α-Synucleinopathy phenotypes

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

Diagnosis and management of dementia with Lewy bodies: Third report of the DLB consortium

McKeith, I. G., Dickson, D. W., Lowe, J., Emre, M., O'Brien, J. T., Feldman, H., Cummings, J., Duda, J. E., Lippa, C., Perry, E. K., et al. (2005) · Neurology · doi:10.1212/01.wnl.0000187889.17253.b1 · Cited by 5,069

The Consortium to Establish a Registry for Alzheimer's Disease (CERAD): Part II. Standardization of the neuropathologic assessment of Alzheimer's disease

Mirra, S. S., Heyman, A., McKeel, D., Sumi, S. M., Crain, B. J., Brownlee, L. M., Vogel, F. S., Hughes, J. P., Belle, G. V., Berg, L., et al. (1991) · Neurology · doi:10.1212/wnl.41.4.479 · Cited by 4,961

Second consensus statement on the diagnosis of multiple system atrophy

Gilman, S., Wenning, G. K., Low, P. A., Brooks, D. J., Mathias, C. J., Trojanowski, J. Q., Wood, N. W., Colosimo, C., Dürr, A., Fowler, C. J., et al. (2008) · Neurology · doi:10.1212/01.wnl.0000324625.00404.15 · Cited by 3,140

Consortium to Establish a Registry for Alzheimer's Disease (CERAD)

Fillenbaum, G., & Heyman, A. (2002) · doi:10.1002/0470846410.ch42(iii · Cited by 2,859

Diagnostic Criteria for Parkinson Disease

Gelb, D. J., Oliver, E., & Gilman, S. (1999) · Archives of Neurology · doi:10.1001/archneur.56.1.33 · Cited by 2,822

The Sydney multicenter study of Parkinson's disease: The inevitability of dementia at 20 years

Hely, M. A., Reid, W. G. J., ADENA, M. A., Halliday, G. M., & Morris, J. G. (2008) · Movement Disorders · doi:10.1002/mds.21956 · Cited by 2,346

Identification of two distinct synucleins from human brain

Jakes, R., Spillantini, M. G., & Goedert, M. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00395-5 · Cited by 1,080

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

Identifying prodromal Parkinson's disease: Pre‐Motor disorders in Parkinson's disease

Postuma, R. B., Aarsland, D., Barone, P., Burn, D. J., Hawkes, C. H., Oertel, W. H., & Ziemssen, T. (2012) · Movement Disorders · doi:10.1002/mds.24996 · Cited by 615

How many human proteoforms are there?

Aebersold, R., Agar, J. N., Amster, I. J., Baker, M. S., Bertozzi, C. R., Boja, E. S., Costello, C. E., Cravatt, B. F., Fenselau, C., Garcia, B. A., et al. (2018) · Nature Chemical Biology · doi:10.1038/nchembio.2576 · Cited by 907

Dementia

Gale, S. A., Acar, D., & Daffner, K. R. (2018) · The American Journal of Medicine · doi:10.1016/j.amjmed.2018.01.022 · Cited by 788

Extracellular vesicles in neurodegenerative disease — pathogenesis to biomarkers

Thompson, A. G., Gray, E., Heman-Ackah, S. M., Mäger, I., Talbot, K., Andaloussi, S. E., Wood, M. J., & Turner, M. R. (2016) · Nature Reviews Neurology · doi:10.1038/nrneurol.2016.68 · Cited by 431

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

Gut-seeded α-synuclein fibrils promote gut dysfunction and brain pathology specifically in aged mice

Challis, C., Hori, A., Sampson, T. R., Yoo, B. B., Challis, R. C., Hamilton, A. M., Mazmanian, S. K., Volpicelli-Daley, L. A., & Gradinaru, V. (2020) · Nature Neuroscience · doi:10.1038/s41593-020-0589-7 · Cited by 405

Implication of Alpha-Synuclein Phosphorylation at S129 in Synucleinopathies: What Have We Learned in the Last Decade?

Oueslati, A. (2016) · Journal of Parkinson s Disease · doi:10.3233/jpd-160779 · Cited by 385

Prying into the Prion Hypothesis for Parkinson's Disease

Brundin, P., & Melki, R. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.1788-16.2017 · Cited by 293

Activation of -Glucocerebrosidase Reduces Pathological -Synuclein and Restores Lysosomal Function in Parkinson's Patient Midbrain Neurons

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 281

Chemoenzymatic Semisynthesis of Proteins

Thompson, R. E., & Muir, T. W. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00450 · Cited by 245

Propagation of alpha-synuclein pathology: hypotheses, discoveries, and yet unresolved questions from experimental and human brain studies

Uchihara, T., & Giasson, B. I. (2016) · Acta Neuropathologica · doi:10.1007/s00401-015-1485-1 · Cited by 249

Therapeutic approaches to target alpha-synuclein pathology

Brundin, P., Dave, K. D., & Kordower, J. H. (2017) · Experimental Neurology · doi:10.1016/j.expneurol.2017.10.003 · Cited by 247

Clinical Features of Parkinson’s Disease: The Evolution of Critical Symptoms

Váradi, C. (2020) · Biology · doi:10.3390/biology9050103 · Cited by 196

The emerging role of α-synuclein truncation in aggregation and disease

Sorrentino, Z. A., & Giasson, B. I. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.rev120.011743 · Cited by 184

Alpha-synuclein research: defining strategic moves in the battle against Parkinson’s disease

Oliveira, L. M. A., Gasser, T., Edwards, R. H., Zweckstetter, M., Melki, R., Stefanis, L., Lashuel, H. A., Sulzer, D., Vekrellis, K., Halliday, G. M., et al. (2021) · npj Parkinson s Disease · doi:10.1038/s41531-021-00203-9 · Cited by 174

Regulation of the mammalian heat shock factor 1

Naidu, S. D., & Dinkova‐Kostova, A. T. (2017) · FEBS Journal · doi:10.1111/febs.13999 · Cited by 174

Autopsy validation of 123 I-FP-CIT dopaminergic neuroimaging for the diagnosis of DLB

Thomas, A. J., Attems, J., Colloby, S. J., O'Brien, J. T., McKeith, I., Walker, R., Lee, L., Burn, D., Lett, D. J., & Walker, Z. (2017) · Neurology · doi:10.1212/wnl.0000000000003512 · Cited by 165

Distinct α-Synuclein strains and implications for heterogeneity among α-Synucleinopathies

Peng, C., Gathagan, R. J., & Lee, V. M. ‐. (2017) · Neurobiology of Disease · doi:10.1016/j.nbd.2017.07.018 · Cited by 173

α-Synuclein in blood exosomes immunoprecipitated using neuronal and oligodendroglial markers distinguishes Parkinson’s disease from multiple system atrophy

Dutta, S., Hornung, S., Kruayatidee, A., Maina, K. N., Rosario, I. D., Paul, K. C., Wong, D. Y., Folle, A. D., Markovic, D., Palma, J., et al. (2021) · Acta Neuropathologica · doi:10.1007/s00401-021-02324-0 · Cited by 166

Oligodendroglia and Myelin in Neurodegenerative Diseases: More Than Just Bystanders?

Ettle, B., Schlachetzki, J. C. M., & Winkler, J. (2016) · Molecular Neurobiology · doi:10.1007/s12035-015-9205-3 · Cited by 160

Extracellular Interactions of Alpha-Synuclein in Multiple System Atrophy

Valdinocci, D., Radford, R. A. W., Goulding, M., Hayashi, J., Chung, R. S., & Pountney, D. L. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19124129 · Cited by 161

Epigenetics of dementia: understanding the disease as a transformation rather than a state

Maloney, B., & Lahiri, D. K. (2016) · The Lancet Neurology · doi:10.1016/s1474-4422(16)00065-x · Cited by 159

Sustained Systemic Glucocerebrosidase Inhibition Induces Brain α-Synuclein Aggregation, Microglia and Complement C1q Activation in Mice

Rocha, E. M., Smith, G. A., Park, E. Y. H., Cao, H., Graham, A.-R., Brown, E., McLean, J. R., Hayes, M. A., Beagan, J. A., Izen, S. C., et al. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6307 · Cited by 149

Structural and functional properties of prefibrillar α-synuclein oligomers

Pieri, L., Madiona, K., & Melki, R. (2016) · Scientific Reports · doi:10.1038/srep24526 · Cited by 149

Exposure to bacterial endotoxin generates a distinct strain of α-synuclein fibril

Kim, C., Lv, G., Lee, J. S., Jung, B. C., Masuda-Suzukake, M., Hong, C.-S., Valera, E., Lee, H.-J., Paik, S. R., Hasegawa, M., et al. (2016) · Scientific Reports · doi:10.1038/srep30891 · Cited by 138

α-Synuclein fibrils subvert lysosome structure and function for the propagation of protein misfolding between cells through tunneling nanotubes

Dilsizoglu Senol, A., Samarani, M., Syan, S., Guardia, C. M., Nonaka, T., Liv, N., Latour-Lambert, P., Hasegawa, M., Klumperman, J., Bonifacino, J. S., et al. (2021) · PLOS Biology · doi:10.1371/journal.pbio.3001287 · Cited by 134

Alpha-Synuclein: Mechanisms of Release and Pathology Progression in Synucleinopathies

Brás, I. C., & Outeiro, T. F. (2021) · Cells · doi:10.3390/cells10020375 · Cited by 136

Antagonizing Neuronal Toll-like Receptor 2 Prevents Synucleinopathy by Activating Autophagy

Kim, C., Rockenstein, E., Spencer, B., Kim, H.-K., Adame, A., Trejo, M., Stafa, K., Lee, H.-J., Lee, S.-J., & Masliah, E. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.09.044 · Cited by 135

Alpha-, Beta-, and Gamma-synuclein Quantification in Cerebrospinal Fluid by Multiple Reaction Monitoring Reveals Increased Concentrations in Alzheimer′s and Creutzfeldt-Jakob Disease but No Alteration in Synucleinopathies

Oeckl, P., Metzger, F., Nagl, M., Arnim, C. A. F. V., Halbgebauer, S., Steinacker, P., Ludolph, A. C., & Otto, M. (2016) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m116.059915 · Cited by 140

Autonomic Dysfunction in α-Synucleinopathies

Mendoza-Velásquez, J. J., Flores-Vázquez, J. F., Barrón-Velázquez, E., Sosa, A. L., Illigens, B. M. W., & Siepmann, T. (2019) · Frontiers in Neurology · doi:10.3389/fneur.2019.00363 · Cited by 130

α-Synuclein Amyloids Hijack Prion Protein to Gain Cell Entry, Facilitate Cell-to-Cell Spreading and Block Prion Replication

Aulić, S., Masperone, L., Narkiewicz, J., Isopi, E., Bistaffa, E., Ambrosetti, E., Pastore, B., Cecco, E. D., Scaini, D., Zago, P., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-10236-x · Cited by 131

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 133

Phenotypic spectrum of alpha-synuclein mutations: New insights from patients and cellular models

Petrucci, S., Ginevrino, M., & Valente, E. M. (2015) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2015.08.015 · Cited by 128

Structural Characteristics of α-Synuclein Oligomers

Cremades, N., Chen, S. W., & Dobson, C. M. (2016) · International review of cytology · doi:10.1016/bs.ircmb.2016.08.010 · Cited by 123

Alpha-Synuclein PET Tracer Development—An Overview about Current Efforts

Korat, Š., Bidesi, N., Bonanno, F., Nanni, A. D., Hoàng, A. N. N., Herfert, K., Maurer, A., Battisti, U. M., Bowden, G. D., Thonon, D., et al. (2021) · Pharmaceuticals · doi:10.3390/ph14090847 · Cited by 120

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 131

Diagnostic function of the neuroinflammatory biomarker YKL-40 in Alzheimer’s disease and other neurodegenerative diseases

Baldacci, F., Lista, S., Cavedo, E., Bonuccelli, U., & Hampel, H. (2017) · Expert Review of Proteomics · doi:10.1080/14789450.2017.1304217 · Cited by 113

Structural and Functional Insights into α-Synuclein Fibril Polymorphism

Mehra, S., Gadhe, L. G., Bera, R., Sawner, A. S., & Maji, S. K. (2021) · Biomolecules · doi:10.3390/biom11101419 · Cited by 111

Lewy Body Dementia

Sanford, A. M. (2018) · Clinics in Geriatric Medicine · doi:10.1016/j.cger.2018.06.007 · Cited by 122

The prion-like spreading of α-synuclein: From in vitro to in vivo models of Parkinson’s disease

Vargas, J., Grudina, C., & Zurzolo, C. (2019) · Ageing Research Reviews · doi:10.1016/j.arr.2019.01.012 · Cited by 112

Potential Modes of Intercellular α-Synuclein Transmission

Valdinocci, D., Radford, R. A. W., Siow, S. M., Chung, R. S., & Pountney, D. L. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18020469 · Cited by 114

The role of the immune system in neurodegenerative disorders: Adaptive or maladaptive?

Doty, K. R., Guillot-Sestier, M.-V., & Town, T. (2015) · Brain Research · doi:10.1016/j.brainres.2014.09.008 · Cited by 104

Mitochondria Can Cross Cell Boundaries: An Overview of the Biological Relevance, Pathophysiological Implications and Therapeutic Perspectives of Intercellular Mitochondrial Transfer

Valenti, D., Vacca, R. A., Moro, L., & Atlante, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22158312 · Cited by 100

Molecular mechanism for the synchronized electrostatic coacervation and co-aggregation of alpha-synuclein and tau

Gracia, P., Polanco, D., Tarancón-Díez, J., Serra, I., Bracci, M. A., Oroz, J., Laurents, D. V., García‐Rubio, I., & Cremades, N. (2022) · Nature Communications · doi:10.1038/s41467-022-32350-9 · Cited by 95

Glymphatic System Dysfunction and Sleep Disturbance May Contribute to the Pathogenesis and Progression of Parkinson’s Disease

Massey, A., Boag, M. K., Magnier, A., Bispo, D. P. C. F., Khoo, T. K., & Pountney, D. L. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232112928 · Cited by 103

Non-cell-autonomous Neurotoxicity of α-synuclein Through Microglial Toll-like Receptor 2

Kim, C., Lee, H.-J., Masliah, E., & Lee, S.-J. (2016) · Experimental Neurobiology · doi:10.5607/en.2016.25.3.113 · Cited by 92

Environmental and genetic factors support the dissociation between α-synuclein aggregation and toxicity

Villar‐Piqué, A., da Fonseca, T. L., Sant’Anna, R., Szegő, É. M., Fonseca‐Ornelas, L., Pinho, R., Čarija, A., Gerhardt, E., Masaracchia, C., Gonzalez, E. A., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1606791113 · Cited by 88

Fibrillar α-synuclein induces neurotoxic astrocyte activation via RIP kinase signaling and NF-κB

Chou, T.-W., Chang, N. P., Krishnagiri, M., Patel, A. P., Lindman, M., Angel, J. P., Kung, P.-L., Atkins, C., & Daniels, B. P. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-04049-0 · Cited by 93

Precision and False Perceptual Inference

Parr, T., Benrimoh, D. A., Vincent, P., & Friston, K. J. (2018) · Frontiers in Integrative Neuroscience · doi:10.3389/fnint.2018.00039 · Cited by 87

α-Synuclein-carrying extracellular vesicles in Parkinson’s disease: deadly transmitters

Chistiakov, D. A., & Chistiakov, A. A. (2016) · Acta Neurologica Belgica · doi:10.1007/s13760-016-0679-1 · Cited by 87

Characterization of circular RNA s landscape in multiple system atrophy brain

Chen, B. J., Mills, J. D., Takenaka, K., Bliim, N., Halliday, G. M., & Janitz, M. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13752 · Cited by 84

Autophagy in Synucleinopathy: The Overwhelmed and Defective Machinery

Arotçarena, M.-L., Teil, M., & Dehay, B. (2019) · Cells · doi:10.3390/cells8060565 · Cited by 91

Lewy body disease or diseases with Lewy bodies?

Menšíková, K., Matěj, R., Colosimo, C., Rosales, R. L., Tučková, L., Ehrmann, J., Hraboš, D., Kolaříková, K., Vodička, R., Vrtěl, R., et al. (2022) · npj Parkinson s Disease · doi:10.1038/s41531-021-00273-9 · Cited by 96

Endogenous alpha-synuclein monomers, oligomers and resulting pathology: let’s talk about the lipids in the room

Killinger, B. A., Melki, R., Brundin, P., & Kordower, J. H. (2019) · npj Parkinson s Disease · doi:10.1038/s41531-019-0095-3 · Cited by 82

Genetics of SynucleinopathiesPreprint

Nussbaum, R. L. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024109 · Cited by 85

Novel self-replicating α-synuclein polymorphs that escape ThT monitoring can spontaneously emerge and acutely spread in neurons

Giorgi, F. D., Laferrière, F., Zinghirino, F., Faggiani, E., Lends, A., Bertoni, M., Yu, X., Grélard, A., Morvan, E., Habenstein, B., et al. (2020) · Science Advances · doi:10.1126/sciadv.abc4364 · Cited by 79

ATP Maintenance via Two Types of ATP Regulators Mitigates Pathological Phenotypes in Mouse Models of Parkinson's Disease

Nakano, M., Imamura, H., Sasaoka, N., Yamamoto, M., Uemura, N., Shudo, T., Fuchigami, T., Takahashi, R., & Kakizuka, A. (2017) · EBioMedicine · doi:10.1016/j.ebiom.2017.07.024 · Cited by 76

Emerging Role of Circular RNAs as Potential Biomarkers for the Diagnosis of Human Diseases

Ojha, R., Nandani, R., Chatterjee, N., & Prajapati, V. K. (2018) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-1426-1_12 · Cited by 76

The Promise and Challenges of Developing miRNA-Based Therapeutics for Parkinson’s Disease

Titze-de-Almeida, S. S., Soto‐Sánchez, C., Fernández, E., Koprich, J. B., Brotchie, J. M., & Titze‐de‐Almeida, R. (2020) · Cells · doi:10.3390/cells9040841 · Cited by 81

In vivo models of alpha-synuclein transmission and propagation

Recasens, A., Ulusoy, A., Kahle, P. J., Monte, D. A. D., & Dehay, B. (2017) · Cell and Tissue Research · doi:10.1007/s00441-017-2730-9 · Cited by 77

Mitochondrial dysfunction is a key pathological driver of early stage Parkinson’s

Toomey, C. E., Heywood, W., Evans, J. R., Lachica, J., Pressey, S. N., Foti, S. C., Shahrani, M. M. A., D’Sa, K., Hargreaves, I. P., Heales, S., et al. (2022) · Acta Neuropathologica Communications · doi:10.1186/s40478-022-01424-6 · Cited by 77

Engineering enhanced protein disaggregases for neurodegenerative disease

Jackrel, M. E., & Shorter, J. (2015) · Prion · doi:10.1080/19336896.2015.1020277 · Cited by 73

The role of lipids in α-synuclein misfolding and neurotoxicity

Ugalde, C. L., Lawson, V., Finkelstein, D. I., & Hill, A. F. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev119.007500 · Cited by 77

α-Helical peptidic scaffolds to target α-synuclein toxic species with nanomolar affinity

Santos, J., Gracia, P., Navarro, S., Peña‐Díaz, S., Pujols, J., Cremades, N., Pallarès, I., & Ventura, S. (2021) · Nature Communications · doi:10.1038/s41467-021-24039-2 · Cited by 72

GLP-1 Receptor Agonists in Neurodegeneration: Neurovascular Unit in the Spotlight

Monti, G., Moreira, D. G., Richner, M., Mutsaers, H. A. M., Ferreira, N., & Jan, A. (2022) · Cells · doi:10.3390/cells11132023 · Cited by 72

Mass Spectrometric Analysis of Lewy Body-Enriched α-Synuclein in Parkinson’s Disease

Bhattacharjee, P., Öhrfelt, A., Lashley, T., Blennow, K., Brinkmalm, A., & Zetterberg, H. (2019) · Journal of Proteome Research · doi:10.1021/acs.jproteome.8b00982 · Cited by 68

Lewy bodies, iron, inflammation and neuromelanin: pathological aspects underlying Parkinson’s disease

Riederer, P. F., Nagatsu, T., Youdim, M. B. H., Wulf, M., Dijkstra, J. M., & Sian‐Hülsmann, J. (2023) · Journal of Neural Transmission · doi:10.1007/s00702-023-02630-9 · Cited by 71

Cellular models as tools for the study of the role of alpha-synuclein in Parkinson's disease

Lázaro, D. F., Pavlou, M. A. S., & Outeiro, T. F. (2017) · Experimental Neurology · doi:10.1016/j.expneurol.2017.05.007 · Cited by 70

Intracellular and Intercellular Mitochondrial Dynamics in Parkinson’s Disease

Valdinocci, D., Simões, R. F., Kovářová, J., Cunha‐Oliveira, T., Neužil, J., & Pountney, D. L. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00930 · Cited by 69

Role of medicinal plants in inhibiting SARS-CoV-2 and in the management of post-COVID-19 complications

Mukherjee, P. K., Efferth, T., Das, B., Kar, A., Ghosh, S., Singha, S., Debnath, P., Sharma, N., Bhardwaj, P. K., & Haldar, P. K. (2022) · Phytomedicine · doi:10.1016/j.phymed.2022.153930 · Cited by 69

Differential Aggregation and Phosphorylation of Alpha Synuclein in Membrane Compartments Associated With Parkinson Disease

Canerina‐Amaro, A., Pereda, D., Díaz, M. L., Rodríguez‐Barreto, D., Casañas‐Sánchez, V., Heffer, M., Garcia‐Esparcia, P., Ferrer, I., Puertas‐Avendaño, R., & Marín, R. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00382 · Cited by 62

Role of Toll-like receptor/MYD88 signaling in neurodegenerative diseases

Xiang, W., Chao, Z.-Y., & Feng, D.-Y. (2015) · Reviews in the Neurosciences · doi:10.1515/revneuro-2014-0067 · Cited by 62

Gastrointestinal Biopsies for the Diagnosis of Alpha-Synuclein Pathology in Parkinson’s Disease

Cersosimo, M. G. (2015) · Gastroenterology Research and Practice · doi:10.1155/2015/476041 · Cited by 63

Autonomic ganglionic injection of α-synuclein fibrils as a model of pure autonomic failure α-synucleinopathy

Wang, X.-J., Ma, M.-M., Zhou, L.-B., Jiang, X.-Y., Hao, M.-M., Teng, R. K. F., Wu, E., Tang, B.-S., Li, J., Teng, J.-F., et al. (2020) · Nature Communications · doi:10.1038/s41467-019-14189-9 · Cited by 61

Autonomic Dysfunction in Early Parkinson's Disease: Results from the United Kingdom Tracking Parkinson's Study

Malek, N., Lawton, M., Grosset, K. A., Bajaj, N. P. S., Barker, R. A., Burn, D. J., Foltynie, T., Hardy, J., Morris, H. R., Williams, N. M., et al. (2016) · Movement Disorders Clinical Practice · doi:10.1002/mdc3.12454 · Cited by 60

Gut microbiota in dementia with Lewy bodies

Nishiwaki, H., Ueyama, J., Kashihara, K., Ito, M., Hamaguchi, T., Maeda, T., Tsuboi, Y., Katsuno, M., Hirayama, M., & Ohno, K. (2022) · npj Parkinson s Disease · doi:10.1038/s41531-022-00428-2 · Cited by 59

Autoimmune antibody decline in Parkinson’s disease and Multiple System Atrophy; a step towards immunotherapeutic strategies

Brudek, T., Winge, K., Folke, J., Christensen, S., Fog, K., Pakkenberg, B., & Pedersen, L. Ø. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0187-7 · Cited by 61

Multiplicity of α-Synuclein Aggregated Species and Their Possible Roles in Disease

Gracia, P., Camino, J. D., Volpicelli‐Daley, L. A., & Cremades, N. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218043 · Cited by 57

Amyloid fibrils act as a reservoir of soluble oligomers, the main culprits in protein deposition diseases

Bigi, A., Cascella, R., Chiti, F., & Cecchi, C. (2022) · BioEssays · doi:10.1002/bies.202200086 · Cited by 56

Melatonin/polydopamine nanostructures for collective neuroprotection-based Parkinson's disease therapy

Srivastava, A. K., Choudhury, S. R., & Karmakar, S. (2019) · Biomaterials Science · doi:10.1039/c9bm01602c · Cited by 55

Simultaneous Determination of the Size and Shape of Single α-Synuclein Oligomers in Solution

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Section II: Genetics

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α-Synuclein Strains and Their Relevance to Parkinson’s Disease, Multiple System Atrophy, and Dementia with Lewy Bodies

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