α-synuclein toxicity in neurodegeneration: mechanism and therapeutic strategies
Open accessAbstract
Alterations in α-synuclein dosage lead to familial Parkinson's disease (PD), and its accumulation results in synucleinopathies that include PD, dementia with Lewy bodies (DLB) and multiple system atrophy (MSA). Furthermore, α-synuclein contributes to the fibrilization of amyloid-b and tau, two key proteins in Alzheimer's disease, which suggests a central role for α-synuclein toxicity in neurodegeneration. Recent studies of factors contributing to α-synuclein toxicity and its disruption of downstream cellular pathways have expanded our understanding of disease pathogenesis in synucleinopathies. In this Review, we discuss these emerging themes, including the contributions of aging, selective vulnerability and non-cell-autonomous factors such as α-synuclein cell-to-cell propagation and neuroinflammation. Finally, we summarize recent efforts toward the development of targeted therapies for PD and related synucleinopathies.
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Accumulation of propagated α-synuclein results in synucleinopathies, including PD, DLB, and multiple system atrophy.
“Accumulation of propagated α-synuclein results in synucleinopathies, including PD, DLB, and multiple system atrophy [137].”
From Degradation of Tyrosine Hydroxylase by the Ubiquitin-Proteasome System in the Pathogenesis of Parkinson’s Disease and Dopa-Responsive Dystonia (2020) · cites this paper as [137]
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2 retracted
Masliah, E., Rockenstein, E. M., Mante, M., Crews, L. A., Spencer, B. J., Adame, A., Patrick, C., Trejo, M., Ubhi, K. K., Rohn, T. T., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0019338 · Cited by 422 · see citing works
RetractedRETRACTED: Soluble α-Synuclein Is a Novel Modulator of Alzheimer's Disease Pathophysiology
Larson, M. E., Sherman, M. A., Greimel, S., Kuskowski, M., Schneider, J. A., Bennett, D. A., & Lesné, S. E. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.0581-12.2012 · Cited by 128 · see citing works
RetractedStaging 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
Oxidants, oxidative stress and the biology of ageing
Finkel, T., & Holbrook, N. J. (2000) · Nature · doi:10.1038/35041687 · Cited by 9,413 · see citing works
Spillantini, M. G., Schmidt, M. L., Lee, V. M.-Y., Trojanowski, J. Q., Jakes, R., & Goedert, M. (1997) · Nature · doi:10.1038/42166 · Cited by 8,382 · see citing works
Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease
Polymeropoulos, M. H., Lavedan, C., Leroy, E., Ide, S. E., Dehejia, A., Dutra, A., Pike, B., Root, H., Rubenstein, J., Boyer, R., et al. (1997) · Science · doi:10.1126/science.276.5321.2045 · Cited by 8,240 · see citing works
Kalia, L. V., & Lang, A. E. (2015) · The Lancet · doi:10.1016/s0140-6736(14)61393-3 · Cited by 6,412 · see citing works
α-Synuclein Locus Triplication Causes Parkinson's Disease
Singleton, A. B., Farrer, M., Johnson, J., Singleton, A., Hague, S., Kachergus, J., Hulihan, M., Peuralinna, T., Dutra, A., Nussbaum, R., et al. (2003) · Science · doi:10.1126/science.1090278 · Cited by 4,383 · see citing works
AlaSOPro mutation in the gene encoding α-synuclein in Parkinson's disease
Krüger, R., Kuhn, W., Müller, T., Woitalla, D., Graeber, M., Kösel, S., Przuntek, H., Epplen, J. T., Schols, L., & Riess, O. (1998) · Nature Genetics · doi:10.1038/ng0298-106 · Cited by 3,836 · see citing works
Mitochondria: In Sickness and in Health
Nunnari, J., & Suomalainen, A. (2012) · Cell · doi:10.1016/j.cell.2012.02.035 · Cited by 3,479 · see citing works
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
Mutations in LRRK2 Cause Autosomal-Dominant Parkinsonism with Pleomorphic Pathology
Zimprich, A. A., Biskup, S., Leitner, P., Lichtner, P., Farrer, M. J., Lincoln, S., Kachergus, J. M., Hulihan, M., Uitti, R. J., Calne, D. B., et al. (2004) · Neuron · doi:10.1016/j.neuron.2004.11.005 · Cited by 3,024 · see citing works
The new mutation, E46K, of α‐synuclein causes parkinson and Lewy body dementia
Zarranz, J. J., Alegre, J., Gómez‐Esteban, J. C., Lezcano, E., Ros, R., Ampuero, I., Vidal, L., Hoenicka, J., Rodriguez, O., Atarés, B., et al. (2004) · Annals of Neurology · doi:10.1002/ana.10795 · Cited by 2,737 · see citing works
Luk, K. C., Kehm, V., Carroll, J., Zhang, B., O’Brien, P., Trojanowski, J. Q., & Lee, V. M.-Y. (2012) · Science · doi:10.1126/science.1227157 · Cited by 2,563 · see citing works
Cloning of the Gene Containing Mutations that Cause PARK8-Linked Parkinson's Disease
Paisán‐Ruiz, C., Jain, S., Evans, E. W., Gilks, W. P., Simón, J., van der Brug, M., de Munaín, A. L., Aparicio, S. F., Gil, A. M., Khan, N. L., et al. (2004) · Neuron · doi:10.1016/j.neuron.2004.10.023 · Cited by 2,416 · see citing works
Multicenter Analysis of Glucocerebrosidase Mutations in Parkinson's Disease
Sidransky, E., Nalls, M. A., Aasly, J. O., Aharon-Peretz, J., Annesi, G., Barbosa, E. R., Bar-Shira, A., Berg, D., Bras, J., Brice, A., et al. (2009) · New England Journal of Medicine · doi:10.1056/nejmoa0901281 · Cited by 2,135 · see citing works
α-synuclein locus duplication as a cause of familial Parkinson's disease
Chartier-Harlin, M.-C., Kachergus, J., Roumier, C., Mouroux, V., Douay, X., Lincoln, S., Levecque, C., Larvor, L., Andrieux, J., Hulihan, M., et al. (2004) · The Lancet · doi:10.1016/s0140-6736(04)17103-1 · Cited by 2,029 · see citing works
Impaired Degradation of Mutant α-Synuclein by Chaperone-Mediated Autophagy
Cuervo, A. M., Stefanis, L., Fredenburg, R., Lansbury, P. T., & Sulzer, D. (2004) · Science · doi:10.1126/science.1101738 · Cited by 2,024 · see citing works
Genome-wide association study reveals genetic risk underlying Parkinson's disease
Simón‐Sánchez, J., Schulte, C., Brás, J., Sharma, M., Gibbs, J. R., Berg, D., Paisán‐Ruiz, C., Lichtner, P., Scholz, S. W., Hernandez, D. G., et al. (2009) · Nature Genetics · doi:10.1038/ng.487 · Cited by 1,916 · see citing works
International Parkinson's Disease Genomics Consortium (IPDGC), Nalls, M. A., Parkinson's Study Group (PSG) Parkinson's Research: The Organized GENetics Initiative (PROGENI), 23andMe, GenePD, NeuroGenetics Research Consortium (NGRC), Hussman Institute of Human Genomics (HIHG), Investigator, T. A. J. D., (CHARGE), C. F. H. A. A. R. I. G. E., North American Brain Expression Consortium (NABEC), et al. (2014) · Nature Genetics · doi:10.1038/ng.3043 · Cited by 1,895 · see citing works
Li, J.-Y., Englund, E., Holton, J. L., Soulet, D., Hagell, P., Lees, A. J., Lashley, T., Quinn, N. P., Rehncrona, S., Björklund, A., et al. (2008) · Nature Medicine · doi:10.1038/nm1746 · Cited by 1,845 · see citing works
α-Synuclein Promotes SNARE-Complex Assembly in Vivo and in Vitro
Burré, J., Sharma, M., Tsetsenis, T., Buchman, V. L., Etherton, M. R., & Südhof, T. C. (2010) · Science · doi:10.1126/science.1195227 · Cited by 1,817 · see citing works
Masliah, E., Rockenstein, E. M., Veinbergs, I., Mallory, M. E., Hashimoto, M., Takeda, A., Sagara, Y., Sisk, A., & Mucke, L. (2000) · Science · doi:10.1126/science.287.5456.1265 · Cited by 1,763 · see citing works
Alzheimer Mechanisms and Therapeutic Strategies
Huang, Y., & Mucke, L. (2012) · Cell · doi:10.1016/j.cell.2012.02.040 · Cited by 1,758 · 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
Mice Lacking α-Synuclein Display Functional Deficits in the Nigrostriatal Dopamine System
Abeliovich, A., Schmitz, Y., Fariñas, I., Choi-Lundberg, D., Ho, W.-H., Castillo, P. E., Shinsky, N., Verdugo, J. M. G., Armanini, M., Ryan, A., et al. (2000) · Neuron · doi:10.1016/s0896-6273(00)80886-7 · Cited by 1,722 · see citing works
Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal
Maroteaux, L., Campanelli, J., & Scheller, R. (1988) · Journal of Neuroscience · doi:10.1523/jneurosci.08-08-02804.1988 · Cited by 1,646 · see citing works
Stabilization of α-Synuclein Secondary Structure upon Binding to Synthetic Membranes
Davidson, W. S., Jonas, A., Clayton, D. F., & George, J. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.16.9443 · Cited by 1,588 · see citing works
Bender, A., Krishnan, K. J., Morris, C. M., Taylor, G. A., Reeve, A. K., Perry, R. H., Jaros, E., Hersheson, J. S., Betts, J., Klopstock, T., et al. (2006) · Nature Genetics · doi:10.1038/ng1769 · Cited by 1,570 · see citing works
Volpicelli-Daley, L. A., Luk, K. C., Patel, T. P., Tanik, S. A., Riddle, D. M., Stieber, A., Meaney, D. F., Trojanowski, J. Q., & Lee, V. M.-Y. (2011) · Neuron · doi:10.1016/j.neuron.2011.08.033 · Cited by 1,569 · see citing works
Giasson, B. I., Duda, J. E., Murray, I. V. J., Chen, Q., Souza, J. M., Hurtig, H. I., Ischiropoulos, H., Trojanowski, J. Q., & Lee, V. M. ‐. (2000) · Science · doi:10.1126/science.290.5493.985 · Cited by 1,551 · see citing works
Conway, K. A., Lee, S., Rochet, J., Ding, T. T., Williamson, R. E., & Lansbury, P. T. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.2.571 · Cited by 1,543 · see citing works
NACP, A Protein Implicated in Alzheimer's Disease and Learning, Is Natively Unfolded
Weinreb, P. H., Zhen, W., Poon, A. W., Conway, K. A., & Lansbury, P. T. (1996) · Biochemistry · doi:10.1021/bi961799n · Cited by 1,524 · 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 1,494 · 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
α-Synuclein Blocks ER-Golgi Traffic and Rab1 Rescues Neuron Loss in Parkinson's Models
Cooper, A. A., Gitler, A. D., Cashikar, A. G., Haynes, C. M., Hill, K. J., Bhullar, B., Liu, K., Xu, K., Strathearn, K. E., Liu, F., et al. (2006) · Science · doi:10.1126/science.1129462 · Cited by 1,377 · see citing works
Mazzulli, J. R., Xu, Y.-H., Sun, Y., Knight, A. L., McLean, P. J., Caldwell, G. A., Sidransky, E., Grabowski, G. A., & Krainc, D. (2011) · Cell · doi:10.1016/j.cell.2011.06.001 · Cited by 1,341 · see citing works
Self-citationIwai, 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
Melanized dopaminergic neurons are differentially susceptible to degeneration in Parkinson's disease
Hirsch, E., Graybiel, A. M., & Agid, Y. A. (1988) · Nature · doi:10.1038/334345a0 · Cited by 1,301 · see citing works
α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation
Bartels, T., Choi, J. G., & Selkoe, D. J. (2011) · Nature · doi:10.1038/nature10324 · Cited by 1,263 · see citing works
Chaperone Suppression of α-Synuclein Toxicity in a <i>Drosophila</i> Model for Parkinson's Disease
Auluck, P. K., Chan, H. Y. E., Trojanowski, J. Q., Lee, V. M.-Y., & Bonini, N. M. (2002) · Science · doi:10.1126/science.1067389 · Cited by 1,227 · 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
Kinetic Stabilization of the α-Synuclein Protofibril by a Dopamine-α-Synuclein Adduct
Conway, K. A., Rochet, J.-C., Bieganski, R. M., & Lansbury, P. T. (2001) · Science · doi:10.1126/science.1063522 · Cited by 1,127 · see citing works
Emmanouilidou, E., Melachroinou, K., Roumeliotis, T., Garbis, S. D., Ntzouni, M., Margaritis, L. H., Stefanis, L., & Vekrellis, K. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.5699-09.2010 · Cited by 1,115 · see citing works
Sirtuin 2 Inhibitors Rescue α-Synuclein-Mediated Toxicity in Models of Parkinson's Disease
Outeiro, T. F., Kontopoulos, E., Altmann, S. M., Kufareva, I., Strathearn, K. E., Amore, A. M., Volk, C. B., Maxwell, M. M., Rochet, J., McLean, P. J., et al. (2007) · Science · doi:10.1126/science.1143780 · Cited by 1,066 · see citing works
Nemani, V. M., Lü, W., Berge‐Seidl, V., Nakamura, K., Onoa, B., Lee, M. K., Chaudhry, F. A., Nicoll, R. A., & Edwards, R. H. (2010) · Neuron · doi:10.1016/j.neuron.2009.12.023 · Cited by 1,051 · see citing works
Spillantini, M. G., Crowther, R. A., Jakes, R., Cairns, N. J., Lantos, P. L., & Goedert, M. (1998) · Neuroscience Letters · doi:10.1016/s0304-3940(98)00504-7 · Cited by 1,026 · see citing works
α-Synuclein Cooperates with CSPα in Preventing Neurodegeneration
Chandra, S. S., Gallardo, G., Fernández‐Chacón, R., Schlüter, O. M., & Südhof, T. C. (2005) · Cell · doi:10.1016/j.cell.2005.09.028 · Cited by 967 · see citing works
Luk, K. C., Song, C., O’Brien, P., Stieber, A., Branch, J. R., Brunden, K. R., Trojanowski, J. Q., & Lee, V. M. ‐. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908005106 · Cited by 957 · see citing works
Structure and function of ER membrane contact sites with other organelles
Phillips, M. J., & Voeltz, G. K. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2015.8 · Cited by 933 · see citing works
Direct Observation of the Interconversion of Normal and Toxic Forms of α-Synuclein
Cremades, N., Cohen, S. I. A., Deas, E., Abramov, A. Y., Chen, A. Y., Orte, Á., Sandal, M., Clarke, R. W., Dunne, P., Aprile, F. A., et al. (2012) · Cell · doi:10.1016/j.cell.2012.03.037 · Cited by 901 · see citing works
Structural and functional characterization of two alpha-synuclein strains
Bousset, L., Pieri, L., Ruiz-Arlandis, G., Gath, J., Jensen, P. H., Habenstein, B., Madiona, K., Oliéric, V., Böckmann, A., Meier, B. H., et al. (2013) · Nature Communications · doi:10.1038/ncomms3575 · Cited by 890 · see citing works
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
Lee, H.-J., Suk, J.-E., Patrick, C., Bae, E.-J., Cho, J.-H., Rho, S., Hwang, D., Masliah, E., & Lee, S.-J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.081125 · Cited by 877 · see citing works
Structural disorder of monomeric α-synuclein persists in mammalian cells
Theillet, F., Binolfi, A., Bekei, B., Martorana, A., Rose, H. M., Stuiver, M., Verzini, S., Lorenz, D., van Rossum, M., Goldfarb, D., et al. (2016) · Nature · doi:10.1038/nature16531 · Cited by 877 · see citing works
Cabin, D. E., Shimazu, K., Murphy, D., Cole, N. B., Gottschalk, W., McIlwain, K. L., Orrison, B., Chen, A., Ellis, C. E., Paylor, R., et al. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-20-08797.2002 · Cited by 865 · see citing works
Kim, C., Ho, D.-H., Suk, J.-E., You, S., Michael, S., Kang, J., Joong Lee, S., Masliah, E., Hwang, D., Lee, H.-J., et al. (2013) · Nature Communications · doi:10.1038/ncomms2534 · Cited by 856 · see citing works
PGC-1 α, A Potential Therapeutic Target for Early Intervention in Parkinson’s Disease
Zheng, B., Liao, Z., Locascio, J. J., Lesniak, K. A., Roderick, S. S., Watt, M. L., Eklund, A. C., Zhang‐James, Y., Kim, P. D., Hauser, M. A., et al. (2010) · Science Translational Medicine · doi:10.1126/scitranslmed.3001059 · Cited by 854 · 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
Microglial activation and dopamine terminal loss in early Parkinson's disease
Ouchi, Y., Yoshikawa, E., Sekine, Y., Futatsubashi, M., Kanno, T., Ogusu, T., & Torizuka, T. (2005) · Annals of Neurology · doi:10.1002/ana.20338 · Cited by 846 · see citing works
Fanciulli, A., & Wenning, G. K. (2015) · New England Journal of Medicine · doi:10.1056/nejmra1311488 · Cited by 827 · see citing works
Bendor, J. T., Logan, T. P., & Edwards, R. H. (2013) · Neuron · doi:10.1016/j.neuron.2013.09.004 · Cited by 825 · see citing works
α-Synuclein impairs macroautophagy: implications for Parkinson’s disease
Winslow, A. R., Chen, C.-W., Corrochano, S., Acevedo-Arozena, A., Gordon, D. E., Peden, A. A., Lichtenberg, M., Menzies, F. M., Ravikumar, B., Imarisio, S., et al. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201003122 · Cited by 825 · see citing works
Yeast Cells Provide Insight into Alpha-Synuclein Biology and Pathobiology
Outeiro, T. F., & Lindquist, S. L. (2003) · Science · doi:10.1126/science.1090439 · Cited by 808 · 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
Hamza, T. H., Zabetian, C. P., Tenesa, A., Laederach, A., Montimurro, J. S., Yearout, D., Kay, D. M., Doheny, K. F., Paschall, J. E., Pugh, E., et al. (2010) · Nature Genetics · doi:10.1038/ng.642 · Cited by 784 · see citing works
Murphy, D. D., Rueter, S. M., Trojanowski, J. Q., & Lee, V. M. ‐. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-09-03214.2000 · Cited by 753 · see citing works
TFEB-mediated autophagy rescues midbrain dopamine neurons from α-synuclein toxicity
Decressac, M., Mattsson, B., Weikop, P., Lundblad, M., Jakobsson, J., & Björklund, A. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1305623110 · Cited by 753 · see citing works
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
G51D α‐synuclein mutation causes a novel Parkinsonian–pyramidal syndrome
Lesage, S., Anheim, M., Letournel, F., Bousset, L., Honoré, A., Rozas, N., Pieri, L., Madiona, K., Dürr, A., Melki, R., et al. (2013) · Annals of Neurology · doi:10.1002/ana.23894 · Cited by 697 · see citing works
The role of protein clearance mechanisms in organismal ageing and age-related diseases
Vı́lchez, D., Sáez, I., & Dillin, A. G. (2014) · Nature Communications · doi:10.1038/ncomms6659 · Cited by 684 · see citing works
Martin, L. J., Pan, Y., Price, A. C., Sterling, W., Copeland, N. G., Jenkins, N. A., Price, D. L., & Lee, M. K. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.4308-05.2006 · Cited by 684 · see citing works
Distinct α-Synuclein Strains Differentially Promote Tau Inclusions in Neurons
Guo, J. L., Covell, D. J., Daniels, J. P., Iba, M., Stieber, A., Zhang, B., Riddle, D. M., Kwong, L. K., Xu, Y., Trojanowski, J. Q., et al. (2013) · Cell · doi:10.1016/j.cell.2013.05.057 · Cited by 680 · see citing works
Evidence for α-synuclein prions causing multiple system atrophy in humans with parkinsonism
Prusiner, S. B., Woerman, A. L., Mordes, D. A., Watts, J. C., Rampersaud, R., Berry, D. B., Patel, S. S., Oehler, A., Lowe, J. K., Kravitz, S. N., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1514475112 · Cited by 679 · see citing works
Alpha‐synuclein p.H50Q, a novel pathogenic mutation for Parkinson's disease
Appel‐Cresswell, S., Vilariño‐Güell, C., Encarnacion, M. J., Sherman, H. E., Yu, I. S., Shah, B., Weir, D. M., Thompson, C., Szu‐Tu, C., Trinh, J., et al. (2013) · Movement Disorders · doi:10.1002/mds.25421 · Cited by 669 · see citing works
Buell, A. K., Galvagnion, C., Gaspar, R., Sparr, E., Vendruscolo, M., Knowles, T. P. J., Linse, S. S., & Dobson, C. M. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1315346111 · Cited by 666 · see citing works
Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation
Galvagnion, C., Buell, A. K., Meisl, G., Michaels, T. C. T., Vendruscolo, M., Knowles, T. P. J., & Dobson, C. M. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1750 · Cited by 661 · see citing works
Kahle, P. J., Neumann, M., Ozmen, L., Müller, V., Jacobsen, H., Schindzielorz, A., Okochi, M., Leimer, U., van der Putten, H., Probst, A., et al. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-17-06365.2000 · Cited by 641 · see citing works
Dopamine-modified α-synuclein blocks chaperone-mediated autophagy
Martínez‐Vicente, M., Tallóczy, Z., Kaushik, S., Massey, A. C., Mazzulli, J. R., Mosharov, E. V., Hodara, R., Fredenburg, R. A., Wu, D.-C., Follenzi, A., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci32806 · Cited by 633 · see citing works
Structure of the toxic core of α-synuclein from invisible crystals
Rodríguez, J. A., Ivanova, M. I., Sawaya, M. R., Cascio, D., Reyes, F. E., Shi, D., Sangwan, S., Guenther, E. L., Johnson, L. M., Zhang, M., et al. (2015) · Nature · doi:10.1038/nature15368 · Cited by 629 · see citing works
α-Synuclein binds to TOM20 and inhibits mitochondrial protein import in Parkinson’s disease
Di Maio, R., Barrett, P. J., Hoffman, E. K., Barrett, C. W., Zharikov, A., Borah, A., Hu, X., McCoy, J., Chu, C. T., Burton, E. A., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aaf3634 · Cited by 619 · see citing works
Chen, L., & Feany, M. Β. (2005) · Nature Neuroscience · doi:10.1038/nn1443 · Cited by 614 · see citing works
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
Nakamura, K., Nemani, V., Azarbal, F., Skibinski, G., Levy, J. M., Egami, K., Munishkina, L. A., Zhang, J., Gardner, B. M., Wakabayashi, J., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.213538 · Cited by 590 · see citing works
Resistance of α-synuclein null mice to the parkinsonian neurotoxin MPTP
Dauer, W. T., Kholodilov, N. G., Vila, M., Trillat, A., Goodchild, R. E., Larsen, K. E., Staal, R. G. W., Tieu, K., Schmitz, Y., Yuan, C. A., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.172514599 · Cited by 580 · see citing works
Sharon, R., Bar-Joseph, I., Frosch, M. P., Walsh, D. M., Hamilton, J. A., & Selkoe, D. J. (2003) · Neuron · doi:10.1016/s0896-6273(03)00024-2 · Cited by 562 · 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
α-synuclein acts in the nucleus to inhibit histone acetylation and promote neurotoxicity
Kontopoulos, E., Parvin, J. D., & Feany, M. Β. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl243 · Cited by 539 · see citing works
Pasanen, P., Myllykangas, L., Siitonen, M., Raunio, A., Kaakkola, S., Lyytinen, J., Tienari, P. J., Pöyhönen, M., & Paetau, A. E. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.03.024 · Cited by 535 · see citing works
Gitler, A. D., Chesi, A., Geddie, M. L., Strathearn, K. E., Hamamichi, S., Hill, K. J., Caldwell, K. A., Caldwell, G. A., Cooper, A. A., Rochet, J., et al. (2009) · Nature Genetics · doi:10.1038/ng.300 · Cited by 535 · see citing works
Mosharov, E. V., Larsen, K. E., Kanter, E., Phillips, K. A., Wilson, K., Schmitz, Y., Krantz, D. E., Kobayashi, K., Edwards, R. H., & Sulzer, D. L. (2009) · Neuron · doi:10.1016/j.neuron.2009.01.033 · Cited by 530 · see citing works
The Parkinson's disease protein α-synuclein disrupts cellular Rab homeostasis
Gitler, A. D., Bevis, B. J., Shorter, J., Strathearn, K. E., Hamamichi, S., Su, L. J., Caldwell, K. A., Caldwell, G. A., Rochet, J., McCaffery, J. M., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0710685105 · Cited by 527 · see citing works
Lin, X. Z., Parisiadou, L., Gu, X., Wang, L., Shim, H., Sun, L., Xie, C., Long, C.-X., Yang, W.-J., Ding, J., et al. (2009) · Neuron · doi:10.1016/j.neuron.2009.11.006 · Cited by 513 · see citing works
Systemic exosomal siRNA delivery reduced alpha‐synuclein aggregates in brains of transgenic mice
Cooper, J. A. D., Wiklander, O. P. B., Nordin, J. Z., Al‐Shawi, R., Wood, M. J. A., Vithlani, M., Schapira, A. H. V., Simons, J. P., Andaloussi, S. E., & Alvarez‐Erviti, L. (2014) · Movement Disorders · doi:10.1002/mds.25978 · Cited by 509 · see citing works
Inhibition of mitochondrial fusion by α‐synuclein is rescued by PINK1, Parkin and DJ‐1
Kamp, F., Exner, N., Lutz, A., Wender, N., Hegermann, J., Brunner, B., Nuscher, B., Bartels, T., Giese, A., Beyer, K., et al. (2010) · EMBO Journal · doi:10.1038/emboj.2010.223 · Cited by 505 · see citing works
Parkinson-associated risk variant in distal enhancer of α-synuclein modulates target gene expression
Soldner, F., Stelzer, Y., Shivalila, C., Abraham, B. J., Latourelle, J. C., Barrasa, M. I., Goldmann, J. E., Myers, R. H., Young, R. A., & Jaenisch, R. (2016) · Nature · doi:10.1038/nature17939 · Cited by 496 · see citing works
α-Synuclein Is Localized to Mitochondria-Associated ER Membranes
Guardia-Laguarta, C., Area-Gómez, E., Rüb, C., Liu, Y.-H., Magrané, J., Becker, D., Voos, W., Schon, E., & Przedborski, S. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.2507-13.2014 · Cited by 489 · see citing works
A soluble α-synuclein construct forms a dynamic tetramer
Wang, W., Perovic, I., Chittuluru, J., Kaganovich, A., Nguyen, L. T. T., Liao, J., Auclair, J. R., Johnson, D., Landeru, A., Simorellis, A. K., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1113260108 · Cited by 478 · see citing works
Burré, J., Sharma, M., & Südhof, T. C. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1416598111 · Cited by 478 · see citing works
A novel α-synuclein missense mutation in Parkinson disease
Proukakis, C., Dudzik, C. G., Brier, T., Mackay, D. S., Cooper, J. A. D., Millhauser, G. L., Houlden, H., & Schapira, A. H. V. (2013) · Neurology · doi:10.1212/wnl.0b013e31828727ba · Cited by 465 · see citing works
Identification and Rescue of α-Synuclein Toxicity in Parkinson Patient–Derived Neurons
Chung, C. Y., Khurana, V., Auluck, P. K., Tardiff, D. F., Mazzulli, J. R., Soldner, F., Baru, V., Lou, Y., Freyzon, Y., Cho, S., et al. (2013) · Science · doi:10.1126/science.1245296 · Cited by 442 · see citing works
Self-citationInduction of α-Synuclein Aggregation by Intracellular Nitrative Insult
Paxinou, E., Chen, Q., Weisse, M., Giasson, B. I., Norris, E. H., Rueter, S. M., Trojanowski, J. Q., Lee, V. M. ‐., & Ischiropoulos, H. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-20-08053.2001 · Cited by 440 · see citing works
Neuroinflammation and Oxidation/Nitration of α-Synuclein Linked to Dopaminergic Neurodegeneration
Gao, H., Kotzbauer, P. T., Uryu, K., Leight, S., Trojanowski, J. Q., & Lee, V. M. ‐. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.0143-07.2008 · Cited by 435 · see citing works
Ryan, S. D., Dolatabadi, N., Chan, S. F., Zhang, X., Akhtar, M. W., Parker, J., Soldner, F., Sunico, C. R., Nagar, S., Talantova, M. V., et al. (2013) · Cell · doi:10.1016/j.cell.2013.11.009 · Cited by 430 · 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
A Randomized Clinical Trial of High-Dosage Coenzyme Q10 in Early Parkinson Disease
The Parkinson Study Group QE3 Investigators, Beal, M. F., Oakes, D., Shoulson, I., Henchcliffe, C., Galpern, W. R., Haas, R., Juncos, J. L., Nutt, J. G., Voss, T., et al. (2014) · JAMA Neurology · doi:10.1001/jamaneurol.2014.131 · Cited by 410 · see citing works
Harms, A. S., Cao, S., Rowse, A. L., Thome, A. D., Li, X., Mangieri, L. R., Cron, R. Q., Shacka, J. J., Raman, C., & Standaert, D. G. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.5610-12.2013 · Cited by 406 · see citing works
Interplay of α-synuclein binding and conformational switching probed by single-molecule fluorescence
Ferreon, A. C. M., Gambin, Y., Lemke, E. A., & Deniz, A. A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809232106 · Cited by 400 · see citing works
Chu, Y., & Kordower, J. H. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.08.021 · Cited by 396 · see citing works
Chung, C. Y., Koprich, J. B., Siddiqi, H. K., & Ole Isacson, A. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.5427-08.2009 · Cited by 392 · see citing works
Endoplasmic Reticulum Stress Is Important for the Manifestations of α-Synucleinopathy In Vivo
Colla, E., Coune, P., Liu, Y., Pletniková, O., Troncoso, J. C., Iwatsubo, T., Schneider, B. L., & Lee, M. K. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.5367-11.2012 · Cited by 389 · see citing works
Rey, N. L., Steiner, J. A., Maroof, N., Luk, K. C., Madaj, Z., Trojanowski, J. Q., Lee, V. M. ‐., & Brundin, P. (2016) · The Journal of Experimental Medicine · doi:10.1084/jem.20160368 · Cited by 389 · see citing works
Mazzulli, J. R., Zunke, F., Ole Isacson, A., Studer, L., & Krainc, D. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1520335113 · Cited by 382 · see citing works
Self-citationTheodore, S., Cao, S., McLean, P. J., & Standaert, D. G. (2008) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31818e5e99 · Cited by 367 · see citing works
Diao, J., Burré, J., Vivona, S., Cipriano, D. J., Sharma, M., Kyoung, M., Südhof, T. C., & Brünger, A. T. (2013) · eLife · doi:10.7554/elife.00592 · Cited by 351 · see citing works
Deficits in dopaminergic transmission precede neuron loss and dysfunction in a new Parkinson model
Janezic, S., Threlfell, S., Dodson, P. D., Dowie, M. J., Taylor, T. N., Potgieter, D., Parkkinen, L., Senior, S. L., Anwar, S., Ryan, B., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1309143110 · Cited by 344 · see citing works
Properties of native brain α-synuclein
Burré, J., Vivona, S., Diao, J., Sharma, M., Brünger, A. T., & Südhof, T. C. (2013) · Nature · doi:10.1038/nature12125 · Cited by 340 · 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
Sacino, A. N., Brooks, M., Thomas, M. A., McKinney, A. B., Lee, S., Regenhardt, R. W., McGarvey, N. H., Ayers, J. I., Notterpek, L. M., Borchelt, D., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1321785111 · Cited by 328 · see citing works
Lewy Body-like α-Synuclein Aggregates Resist Degradation and Impair Macroautophagy
Tanik, S. A., Schultheiss, C. E., Volpicelli-Daley, L. A., Brunden, K. R., & Lee, V. M. Y. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.457408 · Cited by 326 · see citing works
Colla, E., Jensen, P. H., Pletniková, O., Troncoso, J. C., Glabe, C. G., & Lee, M. K. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.5368-11.2012 · Cited by 324 · see citing works
Tran, H., Chung, C. H.-Y., Iba, M., Zhang, B., Trojanowski, J. Q., Luk, K. C., & Lee, V. M. ‐. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.05.033 · Cited by 323 · see citing works
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
Synucleins Regulate the Kinetics of Synaptic Vesicle Endocytosis
Vargas, K. J., Makani, S., Davis, T., Westphal, C. H., Castillo, P. E., & Chandra, S. S. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.4787-13.2014 · Cited by 321 · see citing works
Membrane Curvature Induction and Tubulation Are Common Features of Synucleins and Apolipoproteins
Varkey, J., Isas, J. M., Mizuno, N., Jensen, M. B., Bhatia, V. K., Jao, C. C., Petrlová, J., Voss, J. C., Stamou, D. G., Steven, A. C., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.139576 · Cited by 319 · see citing works
Dettmer, U., Newman, A. J., Soldner, F., Luth, E. S., Kim, N. C., von Saucken, V. E., Sanderson, J. B., Jaenisch, R., Bartels, T., & Selkoe, D. (2015) · Nature Communications · doi:10.1038/ncomms8314 · Cited by 317 · see citing works
Alterations in axonal transport motor proteins in sporadic and experimental Parkinson’s disease
Chu, Y., Morfini, G. A., Langhamer, L. B., He, Y., Brady, S. T., & Kordower, J. H. (2012) · Brain · doi:10.1093/brain/aws133 · Cited by 317 · see citing works
Neuronal vulnerability, pathogenesis, and Parkinson's disease
Sulzer, D. L., & Surmeier, D. J. (2012) · Movement Disorders · doi:10.1002/mds.25095 · Cited by 315 · see citing works
Calí, T., Ottolini, D., Negro, A., & Brini, M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.302794 · Cited by 311 · see citing works
Daniele, S. G., Béraud, D., Davenport, C., Cheng, K., Yin, H., & Maguire-Zeiss, K. A. (2015) · Science Signaling · doi:10.1126/scisignal.2005965 · Cited by 303 · see citing works
Yazawa, I., Giasson, B. I., Sasaki, R., Zhang, B., Joyce, S., Uryu, K., Trojanowski, J. Q., & Lee, V. M.-Y. (2005) · Neuron · doi:10.1016/j.neuron.2005.01.032 · Cited by 301 · see citing works
Large α-synuclein oligomers inhibit neuronal SNARE-mediated vesicle docking
Choi, B.-K., Choi, M., Kim, J.-Y., Yang, Y., Lai, Y., Kweon, D., Lee, N. K., & Shin, Y. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1218424110 · Cited by 301 · see citing works
Impaired neurotransmission caused by overexpression of α-synuclein in nigral dopamine neurons
Lundblad, M., Decressac, M., Mattsson, B., & Björklund, A. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1200575109 · Cited by 292 · see citing works
A critical appraisal of the pathogenic protein spread hypothesis of neurodegeneration
Walsh, D. M., & Selkoe, D. J. (2016) · Nature reviews. Neuroscience · doi:10.1038/nrn.2016.13 · Cited by 290 · see citing works
Functional Consequences of α-Synuclein Tyrosine Nitration
Hodara, R., Norris, E. H., Giasson, B. I., Mishizen-Eberz, A. J., Lynch, D. R., Lee, V. M. ‐., & Ischiropoulos, H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408906200 · Cited by 286 · see citing works
Luth, E. S., Stavrovskaya, I. G., Bartels, T., Kristal, B. S., & Selkoe, D. J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.545749 · Cited by 281 · see citing works
α-Synuclein Multimers Cluster Synaptic Vesicles and Attenuate Recycling
Wang, L., Das, U., Scott, D. A., Tang, Y., McLean, P. J., & Roy, S. (2014) · Current Biology · doi:10.1016/j.cub.2014.08.027 · Cited by 275 · see citing works
Qin, H., Buckley, J. A., Li, X., Liu, Y., Fox, T. H., Meares, G. P., Yu, H., Yan, Z., Harms, A. S., Li, Y., et al. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.4658-15.2016 · Cited by 275 · see citing works
Mazzulli, J. R., Zunke, F., Tsunemi, T., Toker, N., Jeon, S., Burbulla, L. F., Patnaik, S., Sidransky, E., Marugán, J., Sue, C. M., et al. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.0628-16.2016 · Cited by 275 · see citing works
Self-citationUbiquitin ligase Nedd4 promotes α-synuclein degradation by the endosomal–lysosomal pathway
Tofaris, G. K., Kim, H. T., Hourez, R., Jung, J.-W., Kim, K. P., & Goldberg, A. L. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1109356108 · Cited by 271 · see citing works
Lastres‐Becker, I., Ulusoy, A., Innamorato, N. G., Şahin, G., Rábano, A., Kirik, D., & Cuadrado, A. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds143 · Cited by 264 · see citing works
Mutant A53T α-Synuclein Induces Neuronal Death by Increasing Mitochondrial Autophagy
Choubey, V., Safiulina, D., Vaarmann, A., Cagalinec, M., Warȩski, P., Kuum, M., Zharkovsky, A., & Kaasik, A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.132514 · Cited by 259 · see citing works
Sardi, S. P., Clarke, J. L., Viel, C., Chan, M., Tamsett, T. J., Treleaven, C. M., Bu, J., Sweet, L., Passini, M. A., Dodge, J. C., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1220464110 · Cited by 252 · see citing works
Yeast Reveal a “Druggable” Rsp5/Nedd4 Network that Ameliorates α-Synuclein Toxicity in Neurons
Tardiff, D. F., Jui, N. T., Khurana, V., Tambe, M. A., Thompson, M. L., Chung, C. Y., Kamadurai, H., Kim, H. T., Lancaster, A. K., Caldwell, K. A., et al. (2013) · Science · doi:10.1126/science.1245321 · Cited by 250 · see citing works
microRNA-155 Regulates Alpha-Synuclein-Induced Inflammatory Responses in Models of Parkinson Disease
Thome, A. D., Harms, A. S., Volpicelli‐Daley, L. A., & Standaert, D. G. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.3900-15.2016 · Cited by 249 · see citing works
Fibrillar α-Synuclein and Huntingtin Exon 1 Assemblies Are Toxic to the Cells
Pieri, L., Madiona, K., Bousset, L., & Melki, R. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2012.04.050 · Cited by 247 · see citing works
α-Synuclein Inhibits Intersynaptic Vesicle Mobility and Maintains Recycling-Pool Homeostasis
Scott, D. A., & Roy, S. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.0535-12.2012 · 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
Fares, M.-B., Ait‐Bouziad, N., Dikiy, I., Mbefo, M. K., Jovi, A., Kiely, A. P., Holton, J. L., Lee, S., Gitler, A. D., Eliezer, D., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu165 · Cited by 241 · see citing works
Non-A.beta. Component of Alzheimer's Disease Amyloid (NAC) is Amyloidogenic
Iwai, A., Yoshimoto, M., Masliah, E., & Saitoh, T. (1995) · Biochemistry · doi:10.1021/bi00032a006 · Cited by 237 · see citing works
Zecca, L., Casella, L., Albertini, A., Bellei, C., Zucca, F. A., Engelen, M., Żądło, A. C., Szewczyk, G. M., Zaręba, M., & Sarna, T. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05541.x · Cited by 233 · see citing works
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
Volpicelli‐Daley, L. A., Gamble, K. L., Schultheiss, C. E., Riddle, D. M., West, A. B., & Lee, V. M. ‐. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-02-0741 · Cited by 233 · see citing works
Cysteine cathepsins are essential in lysosomal degradation of α-synuclein
McGlinchey, R. P., & Lee, J. C. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1500937112 · Cited by 231 · see citing works
Thayanidhi, N., Helm, J. R., Nycz, D. C., Bentley, M., Liang, Y., & Hay, J. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-09-0801 · Cited by 229 · see citing works
Aflaki, E., Borger, D. K., Moaven, N., Stubblefield, B. K., Rogers, S. A., Patnaik, S., Schoenen, F. J., Westbroek, W., Zheng, W., Sullivan, P., et al. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.0636-16.2016 · Cited by 228 · see citing works
Bellucci, A., Navarria, L., Zaltieri, M., Falarti, E., Bodei, S., Sigala, S., Battistin, L., Spillantini, M. G., Missale, C., & Spano, P. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.07143.x · Cited by 225 · see citing works
Abrogation of α-synuclein–mediated dopaminergic neurodegeneration in LRRK2-deficient rats
Daher, J. P. L., Volpicelli-Daley, L. A., Blackburn, J. P., Moehle, M. S., & West, A. B. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1403215111 · Cited by 223 · see citing works
Stefanova, N., Reindl, M., Neumann, M., Kahle, P. J., Poewe, W. H., & Wenning, G. K. (2007) · Movement Disorders · doi:10.1002/mds.21671 · Cited by 217 · see citing works
Daher, J. P. L., Abdelmotilib, H., Hu, X., Volpicelli‐Daley, L. A., Moehle, M. S., Fraser, K. B., Needle, E., Chen, Y., Steyn, S. J., Galatsis, P., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.660001 · Cited by 212 · see citing works
Lack of Neuronal IFN-β-IFNAR Causes Lewy Body- and Parkinson’s Disease-like Dementia
Ejlerskov, P., Hultberg, J. G., Wang, J., Carlsson, R., Ambjørn, M., Kuss, M., Liu, Y., Porcu, G., Kolkova, K., Friis Rundsten, C., et al. (2015) · Cell · doi:10.1016/j.cell.2015.08.069 · Cited by 211 · see citing works
Oueslati, A., Schneider, B. L., Aebischer, P., & Lashuel, H. A. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1309991110 · Cited by 204 · see citing works
Yoshimoto, M., Iwai, A., Kang, D. E., Otero, D. A., Xia, Y., & Saitoh, T. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.20.9141 · Cited by 202 · see citing works
Lindersson, E., Lundvig, D. M. S., Petersen, C. E. L., Madsen, P., Nyengaard, J. R., Højrup, P., Moos, T., Otzen, D. E., Gai, W.-P., Blumbergs, P. C., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410409200 · Cited by 196 · see citing works
Molecular and Biological Compatibility with Host Alpha-Synuclein Influences Fibril Pathogenicity
Luk, K. C., Covell, D. J., Kehm, V. M., Zhang, B., Song, I. Y., Byrne, M. D., Pitkin, R. M., Decker, S. C., Trojanowski, J. Q., & Lee, V. M.-Y. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.08.053 · Cited by 191 · see citing works
Chen, L., Xie, Z., Turkson, S., & Zhuang, X. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.0089-14.2015 · Cited by 185 · 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
Li, W., Lesuisse, C., Xu, Y., Troncoso, J. C., Price, D. L., & Lee, M. K. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.1370-04.2004 · Cited by 178 · see citing works
Dettmer, U., Newman, A. J., von Saucken, V. E., Bartels, T., & Selkoe, D. J. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1505953112 · Cited by 177 · see citing works
Burré, J., Sharma, M., & Südhof, T. C. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.3545-12.2012 · Cited by 175 · see citing works
α-Synuclein fate is determined by USP9X-regulated monoubiquitination
Rott, R., Szargel, R., Haskin, J., Bandopadhyay, R., Lees, A. J., Shani, V., & Engelender, S. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1105725108 · Cited by 174 · see citing works
Frigerio, R., Fujishiro, H., Ahn, T. B., Josephs, K. A., Maraganore, D. M., DelleDonne, A., Parisi, J. E., Klos, K. J., Boeve, B. F., Dickson, D. W., et al. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.05.019 · Cited by 174 · 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
Self-citationIhara, M., Yamasaki, N., Hagiwara, A., Tanigaki, A., Kitano, A., Hikawa, R., Tomimoto, H., Noda, M., Takanashi, M., Mori, H., et al. (2007) · Neuron · doi:10.1016/j.neuron.2007.01.019 · Cited by 165 · see citing works
Tsunemi, T., & Krainc, D. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt572 · Cited by 159 · see citing works
Self-citationGlucocerebrosidase gene therapy prevents α-synucleinopathy of midbrain dopamine neurons
Rocha, E. M., Smith, G. A., Park, E. Y. H., Cao, H., Brown, E., Hayes, M. A., Beagan, J. A., McLean, J. R., Izen, S. C., Perez-Torres, E., et al. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.09.009 · Cited by 157 · see citing works
Wang, S., Chu, C., Stewart, T., Ginghină, C., Wang, Y., Nie, H., Guo, M., Wilson, B. C., Hong, J., & Zhang, J. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1417883112 · Cited by 156 · see citing works
Mazzulli, J. R., Mishizen-Eberz, A. J., Giasson, B. I., Lynch, D. R., THOMAS, S. A., Nakashima, A., Nagatsu, T., Ota, A., & Ischiropoulos, H. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.0896-06.2006 · Cited by 152 · see citing works
Lysosomal storage disorders and Parkinson's disease: Gaucher disease and beyond
Shachar, T., Bianco, C. L., Recchia, A., Wießner, C., Raas‐Rothschild, A., & Futerman, A. H. (2011) · Movement Disorders · doi:10.1002/mds.23774 · Cited by 150 · see citing works
TRIM28 regulates the nuclear accumulation and toxicity of both alpha-synuclein and tau
Rousseaux, M. W. C., de Haro, M., Lasagna‐Reeves, C. A., Maio, A. D., Park, J., Jafar‐Nejad, P., Al‐Ramahi, I., Sharma, A., See, L., Lü, N., et al. (2016) · eLife · doi:10.7554/elife.19809 · Cited by 150 · see citing works
In vivo silencing of alpha-synuclein using naked siRNA
Lewis, J. M., Melrose, H. L., Bumcrot, D. A., et al. (2008) · Molecular Neurodegeneration · doi:10.1186/1750-1326-3-19 · Cited by 148 · see citing works
Ubhi, K., Rockenstein, E., Mante, M., Inglis, C., Adame, A., Patrick, C., Whitney, K., & Masliah, E. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.0567-10.2010 · Cited by 147 · see citing works
The spectrum of cognitive impairment in Lewy body diseases
Goldman, J. G., Williams‐Gray, C. H., Barker, R. A., Duda, J. E., & Galvin, J. E. (2014) · Movement Disorders · doi:10.1002/mds.25866 · Cited by 142 · see citing works
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Prots, I., Veber, V., Brey, S., Campioni, S., Buder, K., Riek, R., Böhm, K. J., & Winner, B. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.451815 · Cited by 140 · see citing works
Arber, C., Li, A., Houlden, H., & Wray, S. (2015) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12242 · Cited by 136 · see citing works
Lindström, V., Fagerqvist, T., Nordström, E. K. L., Eriksson, F., Lord, A., Tucker, S. M., Andersson, J., Johannesson, M., Schell, H., Kahle, P. J., et al. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.05.009 · Cited by 135 · see citing works
Calcineurin determines toxic versus beneficial responses to α-synuclein
Caraveo, G., Auluck, P. K., Whitesell, L. J., Chung, C. Y., Baru, V., Mosharov, E. V., Yan, X., Johny, M. B., Soste, M., Picotti, P., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1413201111 · Cited by 127 · see citing works
Eschbach, J., von Einem, B., Müller, K., Bayer, H., Scheffold, A., Morrison, B. E., Rudolph, K. L., Thal, D. R., Witting, A., Weydt, P., et al. (2014) · Annals of Neurology · doi:10.1002/ana.24294 · Cited by 126 · see citing works
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Trinh, J., Guella, I., & Farrer, M. J. (2014) · JAMA Neurology · doi:10.1001/jamaneurol.2014.1909 · Cited by 125 · see citing works
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Bachhuber, T., Katzmarski, N., McCarter, J. F., Loreth, D., Tahirović, S., Kamp, F., Abou‐Ajram, C., Nuscher, B., Serrano‐Pozo, A., Müller, A., et al. (2015) · Nature Medicine · doi:10.1038/nm.3885 · Cited by 116 · see citing works
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Wong, Y. C., & Holzbaur, E. L. F. (2015) · Journal of Cell Science · doi:10.1242/jcs.161216 · Cited by 116 · see citing works
Self-citationHalliday, G. M., Macdonald, V., & Henderson, J. M. (2005) · Brain · doi:10.1093/brain/awh596 · Cited by 115 · see citing works
Induction of de novo α-synuclein fibrillization in a neuronal model for Parkinson’s disease
Fares, M.-B., Maco, B., Oueslati, A., Rockenstein, E. M., Ninkina, N. N., Buchman, V. L., Masliah, E., & Lashuel, H. A. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1512876113 · Cited by 109 · see citing works
Fonseca‐Ornelas, L., Eisbach, S. E., Paulat, M., Giller, K., Fernández, C. O., Outeiro, T. F., Becker, S., & Zweckstetter, M. (2014) · Nature Communications · doi:10.1038/ncomms6857 · Cited by 102 · see citing works
Mazzulli, J. R., Armakola, M., Bridi, M., Parastatidis, I., & Ischiropoulos, H. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704737200 · Cited by 93 · see citing works
Development of P assive I mmunotherapies for S ynucleinopathies
Bergström, A., Kallunki, P., & Fog, K. (2015) · Movement Disorders · doi:10.1002/mds.26481 · Cited by 89 · see citing works
der Perren, A. V., Macchi, F., Toelen, J., Carlon, M. S., Maris, M., de Loor, H., Kuypers, D. R. J., Gijsbers, R., den Haute, C. V., Debyser, Z., et al. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.01.014 · Cited by 83 · see citing works
Oh, S. H., Kim, H., Park, H. J., Shin, J. Y., Bae, E.-J., Sunwoo, M. K., Lee, S., & Lee, P. H. (2016) · Cell Reports · doi:10.1016/j.celrep.2015.12.075 · Cited by 83 · see citing works
Chutna, O., Gonçalves, S. A., Villar‐Piqué, A., Guerreiro, P. S., Marijanovic, Z., Mendes, T., Ramalho, J. S., Emmanouilidou, E., Ventura, S., Klucken, J., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu391 · Cited by 82 · see citing works
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Mattson, M. P., & Arumugam, T. V. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.05.011 · Cited by 1,242 · see citing works
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Burbulla, L. F., Song, P., Mazzulli, J. R., Zampese, E., Wong, Y. C., Jeon, S., Santos, D. P., Blanz, J., Obermaier, C. D., Strojny, C., et al. (2017) · Science · doi:10.1126/science.aam9080 · Cited by 874 · see citing works
Self-citationHan, X., Sun, S., Sun, Y., Song, Q., Zhu, J., Song, N., Chen, M., Sun, T., Xia, M., Ding, J., et al. (2019) · Autophagy · doi:10.1080/15548627.2019.1596481 · Cited by 408 · see citing works
Zou, W., Pu, T., Feng, W., Lu, M., Zheng, Y., Du, R., Xiao, M., & Hu, G. (2019) · Translational Neurodegeneration · doi:10.1186/s40035-019-0147-y · Cited by 396 · see citing works
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Wendimu, M. Y., & Hooks, S. B. (2022) · Cells · doi:10.3390/cells11132091 · Cited by 336 · see citing works
Thomas, C. A., Tejwani, L., Trujillo, C. A., Negraes, P. D., Herai, R. H., Mesci, P., Macia, A., Crow, Y. J., & Muotri, A. R. (2017) · Cell Stem Cell · doi:10.1016/j.stem.2017.07.009 · Cited by 330 · see citing works
Schaser, A. J., Osterberg, V. R., Dent, S. E., Stackhouse, T. L., Wakeham, C. M., Boutros, S. W., Weston, L. J., Owen, N., Weissman, T. A., Luna, E., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-47227-z · Cited by 256 · see citing works
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Hinkle, J. T., Patel, J., Panicker, N., Karuppagounder, S. S., Biswas, D., Belingon, B., Chen, R., Brahmachari, S., Pletnikova, O., Troncoso, J. C., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2118819119 · Cited by 240 · see citing works
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Ordonez, D. G., Lee, M. K., & Feany, M. B. (2018) · Neuron · doi:10.1016/j.neuron.2017.11.036 · Cited by 227 · see citing works
Wang, L., Zhao, Z., Zhao, L., Zhao, Y., Yang, G., Wang, C., Gao, L., Niu, C., & Li, S. (2022) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.1c07711 · Cited by 203 · see citing works
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Rousseaux, M. W. C., Vázquez-Vélez, G. E., Al-Ramahi, I., Jeong, H.-H., Bajić, A., Revelli, J.-P., Ye, H., Phan, E. T., Deger, J. M., Perez, A. M., et al. (2018) · The Journal of Neuroscience · doi:10.1523/jneurosci.0254-18.2018 · Cited by 61 · see citing works
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Vergallo, A., Bun, R., Toschi, N., Baldacci, F., Zetterberg, H., Blennow, K., Cavedo, E., Lamari, F., Habert, M., Dubois, B., et al. (2018) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2018.06.3053 · Cited by 59 · see citing works
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He, X., Yang, S., Zhang, R., Hou, L., Xu, J., Hu, Y., Xu, R., Wang, H., & Zhang, Y. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00018 · Cited by 27 · see citing works
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Drobny, A., Ngo, P. A., Neurath, M. F., Zunke, F., & López-Posadas, R. (2021) · Frontiers in Medicine · doi:10.3389/fmed.2021.655123 · Cited by 24 · see citing works
- Authors
- Wong, Y. C., & Krainc, D.
- Affiliations
- Northwestern University (US)
- Corresponding author
- Krainc, Dimitri
- Venue
- Nature Medicine
- Published
- 2017-02
- Volume
- 23
- Issue
- 2
- Pages
- 1-13
- ISSN
- 1078-8956 (ISSN-L)
- 1546-170X
- PMC
- PMC8480197
- OpenAlex
- W2587082207
- Cited by
- 897
- References
- 215
- Citations by year
- 2026: 77 · 2025: 95 · 2024: 89 · 2023: 104 · 2022: 118 · 2021: 109 · 2020: 99 · 2019: 91 · 2018: 80 · 2017: 35
- FWCI
- 11.12
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Nature Medicine (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Institute of Neurological Disorders and Stroke (T32NS041234, R01NS076054)
- Topics
- Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Nuclear Receptors and Signaling
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Keywords
- alpha-synuclein, Parkinson's disease, synucleinopathies, neurodegeneration, alpha-synuclein toxicity, familial Parkinson's disease, dementia with Lewy bodies, multiple system atrophy, aging, selective neuronal vulnerability, cell-to-cell transmission, neuroinflammation, targeted therapy
- MeSH terms
- Alzheimer Disease, Autophagy, Axonal Transport, Endoplasmic Reticulum, Golgi Apparatus, Humans, Lysosomes, Mitochondria, Neurons, Parkinson Disease, Synapses, Amyloid beta-Peptides, tau Proteins, Multiple System Atrophy, Lewy Body Disease, alpha-Synuclein, Molecular Targeted Therapy, Protein Aggregation, Pathological, Protein Aggregates
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