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

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

α-Synuclein in Lewy bodies

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

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

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

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

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

Adapting Proteostasis for Disease Intervention

Balch, W. E., Morimoto, R. I., Dillin, A., & Kelly, J. W. (2008) · Science · doi:10.1126/science.1141448 · Cited by 2,495

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 1,904

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

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

Cryo-EM structure of alpha-synuclein fibrils amplified by PMCA from PD and MSA patient brainsPreprint

Burger, D., Fenyi, A., Bousset, L., Stahlberg, H., & Melki, R. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.07.08.451588 · Cited by 43

Transmission of Synucleinopathies in the Enteric Nervous System of A53T Alpha-Synuclein Transgenic Mice

Lee, H.-J., Suk, J., Lee, K.-W., Park, S.-H., Blumbergs, P. C., Gai, W., & Lee, S. (2011) · Experimental Neurobiology · doi:10.5607/en.2011.20.4.181 · Cited by 41

Alpha-synuclein alters differently gene expression of Sirts, PARPs and other stress response proteins: implications for neurodegenerative disorders

Motyl, J. A., Wencel, P. L., Cieślik, M., Strosznajder, R. P., & Strosznajder, J. B. (2017) · Molecular Neurobiology · doi:10.1007/s12035-016-0317-1 · Cited by 42

The BSSG rat model of Parkinson’s disease: progressing towards a valid, predictive model of disease

Kampen, J. M. V., & Robertson, H. A. (2017) · The EPMA Journal · doi:10.1007/s13167-017-0114-6 · Cited by 43

Pα-syn* mitotoxicity is linked to MAPK activation and involves tau phosphorylation and aggregation at the mitochondria

Grassi, D., Diaz-Perez, N., Volpicelli‐Daley, L. A., & Lasmézas, C. I. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.11.015 · Cited by 42

Contribution of Autophagy-Lysosomal Pathway in the Exosomal Secretion of Alpha-Synuclein and Its Impact in the Progression of Parkinson’s Disease

Sepúlveda, D., Cisternas-Olmedo, M., Arcos, J., Nassif, M., & Vidal, R. L. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.805087 · Cited by 42

Neurogenic potential of progenitor cells isolated from postmortem human Parkinsonian brains

Wang, S., Okun, M. S., Suslov, O. N., Zheng, T., McFarland, N. R., Vedam‐Mai, V., Foote, K. D., Roper, S. N., Yachnis, A. T., Siebzehnrübl, F. A., et al. (2012) · Brain Research · doi:10.1016/j.brainres.2012.04.039 · Cited by 41

Stabilization of α-Synuclein Fibril Clusters Prevents Fragmentation and Reduces Seeding Activity and Toxicity

Lam, H. T., Graber, M. C., Gentry, K. A., & Bieschke, J. (2016) · Biochemistry · doi:10.1021/acs.biochem.5b01168 · Cited by 40

Genetic modification increases the survival and the neuroregenerative properties of transplanted neural stem cells

Korshunova, I., Rhein, S., García‐González, D., Stölting, I., Pfisterer, U., Barta, A., Dmytriyeva, O., Kirkeby, A., Schwaninger, M., & Khodosevich, K. (2020) · JCI Insight · doi:10.1172/jci.insight.126268 · Cited by 40

Do prions cause Parkinson disease?: The evidence accumulates

Olanow, C. W. (2014) · Annals of Neurology · doi:10.1002/ana.24098 · Cited by 40

Transcellular propagation of fibrillar α-synuclein from enteroendocrine to neuronal cells requires cell-to-cell contact and is Rab35-dependent

Rodrigues, P. V., de Godoy, J. V. P., Bosque, B. P., Neto, D. P. A., Tostes, K., Palameta, S., Garcia-Rosa, S., Tonoli, C. C. C., Carvalho, H. F., & Fonseca, M. D. C. (2022) · Scientific Reports · doi:10.1038/s41598-022-08076-5 · Cited by 40

Biophysical groundwork as a hinge to unravel the biology of α-synuclein aggregation and toxicity

Plotegher, N., Greggio, E., Bisaglia, M., & Bubacco, L. (2014) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583513000097 · Cited by 40

Towards translational therapies for multiple system atrophy

Kuzdas-Wood, D., Stefanova, N., Jellinger, K. A., Seppi, K., Schlossmacher, M. G., Poewe, W. H., & Wenning, G. K. (2014) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2014.02.007 · Cited by 39

Studying Parkinson’s disease using Caenorhabditis elegans models in microfluidic devices

Youssef, K., Tandon, A., & Rezai, P. (2019) · Integrative Biology · doi:10.1093/intbio/zyz017 · Cited by 39

Electroacupuncture remediates glial dysfunction and ameliorates neurodegeneration in the astrocytic α-synuclein mutant mouse model

Deng, J., Lv, E., Yang, J., Gong, X., Zhang, W., Liang, X., Wang, J., Jia, J., & Wang, X. (2015) · Journal of Neuroinflammation · doi:10.1186/s12974-015-0302-z · Cited by 40

Cyclosporin promotes neurorestoration and cell replacement therapy in pre-clinical models of Parkinson’s disease

Tamburrino, A., Churchill, M. J., Wan, O. W., Colino‐Sanguino, Y., Ippolito, R., Bergstrand, S., Wolf, D. A., Herz, N. J., Sconce, M. D., Björklund, A., et al. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0263-6 · Cited by 41

Idiopathic Parkinson's disease patient‐derived induced pluripotent stem cells function as midbrain dopaminergic neurons in rodent brains

Kikuchi, T., Morizane, A., Doi, D., Okita, K., Nakagawa, M., Yamakado, H., Inoue, H., Takahashi, R., & Takahashi, J. B. (2017) · Journal of Neuroscience Research · doi:10.1002/jnr.24014 · Cited by 41

Prion-Like Propagation of Protein Aggregation and Related Therapeutic Strategies

Kaufman, S. K., & Diamond, M. I. (2013) · Neurotherapeutics · doi:10.1007/s13311-013-0196-3 · Cited by 40

Cellular Uptake of α-Synuclein Oligomer-Selective Antibodies is Enhanced by the Extracellular Presence of α-Synuclein and Mediated via Fcγ Receptors

Gustafsson, G., Eriksson, F., Möller, C., da Fonseca, T. L., Outeiro, T. F., Lannfelt, L., Bergström, J. J. E., & Ingelsson, M. (2016) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-016-0352-5 · Cited by 38

Direct Observation of α-Synuclein Amyloid Aggregates in Endocytic Vesicles of Neuroblastoma Cells

Apetri, M. M., Harkes, R., Subramaniam, V., Canters, G. W., Schmidt, T., & Aartsma, T. J. (2016) · PLoS ONE · doi:10.1371/journal.pone.0153020 · Cited by 38

ZPD-2, a Small Compound That Inhibits α-Synuclein Amyloid Aggregation and Its Seeded Polymerization

Peña‐Díaz, S., Pujols, J., Conde-Giménez, M., Čarija, A., Dalfó, E., García, J., Navarro, S., Pinheiro, F., Santos, J., Salvatella, X., et al. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00306 · Cited by 38

Inhibition of copper transporter 1 prevents α-synuclein pathology and alleviates nigrostriatal degeneration in AAV-based mouse model of Parkinson's disease

Gou, D.-H., Huang, T., Li, W., Gao, X.-D., Haikal, C., Wang, X.-H., Song, D., Liang, X., Zhu, L., Tang, Y. C., et al. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101795 · Cited by 40

Evidence for Prion-Like Mechanisms in Several Neurodegenerative Diseases: Potential Implications for Immunotherapy

Marciniuk, K., Taschuk, R., & Napper, S. (2013) · Clinical and Developmental Immunology · doi:10.1155/2013/473706 · Cited by 39

The Transcellular Propagation and Intracellular Trafficking of α-SynucleinPreprint

Tofaris, G. K., Goedert, M., & Spillantini, M. G. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024380 · Cited by 39

Functionally different α-synuclein inclusions yield insight into Parkinson’s disease pathology

Raiss, C. C., Braun, T., Konings, I. B. M., Grabmayr, H., Hassink, G. C., Sidhu, A., le Feber, J., Bausch, A. R., Jansen, C., Subramaniam, V., et al. (2016) · Scientific Reports · doi:10.1038/srep23116 · Cited by 37

The Evidence for the Spread and Seeding Capacities of the Mutant Huntingtin Protein in in Vitro Systems and Their Therapeutic Implications

Masnata, M., & Cicchetti, F. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00647 · Cited by 39

Predictive Model of Spread of Progressive Supranuclear Palsy Using Directional Network Diffusion

Pandya, S., Mezias, C., & Raj, A. (2017) · Frontiers in Neurology · doi:10.3389/fneur.2017.00692 · Cited by 39

Human NPCs can degrade α–syn fibrils and transfer them preferentially in a cell contact-dependent manner possibly through TNT-like structures

Grudina, C., Kouroupi, G., Nonaka, T., Hasegawa, M., Matsas, R., & Zurzolo, C. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.104609 · Cited by 39

Microglia in Neurodegenerative Events—An Initiator or a Significant Other?

Harry, G. J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115818 · Cited by 37

α-Synuclein Strains: Does Amyloid Conformation Explain the Heterogeneity of Synucleinopathies?

Hoppe, S. O., Uzunoğlu, G., & Nussbaum-Krammer, C. I. (2021) · Biomolecules · doi:10.3390/biom11070931 · Cited by 37

Extracellular alpha-synuclein: Sensors, receptors, and responses

Domingues, R., Sant’Anna, R., da Fonseca, A. C. C., Robbs, B. K., Foguel, D., & Outeiro, T. F. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105696 · Cited by 38

Toxicity of extracellular secreted alpha-synuclein: Its role in nitrosative stress and neurodegeneration

Wilkaniec, A., Strosznajder, J. B., & Adamczyk, A. (2013) · Neurochemistry International · doi:10.1016/j.neuint.2013.02.004 · Cited by 37

Distinct higher-order α-synuclein oligomers induce intracellular aggregation

Illes‐Toth, E., Ramos, M. R., Cappai, R., Dalton, C., & Smith, D. P. (2015) · Biochemical Journal · doi:10.1042/bj20150159 · Cited by 37

Neuroprotective effects of melatonin on amphetamine‐induced dopaminergic fiber degeneration in the hippocampus of postnatal rats

Leeboonngam, T., Pramong, R., Sae‐ung, K., Govitrapong, P., & Phansuwan‐Pujito, P. (2017) · Journal of Pineal Research · doi:10.1111/jpi.12456 · Cited by 36

In Vivo Protein Complementation Demonstrates Presynaptic α-Synuclein Oligomerization and Age-Dependent Accumulation of 8–16-mer Oligomer Species

Kiechle, M., von Einem, B., Höfs, L., Voehringer, P., Grozdanov, V., Markx, D., Parlato, R., Wiesner, D., Mayer, B., Sakk, O., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.10.089 · Cited by 36

Anti-aggregation Effects of Phenolic Compounds on α-synuclein

Ono, K., Tsuji, M., Yamasaki, T. R., & Pasinetti, G. M. (2020) · Molecules · doi:10.3390/molecules25102444 · Cited by 37

Parkinson Disease: Translating Insights from Molecular Mechanisms to Neuroprotection

Pirooznia, S. K., Rosenthal, L. S., Dawson, V. L., & Dawson, T. M. (2021) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000189 · Cited by 36

Targeting Microglial and Neuronal Toll-like Receptor 2 in Synucleinopathies

Kwon, S., Iba, M., Masliah, E., & Kim, C. (2019) · Experimental Neurobiology · doi:10.5607/en.2019.28.5.547 · Cited by 35

Overlaps and divergences between tauopathies and synucleinopathies: a duet of neurodegeneration

Li, W., & Li, J. (2024) · Translational Neurodegeneration · doi:10.1186/s40035-024-00407-y · Cited by 37

Promising Targets for the Treatment of Neurodegenerative Diseases

Haeberlein, S. B., & Harris, T. (2015) · Clinical Pharmacology & Therapeutics · doi:10.1002/cpt.195 · Cited by 35

An update on MSA: premotor and non-motor features open a window of opportunities for early diagnosis and intervention

Chelban, V., Catereniuc, D., Daniela, A., Gasnaș, D., Vichayanrat, E., Iodice, V., Groppa, S. A., & Houlden, H. (2020) · Journal of Neurology · doi:10.1007/s00415-020-09881-6 · Cited by 35

Fast kinetics of environmentally induced α-synuclein aggregation mediated by structural alteration in NAC region and result in structure dependent cytotoxicity

Srivastava, T., Raj, R., Dubey, A., Kumar, D., Chaturvedi, R. K., Sharma, S., & Priya, S. (2020) · Scientific Reports · doi:10.1038/s41598-020-75361-6 · Cited by 36

“Prion-like” seeding and propagation of oligomeric protein assemblies in neurodegenerative disorders

Zampar, S., Gregorio, S. E. D., Grimmer, G., Watts, J. C., & Ingelsson, M. (2024) · Frontiers in Neuroscience · doi:10.3389/fnins.2024.1436262 · Cited by 39

Treatment with diphenyl–pyrazole compound anle138b/c reveals that α-synuclein protects melanoma cells from autophagic cell death

Turriani, E., Lázaro, D. F., Ryazanov, S., Leonov, A., Giese, A., Schön, M., Schön, M. P., Griesinger, C., Outeiro, T. F., Arndt‐Jovin, D. J., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1700200114 · Cited by 35

Prodromal PD: A new nosological entity

Schaeffer, E., Postuma, R. B., & Berg, D. (2020) · Progress in brain research · doi:10.1016/bs.pbr.2020.01.003 · Cited by 37

Modeling Parkinson’s Disease Neuropathology and Symptoms by Intranigral Inoculation of Preformed Human α-Synuclein Oligomers

Boi, L., Pisanu, A., Palmas, M. F., Fusco, G., Carboni, E., Casu, M. A., Satta, V., Scherma, M., Janda, E., Mocci, I., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228535 · Cited by 33

Natural Alkaloid Compounds as Inhibitors for Alpha-Synuclein Seeded Fibril Formation and Toxicity

Ghanem, S. S., Fayed, H. S., Zhu, Q., Lu, J., Vaikath, N. N., Ponraj, J., Mansour, S. A., & El‐Agnaf, O. M. A. (2021) · Molecules · doi:10.3390/molecules26123736 · Cited by 33

Overexpression of α-synuclein simultaneously increases glutamate NMDA receptor phosphorylation and reduces glucocerebrosidase activity

Yang, J., Hertz, E., Zhang, X., Leinartaité, L., Lundius, E. G., Li, J., & Svenningsson, P. (2015) · Neuroscience Letters · doi:10.1016/j.neulet.2015.11.023 · Cited by 33

Differential seeding and propagating efficiency of α-synuclein strains generated in different conditions

Liu, D., Guo, J.-J., Su, J.-H., Svanbergsson, A., Yuan, L., Haikal, C., Li, W., Gouras, G., & Li, J.-Y. (2021) · Translational Neurodegeneration · doi:10.1186/s40035-021-00242-5 · Cited by 32

Prion-like Mechanisms in Alzheimer's Disease

Yin, R., Tan, L., Jiang, T., & Yu, J. (2014) · Current Alzheimer Research · doi:10.2174/156720501108140910121425 · Cited by 33

Current Management and Emerging Therapies in Multiple System Atrophy

Burns, M. R., & McFarland, N. R. (2020) · Neurotherapeutics · doi:10.1007/s13311-020-00890-x · Cited by 34

Truncation or proteolysis of α-synuclein in Parkinsonism

Suthar, S. K., & Lee, S. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101978 · Cited by 34

Cell-to-cell transmitted alpha-synuclein recapitulates experimental Parkinson’s disease

Prymaczok, N. C., Francesco, P. N. D., Mazzetti, S., Humbert‐Claude, M., Tenenbaum, L., Cappelletti, G., Masliah, E., Perelló, M., Riek, R., & Gerez, J. (2024) · npj Parkinson s Disease · doi:10.1038/s41531-023-00618-6 · Cited by 32

Age-related increase in caveolin-1 expression facilitates cell-to-cell transmission of α-synuclein in neurons

Ha, T.-Y., Choi, Y. R., Noh, H. R., Cha, S., Kim, J.-B., & Park, S. M. (2021) · Molecular Brain · doi:10.1186/s13041-021-00834-2 · Cited by 31

Pathophysiology of Parkinson's disease: Mitochondria, alpha-synuclein and much more…

Rouaud, T., Corbillé, A.-G., Leclair‐Visonneau, L., de Lataillade, A. D. G., Lionnet, A., Preterre, C., Damier, P., & Derkinderen, P. (2020) · Revue Neurologique · doi:10.1016/j.neurol.2020.07.016 · Cited by 32

Extracellular alpha‐synuclein induces calpain‐dependent overactivation of cyclin‐dependent kinase 5 in vitro

Czapski, G. A., Gąssowska-Dobrowolska, M., Wilkaniec, A., Cieślik, M., & Adamczyk, A. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.07.053 · Cited by 32

Parkinson's disease as a member of Prion-like disorders

Herva, M. E., & Spillantini, M. G. (2014) · Virus Research · doi:10.1016/j.virusres.2014.10.016 · Cited by 33

Reciprocal signals between microglia and neurons regulate α-synuclein secretion by exophagy through a neuronal cJUN-N-terminal kinase-signaling axis

Christensen, D. P., Ejlerskov, P., Rasmussen, I., & Vilhardt, F. (2016) · Journal of Neuroinflammation · doi:10.1186/s12974-016-0519-5 · Cited by 32

Exogenous α-synuclein hinders synaptic communication in cultured cortical primary rat neurons

Hassink, G. C., Raiss, C. C., Segers‐Nolten, I. M. J., Wezel, R. J. A. V., Subramaniam, V., le Feber, J., & Claessens, M. M. A. E. (2018) · PLoS ONE · doi:10.1371/journal.pone.0193763 · Cited by 33

Neuronal to oligodendroglial alpha-synuclein redistribution in a double transgenic model of multiple system atrophy

Rockenstein, E. M., Ubhi, K. K., Inglis, C. A., Mante, M., Patrick, C., Adame, A., & Masliah, E. (2012) · Neuroreport · doi:10.1097/wnr.0b013e3283509842 · Cited by 31

Propagation of the Prion Phenomenon: Beyond the Seeding Principle

Münch, C., & Bertolotti, A. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.12.061 · Cited by 31

Interaction of LRRK2 and α-Synuclein in Parkinson’s Disease

Daher, J. P. L. (2017) · Advances in neurobiology · doi:10.1007/978-3-319-49969-7_11 · Cited by 30

Nonmotor Symptoms in Experimental Models of Parkinson's Disease

Titova, N., Schapira, A. H. V., Chaudhuri, К. R., Qamar, M. A., Катунина, Е. А., & Jenner, P. G. (2017) · International review of neurobiology · doi:10.1016/bs.irn.2017.05.018 · Cited by 30

Mechanistic insights into the protective roles of polyphosphate against amyloid cytotoxicity

Lempart, J., Tse, E., Lauer, J. A., Ivanova, M. I., Sutter, A., Yoo, N. G., Huettemann, P., Southworth, D. R., & Jakob, U. (2019) · Life Science Alliance · doi:10.26508/lsa.201900486 · Cited by 30

The small aromatic compound SynuClean-D inhibits the aggregation and seeded polymerization of multiple α-synuclein strains

Peña‐Díaz, S., Pujols, J., Vasili, E., Pinheiro, F., Santos, J., Manglano-Artuñedo, Z., Outeiro, T. F., & Ventura, S. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101902 · Cited by 31

Is Parkinson’s Disease Truly a Prion-Like Disorder? An Appraisal of Current Evidence

Chauhan, A., & Jeans, A. F. (2015) · Neurology Research International · doi:10.1155/2015/345285 · Cited by 34

NADH fluorescence lifetime is an endogenous reporter of α‐synuclein aggregation in live cells

Plotegher, N., Stringari, C., Jahid, S., Veronesi, M., Girotto, S., Gratton, E., & Bubacco, L. (2015) · The FASEB Journal · doi:10.1096/fj.14-260281 · Cited by 31

Immunotherapy Targeting Neurodegenerative Proteinopathies: α-Synucleinopathies and Tauopathies

Shin, J. H., Kim, H., & Jeon, B. (2019) · Journal of Movement Disorders · doi:10.14802/jmd.19057 · Cited by 31

α-Synuclein filaments from transgenic mouse and human synucleinopathy-containing brains are major seed-competent species

Morgan, S., Lavenir, I., Fan, J., Masuda‐Suzukake, M., Passarella, D., Deture, M. A., Dickson, D. W., Ghetti, B. F., & Goedert, M. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.012179 · Cited by 31

Glycosylation in neuroinflammation: mechanisms, implications, and therapeutic strategies for neurodegenerative diseases

Cheng, S., Xiao, B., & Luo, Z. (2025) · Translational Neurodegeneration · doi:10.1186/s40035-025-00506-4 · Cited by 31

Gut–Brain Axis in Focus: Polyphenols, Microbiota, and Their Influence on α-Synuclein in Parkinson’s Disease

Riegelman, E., Xue, K. S., Wang, J.-S., & Tang, L. (2024) · Nutrients · doi:10.3390/nu16132041 · Cited by 29

Seeding Propensity and Characteristics of Pathogenic αSyn Assemblies in Formalin-Fixed Human Tissue from the Enteric Nervous System, Olfactory Bulb, and Brainstem in Cases Staged for Parkinson’s Disease

Fenyi, A., Duyckaerts, C. J., Bousset, L., Braak, H., Tredici, K. D., Melki, R., & on behalf of the Brainbank Neuro-CEB Neuropathology Network (2021) · Cells · doi:10.3390/cells10010139 · Cited by 31

Protein aggregation and prionopathies

Renner, M. L., & Melki, R. (2014) · Pathologie Biologie · doi:10.1016/j.patbio.2014.01.003 · Cited by 31

Methods for detecting toxic α-synuclein species as a biomarker for Parkinson’s disease

O’Hara, D. M., Kalia, S. K., & Kalia, L. V. (2020) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408363.2019.1711359 · Cited by 29

Non-cell-autonomous actions of α-synuclein: Implications in glial synucleinopathies

Lim, S., Kim, H., Kim, D., & Lee, S. (2018) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.06.010 · Cited by 28

α-Synuclein pathology and mitochondrial dysfunction: Toxic partners in Parkinson's disease

Mingo, Y. B., Galvis, M. L. E., & Henderson, M. X. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.106889 · Cited by 30

Prion-like properties of disease-relevant proteins in amyotrophic lateral sclerosis

Bräuer, S., Zimyanin, V. L., & Hermann, A. (2018) · Journal of Neural Transmission · doi:10.1007/s00702-018-1851-y · Cited by 29

Outcome of cell suspension allografts in a patient with Huntington's disease

Maxan, A., Mason, S., Saint‐Pierre, M., Smith, E., Ho, A. K., Harrower, T., Watts, C., Tai, Y., Pavese, N., Savage, J. C., et al. (2018) · Annals of Neurology · doi:10.1002/ana.25354 · Cited by 27

Brain MRI Reveals Ascending Atrophy in Parkinson's Disease Across Severity

Blair, J. C., Barrett, M. J., Patrie, J. T., Flanigan, J. L., Sperling, S. A., Elias, W. J., & Druzgal, T. J. (2019) · Frontiers in Neurology · doi:10.3389/fneur.2019.01329 · Cited by 29

Neurodegeneration models in Parkinson’s disease: cellular and molecular paths to neuron death

Álvarez‐Luquín, D. D., González-Fernández, R. R., Torres-Velasco, M. E., Ichikawa-Escamilla, E., Arce-Sillas, A., Martínez‐Martínez, E., Miranda-Narváez, C. L., Rodríguez-Ramírez, J. F., & Adalid-Peralta, L. V. (2025) · Behavioral and Brain Functions · doi:10.1186/s12993-025-00279-w · Cited by 29

Molecular Mechanism for the Suppression of Alpha Synuclein Membrane Toxicity by an Unconventional Extracellular Chaperone

Ahmed, R., Huang, J., Weber, D. K., Gopinath, T., Veglia, G., Akimoto, M., Khondker, A., Rheinstadter, M. C., Huynh, V. A., Wylie, R. G., et al. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c01894 · Cited by 26

In Search of Effective Treatments Targeting α-Synuclein Toxicity in Synucleinopathies: Pros and Cons

Fouka, M., Mavroeidi, P., Tsaka, G., & Xilouri, M. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.559791 · Cited by 27

Peripherally misfolded proteins exacerbate ischemic stroke-induced neuroinflammation and brain injury

Liu, Y., Subedi, K., Baride, A., Romanova, S., Callegari, E. A., Huber, C. C., Wang, X., & Wang, H. (2021) · Journal of Neuroinflammation · doi:10.1186/s12974-021-02081-7 · Cited by 26

The secreted oligomeric form of α‐synuclein affects multiple steps of membrane trafficking

Chai, Y.-J., Kim, D., Park, J., Zhao, H., Lee, S., & Chang, S. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.01.008 · Cited by 27

Self-Propagative Replication of Aβ Oligomers Suggests Potential Transmissibility in Alzheimer Disease

Kumar, A., Pate, K. M., Moss, M. A., Dean, D. N., & Rangachari, V. (2014) · PLoS ONE · doi:10.1371/journal.pone.0111492 · Cited by 26

Visualization of prion-like transfer in Huntington's disease models

Jansen, A. H. P., Batenburg, K. L., Pecho‐Vrieseling, E., & Reits, E. A. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.12.015 · Cited by 26

Transfer of disrupted-in-schizophrenia 1 aggregates between neuronal-like cells occurs in tunnelling nanotubes and is promoted by dopamine

Zhu, S., Abounit, S., Korth, C., & Zurzolo, C. (2017) · Open Biology · doi:10.1098/rsob.160328 · Cited by 26

The MHC class II transactivator modulates seeded alpha-synuclein pathology and dopaminergic neurodegeneration in an in vivo rat model of Parkinson's disease

Jimenez-Ferrer, I., Bäckström, F., Dueñas-Rey, A., Jewett, M., Boza-Serrano, A., Luk, K. C., Deierborg, T., & Swanberg, M. (2021) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2020.10.017 · Cited by 26

Pharmacological Inhibition of Brain EGFR Activation By a BBB-penetrating Inhibitor, AZD3759, Attenuates α-synuclein Pathology in a Mouse Model of α-Synuclein Propagation

Tavassoly, O., del Cid‐Pellitero, E., Larroquette, F., Cai, E., Thomas, R. A., Soubannier, V., Luo, W., Durcan, T. M., & Fon, E. A. (2021) · Neurotherapeutics · doi:10.1007/s13311-021-01017-6 · Cited by 26

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

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

Emerging Developments in Targeting Proteotoxicity in Neurodegenerative Diseases

McAlary, L., Plotkin, S. S., & Cashman, N. R. (2019) · CNS Drugs · doi:10.1007/s40263-019-00657-9 · Cited by 26

Peri‐arterial pathways for clearance of α‐Synuclein and tau from the brain: Implications for the pathogenesis of dementias and for immunotherapy

Nimmo, J., Johnston, D. A., Dodart, J., Sharp, M. M., Weller, R. O., Nicoll, J. A. R., Verma, A. K., & Carare, R. O. (2020) · Alzheimer s & Dementia Diagnosis Assessment & Disease Monitoring · doi:10.1002/dad2.12070 · Cited by 27

Postmortem Studies of Fetal Grafts in Parkinson’s Disease: What Lessons Have We Learned?

Li, J., & Li, W. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.666675 · Cited by 26

Modeling seeding and neuroanatomic spread of pathology in amyotrophic lateral sclerosis

Pandya, S., Maia, P. D., Freeze, B. S., Menke, R., Talbot, K., Turner, M. R., & Raj, A. (2022) · NeuroImage · doi:10.1016/j.neuroimage.2022.118968 · Cited by 26

C. elegans as an Animal Model to Study the Intersection of DNA Repair, Aging and Neurodegeneration

Naranjo-Galindo, F. J., Ai, R., Fang, E. F., Nilsen, H. L., & SenGupta, T. (2022) · Frontiers in Aging · doi:10.3389/fragi.2022.916118 · Cited by 29

Infectivity versus Seeding in Neurodegenerative Diseases Sharing a Prion-Like Mechanism

Fernández‐Borges, N., Eraña, H., Elezgarai, S. R., Harrathi, C., Gayosso, M., & Castilla, J. (2013) · International Journal of Cell Biology · doi:10.1155/2013/583498 · Cited by 26

Prelysosomal Compartments in the Unconventional Secretion of Amyloidogenic Seeds

Madsen, H. B., & Vilhardt, F. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18010227 · Cited by 26

Advantages of Vasoactive Intestinal Peptide for the Future Treatment of Parkinson’s Disease

Korkmaz, O. T., & Tunçel, N. (2019) · Current Pharmaceutical Design · doi:10.2174/1381612825666190111150953 · Cited by 25

Advances in modelling alpha-synuclein-induced Parkinson’s diseases in rodents: Virus-based models versus inoculation of exogenous preformed toxic species

Carta, A. R., Boi, L., Pisanu, A., Palmas, M. F., Carboni, E., & Simone, A. D. (2020) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2020.108685 · Cited by 27

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

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

Aggregated Alpha-Synuclein Transfer Efficiently between Cultured Human Neuron-Like Cells and Localize to Lysosomes

Domert, J., Sackmann, C., Severinsson, E., Agholme, L., Bergström, J. J. E., Ingelsson, M., & Hallbeck, M. (2016) · PLoS ONE · doi:10.1371/journal.pone.0168700 · Cited by 59

A cell culture model for monitoring α-synuclein cell-to-cell transfer

Reyes, J. F., Olsson, T. T., Lamberts, J. T., Devine, M. J., Kunath, T., & Brundin, P. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.07.003 · Cited by 89

α-Synuclein Seeding in Dopaminergic Neurons Transplanted into the Putamen of Parkinson’s Disease PatientsPreprint

Duvernay, J. B., Killinger, B. A., Choi, S. G., Tittle, T., Bahrami, A., Tharp, M. E., Mercado, G., Chu, Y., Brundin, P., & Kordower, J. H. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.09.22.751740

Beyond α-synuclein transfer: pathology propagation in Parkinson's disease

Hansen, C., & Li, J. (2012) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2012.03.002 · Cited by 85