980537d · Cited by 401 · see citing works

Colocalization of Tau and Alpha-Synuclein Epitopes in Lewy Bodies

Ishizawa, T., Mattila, P. M., Davies, P., Wang, D., & Dickson, D. W. (2003) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/62.4.389 · Cited by 391 · see citing works

A Population-Based Investigation of Parkinson's Disease With and Without Dementia

Mayeux, R. P. (1992) · Archives of Neurology · doi:10.1001/archneur.1992.00530290076015 · Cited by 383 · see citing works

The Neural Cell Adhesion Molecule Is a Receptor for Rabies Virus

Thoulouze, M., Lafage, M., Schachner, M., Hartmann, U., Cremer, H., & Lafon, M. (1998) · Journal of Virology · doi:10.1128/jvi.72.9.7181-7190.1998 · Cited by 379 · see citing works

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 370 · 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

Alzheimer’s pathogenesis: is there neuron-to-neuron propagation?

Braak, H., & Tredici, K. D. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0825-z · Cited by 359 · see citing works

Annular α-Synuclein Protofibrils Are Produced When Spherical Protofibrils Are Incubated in Solution or Bound to Brain-Derived Membranes

Ding, T. T., Lee, S., Rochet, J., & Lansbury, P. T. (2002) · Biochemistry · doi:10.1021/bi020139h · Cited by 356 · see citing works

Characterization of Prefibrillar Tau Oligomers in Vitro and in Alzheimer Disease

Patterson, K. R., Remmers, C. L., Fu, Y., Brooker, S. M., Kanaan, N. M., Vana, L., Ward, S., Reyes, J. F., Philibert, K., Glucksman, M., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.237974 · Cited by 354 · see citing works

Molecular Mechanisms of Prion Pathogenesis

Aguzzi, A., Sigurdson, C. J., & Heikenwaelder, M. (2008) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev.pathmechdis.3.121806.154326 · Cited by 354 · see citing works

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

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

Degeneration of skeletal muscle, peripheral nerves, and the central nervous system in transgenic mice overexpressing wild-type prion proteins

Westaway, D. A., DeArmond, S. J., Cayetano, J., Groth, D., FOSTER, D. B., Yang, S.-L., Torchia, M., Carlson, G. A., & Prusiner, S. B. (1994) · Cell · doi:10.1016/0092-8674(94)90177-5 · Cited by 337 · 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

Insights into prion strains and neurotoxicity

Aguzzi, A., Heikenwälder, M. F., & Polymenidou, M. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2204 · Cited by 327 · 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

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

Granular Tau Oligomers as Intermediates of Tau Filaments

Maeda, S., Sahara, N., Saito, Y., Murayama, M., Yoshiike, Y., Kim, H., Miyasaka, T., Murayama, S., Ikai, A., & Takashima, A. (2007) · Biochemistry · doi:10.1021/bi061359o · Cited by 309 · see citing works

Cell-to-cell transmission of non-prion protein aggregates

Lee, S., Desplats, P., Sigurdson, C. J., Tsigelny, I. F., & Masliah, E. (2010) · Nature Reviews Neurology · doi:10.1038/nrneurol.2010.145 · Cited by 307 · see citing works

Neuroanatomy and Pathology of Sporadic Parkinson's Disease

Braak, H., & Tredici, K. D. (2008) · Advances in anatomy, embryology and cell biology · doi:10.1007/978-3-540-79850-7 · Cited by 297 · see citing works

Serial transmission in rodents of neurodegeneration from transgenic mice expressing mutant prion protein.

Hsiao, K., Groth, D., Scott, M., Yang, S., Serban, H., Rapp, D., Foster, D., Torchia, M., DeArmond, S. J., & Prusiner, S. B. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.19.9126 · Cited by 281 · see citing works

Functional genomics identifies five distinct molecular subtypes with clinical relevance and pathways for growth control in epithelial ovarian cancer

Tan, T. Z., Miow, Q. H., Huang, R. Y., Wong, M. K., Ye, J., Lau, J. A., Wu, M., Hadi, L. A., Soong, R., Choolani, M. A., et al. (2013) · EMBO Molecular Medicine · doi:10.1002/emmm.201201823 · Cited by 281 · see citing works

Recombinant prion protein induces a new transmissible prion disease in wild-type animals

Makarava, N., Kovács, G. G., Bocharova, O. V., Savtchenko, R. S., Alexeeva, I., Budka, H., Rohwer, R. G., & Baskakov, I. V. (2010) · Acta Neuropathologica · doi:10.1007/s00401-009-0633-x · Cited by 276 · see citing works

Addressing Safety Liabilities of TfR Bispecific Antibodies That Cross the Blood-Brain Barrier

Couch, J. A., Yu, Y. J., Zhang, Y., Tarrant, J. M., Fuji, R. N., Meilandt, W. J., Solanoy, H. O., Tong, R. K., Hoyte, K., Luk, W., et al. (2013) · Science Translational Medicine · doi:10.1126/scitranslmed.3005338 · Cited by 270 · see citing works

Interface between tauopathies and synucleinopathies: A tale of two proteins

Galpern, W. R., & Lang, A. E. (2006) · Annals of Neurology · doi:10.1002/ana.20819 · Cited by 262 · see citing works

Caudo‐rostral brain spreading of α‐synuclein through vagal connections

Ulusoy, A., Rusconi, R., Pérez‐Revuelta, B. I., Musgrove, R. E., Helwig, M., Winzen‐Reichert, B., & Monte, D. A. D. (2013) · EMBO Molecular Medicine · doi:10.1002/emmm.201302475 · Cited by 250 · see citing works

Acquired prion disease: iatrogenic CJD, variant CJD, kuru

Will, R. G. (2003) · British Medical Bulletin · doi:10.1093/bmb/66.1.255 · Cited by 248 · see citing works

Potential Epidemic of Creutzfeldt–Jakob Disease from Human Growth Hormone Therapy

Brown, P., Gajdusek, D. C., Gibbs, C. J., et al. (1985) · New England Journal of Medicine · doi:10.1056/nejm198509193131205 · Cited by 233 · see citing works

Design and construction of diverse mammalian prion strains

Colby, D. W., Giles, K., Legname, G., Wille, H., Baskakov, I. V., DeArmond, S. J., & Prusiner, S. B. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0910350106 · Cited by 229 · see citing works

Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity

Nekooki-Machida, Y., Kurosawa, M., Nukina, N., Ito, K., Oda, T., & Tanaka, M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812083106 · Cited by 218 · see citing works

A Single Injection of an Adeno-Associated Virus Vector into Nuclei with Divergent Connections Results in Widespread Vector Distribution in the Brain and Global Correction of a Neurogenetic Disease

Cearley, C. N., & Wolfe, J. H. N. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.2185-07.2007 · Cited by 212 · see citing works

Passage of amyloid β protein antibody across the blood–brain barrier in a mouse model of Alzheimer’s disease

Banks, W. A., Terrell, B., Farr, S. A., Robinson, S. M., Nonaka, N., & Morley, J. E. (2002) · Peptides · doi:10.1016/s0196-9781(02)00261-9 · Cited by 184 · see citing works

Expanded Repertoire of AAV Vector Serotypes Mediate Unique Patterns of Transduction in Mouse Brain

Cearley, C. N., Vandenberghe, L. H., Parente, M. K., Carnish, E. R., Wilson, J. M., & Wolfe, J. H. (2008) · Molecular Therapy · doi:10.1038/mt.2008.166 · Cited by 182 · see citing works

Filamentous nerve cell inclusions in neurodegenerative diseases: tauopathies and alpha-synucleinopathies

Goedert, M. (1999) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.1999.0466 · Cited by 171 · see citing works

Evaluation of Potential Infectivity of Alzheimer and Parkinson Disease Proteins in Recipients of Cadaver-Derived Human Growth Hormone

Irwin, D. J., Abrams, J. Y., Schonberger, L. B., Leschek, E., Mills, J. L., Lee, V. M. ‐., & Trojanowski, J. Q. (2013) · JAMA Neurology · doi:10.1001/jamaneurol.2013.1933 · Cited by 167 · see citing works

Assessment of α-Synuclein Secretion in Mouse and Human Brain Parenchyma

Emmanouilidou, E., Elenis, D., Papasilekas, T., Stranjalis, G., Gerozissis, K., Ioannou, P. C., & Vekrellis, K. (2011) · PLoS ONE · doi:10.1371/journal.pone.0022225 · Cited by 163 · see citing works

Transmission of prions

Weissmann, C., Enari, M., Klöhn, P., Rossi, D., & Flechsig, E. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.172403799 · Cited by 161 · see citing works

Differences in cell-to-cell spread of pathogenic and apathogenic rabies virus in vivo and in vitro

Dietzschold, B., Wiktor, T. J., Trojanowski, J. Q., Macfarlan, R. I., Wunner, W. H., Torres-Anjel, M. J., & Koprowski, H. (1985) · Journal of Virology · doi:10.1128/jvi.56.1.12-18.1985 · Cited by 155 · see citing works

Induction of Amyloid Fibrils by the C-Terminal Fragments of TDP-43 in Amyotrophic Lateral Sclerosis

Chen, A. K.-H., Lin, R. Y., Hsieh, E. Z.-J., Tu, P., Chen, R. P. ‐., Liao, T., Chen, W., Wang, C., & Huang, J. J. (2010) · Journal of the American Chemical Society · doi:10.1021/ja9066207 · Cited by 145 · see citing works

Total CSF α-synuclein is lower in de novo Parkinson patients than in healthy subjects

Mollenhauer, B., Trautmann, E., Taylor, P., Manninger, P., Sixel‐Döring, F., Ebentheuer, J., Trenkwalder, C., & Schlossmacher, M. G. (2012) · Neuroscience Letters · doi:10.1016/j.neulet.2012.11.004 · Cited by 139 · see citing works

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 139 · see citing works

Clinical and Pathological Aspects of Parkinsonism in Alzheimer's Disease

Morris, J. C. (1989) · Archives of Neurology · doi:10.1001/archneur.1989.00520420071025 · Cited by 138 · see citing works

Ultrastructural localization of TDP-43 in filamentous neuronal inclusions in various neurodegenerative diseases

Lin, W.-L., & Dickson, D. W. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0408-9 · Cited by 134 · see citing works

Pathogenesis of mouse scrapie: Effect of route of inoculation on infectivity titres and dose-response curves

Kimberlin, R. H., & Walker, C. A. (1978) · Journal of Comparative Pathology · doi:10.1016/0021-9975(78)90059-2 · Cited by 134 · see citing works

Neurofibrillary tangle‐like tau pathology induced by synthetic tau fibrils in primary neurons over‐expressing mutant tau

Guo, J., & Lee, V. M. ‐. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.01.051 · Cited by 113 · see citing works

Conversion of Wild-type α-Synuclein into Mutant-type Fibrils and Its Propagation in the Presence of A30P Mutant

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

Subclinical prion infection

Hill, A. F., & Collinge, J. (2003) · Trends in Microbiology · doi:10.1016/j.tim.2003.10.007 · Cited by 105 · see citing works

Mutation-dependent Polymorphism of Cu,Zn-Superoxide Dismutase Aggregates in the Familial Form of Amyotrophic Lateral Sclerosis

Furukawa, Y., Kaneko, K., Yamanaka, K., & Nukina, N. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.113597 · Cited by 105 · see citing works

Lewy body disease with and without dementia: a clinicopathological study of 35 cases.

Kosaka, K., Tsuchiya, K., & Yoshimura, M. (1989) · PubMed · Cited by 103 · see citing works

Reduced α‐synuclein levels in cerebrospinal fluid in <scp>P</scp>arkinson's disease are unrelated to clinical and imaging measures of disease severity

van Dijk, K. D., Bidinosti, M., Weiss, A., Raijmakers, P., Berendse, H. W., & van de Berg, W. D. J. (2014) · European Journal of Neurology · doi:10.1111/ene.12176 · Cited by 88 · see citing works

Conformational Features of Tau Fibrils from Alzheimer’s Disease Brain Are Faithfully Propagated by Unmodified Recombinant Protein

Morozova, O. A., March, Z. M., Robinson, A. S., & Colby, D. W. (2013) · Biochemistry · doi:10.1021/bi400866w · Cited by 87 · see citing works

Fibrillogenic Nuclei Composed of P301L Mutant Tau Induce Elongation of P301L Tau but Not Wild-type Tau

Aoyagi, H., Hasegawa, M., & Tamaoka, A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611876200 · Cited by 83 · see citing works

Transmission of prions

Weissmann, C., Klöhn, P.-C., Mahal, S., et al. (2005) · GBM Annual Fall meeting Berlin/Potsdam 2005 · doi:10.1240/sav_gbm_2005_h_001471 · Cited by 67 · see citing works

Aβ Immunotherapy: Lessons Learned for Potential Treatment of Alzheimer’s Disease

Schenk, D. B., Seubert, P. A., Grundman, M., & Black, R. (2005) · Neurodegenerative Diseases · doi:10.1159/000090365 · Cited by 60 · see citing works

The presence of tau distinguishes Lewy bodies of diffuse Lewy body disease from those of idiopathic Parkinson disease

Galloway, P. G., Bergeron, C., & Perry, G. L. (1989) · Neuroscience Letters · doi:10.1016/0304-3940(89)90651-4 · Cited by 57 · see citing works

The Neuropathological Spectrum of Neurodegenerative Tauopathies

Tolnay, M., & Probst, A. (2003) · IUBMB Life · doi:10.1080/1521654032000114348 · Cited by 56 · see citing works

Fine structural analysis of the neuronal inclusions of frontotemporal lobar degeneration with TDP-43 proteinopathy

Thorpe, J. R., Tang, H., Atherton, J., & Cairns, N. J. (2008) · Journal of Neural Transmission · doi:10.1007/s00702-008-0137-1 · Cited by 55 · see citing works

Conformational Transformation and Selection of Synthetic Prion Strains

Ghaemmaghami, S., Watts, J. C., Nguyen, H.-O. B., Hayashi, S., DeArmond, S. J., & Prusiner, S. B. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.07.021 · Cited by 53 · see citing works

Cell-Replacement and Gene-Therapy Strategies for Parkinson‘s and Alzheimer‘s Disease

Korecka, J. A., Verhaagen, J., & Hol, E. M. (2007) · Regenerative Medicine · doi:10.2217/17460751.2.4.425 · Cited by 49 · see citing works

The Continuum of Aging and Age-Related Diseases: Common Mechanisms but Different Rates

Franceschi, C., Garagnani, P., Morsiani, C., Conte, M., Santoro, A., Grignolio, A., Monti, D., Capri, M., & Salvioli, S. (2018) · Frontiers in Medicine · doi:10.3389/fmed.2018.00061 · Cited by 945 · see citing works

Spreading of pathology in neurodegenerative diseases: a focus on human studies

Brettschneider, J., Tredici, K. D., Lee, V. M.-Y., & Trojanowski, J. Q. (2015) · Nature Reviews Neuroscience · doi:10.1038/nrn3887 · Cited by 790 · see citing works

Tau and tauopathies

Arendt, T., Stieler, J. T., & Holzer, M. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.08.018 · Cited by 609 · see citing works

Protein transmission in neurodegenerative disease

Peng, C., Trojanowski, J. Q., & Lee, V. M.-Y. (2020) · Nature Reviews Neurology · doi:10.1038/s41582-020-0333-7 · Cited by 625 · see citing works

Animal models of neurodegenerative diseases

Dawson, T. M., Golde, T. E., & Lagier-Tourenne, C. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0236-8 · Cited by 576 · see citing works

Current state of Alzheimer’s fluid biomarkers

Molinuevo, J. L., Ayton, S., Batrla, R., Bednar, M. M., Bittner, T., Cummings, J., Fagan, A. M., Hampel, H., Mielke, M. M., Mikulskis, A., et al. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1932-x · Cited by 518 · see citing works

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

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

Invited review: Neuropathology of tauopathies: principles and practice

Kovacs, G. G. (2015) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12208 · Cited by 492 · see citing works

Unique pathological tau conformers from Alzheimer’s brains transmit tau pathology in nontransgenic mice

Guo, J. L., Narasimhan, S., Changolkar, L., He, Z., Stieber, A., Zhang, B., Gathagan, R. J., Iba, M., McBride, J. D., Trojanowski, J. Q., et al. (2016) · Journal of Experimental Medicine · doi:10.1084/jem.20160833 · Cited by 440 · see citing works

Glial contributions to neurodegeneration in tauopathies

Leyns, C. E. G., & Holtzman, D. M. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0192-x · Cited by 409 · 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

Like prions: the propagation of aggregated tau and α-synuclein in neurodegeneration

Goedert, M., Masuda-Suzukake, M., & Falcon, B. (2017) · Brain · doi:10.1093/brain/aww230 · Cited by 323 · see citing works

Meta-Analysis of the Alzheimer’s Disease Human Brain Transcriptome and Functional Dissection in Mouse Models

Wan, Y.-W., Al-Ouran, R., Mangleburg, C. G., Perumal, T. M., Lee, T. V., Allison, K., Swarup, V., Funk, C. C., Gaiteri, C., Allen, M., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107908 · Cited by 295 · see citing works

Impact of Anti-amyloid-β Monoclonal Antibodies on the Pathology and Clinical Profile of Alzheimer’s Disease: A Focus on Aducanumab and Lecanemab

Shi, M., Chu, F., Zhu, F., & Zhu, J. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.870517 · Cited by 275 · see citing works

Models of β-amyloid induced Tau-pathology: The long and “folded” road to understand the mechanism

Stancu, I.-C., Vasconcelos, B., Terwel, D., & Dewachter, I. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-51 · Cited by 256 · see citing works

Patient-derived frontotemporal lobar degeneration brain extracts induce formation and spreading of TDP-43 pathology in vivo

Porta, S., Xu, Y., Restrepo, C. R., Kwong, L. K., Zhang, B., Brown, H. J., Lee, E. B., Trojanowski, J. Q., & Lee, V. M.-Y. (2018) · Nature Communications · doi:10.1038/s41467-018-06548-9 · Cited by 248 · see citing works

Protein misfolding and aggregation in Alzheimer’s disease and type 2 diabetes mellitus

Ashraf, G., Greig, N., Khan, T., Hassan, I., Tabrez, S., Shakil, S., Sheikh, I., Zaidi, S., Akram, M., Jabir, N., et al. (2014) · CNS &amp; Neurological Disorders - Drug Targets · doi:10.2174/1871527313666140917095514 · Cited by 236 · see citing works

Tau Trimers Are the Minimal Propagation Unit Spontaneously Internalized to Seed Intracellular Aggregation

Mirbaha, H., Holmes, B. B., Sanders, D. W., Bieschke, J., & Diamond, M. I. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.652693 · Cited by 215 · see citing works

Tau pathology spread in PS19 tau transgenic mice following locus coeruleus (LC) injections of synthetic tau fibrils is determined by the LC's afferent and efferent connections

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

Spread of aggregates after olfactory bulb injection of α-synuclein fibrils is associated with early neuronal loss and is reduced long term

Rey, N. L., George, S., Steiner, J. A., Madaj, Z., Luk, K. C., Trojanowski, J. Q., Lee, V. M.-Y., & Brundin, P. (2018) · Acta Neuropathologica · doi:10.1007/s00401-017-1792-9 · Cited by 215 · see citing works

Distinct roles for motor neuron autophagy early and late in the SOD1 ^G93A mouse model of ALS

Rudnick, N. D., Griffey, C. J., Guarnieri, P., Gerbino, V., Wang, X., Piersaint, J. A., Tapia, J. C., Rich, M. M., & Maniatis, T. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1704294114 · Cited by 189 · see citing works

Fluid Biomarkers for Synaptic Dysfunction and Loss

Camporesi, E., Nilsson, J., Brinkmalm, A., Becker, B., Ashton, N. J., Blennow, K., & Zetterberg, H. (2020) · Biomarker Insights · doi:10.1177/1177271920950319 · Cited by 165 · see citing works

BIN1 favors the spreading of Tau via extracellular vesicles

Crotti, A., Sait, H. R., McAvoy, K. M., Estrada, K., Ergun, A., Szak, S., Marsh, G., Jandreski, L., Peterson, M., Reynolds, T. L., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-45676-0 · Cited by 171 · see citing works

Prion-like transmission of neuronal huntingtin aggregates to phagocytic glia in the Drosophila brain

Pearce, M. M. P., Spartz, E. J., Hong, W., Luo, L., & Kopito, R. R. (2015) · Nature Communications · doi:10.1038/ncomms7768 · Cited by 159 · 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

Impaired endo-lysosomal membrane integrity accelerates the seeding progression of α-synuclein aggregates

Jiang, P., Gan, M., Yen, S.-H., McLean, P. J., & Dickson, D. W. (2017) · Scientific Reports · doi:10.1038/s41598-017-08149-w · Cited by 115 · see citing works

Asynchronous, contagious and digital aging

Rando, T. A., & Wyss-Coray, T. (2021) · Nature Aging · doi:10.1038/s43587-020-00015-1 · Cited by 121 · see citing works

Transcriptional network analysis of human astrocytic endfoot genes reveals region-specific associations with dementia status and tau pathology

Simon, M. J., Wang, M. X., Murchison, C. F., Roese, N. E., Boespflug, E. L., Woltjer, R. L., & Iliff, J. J. (2018) · Scientific Reports · doi:10.1038/s41598-018-30779-x · Cited by 71 · see citing works

Potential Role of Natural Polyphenols against Protein Aggregation Toxicity: In Vitro, In Vivo, and Clinical Studies

Henríquez, G., Gomez, A., Guerrero, E., & Narayan, M. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00381 · Cited by 83 · see citing works

IL‐1β/IL‐1R1 signaling induced by intranasal lipopolysaccharide infusion regulates alpha‐Synuclein pathology in the olfactory bulb, substantia nigra and striatum

Niu, H., Wang, Q., Zhao, W., Liu, J., Wang, D., Muhammad, B., Liu, X., Quan, N., Zhang, H., Zhang, F., et al. (2020) · Brain Pathology · doi:10.1111/bpa.12886 · Cited by 62 · see citing works

Aggregation Properties of the Small Nuclear Ribonucleoprotein U1-70K in Alzheimer Disease

Diner, I., Hales, C. M., Bishof, I., Rabenold, L., Duong, D. M., Yi, H., Laur, O., Gearing, M., Troncoso, J., Thambisetty, M., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.562959 · Cited by 63 · see citing works

Selective lowering of synapsins induced by oligomeric α-synuclein exacerbates memory deficits

Larson, M. E., Greimel, S. J., Amar, F., LaCroix, M., Boyle, G., Sherman, M. A., Schley, H., Miel, C., Schneider, J. A., Kayed, R., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1704698114 · Cited by 61 · see citing works

Measurements of auto‐antibodies to α‐synuclein in the serum and cerebral spinal fluids of patients with Parkinson's disease

Akhtar, R. S., Licata, J. P., Luk, K. C., Shaw, L. M., Trojanowski, J. Q., & Lee, V. M. ‐. (2018) · Journal of Neurochemistry · doi:10.1111/jnc.14330 · Cited by 60 · see citing works

Primary cilia and autophagic dysfunction in Huntington’s disease

Kaliszewski, M., Knott, A. B., & Bossy-Wetzel, E. (2015) · Cell Death &amp; Differentiation · doi:10.1038/cdd.2015.80 · Cited by 55 · see citing works

Relevance of chronic stress and the two faces of microglia in Parkinson's disease

Herrera, A. J., Espinosa-Oliva, A. M., Carrillo-Jiménez, A., Oliva-Martín, M. J., García-Revilla, J., García-Quintanilla, A., de Pablos, R. M., & Venero, J. L. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00312 · Cited by 42 · see citing works

Regional vulnerability and spreading of hyperphosphorylated tau in seeded mouse brain

Detrez, J. R., Maurin, H., Van Kolen, K., Willems, R., Colombelli, J., Lechat, B., Roucourt, B., Van Leuven, F., Baatout, S., Larsen, P., et al. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.03.010 · Cited by 39 · see citing works

Liquid-liquid phase separation in Alzheimer’s disease

Fu, Q., Zhang, B., Chen, X., & Chu, L. (2024) · Journal of Molecular Medicine · doi:10.1007/s00109-023-02407-3 · Cited by 33 · see citing works

Post-COVID-19 Parkinsonism and Parkinson’s Disease Pathogenesis: The Exosomal Cargo Hypothesis

Mysiris, D. S., Vavougios, G. D., Karamichali, E., Papoutsopoulou, S., Stavrou, V. T., Papayianni, E., Boutlas, S., Mavridis, T., Foka, P., Zarogiannis, S. G., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23179739 · Cited by 25 · see citing works

Cloning and Characterization of Rat BAT3 cDNA

Ozaki, T., Hanaoka, E., Naka, M., et al. (1999) · DNA and Cell Biology · doi:10.1089/104454999315222 · Cited by 22 · see citing works

EFFECT OF THE NEMATODE PHASMARHABDITIS HERMAPHRODITA ON YOUNG STAGES OF THE PEST SLUG ARION LUSITANICUS

Grimm, B. (2002) · Journal of Molluscan Studies · doi:10.1093/mollus/68.1.25 · Cited by 41 · see citing works

HLA-B-associated transcript 3 (Bat3)/Scythe is essential for p300-mediated acetylation of p53Preprint

Sasaki, T., Gan, E. C., Wakeham, A. C., Kornbluth, S. A., Mak, T. W., & Okada, H. (2007) · Genes & Development · doi:10.1101/gad.1534107 · Cited by 127 · see citing works

Anthoxanthum Mosaic Virus

Catherall, P. L. (1970) · Plant Pathology · doi:10.1111/j.1365-3059.1970.tb00999.x · Cited by 6 · see citing works

Ecological and evolutionary importance of neighbors in the grass Anthoxanthum odoratum

Platenkamp, G. A. J., & Foin, T. C. (1990) · Oecologia · doi:10.1007/bf00317753 · Cited by 21 · see citing works