Protein transmission in neurodegenerative disease

Neuropathological stageing of Alzheimer-related changes.

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

The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics

Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864 · 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

Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy

Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359 · see citing works

Gene Dose of Apolipoprotein E Type 4 Allele and the Risk of Alzheimer's Disease in Late Onset Families

Corder, E. H., Saunders, A. M., Strittmatter, W. J., Schmechel, D. E., Gaskell, P. C., Small, G. W., Roses, A. D., Haines, J. L., & Pericak-Vance, M. A. (1993) · Science · doi:10.1126/science.8346443 · Cited by 9,429 · see citing works

Alzheimer's disease: the amyloid cascade hypothesis

Hardy, J. A., & Higgins, G. A. (1992) · Science · doi:10.1126/science.1566067 · Cited by 7,484 · 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

A Unique Microglia Type Associated with Restricting Development of Alzheimer’s Disease

Keren-Shaul, H., Spinrad, A., Weiner, A., Matcovitch-Natan, O., Dvir-Szternfeld, R., Ulland, T. K., David, E., Baruch, K., Lara-Astaiso, D., Toth, B., et al. (2017) · Cell · doi:10.1016/j.cell.2017.05.018 · Cited by 5,493 · 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

Hypothetical model of dynamic biomarkers of the Alzheimer's pathological cascade

Jack, C. R., Knopman, D. S., Jagust, W. J., Shaw, L. M., Aisen, P. S., Weiner, M. W., Petersen, R. C., & Trojanowski, J. Q. (2010) · The Lancet Neurology · doi:10.1016/s1474-4422(09)70299-6 · Cited by 4,806 · see citing works

Overdependence on degraded gist memory in Alzheimer's disease.

Gallo, D. A., Shahid, K. R., Olson, M. A., Solomon, T. M., Schacter, D. L., & Budson, A. E. (2006) · Neuropsychology · doi:10.1037/0894-4105.20.6.625 · Cited by 4,756 · see citing works

Tracking pathophysiological processes in Alzheimer's disease: an updated hypothetical model of dynamic biomarkers

Jack, C. R., Knopman, D. S., Jagust, W. J., Petersen, R. C., Weiner, M. W., Aisen, P. S., Shaw, L. M., Vemuri, P., Wiste, H. J., Weigand, S. D., et al. (2013) · The Lancet Neurology · doi:10.1016/s1474-4422(12)70291-0 · Cited by 4,396 · 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

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

Staging of Alzheimer disease-associated neurofibrillary pathology using paraffin sections and immunocytochemistry

Braak, H., Alafuzoff, I., Arzberger, T., Kretzschmar, H., & Del Tredici, K. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0127-z · Cited by 3,172 · 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

The antibody aducanumab reduces Aβ plaques in Alzheimer’s disease

Sevigny, J., Chiao, P., Bussière, T., Weinreb, P. H., Williams, L., Maier, M., Dunstan, R., Salloway, S., Chen, T., Ling, Y., et al. (2016) · Nature · doi:10.1038/nature19323 · Cited by 3,059 · 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

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

Neurodegenerative Tauopathies

Lee, V. M.-Y., Goedert, M., & Trojanowski, J. Q. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1121 · Cited by 2,480 · see citing works

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

Protein misfolding, evolution and disease

Dobson, C. M. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01445-0 · Cited by 1,960 · 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

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

Microglia in neurodegeneration

Hickman, S., Izzy, S., Sen, P., Morsett, L., & El Khoury, J. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0242-x · Cited by 1,710 · 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

Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP

Lewis, J., Dickson, D. W., Lin, W.-L., Chisholm, L., Corral, A., Jones, G., Yen, S.-H., Sahara, N., Skipper, L., Yager, D., et al. (2001) · Science · doi:10.1126/science.1058189 · Cited by 1,611 · 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

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

Amyloid-β Dynamics Are Regulated by Orexin and the Sleep-Wake Cycle

Kang, J.-E., Lim, M. M., Bateman, R. J., Lee, J. J., Smyth, L. P., Cirrito, J. R., Fujiki, N., Nishino, S., & Holtzman, D. M. (2009) · Science · doi:10.1126/science.1180962 · Cited by 1,565 · see citing works

Formation of Neurofibrillary Tangles in P301L Tau Transgenic Mice Induced by Aβ42 Fibrils

Götz, J., Chen, F., van Dorpe, J., & Nitsch, R. M. (2001) · Science · doi:10.1126/science.1062097 · Cited by 1,526 · see citing works

Phenotype, genotype, and worldwide genetic penetrance of LRRK2-associated Parkinson's disease: a case-control study

Healy, D. G., Falchi, M., O’Sullivan, S. S., Bonifati, V., Dürr, A., Bressman, S., Brice, A., Aasly, J. O., Zabetian, C. P., Goldwurm, S., et al. (2008) · The Lancet Neurology · doi:10.1016/s1474-4422(08)70117-0 · Cited by 1,523 · 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

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

Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity

West, A. B., Moore, D. J., Biskup, S., Bugayenko, A., Smith, W. W., Ross, C. A., Dawson, V. L., & Dawson, T. M. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507360102 · Cited by 1,228 · see citing works

Genome-wide Analysis of Genetic Loci Associated With Alzheimer Disease

Seshadri, S. (2010) · JAMA · doi:10.1001/jama.2010.574 · Cited by 1,219 · see citing works

PET Imaging of Tau Deposition in the Aging Human Brain

Schöll, M., Lockhart, S. N., Schonhaut, D. R., O’Neil, J. P., Janabi, M., Ossenkoppele, R., Baker, S. L., Vogel, J. W., Faria, J., Schwimmer, H. D., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.01.028 · Cited by 1,214 · 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

Selective neuronal vulnerability in Parkinson disease

Surmeier, D. J., Obeso, J. A., & Halliday, G. M. (2017) · Nature reviews. Neuroscience · doi:10.1038/nrn.2016.178 · Cited by 1,120 · 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

Construction of a human cell landscape at single-cell level

Han, X., Zhou, Z., Fei, L., Sun, H., Wang, R., Chen, Y., Chen, H., Wang, J., Tang, H., Ge, W., et al. (2020) · Nature · doi:10.1038/s41586-020-2157-4 · Cited by 1,087 · see citing works

Phosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates a subset of Rab GTPases

Steger, M., Tonelli, F., Ito, G., Davies, P., Trost, M., Vetter, M., Wachter, S., Lorentzen, E., Duddy, G., Wilson, S., et al. (2016) · eLife · doi:10.7554/elife.12813 · Cited by 990 · 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

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

Microglia-derived ASC specks cross-seed amyloid-β in Alzheimer’s disease

Venegas, C., Kumar, S., Franklin, B. S., Dierkes, T., Brinkschulte, R., Tejera, D., Vieira-Saecker, A., Schwartz, S., Santarelli, F., Kummer, M. P., et al. (2017) · Nature · doi:10.1038/nature25158 · Cited by 983 · 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

Identification of preclinical Alzheimer's disease by a profile of pathogenic proteins in neurally derived blood exosomes: A case‐control study

Fiandaca, M. S., Kapogiannis, D., Mapstone, M., Boxer, A., Eitan, E., Schwartz, J. B., Abner, E. L., Petersen, R. C., Federoff, H. J., Miller, B. L., et al. (2015) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2014.06.008 · Cited by 959 · 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 957 · 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

Neuronal activity regulates the regional vulnerability to amyloid-β deposition

Bero, A. W., Yan, P., Roh, J. H., Cirrito, J. R., Stewart, F. R., Raichle, M. E., Lee, J.-M., & Holtzman, D. M. (2011) · Nature Neuroscience · doi:10.1038/nn.2801 · Cited by 880 · see citing works

Initiation and Synergistic Fibrillization of Tau and Alpha-Synuclein

Giasson, B. I., Forman, M. S., Higuchi, M., Golbe, L. I., Graves, C. L., Kotzbauer, P. T., Trojanowski, J. Q., & Lee, V. M.-Y. (2003) · Science · doi:10.1126/science.1082324 · Cited by 879 · 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 853 · see citing works

Structures of filaments from Pick’s disease reveal a novel tau protein fold

Falcon, B., Zhang, W., Murzin, A. G., Murshudov, G. N., Garringer, H. J., Vidal, R., Crowther, R. A., Ghetti, B. F., Scheres, S. H. W., & Goedert, M. (2018) · Nature · doi:10.1038/s41586-018-0454-y · Cited by 837 · see citing works

Neuronal activity enhances tau propagation and tau pathology in vivo

Wu, J. W., Hussaini, S. A., Bastille, I. M., Rodriguez, G. A., Mrejeru, A., Rilett, K., Sanders, D. W., Cook, C., Fu, H., Boonen, R. A. C. M., et al. (2016) · Nature Neuroscience · doi:10.1038/nn.4328 · Cited by 820 · see citing works

The sleep-wake cycle regulates brain interstitial fluid tau in mice and CSF tau in humans

Holth, J. K., Fritschi, S. K., Wang, C., Pedersen, N. P., Cirrito, J. R., Mahan, T. E., Finn, M. B., Manis, M., Geerling, J. C., Fuller, P. M., et al. (2019) · Science · doi:10.1126/science.aav2546 · Cited by 813 · see citing works

The pathological process underlying Alzheimer’s disease in individuals under thirty

Braak, H., & Del Tredici, K. (2011) · Acta Neuropathologica · doi:10.1007/s00401-010-0789-4 · Cited by 812 · 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

Different Species of α-Synuclein Oligomers Induce Calcium Influx and Seeding

Danzer, K. M., Haasen, D., Karow, A. R., Moussaud, S., Habeck, M., Giese, A., Kretzschmar, H. A., Hengerer, B., & Kostka, M. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.2617-07.2007 · Cited by 798 · 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 759 · see citing works

Lewy Bodies in Alzheimer's Disease: A Neuropathological Review of 145 Cases Using α‐Synuclein Immunohistochemistry

Hamilton, R. L. (2000) · Brain Pathology · doi:10.1111/j.1750-3639.2000.tb00269.x · Cited by 754 · see citing works

Lysosomal 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

Pathological α-synuclein transmission initiated by binding lymphocyte-activation gene 3

Mao, X., Ou, M. T., Karuppagounder, S. S., Kam, T., Yin, X., Xiong, Y., Ge, P., Umanah, G. K. E., Brahmachari, S., Shin, J., et al. (2016) · Science · doi:10.1126/science.aah3374 · Cited by 739 · see citing works

Kinase activity is required for the toxic effects of mutant LRRK2/dardarin

Greggio, E., Jain, S., Kingsbury, A. E., Bandopadhyay, R., Lewis, P. A., Kaganovich, A., van der Brug, M. P., Beilina, A. G., Blackinton, J. G., Craig, K. J. T., et al. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.04.001 · Cited by 731 · see citing works

Detection of oligomeric forms of α‐synuclein protein in human plasma as a potential biomarker for Parkinson's disease

El‐Agnaf, O. M. A., Salem, S. A., Paleologou, K. E., Curran, M. D., Gibson, M. J., Court, J. A., Schlossmacher, M. G., & Allsop, D. (2006) · The FASEB Journal · doi:10.1096/fj.03-1449com · Cited by 715 · see citing works

Novel tau filament fold in chronic traumatic encephalopathy encloses hydrophobic molecules

Falcon, B., Zivanov, J., Zhang, W., Murzin, A. G., Garringer, H. J., Vidal, R., Crowther, R. A., Newell, K. L., Ghetti, B. F., Goedert, M., et al. (2019) · Nature · doi:10.1038/s41586-019-1026-5 · Cited by 703 · see citing works

The role of microglia in amyloid clearance from the AD brain

Lee, C. Y. D., & Landreth, G. E. (2010) · Journal of Neural Transmission · doi:10.1007/s00702-010-0433-4 · Cited by 701 · see citing works

Toll‐like receptor 4 is required for α‐synuclein dependent activation of microglia and astroglia

Fellner, L., Irschick, R., Schanda, K., Reindl, M., Klimaschewski, L., Poewe, W., Wenning, G. K., & Stefanova, N. (2013) · Glia · doi:10.1002/glia.22437 · Cited by 697 · see citing works

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 · 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

Cerebral Amyloid Angiopathy

Weller, R. O., Massey, A., Newman, T. A., Hutchings, M., Kuo, Y.-M., & Roher, A. E. (1998) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)65616-7 · Cited by 679 · 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

Plasma exosomal α-synuclein is likely CNS-derived and increased in Parkinson’s disease

Shi, M., Liu, C., Cook, T. J., Bullock, K. M., Zhao, Y., Ginghina, C., Li, Y., Aro, P., Dator, R., He, C., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1314-y · Cited by 676 · see citing works

The release and trans-synaptic transmission of Tau via exosomes

Wang, Y., Balaji, V., Kaniyappan, S., Krüger, L., Irsen, S., Tepper, K., Chandupatla, R., Maetzler, W., Schneider, A., Mandelkow, E., et al. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0143-y · Cited by 674 · 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

Progressive supranuclear palsy: clinicopathological concepts and diagnostic challenges

Williams, D. R., & Lees, A. J. (2009) · The Lancet Neurology · doi:10.1016/s1474-4422(09)70042-0 · Cited by 650 · see citing works

Amyloid-β plaques enhance Alzheimer's brain tau-seeded pathologies by facilitating neuritic plaque tau aggregation

He, Z., Guo, J. L., McBride, J. D., Narasimhan, S., Kim, H., Changolkar, L., Zhang, B., Gathagan, R. J., Yue, C., Dengler, C., et al. (2018) · Nature Medicine · doi:10.1038/nm.4443 · Cited by 645 · 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

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

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

Lewy body extracts from Parkinson disease brains trigger α‐synuclein pathology and neurodegeneration in mice and monkeys

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

β-Amyloid peptides enhance α-synuclein accumulation and neuronal deficits in a transgenic mouse model linking Alzheimer's disease and Parkinson's disease

Masliah, E., Rockenstein, E., Veinbergs, I., Sagara, Y., Mallory, M., Hashimoto, M., & Mucke, L. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.211412398 · Cited by 607 · see citing works

Cellular milieu imparts distinct pathological α-synuclein strains in α-synucleinopathies

Peng, C., Gathagan, R. J., Covell, D. J., Medellin, C., Stieber, A., Robinson, J. L., Zhang, B., Pitkin, R. M., Olufemi, M. F., Luk, K. C., et al. (2018) · Nature · doi:10.1038/s41586-018-0104-4 · Cited by 605 · see citing works

Alternative conformations of amyloidogenic proteins govern their behavior

Kelly, J. W. (1996) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(96)80089-3 · Cited by 589 · see citing works

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 584 · see citing works

Synergistic Interactions between Aβ, Tau, and α-Synuclein: Acceleration of Neuropathology and Cognitive Decline

Clinton, L. K., Blurton-Jones, M., Myczek, K., Trojanowski, J. Q., & LaFerla, F. M. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.0490-10.2010 · Cited by 576 · 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

Novel tau filament fold in corticobasal degeneration

Zhang, W., Tarutani, A., Newell, K. L., Murzin, A. G., Matsubara, T., Falcon, B., Vidal, R., Garringer, H. J., Shi, Y., Ikeuchi, T., et al. (2020) · Nature · doi:10.1038/s41586-020-2043-0 · Cited by 546 · see citing works

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 · 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

Parkinson's disease: the presence of Lewy bodies in Auerbach's and Meissner's plexuses

Wakabayashi, K., Takahashi, H., Takeda, S., Ohama, E., & Ikuta, F. (1988) · Acta Neuropathologica · doi:10.1007/bf00687767 · Cited by 528 · 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

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

Neuropathologic substrates of Parkinson disease dementia

Irwin, D. J., White, M. T., Toledo, J. B., Xie, S. X., Robinson, J. L., Van Deerlin, V., Lee, V. M. ‐., Leverenz, J. B., Montine, T. J., Duda, J. E., et al. (2012) · Annals of Neurology · doi:10.1002/ana.23659 · Cited by 518 · 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

Heparin-induced tau filaments are polymorphic and differ from those in Alzheimer’s and Pick’s diseases

Zhang, W., Falcon, B., Murzin, A. G., Fan, J., Crowther, R. A., Goedert, M., & Scheres, S. H. W. (2019) · eLife · doi:10.7554/elife.43584 · Cited by 500 · see citing works

Exosome reduction in vivo is associated with lower amyloid plaque load in the 5XFAD mouse model of Alzheimer's disease

Dinkins, M. B., Dasgupta, S., Wang, G., Zhu, G., & Bieberich, E. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.02.012 · Cited by 494 · see citing works

Development of a Biochemical Diagnosis of Parkinson Disease by Detection of α-Synuclein Misfolded Aggregates in Cerebrospinal Fluid

Shahnawaz, M., Tokuda, T., Waragai, M., Méndez, N., Ishii, R., Trenkwalder, C., Mollenhauer, B., & Soto, C. A. (2016) · JAMA Neurology · doi:10.1001/jamaneurol.2016.4547 · Cited by 485 · 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

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 &amp; Cell Biology · doi:10.1016/j.biocel.2008.01.017 · Cited by 470 · see citing works

Tau prion strains dictate patterns of cell pathology, progression rate, and regional vulnerability in vivo

Kaufman, S. K., Sanders, D. W., Thomas, T. L., Ruchinskas, A. J., Vaquer-Alicea, J., Sharma, A. M., Miller, T. M., & Diamond, M. I. (2016) · Neuron · doi:10.1016/j.neuron.2016.09.055 · Cited by 450 · 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

Transmission of multiple system atrophy prions to transgenic mice

Watts, J. C., Giles, K., Oehler, A., Middleton, L. T., Dexter, D. T., Gentleman, S., DeArmond, S. J., & Prusiner, S. B. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1318268110 · Cited by 433 · see citing works

Regional profiles of the candidate tau PET ligand ¹⁸ F-AV-1451 recapitulate key features of Braak histopathological stages

Schwarz, A. J., Yu, P., Miller, B. B., Shcherbinin, S., Dickson, J., Navitsky, M., Joshi, A. D., Devous, M. D., & Mintun, M. S. (2016) · Brain · doi:10.1093/brain/aww023 · Cited by 425 · see citing works

Tunneling nanotubes spread fibrillar α-synuclein by intercellular trafficking of lysosomes

Abounit, S., Bousset, L., Loria, F., Zhu, S., de Chaumont, F., Pieri, L., Olivo‐Marin, J., Melki, R., & Zurzolo, C. (2016) · The EMBO Journal · doi:10.15252/embj.201593411 · Cited by 414 · 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

Neuronal overexpression of mutant amyloid precursor protein results in prominent deposition of cerebrovascular amyloid

Calhoun, M. E., Burgermeister, P., Phinney, A. L., Stalder, M., Tolnay, M., Wiederhold, K.-H., Abramowski, D., Sturchler-Pierrat, C., Sommer, B., Staufenbiel, M., et al. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.24.14088 · Cited by 410 · see citing works

Environmental toxins trigger PD-like progression via increased alpha-synuclein release from enteric neurons in mice

Pan-Montojo, F., Schwarz, M., Winkler, C., Arnhold, M., O'Sullivan, G. A., Pal, A., Said, J., Marsico, G., Verbavatz, J.-M., Rodrigo-Angulo, M., et al. (2012) · Scientific Reports · doi:10.1038/srep00898 · Cited by 405 · see citing works

Posttranslational Modifications Mediate the Structural Diversity of Tauopathy Strains

Arakhamia, T., Lee, C. E., Carlomagno, Y., Kumar, M., Duong, D. M., Wesseling, H., Kundinger, S. R., Wang, K., Williams, D., Deture, M. A., et al. (2020) · Cell · doi:10.1016/j.cell.2020.01.027 · Cited by 400 · see citing works

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 · see citing works

Aβ is targeted to the vasculature in a mouse model of hereditary cerebral hemorrhage with amyloidosis

Herzig, M. C., Winkler, D. T., Burgermeister, P., Pfeifer, M., Kohler, E., Schmidt, S. D., Danner, S., Abramowski, D., Stürchler-Pierrat, C., Bürki, K., et al. (2004) · Nature Neuroscience · doi:10.1038/nn1302 · Cited by 391 · 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 388 · see citing works

The Exosome Secretory Pathway Transports Amyloid Precursor Protein Carboxyl-terminal Fragments from the Cell into the Brain Extracellular Space

Pérez‐González, R., Gauthier, S. A., Kumar, A. R., & Levy, E. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.404467 · Cited by 385 · see citing works

Direct quantification of CSF α-synuclein by ELISA and first cross-sectional study in patients with neurodegeneration

Mollenhauer, B., Cullen, V., Kahn, I., Krastins, B., Outeiro, T. F., Pepivani, I., Ng, J., Schulz-Schaeffer, W., Kretzschmar, H. A., McLean, P. J., et al. (2008) · Experimental Neurology · doi:10.1016/j.expneurol.2008.06.004 · Cited by 382 · see citing works

Matrix Metalloproteinase-9 Degrades Amyloid-β Fibrils in Vitro and Compact Plaques in Situ

Yan, P., Hu, X., Song, H., Yin, K., Bateman, R. J., Cirrito, J. R., Xiao, Q., Hsu, F. F., Turk, J. W., Xu, J., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602440200 · Cited by 380 · see citing works

Pathological Tau Strains from Human Brains Recapitulate the Diversity of Tauopathies in Nontransgenic Mouse Brain

Narasimhan, S., Guo, J. L., Changolkar, L., Stieber, A., McBride, J. D., Silva, L. V., He, Z., Zhang, B., Gathagan, R. J., Trojanowski, J. Q., et al. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.1230-17.2017 · Cited by 374 · see citing works

Early-onset and Robust Cerebral Microvascular Accumulation of Amyloid β-Protein in Transgenic Mice Expressing Low Levels of a Vasculotropic Dutch/Iowa Mutant Form of Amyloid β-Protein Precursor

Davis, J., Xu, F., Deane, R., Romanov, G., Previti, M. L., Zeigler, K., Zlokovic, B. V., & Van Nostrand, W. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312946200 · Cited by 373 · see citing works

Neuronal uptake and propagation of a rare phosphorylated high-molecular-weight tau derived from Alzheimer’s disease brain

Takeda, S., Wegmann, S., Cho, H., DeVos, S. L., Commins, C., Roe, A. D., Nicholls, S. B., Carlson, G. A., Pitstick, R., Nobuhara, C. K., et al. (2015) · Nature Communications · doi:10.1038/ncomms9490 · Cited by 371 · see citing works

Sequence of Aβ-protein deposition in the human medial temporal lobe

Thal, D. R., Rüb, U., Schultz, C., Sassin, I., Ghebremedhin, E., Del Tredici, K., Braak, E., & Braak, H. (2000) · Journal of Neuropathology &amp; Experimental Neurology · doi:10.1093/jnen/59.8.733 · Cited by 370 · 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

Ser1292 Autophosphorylation Is an Indicator of LRRK2 Kinase Activity and Contributes to the Cellular Effects of PD Mutations

Sheng, Z., Zhang, S., Bustos, D., Kleinheinz, T., Pichon, C. E. L., Dominguez, S. L., Solanoy, H., Drummond, J., Zhang, X.-L., Ding, X., et al. (2012) · Science Translational Medicine · doi:10.1126/scitranslmed.3004485 · Cited by 366 · see citing works

Excessive production of amyloid beta-protein by peripheral cells of symptomatic and presymptomatic patients carrying the Swedish familial Alzheimer disease mutation.

Citron, M., Vigo-Pelfrey, C., Teplow, D. B., Miller, C., Schenk, D., Johnston, J., Winblad, B., Venizelos, N., Lannfelt, L., & Selkoe, D. J. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.25.11993 · Cited by 366 · see citing works

Role of the Blood-Brain Barrier in the Pathogenesis of Alzheimers Disease

Deane, R., & Zloković, B. V. (2007) · Current Alzheimer Research · doi:10.2174/156720507780362245 · Cited by 365 · 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

<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

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 · see citing works

Human Astrocytes Transfer Aggregated Alpha-Synuclein via Tunneling Nanotubes

Rostami, J., Holmqvist, S., Lindström, V., Sigvardson, J., Westermark, G. T., Ingelsson, M., Bergström, J., Roybon, L., & Erlandsson, A. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.0983-17.2017 · Cited by 339 · see citing works

Intramuscular injection of α-synuclein induces CNS α-synuclein pathology and a rapid-onset motor phenotype in transgenic mice

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

Inoculation of α-synuclein preformed fibrils into the mouse gastrointestinal tract induces Lewy body-like aggregates in the brainstem via the vagus nerve

Uemura, N., Yagi, H., Uemura, M. T., Hatanaka, Y., Yamakado, H., & Takahashi, R. (2018) · Molecular Neurodegeneration · doi:10.1186/s13024-018-0257-5 · Cited by 328 · 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

α-Synuclein Immunotherapy Blocks Uptake and Templated Propagation of Misfolded α-Synuclein and Neurodegeneration

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 323 · see citing works

Reducing C-Terminal-Truncated Alpha-Synuclein by Immunotherapy Attenuates Neurodegeneration and Propagation in Parkinson's Disease-Like Models

Games, D., Valera, E., Spencer, B. J., Rockenstein, E. M., Mante, M., Adame, A., Patrick, C., Ubhi, K. K., Nuber, S., Sacayon, P., et al. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.5314-13.2014 · Cited by 322 · see citing works

Parkinson's disease: an immunohistochemical study of Lewy body-containing neurons in the enteric nervous system

Wakabayashi, K., Takahashi, H., Ohama, E., & Ikuta, F. (1990) · Acta Neuropathologica · doi:10.1007/bf00294234 · Cited by 319 · see citing works

The identity and function of microglia in neurodegeneration

Song, W. M., & Colonna, M. (2018) · Nature Immunology · doi:10.1038/s41590-018-0212-1 · Cited by 308 · 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

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

Lewy pathology in the submandibular gland of individuals with incidental Lewy body disease and sporadic Parkinson’s disease

Tredici, K. D., Hawkes, C. H., Ghebremedhin, E., & Braak, H. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0665-2 · Cited by 296 · see citing works

Best Practices for Generating and Using Alpha-Synuclein Pre-Formed Fibrils to Model Parkinson’s Disease in Rodents

Polinski, N. K., Volpicelli-Daley, L. A., Sortwell, C. E., Luk, K. C., Cremades, N., Gottler, L. M., Froula, J., Duffy, M. F., Lee, V. M. Y., Martinez, T. N., et al. (2018) · Journal of Parkinson’s Disease · doi:10.3233/jpd-171248 · Cited by 288 · see citing works

Induction of Tau Pathology by Intracerebral Infusion of Amyloid-β-Containing Brain Extract and by Amyloid-β Deposition in APP × Tau Transgenic Mice

Bolmont, T., Clavaguera, F., Meyer-Luehmann, M., Herzig, M. C., Radde, R., Staufenbiel, M., Lewis, J., Hutton, M., Tolnay, M., & Jucker, M. (2007) · The American Journal of Pathology · doi:10.2353/ajpath.2007.070403 · Cited by 281 · see citing works

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 · see citing works

Serial propagation of distinct strains of Aβ prions from Alzheimer’s disease patients

Watts, J. C., Condello, C., Stöhr, J., Oehler, A., Lee, J., DeArmond, S. J., Lannfelt, L., Ingelsson, M., Giles, K., & Prusiner, S. B. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1408900111 · Cited by 279 · see citing works

α-Synuclein transfer between neurons and astrocytes indicates that astrocytes play a role in degradation rather than in spreading

Loría, F., Vargas, J., Bousset, L., Syan, S., Salles, A., Melki, R., & Zurzolo, C. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1746-2 · Cited by 278 · see citing works

The vermiform appendix impacts the risk of developing Parkinson’s disease

Killinger, B. A., Madaj, Z., Sikora, J. W., Rey, N. L., Haas, A. J., Vepa, Y., Lindqvist, D., Chen, H., Thomas, P. M., Brundin, P., et al. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aar5280 · Cited by 274 · see citing works

Toll-Like Receptor 4 Promotes α-Synuclein Clearance and Survival of Nigral Dopaminergic Neurons

Stefanova, N., Fellner, L., Reindl, M., Masliah, E., Poewe, W., & Wenning, G. K. (2011) · The American Journal of Pathology · doi:10.1016/j.ajpath.2011.04.013 · Cited by 272 · see citing works

Loss of Bin1 Promotes the Propagation of Tau Pathology

Calafate, S., Flavin, W., Verstreken, P., & Moechars, D. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.09.063 · Cited by 265 · see citing works

Differential induction and spread of tau pathology in young PS19 tau transgenic mice following intracerebral injections of pathological tau from Alzheimer’s disease or corticobasal degeneration brains

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

Tau seeding activity begins in the transentorhinal/entorhinal regions and anticipates phospho-tau pathology in Alzheimer’s disease and PART

Kaufman, S. K., Del Tredici, K., Thomas, T. L., Braak, H., & Diamond, M. I. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1855-6 · Cited by 259 · see citing works

Endocytic vesicle rupture is a conserved mechanism of cellular invasion by amyloid proteins

Flavin, W. P., Bousset, L., Green, Z. C., Chu, Y., Skarpathiotis, S., Chaney, M. J., Kordower, J. H., Melki, R., & Campbell, E. M. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1722-x · Cited by 254 · see citing works

Inhibition of γ‐secretase causes increased secretion of amyloid precursor protein C‐terminal fragments in association with exosomes

Sharples, R. A., Vella, L. J., Nisbet, R. M., Naylor, R., Perez, K. A., Barnham, K. J., Masters, C. L., & Hill, A. F. (2008) · The FASEB Journal · doi:10.1096/fj.07-9357com · Cited by 253 · see citing works

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

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

Unconventional Secretion Mediates the Trans-cellular Spreading of Tau

Katsinelos, T., Zeitler, M., Dimou, E., Karakatsani, A., Müller, H., Nachman, E., Steringer, J. P., de Almodóvar, C. R., Nickel, W., & Jahn, T. R. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.04.056 · Cited by 252 · 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

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

Atomic structures of TDP-43 LCD segments and insights into reversible or pathogenic aggregation

Guenther, E. L., Cao, Q., Trinh, H., Lu, J., Sawaya, M. R., Cascio, D., Boyer, D. R., Rodríguez, J. A., Hughes, M. P., & Eisenberg, D. S. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0064-2 · Cited by 247 · see citing works

Molecular Structure of beta-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:10.2210/pdb2m4j/pdb · Cited by 246 · see citing works

Amyloid-Beta (Aβ) Plaques Promote Seeding and Spreading of Alpha-Synuclein and Tau in a Mouse Model of Lewy Body Disorders with Aβ Pathology

Bassil, F., Brown, H. J., Pattabhiraman, S., Iwasyk, J. E., Maghames, C. M., Meymand, E. S., Cox, T. O., Riddle, D. M., Zhang, B., Trojanowski, J. Q., et al. (2019) · Neuron · doi:10.1016/j.neuron.2019.10.010 · Cited by 243 · 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

Microglial internalization and degradation of pathological tau is enhanced by an anti-tau monoclonal antibody

Luo, W., Liu, W., Hu, X., Hanna, M., Caravaca, A., & Paul, S. M. (2015) · Scientific Reports · doi:10.1038/srep11161 · Cited by 241 · see citing works

Tau burden and the functional connectome in Alzheimer’s disease and progressive supranuclear palsy

Cope, T., Rittman, T., Borchert, R. J., Jones, P. S., Vatansever, D., Allinson, K. S. J., Passamonti, L., Rodríguez, P. V., Bevan-Jones, W. R., O'Brien, J. T., et al. (2017) · Brain · doi:10.1093/brain/awx347 · Cited by 240 · see citing works

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 · see citing works

Tubulin Polymerization-promoting Protein (TPPP/p25α) Promotes Unconventional Secretion of α-Synuclein through Exophagy by Impairing Autophagosome-Lysosome Fusion

Ejlerskov, P., Rasmussen, I., Nielsen, T. T., Bergström, A., Tohyama, Y., Jensen, P. H., & Vilhardt, F. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.401174 · Cited by 236 · see citing works

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

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

Inert and seed-competent tau monomers suggest structural origins of aggregation

Mirbaha, H., Chen, D., Morazova, O. A., Ruff, K. M., Sharma, A. M., Liu, X., Goodarzi, M., Pappu, R. V., Colby, D. W., Mirzaei, H., et al. (2018) · eLife · doi:10.7554/elife.36584 · Cited by 234 · see citing works

Parkinson's disease-linked human PARK9/ATP13A2 maintains zinc homeostasis and promotes α-Synuclein externalization via exosomes

Kong, S. M. Y., Chan, B. K. K., Park, J., Hill, K. J., Aitken, J. B., Cottle, L., Farghaian, H., Cole, A. R., Lay, P. A., Sue, C. M., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu099 · Cited by 233 · see citing works

Blood-derived amyloid-β protein induces Alzheimer’s disease pathologies

Bu, X., Xiang, Y., Jin, W.-S., Wang, J., Shen, L.-L., Huang, Z.-L., Zhang, K., Liu, Y.-H., Zeng, F., Liu, H., et al. (2017) · Molecular Psychiatry · doi:10.1038/mp.2017.204 · Cited by 228 · see citing works

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

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

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 224 · 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 220 · see citing works

Ectosomes: A New Mechanism for Non-Exosomal Secretion of Tau Protein

Dujardin, S., Bégard, S., Caillierez, R., Lachaud, C., Delattre, L., Carrier, S., Loyens, A., Galas, M., Bousset, L., Melki, R., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0100760 · Cited by 219 · see citing works

LRRK2 Antisense Oligonucleotides Ameliorate α-Synuclein Inclusion Formation in a Parkinson’s Disease Mouse Model

Zhao, H. T., John, N., Delic, V., Ikeda-Lee, K., Kim, A., Weihofen, A., Swayze, E. E., Kordasiewicz, H. B., West, A. B., & Volpicelli‐Daley, L. A. (2017) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2017.08.002 · Cited by 217 · 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

Intracerebral injection of preformed synthetic tau fibrils initiates widespread tauopathy and neuronal loss in the brains of tau transgenic mice

Peeraer, E., Bottelbergs, A., Van Kolen, K., Stancu, I.-C., Vasconcelos, B., Mahieu, M., Duytschaever, H., Ver Donck, L., Torremans, A., Sluydts, E., et al. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.08.032 · Cited by 214 · see citing works

Cross‐seeding effects of amyloid β‐protein and α‐synuclein

Ono, K., Takahashi, R., Ikeda, T., & Yamada, M. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2012.07847.x · Cited by 213 · see citing works

Autophagy modulates SNCA/α-synuclein release, thereby generating a hostile microenvironment

Poehler, A.-M., Xiang, W., Spitzer, P., May, V. E. L., Meixner, H., Rockenstein, E. M., Chutna, O., Outeiro, T. F., Winkler, J., Masliah, E., et al. (2014) · Autophagy · doi:10.4161/auto.36436 · Cited by 210 · see citing works

Transfer of polyglutamine aggregates in neuronal cells occurs in tunneling nanotubes

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

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

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

Biochemical classification of tauopathies by immunoblot, protein sequence and mass spectrometric analyses of sarkosyl-insoluble and trypsin-resistant tau

Taniguchi-Watanabe, S., Arai, T., Kametani, F., Nonaka, T., Masuda-Suzukake, M., Tarutani, A., Murayama, S., Saito, Y., Arima, K., Yoshida, M., et al. (2016) · Acta Neuropathologica · doi:10.1007/s00401-015-1503-3 · Cited by 200 · see citing works

Alkalizing Drugs Induce Accumulation of Amyloid Precursor Protein By-products in Luminal Vesicles of Multivesicular Bodies

Vingtdeux, V., Hamdane, M., Loyens, A., Gelé, P., Drobeck, H., Bégard, S., Galas, M., Delacourte, A., Beauvillain, J., Buée, L., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609475200 · Cited by 195 · see citing works

Tissue plasminogen activator in central nervous system physiology and pathology

Melchor, J. P., & Strickland, S. (2005) · Thrombosis and Haemostasis · doi:10.1160/th04-12-0838 · Cited by 193 · see citing works

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

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

Propagation of pathological α-synuclein in marmoset brain

Shimozawa, A., Ono, M., Takahara, D., Tarutani, A., Imura, S., Masuda‐Suzukake, M., Higuchi, M., Yanai, K., Hisanaga, S., & Hasegawa, M. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0413-0 · Cited by 190 · see citing works

Neurogenetic contributions to amyloid beta and tau spreading in the human cortex

Sepulcre, J., Grothe, M. J., Uquillas, F. D., Ortiz-Terán, L., Diez, I. P., Yang, H., Jacobs, H. I. L., Hanseeuw, B. J., Li, Q., Fakhri, G. E., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0206-4 · Cited by 190 · see citing works

Exosomes neutralize synaptic-plasticity-disrupting activity of Aβ assemblies in vivo

An, K., Klyubin, I. V., Kim, Y., Jung, J. H., Mably, A. J., O’Dowd, S., Lynch, T., Kanmert, D., Lemere, C. A., Finan, G. M., et al. (2013) · Molecular Brain · doi:10.1186/1756-6606-6-47 · Cited by 187 · see citing works

TDP-43 extracted from frontotemporal lobar degeneration subject brains displays distinct aggregate assemblies and neurotoxic effects reflecting disease progression rates

Laferrière, F., Maniecka, Z., Pérez‐Berlanga, M., Hruška-Plocháň, M., Gilhespy, L. A. B., Hock, E., Wagner, U., Afroz, T., Boersema, P. J., Barmettler, G., et al. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0294-y · Cited by 186 · see citing works

G2019S-LRRK2 Expression Augments -Synuclein Sequestration into Inclusions in Neurons

Volpicelli‐Daley, L. A., Abdelmotilib, H., Liu, Z., Stoyka, L. E., Daher, J. P. L., Milnerwood, A. J., Unni, V. K., Hirst, W. D., Yue, Z., Zhao, H., et al. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.3642-15.2016 · Cited by 185 · see citing works

In Vivo Tau, Amyloid, and Gray Matter Profiles in the Aging Brain

Sepulcre, J., Schultz, A. P., Sabuncu, M. R., Gómez‐Isla, T., Chhatwal, J. P., Becker, A., Sperling, R. A., & Johnson, K. A. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.0639-16.2016 · Cited by 175 · see citing works

The Complex Molecular Biology of Amyotrophic Lateral Sclerosis (ALS)

Redler, R. L., & Dokholyan, N. V. (2012) · Progress in Molecular Biology and Translational Science · doi:10.1016/b978-0-12-385883-2.00002-3 · Cited by 172 · see citing works

ATP13A2/PARK9 Regulates Secretion of Exosomes and α-Synuclein

Tsunemi, T., Hamada, K., & Krainc, D. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.1629-14.2014 · Cited by 172 · see citing works

Extracellular vesicle sorting of α-Synuclein is regulated by sumoylation

Kunadt, M., Eckermann, K., Stuendl, A., Gong, J., Russo, B., Strauss, K., Rai, S., Kügler, S., Falomir‐Lockhart, L. J., Schwalbe, M., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1408-1 · Cited by 171 · see citing works

Elevated Aβ42 in Skeletal Muscle of Alzheimer Disease Patients Suggests Peripheral Alterations of AβPP Metabolism

Kuo, Y.-M., Kokjohn, T. A., Watson, M. D., Woods, A. S., Cotter, R. J., Sue, L. I., Kalback, W. M., Emmerling, M. R., Beach, T. G., & Roher, A. E. (2000) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64947-4 · Cited by 167 · see citing works

Synergy between amyloid-β and tau in Alzheimer’s disease

Busche, M. A., & Hyman, B. T. (2020) · Nature Neuroscience · doi:10.1038/s41593-020-0687-6 · Cited by 1,242 · see citing works

Biomarkers for neurodegenerative diseases

Hansson, O. (2021) · Nature Medicine · doi:10.1038/s41591-021-01382-x · Cited by 1,159 · see citing works

Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer’s Disease, Parkinson’s Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis

Nguyen, P. H., Ramamoorthy, A., Sahoo, B. R., Zheng, J., Faller, P., Straub, J. E., Domı́nguez, L., Shea, J., Dokholyan, N. V., Simone, A. D., et al. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01122 · Cited by 676 · see citing works

Mental health care for older adults: recent advances and new directions in clinical practice and research

Reynolds, C. F., Jeste, D. V., Sachdev, P. S., & Blazer, D. G. (2022) · World Psychiatry · doi:10.1002/wps.20996 · Cited by 465 · see citing works

Genetics and Pathogenesis of Parkinson's Syndrome

Ye, H., Robak, L. A., Yu, M., Cykowski, M. D., & Shulman, J. M. (2022) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathmechdis-031521-034145 · Cited by 474 · see citing works

The role of TDP-43 propagation in neurodegenerative diseases: integrating insights from clinical and experimental studies

Jo, M., Lee, S., Jeon, Y., Kim, S., Kwon, Y., & Kim, H. (2020) · Experimental & Molecular Medicine · doi:10.1038/s12276-020-00513-7 · Cited by 405 · see citing works

The immunology of multiple sclerosis

Attfield, K. E., Jensen, L. T., Kaufmann, M., Friese, M. A., & Fugger, L. (2022) · Nature Reviews Immunology · doi:10.1038/s41577-022-00718-z · Cited by 380 · see citing works

Solving neurodegeneration: common mechanisms and strategies for new treatments

Wareham, L. K., Liddelow, S. A., Temple, S., Benowitz, L. I., Di Polo, A., Wellington, C., Goldberg, J. L., He, Z., Duan, X., Bu, G., et al. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00524-0 · Cited by 324 · see citing works

Molecular pathology of neurodegenerative diseases by cryo-EM of amyloids

Scheres, S. H. W., Falcon, B., & Goedert, M. (2023) · Nature · doi:10.1038/s41586-023-06437-2 · Cited by 293 · see citing works

Mitochondrial dysfunction and oxidative stress in Alzheimer’s disease, and Parkinson’s disease, Huntington’s disease and Amyotrophic Lateral Sclerosis -An updated review

Alqahtani, T., Deore, S. L., Kide, A. A., Shende, B. A., Sharma, R., Chakole, R. D., Nemade, L. S., Kale, N. K., Borah, S., Deokar, S. S., et al. (2023) · Mitochondrion · doi:10.1016/j.mito.2023.05.007 · Cited by 289 · see citing works

The human connectome in Alzheimer disease — relationship to biomarkers and genetics

Yu, M., Sporns, O., & Saykin, A. J. (2021) · Nature Reviews Neurology · doi:10.1038/s41582-021-00529-1 · Cited by 265 · see citing works

Proteomic landscape of Alzheimer’s Disease: novel insights into pathogenesis and biomarker discovery

Bai, B., Vanderwall, D., Li, Y., Wang, X., Poudel, S., Wang, H., Dey, K. K., Chen, P., Yang, K., & Peng, J. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00474-z · Cited by 252 · see citing works

Mechanisms and pathology of protein misfolding and aggregation

Louros, N. N., Schymkowitz, J. W. H., & Rousseau, F. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00647-2 · Cited by 259 · see citing works

The Role of α-Synuclein Oligomers in Parkinson’s Disease

Du, X.-Y., Xie, X.-X., & Liu, R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228645 · Cited by 242 · see citing works

Amyloid-type Protein Aggregation and Prion-like Properties of Amyloids

Willbold, D., Strodel, B., Schroeder, G. F., Hoyer, W., & Heise, H. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00196 · Cited by 222 · see citing works

Disease-specific tau filaments assemble via polymorphic intermediates

Lövestam, S., Li, D., Wagstaff, J. L., Kotecha, A., Kimanius, D., McLaughlin, S. H., Murzin, A. G., Freund, S. M. V., Goedert, M., & Scheres, S. H. W. (2023) · Nature · doi:10.1038/s41586-023-06788-w · Cited by 202 · see citing works

Microglia-specific overexpression of α-synuclein leads to severe dopaminergic neurodegeneration by phagocytic exhaustion and oxidative toxicity

Bido, S., Muggeo, S., Massimino, L., Marzi, M. J., Giannelli, S. G., Melacini, E., Nannoni, M., Gambarè, D., Bellini, E., Ordazzo, G., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-26519-x · Cited by 190 · see citing works

Age-dependent formation of TMEM106B amyloid filaments in human brains

Schweighauser, M., Arseni, D., Bacioglu, M., Huang, M., Lövestam, S., Shi, Y., Yang, Y., Zhang, W., Kotecha, A., Garringer, H. J., et al. (2022) · Nature · doi:10.1038/s41586-022-04650-z · Cited by 194 · see citing works

Calcium Dyshomeostasis in Alzheimer’s Disease Pathogenesis

Cascella, R., & Cecchi, C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094914 · Cited by 189 · see citing works

Cryo-EM structures of tau filaments from Alzheimer’s disease with PET ligand APN-1607

Shi, Y., Murzin, A. G., Falcon, B., Epstein, A., Machin, J., Tempest, P. A., Newell, K. L., Vidal, R., Garringer, H. J., Sahara, N., et al. (2021) · Acta Neuropathologica · doi:10.1007/s00401-021-02294-3 · Cited by 184 · see citing works

Targeting autophagy, oxidative stress, and ER stress for neurodegenerative disease treatment

Esmaeili, Y., Yarjanli, Z., Paknia, F., Bidram, E., Łoś, M., Eshraghi, M., Klionsky, D. J., Ghavami, S., & Zarrabi, A. (2022) · Journal of Controlled Release · doi:10.1016/j.jconrel.2022.03.001 · Cited by 180 · see citing works

Innate immune activation in neurodegenerative diseases

Castro‐Gomez, S., & Heneka, M. T. (2024) · Immunity · doi:10.1016/j.immuni.2024.03.010 · Cited by 167 · see citing works

Past, present and future role of retinal imaging in neurodegenerative disease

Kashani, A. H., Asanad, S., Chan, J. W., Singer, M., Zhang, J., Sharifi, M., Khansari, M. M., Abdolahi, F., Shi, Y., Biffi, A., et al. (2021) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2020.100938 · Cited by 164 · see citing works

Connectome-based modelling of neurodegenerative diseases: towards precision medicine and mechanistic insight

Vogel, J. W., Corriveau‐Lecavalier, N., Franzmeier, N., Pereira, J. B., Brown, J. A., Maaß, A., Botha, H., Seeley, W. W., Bassett, D. S., Jones, D. T., et al. (2023) · Nature reviews. Neuroscience · doi:10.1038/s41583-023-00731-8 · Cited by 160 · see citing works

Insights into Manganese Superoxide Dismutase and Human Diseases

Liu, M., Sun, X., Chen, B., Dai, R., Xi, Z., & Xu, H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232415893 · Cited by 151 · see citing works

Exosomes in Parkinson disease

Pinnell, J. R., Cui, M., & Tieu, K. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15288 · Cited by 144 · see citing works

The interaction between ageing and Alzheimer's disease: insights from the hallmarks of ageing

Liu, Y., Tan, Y., Zhang, Z., Yi, M., Zhu, L., & Peng, W. (2024) · Translational Neurodegeneration · doi:10.1186/s40035-024-00397-x · Cited by 144 · see citing works

Tau Oligomers Neurotoxicity

Niewiadomska, G., Niewiadomski, W., Steczkowska, M., & Gąsiorowska, A. (2021) · Life · doi:10.3390/life11010028 · Cited by 132 · see citing works

lncRNA NEAT1: Key player in neurodegenerative diseases

Li, K., & Wang, Z. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101878 · Cited by 132 · see citing works

Human pluripotent-stem-cell-derived organoids for drug discovery and evaluation

Vandana, J. J., Manrique, C., Lacko, L. A., & Chen, S. (2023) · Cell stem cell · doi:10.1016/j.stem.2023.04.011 · Cited by 132 · see citing works

Amyloid-associated increases in soluble tau relate to tau aggregation rates and cognitive decline in early Alzheimer’s disease

(2022) · doi:10.1038/s41467-022-34129-4 · Cited by 128 · see citing works

Genetic and environmental factors in Alzheimer’s and Parkinson’s diseases and promising therapeutic intervention via fecal microbiota transplantation

Wang, H., Yang, F., Zhang, S., Xin, R., & Sun, Y. (2021) · npj Parkinson s Disease · doi:10.1038/s41531-021-00213-7 · Cited by 130 · see citing works

The Prion-Like Spreading of Alpha-Synuclein in Parkinson’s Disease: Update on Models and Hypotheses

Jan, A., Gonçalves, N. P., Vægter, C. B., Jensen, P. H., & Ferreira, N. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22158338 · Cited by 126 · see citing works

Performance of αSynuclein RT-QuIC in relation to neuropathological staging of Lewy body disease

Hall, S., Orru, C. D., Serrano, G. E., Galasko, D. R., Hughson, A. G., Groveman, B. R., Adler, C. H., Beach, T. G., Caughey, B. W., & Hansson, O. (2022) · Acta Neuropathologica Communications · doi:10.1186/s40478-022-01388-7 · Cited by 125 · see citing works

Conformational strains of pathogenic amyloid proteins in neurodegenerative diseases

Li, D., & Liu, C. (2022) · Nature reviews. Neuroscience · doi:10.1038/s41583-022-00603-7 · Cited by 122 · see citing works

Disease-Modifying Therapies for Alzheimer’s Disease: More Questions than Answers

Golde, T. E. (2022) · Neurotherapeutics · doi:10.1007/s13311-022-01201-2 · Cited by 119 · see citing works

Ageing promotes pathological alpha-synuclein propagation and autonomic dysfunction in wild-type rats

Berge, N. V. D., Ferreira, N., Mikkelsen, T. W., Alstrup, A. K. O., Tamgüney, G., Karlsson, P., Terkelsen, A. J., Nyengaard, J. R., Jensen, P. H., & Borghammer, P. (2021) · Brain · doi:10.1093/brain/awab061 · Cited by 121 · see citing works

Neuropathogenesis-on-chips for neurodegenerative diseases

Amartumur, S., Nguyen, H. M., Huynh, T., Kim, T. S., Woo, R., Oh, E., Kim, K. K., Lee, L. P., & Heo, C. (2024) · Nature Communications · doi:10.1038/s41467-024-46554-8 · Cited by 120 · see citing works

Macropinocytosis: Biology and mechanisms

Kay, R. R. (2021) · Cells and Development · doi:10.1016/j.cdev.2021.203713 · Cited by 112 · see citing works

Progression of grey and white matter brain damage in Parkinson's disease: a critical review of structural MRI literature

Sarasso, E., Agosta, F., Piramide, N., & Filippi, M. (2020) · Journal of Neurology · doi:10.1007/s00415-020-09863-8 · Cited by 115 · see citing works

Brain-targeted delivery shuttled by black phosphorus nanostructure to treat Parkinson's disease

Xiong, S., Li, Z., Liu, Y., Wang, Q., Luo, J., Chen, X., Xie, Z., Zhang, Y., Zhang, H., & Chen, T. (2020) · Biomaterials · doi:10.1016/j.biomaterials.2020.120339 · Cited by 113 · see citing works

Green Tea Epigallocatechin-3-gallate (EGCG) Targeting Protein Misfolding in Drug Discovery for Neurodegenerative Diseases

Gonçalves, P. B., Sodero, A. C. R., & Cordeiro, Y. (2021) · Biomolecules · doi:10.3390/biom11050767 · Cited by 115 · see citing works

Recent advances in the use of extracellular vesicles from adipose-derived stem cells for regenerative medical therapeutics

Yang, S., Sun, Y., & Yan, C. (2024) · Journal of Nanobiotechnology · doi:10.1186/s12951-024-02603-4 · Cited by 110 · see citing works

Small-Molecule Hydrophobic Tagging: A Promising Strategy of Druglike Technology for Targeted Protein Degradation

Xie, S., Zhu, J., Li, J., Zhan, F., Yao, H., Xu, J., & Xu, S. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00736 · Cited by 109 · see citing works

Lysosomal exocytosis releases pathogenic α-synuclein species from neurons in synucleinopathy models

Xie, Y. X., Naseri, N. N., Fels, J. A., Kharel, P., Na, Y., Lane, D., Burré, J., & Sharma, M. (2022) · Nature Communications · doi:10.1038/s41467-022-32625-1 · Cited by 107 · see citing works

α-Synuclein pathology as a target in neurodegenerative diseases

Park, H.-J., Kam, T., Dawson, V. L., & Dawson, T. M. (2024) · Nature Reviews Neurology · doi:10.1038/s41582-024-01043-w · Cited by 112 · see citing works

Therapeutics in the Pipeline Targeting α-Synuclein for Parkinson's Disease

Jasutkar, H. G., Oh, S. E., & Mouradian, M. M. (2022) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000133 · Cited by 102 · see citing works

Applications of brain organoids in neurodevelopment and neurological diseases

Sun, N., Meng, X., Liu, Y., Song, D., Jiang, C., & Cai, J. (2021) · Journal of Biomedical Science · doi:10.1186/s12929-021-00728-4 · Cited by 100 · see citing works

Creutzfeldt–Jakob disease and other prion diseases

Zerr, I., Ladogana, A., Mead, S., Hermann, P., Forloni, G., & Appleby, B. S. (2024) · Nature Reviews Disease Primers · doi:10.1038/s41572-024-00497-y · Cited by 106 · see citing works

Histone Methylation Regulation in Neurodegenerative Disorders

Basavarajappa, B. S., & Subbanna, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094654 · Cited by 99 · see citing works

CGG repeat RNA G-quadruplexes interact with FMRpolyG to cause neuronal dysfunction in fragile X-related tremor/ataxia syndrome

Asamitsu, S., Yabuki, Y., Ikenoshita, S., Kawakubo, K., Kawasaki, M., Usuki, S., Nakayama, Y., Adachi, K., Kugoh, H., Ishii, K., et al. (2021) · Science Advances · doi:10.1126/sciadv.abd9440 · Cited by 97 · see citing works

Hierarchical chemical determination of amyloid polymorphs in neurodegenerative disease

Li, D., & Liu, C. (2021) · Nature Chemical Biology · doi:10.1038/s41589-020-00708-z · Cited by 95 · see citing works

Brain connectomics: time for a molecular imaging perspective?

Sala, A., Lizarraga, A., Caminiti, S. P., Calhoun, V. D., Eickhoff, S. B., Habeck, C. G., Jamadar, S. D., Perani, D., Pereira, J. B., Veronese, M., et al. (2023) · Trends in Cognitive Sciences · doi:10.1016/j.tics.2022.11.015 · Cited by 91 · see citing works

Caspase-8 in inflammatory diseases: a potential therapeutic target

Zhang, W., Zhu, C., Liao, Y., Zhou, M., Xu, W., & Zou, Z. (2024) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-024-00646-x · Cited by 97 · see citing works

Intranasal Delivery of Mesenchymal Stem Cells-Derived Extracellular Vesicles for the Treatment of Neurological Diseases

Herman, S., Fishel, I., & Offen, D. (2021) · Stem Cells · doi:10.1002/stem.3456 · Cited by 92 · see citing works

Network structure and transcriptomic vulnerability shape atrophy in frontotemporal dementia

Shafiei, G., Bazinet, V., Dadar, M., Manera, A. L., Collins, D. L., Dagher, A., Borroni, B., Sánchez‐Valle, R., Moreno, F., Laforce, R. J., et al. (2022) · Brain · doi:10.1093/brain/awac069 · Cited by 86 · see citing works

Defining circadian disruption in neurodegenerative disorders

Colwell, C. S. (2021) · Journal of Clinical Investigation · doi:10.1172/jci148288 · Cited by 90 · see citing works

Alzheimer’s disease – the journey of a healthy brain into organ failure

Golde, T. E. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00523-1 · Cited by 90 · see citing works

Oral Nanomedicine: Challenges and Opportunities

Deng, B., Liu, S., Wang, Y., Ali, B., Kong, N., Xie, T., Koo, S., Ouyang, J., & Tao, W. (2023) · Advanced Materials · doi:10.1002/adma.202306081 · Cited by 87 · see citing works

Advanced nanomaterials as sample technique for bio-analysis

Sun, N., Yu, H., Wu, H., Shen, X., & Deng, C. (2021) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2020.116168 · Cited by 85 · see citing works

New Therapeutic Approaches to and Mechanisms of Ginsenoside Rg1 against Neurological Diseases

Sun, Y., Yang, Y., Liu, S., Yang, S., Chen, C., Lin, M., Zeng, Q., Long, J., Yao, J., Yi, F., et al. (2022) · Cells · doi:10.3390/cells11162529 · Cited by 81 · see citing works

Neuronal FAM171A2 mediates α-synuclein fibril uptake and drives Parkinson’s disease

Wu, K., Xu, Q., Liu, Y., Feng, Y., Han, S., Zhang, Y.-R., Chen, S.-D., Guo, Y. X., Wu, B., Ma, L., et al. (2025) · Science · doi:10.1126/science.adp3645 · Cited by 84 · see citing works

Doxycycline Inhibits α-Synuclein-Associated Pathologies in Vitro and in Vivo

Dominguez-Meijide, A., Parrales, V., Vasili, E., González-Lizárraga, F., König, A., Lázaro, D. F., Lannuzel, A., Haik, S., Del Bel, E., Chehín, R., et al. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105256 · Cited by 81 · see citing works

Extracellular vesicles in neuroinflammation: Pathogenesis, diagnosis, and therapy

Ruan, J., Miao, X., Schlüter, D., Li, L., & Wang, X. (2021) · Molecular Therapy · doi:10.1016/j.ymthe.2021.04.020 · Cited by 80 · see citing works

Medial Temporal Lobe Networks in Alzheimer's Disease: Structural and Molecular Vulnerabilities

de Florès, R., Das, S. R., Xie, L., Wisse, L. E. M., Lyu, X., Shah, P., Yushkevich, P. A., & Wolk, D. A. (2022) · Journal of Neuroscience · doi:10.1523/jneurosci.0949-21.2021 · Cited by 79 · see citing works

Tau fibrils induce nanoscale membrane damage and nucleate cytosolic tau at lysosomes

Rose, K. M., Jepson, T. A., Shukla, S., Maya-Romero, A., Kampmann, M., Xu, K., & Hurley, J. H. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2315690121 · Cited by 79 · see citing works

Extracellular vesicles and amyotrophic lateral sclerosis: from misfolded protein vehicles to promising clinical biomarkers

Gagliardi, D., Bresolin, N., Comi, G. P., & Corti, S. P. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03619-3 · Cited by 78 · see citing works

Self‐Catalytic Small Interfering RNA Nanocarriers for Synergistic Treatment of Neurodegenerative Diseases

Ji, W., Li, Y., Peng, H., Zhao, R., Shen, J., Wu, Y., Wang, J., Hao, Q., Lü, Z., Yang, J., et al. (2021) · Advanced Materials · doi:10.1002/adma.202105711 · Cited by 79 · see citing works

The extracellular chaperone Clusterin enhances Tau aggregate seeding in a cellular model

Yuste‐Checa, P., Trinkaus, V. A., Riera-Tur, I., Imamoglu, R., Schaller, T., Wang, H., Dudanova, I., Hipp, M. S., Bracher, A., & Hartl, F. U. (2021) · Nature Communications · doi:10.1038/s41467-021-25060-1 · Cited by 77 · see citing works

Where and how alpha‐synuclein pathology spreads in Parkinson’s disease:

Wakabayashi, K. (2020) · Neuropathology · doi:10.1111/neup.12691 · Cited by 74 · see citing works

Propagation of tau and α-synuclein in the brain: therapeutic potential of the glymphatic system

Lopes, D. M., Llewellyn, S. K., & Harrison, I. F. (2022) · Translational Neurodegeneration · doi:10.1186/s40035-022-00293-2 · Cited by 74 · see citing works

Proteotoxic Stress and Cell Death in Cancer Cells

Brancolini, C., & Iuliano, L. (2020) · Cancers · doi:10.3390/cancers12092385 · Cited by 70 · see citing works

Multivalent Aptamer‐Based Lysosome‐Targeting Chimeras (LYTACs) Platform for Mono‐ or Dual‐Targeted Proteins Degradation on Cell Surface

Duan, Q., Jia, H., Chen, W., Qin, C., Zhang, K., Jia, F., Fu, T., Wei, Y., Fan, M., Wu, Q., et al. (2024) · Advanced Science · doi:10.1002/advs.202308924 · Cited by 71 · see citing works

Detecting Early Cognitive Decline in Alzheimer’s Disease with Brain Synaptic Structural and Functional Evaluation

Ribarič, S. (2023) · Biomedicines · doi:10.3390/biomedicines11020355 · Cited by 66 · see citing works

Circadian clock protein BMAL1 broadly influences autophagy and endolysosomal function in astrocytes

McKee, C. A., Polino, A. J., King, M. W., & Musiek, E. S. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2220551120 · Cited by 68 · see citing works

The Human Hippocampus in Parkinson’s Disease: An Integrative Stereological and Proteomic Study

Villar‐Conde, S., Astillero‐Lopez, V., González-Rodríguez, M., Villanueva‐Anguita, P., Saiz‐Sánchez, D., Martı́nez-Marcos, A., Flores‐Cuadrado, A., & Úbeda‐Bañón, I. (2021) · Journal of Parkinson s Disease · doi:10.3233/jpd-202465 · Cited by 67 · see citing works

Extracellular vesicles in the treatment of neurological disorders

Reed, S. L., & Escayg, A. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105445 · Cited by 65 · see citing works

α-Synuclein in Parkinson's disease and advances in detection

Chen, R., Gu, X., & Wang, X. (2022) · Clinica Chimica Acta · doi:10.1016/j.cca.2022.02.006 · Cited by 67 · see citing works

Phosphorylation and O-GlcNAcylation at the same α-synuclein site generate distinct fibril structures

Hu, J., Xia, W., Zeng, S., Lim, Y., Tao, Y., Sun, Y., Zhao, L., Wang, H., Le, W., Li, D., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-46898-1 · Cited by 66 · see citing works

Targeting tau in Alzheimer's disease: from mechanisms to clinical therapy

Ye, J., Wan, H., Chen, S., & Liu, G. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.385847 · Cited by 69 · see citing works

Current Trends of Raman Spectroscopy in Clinic Settings: Opportunities and Challenges

Wang, Y., Fang, L., Wang, Y., & Xiong, Z. (2023) · Advanced Science · doi:10.1002/advs.202300668 · Cited by 68 · see citing works

The S1P–S1PR Axis in Neurological Disorders—Insights into Current and Future Therapeutic Perspectives

Lucaciu, A., Brunkhorst, R., Pfeilschifter, J. M., Pfeilschifter, W., & Subburayalu, J. (2020) · Cells · doi:10.3390/cells9061515 · Cited by 65 · see citing works

Developing Therapies for Neurodegenerative Disorders: Insights from Protein Aggregation and Cellular Stress Responses

Mallucci, G. R., Klenerman, D., & Rubinsztein, D. C. (2020) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-040320-120625 · Cited by 62 · see citing works

Molecular mechanisms of amyloid formation in living systems

Sinnige, T. (2022) · Chemical Science · doi:10.1039/d2sc01278b · Cited by 64 · see citing works

Proteostasis failure exacerbates neuronal circuit dysfunction and sleep impairments in Alzheimer’s disease

Morrone, C. D., Raghuraman, R., Hussaini, S. A., & Yu, W. H. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00617-4 · Cited by 64 · see citing works

Exosomes in brain diseases: Pathogenesis and therapeutic targets

Si, Q., Wu, L., Pang, D., & Jiang, P. (2023) · MedComm · doi:10.1002/mco2.287 · Cited by 63 · see citing works

Particulate matter exposure and neurodegenerative diseases: A comprehensive update on toxicity and mechanisms

Lee, J., Weerasinghe-Mudiyanselage, P. D. E., Kim, B., Kang, S., Kim, J., & Moon, C. (2023) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2023.115565 · Cited by 63 · see citing works

Inefficient quality control of ribosome stalling during APP synthesis generates CAT-tailed species that precipitate hallmarks of Alzheimer’s disease

Rimal, S., Li, Y., Vartak, R. S., Geng, J., Tantray, I., Li, S., Huh, S., Vogel, H. S., Glabe, C. G., Grinberg, L. T., et al. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01268-6 · Cited by 59 · see citing works

Soluble endogenous oligomeric α-synuclein species in neurodegenerative diseases: Expression, spreading, and cross-talk

Kayed, R., Dettmer, U., & Lesné, S. (2020) · Journal of Parkinson s Disease · doi:10.3233/jpd-201965 · Cited by 62 · see citing works

Secreted Chaperones in Neurodegeneration

Chaplot, K., Jarvela, T. S., & Lindberg, I. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00268 · Cited by 59 · see citing works

cGAS-STING signaling in brain aging and neurodegeneration: molecular links and therapeutic perspectives

Li, H., Cai, R., Zhou, Y., Jiang, Y., & Tan, S. (2025) · Journal of Neuroinflammation · doi:10.1186/s12974-025-03563-8 · Cited by 70 · see citing works

Alpha-synuclein oligomers and small nerve fiber pathology in skin are potential biomarkers of Parkinson’s disease

Vacchi, E., Senese, C., Chiaro, G., Disanto, G., Pinton, S., Morandi, S., Bertaina, I., Bianco, G., Staedler, C., Galati, S., et al. (2021) · npj Parkinson s Disease · doi:10.1038/s41531-021-00262-y · Cited by 59 · see citing works

Co-opting templated aggregation to degrade pathogenic tau assemblies and improve motor function

Miller, L. V. C., Papa, G., Vaysburd, M., Cheng, S., Sweeney, P. W., Smith, A. N., Franco, C. D. M. F., Katsinelos, T., Huang, M., Sanford, S., et al. (2024) · Cell · doi:10.1016/j.cell.2024.08.024 · Cited by 58 · see citing works

Neurodegeneration and Astrogliosis in the Human CA1 Hippocampal Subfield Are Related to hsp90ab1 and bag3 in Alzheimer’s Disease

González-Rodríguez, M., Villar‐Conde, S., Astillero‐Lopez, V., Villanueva‐Anguita, P., Úbeda‐Bañón, I., Flores‐Cuadrado, A., Martı́nez-Marcos, A., & Saiz‐Sánchez, D. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms23010165 · Cited by 57 · see citing works

The Cell Biology of Tau Secretion

Merezhko, M., Uronen, R., & Huttunen, H. J. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.569818 · Cited by 57 · see citing works

Extracellular vesicles and Alzheimer’s disease in the novel era of Precision Medicine: implications for disease progression, diagnosis and treatment

Gomes, P., Tzouanou, F., Skolariki, K., Vamvaka-Iakovou, A., Nogueras‐Ortiz, C. J., Tsirtsaki, K., Waites, C. L., Vlamos, P., Sousa, N., Costa‐Silva, B., et al. (2022) · Experimental Neurology · doi:10.1016/j.expneurol.2022.114183 · Cited by 57 · see citing works

Molecular mechanisms in Alzheimer's disease and the impact of physical exercise with advancements in therapeutic approaches

Siddappaji, K. K., & Gopal, S. (2021) · AIMS neuroscience · doi:10.3934/neuroscience.2021020 · Cited by 57 · see citing works

Protein amyloid aggregate: Structure and function

Xu, Q., Ma, Y., Sun, Y., Li, D., Zhang, X., & Liu, C. (2023) · Aggregate · doi:10.1002/agt2.333 · Cited by 56 · see citing works

Cognitive heterogeneity in Parkinson’s disease: A mechanistic view

Carceles‐Cordon, M., Weintraub, D., & Chen‐Plotkin, A. S. (2023) · Neuron · doi:10.1016/j.neuron.2023.03.021 · Cited by 58 · see citing works

Highly BBB-permeable nanomedicine reverses neuroapoptosis and neuroinflammation to treat Alzheimer's disease

Xie, A., Cheng, G., Wu, J., Li, Z., Yu, G., Zhu, X., & Chen, T. (2024) · Biomaterials · doi:10.1016/j.biomaterials.2024.122749 · Cited by 56 · 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

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

Transcellular transmission and molecular heterogeneity of aggregation-prone proteins in neurodegenerative diseases

Lee, E., Park, H., & Kim, S. (2024) · Molecules and Cells · doi:10.1016/j.mocell.2024.100089 · Cited by 11 · see citing works

Prion-like Spreading of Protein Aggregation in Neurodegenerative Diseases

Vaquer‐Alicea, J., & Diamond, M. I. (2016) · Cited by 1 · see citing works

Protein aggregate spreading in neurodegenerative diseases: Problems and perspectives

Lee, S., Lim, H.-S., Masliah, E., & Lee, H.-J. (2011) · Neuroscience Research · doi:10.1016/j.neures.2011.05.008 · Cited by 180 · see citing works