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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 2,245 · see citing works

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 · see citing works

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

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

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 · see citing works

Lewy- and Alzheimer-type pathologies in Parkinson's disease dementia: which is more important?

Compta, Y., Parkkinen, L., O’Sullivan, S. S., Vandrovcová, J., Holton, J. L., Collins, C., Lashley, T., Kallis, C., Williams, D. R., de Silva, R., et al. (2011) · Brain · doi:10.1093/brain/awr031 · Cited by 585 · see citing works

The spectrum of pathological involvement of the striatonigral and olivopontocerebellar systems in multiple system atrophy: clinicopathological correlations

Ozawa, T. (2004) · Brain · doi:10.1093/brain/awh303 · Cited by 515 · see citing works

A Protein-Chameleon: Conformational Plasticity of α-Synuclein, a Disordered Protein Involved in Neurodegenerative Disorders

Uversky, V. N. (2003) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2003.10506918 · Cited by 502 · see citing works

A clinico-pathological study of subtypes in Parkinson's disease

Selikhova, M. V., Williams, D. R., Kempster, P. A., Holton, J. L., Révész, T., & Lees, A. J. (2009) · Brain · doi:10.1093/brain/awp234 · Cited by 462 · see citing works

Clinical outcomes of progressive supranuclear palsy and multiple system atrophy

O’Sullivan, S. S., Massey, L. A., Williams, D. R., Silveira‐Moriyama, L., Kempster, P. A., Holton, J. L., Révész, T., & Lees, A. J. (2008) · Brain · doi:10.1093/brain/awn065 · Cited by 423 · see citing works

A comparison of clinical and pathological features of young‐ and old‐onset Parkinson's disease

Gibb, W. R. G., & Lees, A. J. (1988) · Neurology · doi:10.1212/wnl.38.9.1402 · Cited by 371 · see citing works

Alzheimer Disease With Amygdala Lewy Bodies: A Distinct Form of α-Synucleinopathy

Uchikado, H., Lin, W.-L., DeLucia, M. W., & Dickson, D. W. (2006) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/01.jnen.0000225908.90052.07 · Cited by 359 · see citing works

Applicability of current staging/categorization of α-synuclein pathology and their clinical relevance

Parkkinen, L., Pirttilä, T., & Alafuzoff, I. I. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0346-6 · Cited by 357 · see citing works

Cognitive impairment in patients with multiple system atrophy and progressive supranuclear palsy

Brown, R. G., Lacomblez, L., Landwehrmeyer, G. B., Bak, T. H., Uttner, I., Dubois, B., Agid, Y., Ludolph, A. C., Bensimon, G., Payan, C., et al. (2010) · Brain · doi:10.1093/brain/awq158 · Cited by 312 · see citing works

The progression of pathology in Parkinson's disease

Halliday, G. M., & McCann, H. (2009) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2009.05118.x · Cited by 298 · see citing works

Cognitive differences in dementia patients with autopsy-verified AD, Lewy body pathology, or both

Kraybill, M., Larson, E. B., Tsuang, D. W., Teri, L. L., McCormick, W. C., Bowen, J. D., Kukull, W. A., Leverenz, J. B., & Cherrier, M. M. (2005) · Neurology · doi:10.1212/01.wnl.0000165987.89198.65 · Cited by 286 · see citing works

Low sensitivity in clinical diagnoses of dementia with Lewy bodies

Nelson, P. T., Jicha, G. A., Kryscio, R. J., Abner, E. L., Schmitt, F. A., Cooper, G. E., Xu, L., Smith, C. D., & Markesbery, W. R. (2009) · Journal of Neurology · doi:10.1007/s00415-009-5324-y · Cited by 273 · see citing works

The neuropathology, pathophysiology and genetics of multiple system atrophy

Ahmed, Z., Asi, Y. T., Sailer, A., Lees, A. J., Houlden, H., Révész, T., & Holton, J. L. (2011) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2011.01234.x · Cited by 267 · see citing works

The identification of Parkinson's disease subtypes using cluster analysis: A systematic review

van Rooden, S. M., Heiser, W. J., Kok, J. N., Verbaan, D., van Hilten, J. J., & Marinus, J. (2010) · Movement Disorders · doi:10.1002/mds.23116 · Cited by 238 · see citing works

Grading of neuropathology in multiple system atrophy: Proposal for a novel scale

Jellinger, K. A., Seppi, K., & Wenning, G. K. (2005) · Movement Disorders · doi:10.1002/mds.20537 · Cited by 202 · see citing works

The dopaminergic response in multiple system atrophy.

Hughes, A. J., Colosimo, C., Kleedorfer, B., Daniel, S. E., & Lees, A. J. (1992) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.55.11.1009 · Cited by 178 · see citing works

Cortical α-synuclein load is associated with amyloid-β plaque burden in a subset of Parkinson’s disease patients

Lashley, T., Holton, J. L., Gray, E., Kirkham, K., O’Sullivan, S. S., Hilbig, A., Wood, N. W., Lees, A. J., & Révész, T. (2008) · Acta Neuropathologica · doi:10.1007/s00401-007-0336-0 · Cited by 172 · see citing works

Characteristics of executive function impairment in Parkinson’s disease patients without dementia

McKinlay, A., Grace, R. C., Dalrymple‐Alford, J. C., & Roger, D. (2009) · Journal of the International Neuropsychological Society · doi:10.1017/s1355617709991299 · Cited by 161 · see citing works

Nonmotor Symptoms in Parkinson’s Disease in 2012: Relevant Clinical Aspects

Bonnet, A. M., Jutras, M., Czernecki, V., Corvol, J., & Vidailhet, M. (2012) · Parkinson s Disease · doi:10.1155/2012/198316 · Cited by 119 · see citing works

In dementia with Lewy bodies, Braak stage determines phenotype, not Lewy body distribution

Weisman, D., Cho, M., Taylor, C., Adame, A., Thal, L. J., & Hansen, L. A. (2007) · Neurology · doi:10.1212/01.wnl.0000266626.64913.0f · Cited by 100 · see citing works

Lewy bodies in the amygdala increase risk for major depression in subjects with Alzheimer disease

López, O. L., Becker, J. T., Sweet, R. A., Martín‐Sánchez, F. J., & Hamilton, R. L. (2006) · Neurology · doi:10.1212/01.wnl.0000230161.28299.3c · Cited by 46 · see citing works

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 · see citing works

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 702 · see citing works

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 · 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

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 · see citing works

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 375 · see citing works

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 274 · see citing works

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 275 · see citing works

Chemoenzymatic Semisynthesis of Proteins

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

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 · see citing works

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 242 · see citing works

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

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

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 173 · see citing works

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. L., Vekrellis, K., Halliday, G. M., et al. (2021) · npj Parkinson s Disease · doi:10.1038/s41531-021-00203-9 · Cited by 169 · see citing works

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 159 · see citing works

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 · see citing works

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 164 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 154 · see citing works

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 144 · see citing works

Structural and functional properties of prefibrillar α-synuclein oligomers

Pieri, L., Madiona, K., & Melki, R. (2016) · Scientific Reports · doi:10.1038/srep24526 · Cited by 142 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 135 · see citing works

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 · see citing works

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 125 · see citing works

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

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

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 123 · see citing works

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 118 · see citing works

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 116 · see citing works

Neuropathogenesis-on-chips for neurodegenerative diseases

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

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 · see citing works

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 109 · see citing works

Lewy Body Dementia

Sanford, A. M. (2018) · Clinics in Geriatric Medicine · doi:10.1016/j.cger.2018.06.007 · Cited by 111 · see citing works

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 106 · see citing works

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 108 · see citing works

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 · see citing works

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 99 · see citing works

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 · see citing works

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 101 · see citing works

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 · see citing works

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 87 · see citing works

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 90 · see citing works

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 · see citing works

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 86 · see citing works

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 · see citing works

Autophagy in Synucleinopathy: The Overwhelmed and Defective Machinery

Arotçarena, M.-L., Teil, M., & Dehay, B. (2019) · Cells · doi:10.3390/cells8060565 · Cited by 85 · see citing works

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 82 · see citing works

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 80 · see citing works

Genetics of SynucleinopathiesPreprint

Nussbaum, R. L. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024109 · Cited by 81 · see citing works

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 80 · see citing works

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 80 · see citing works

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 · see citing works

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 76 · see citing works

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 72 · see citing works

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 75 · see citing works

Engineering enhanced protein disaggregases for neurodegenerative disease

Jackrel, M. E., & Shorter, J. (2015) · Prion · doi:10.1080/19336896.2015.1020277 · Cited by 72 · see citing works

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 72 · see citing works

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 · see citing works

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 69 · see citing works

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 63 · see citing works

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 68 · see citing works

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 67 · see citing works

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 65 · see citing works

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 65 · see citing works

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 · see citing works

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 · see citing works

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 61 · see citing works

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 60 · see citing works

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 · see citing works

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 · see citing works

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 58 · see citing works

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 55 · see citing works

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 54 · see citing works

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 · see citing works

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

Awasthi, S., Ying, C., Li, J., & Mayer, M. (2023) · ACS Nano · doi:10.1021/acsnano.3c01393 · Cited by 54 · see citing works

Brain regions susceptible to alpha-synuclein spreading

Guo, Y., Xiong, H., Chen, K., Zou, J.-J., & Lei, P. (2021) · Molecular Psychiatry · doi:10.1038/s41380-021-01296-7 · Cited by 53 · see citing works

11C Radiolabeling of anle253b: a Putative PET Tracer for Parkinson's Disease That Binds to α‐Synuclein Fibrils in vitro and Crosses the Blood‐Brain Barrier

Maurer, A., Leonov, A., Ryazanov, S., Herfert, K., Kuebler, L., Buss, S., Schmidt, F., Weckbecker, D., Linder, R., Bender, D., et al. (2019) · ChemMedChem · doi:10.1002/cmdc.201900689 · Cited by 50 · see citing works

Perspectives in fluid biomarkers in neurodegeneration from the 2019 biomarkers in neurodegenerative diseases course—a joint PhD student course at University College London and University of Gothenburg

Obrocki, P., Khatun, A., Ness, D., Senkevich, K. A., Hanrieder, J., Capraro, F., Mattsson, N., Andréasson, U., Portelius, E., Ashton, N. J., et al. (2020) · Alzheimer s Research & Therapy · doi:10.1186/s13195-020-00586-6 · Cited by 51 · see citing works

New insights in animal models of neurotoxicity-induced neurodegeneration

Sanfeliu, C., Bartra, C., Sunol, C. E., & Rodrı́guez-Farré, E. (2024) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1248727 · Cited by 54 · see citing works

Synucleinopathies: common features and hippocampal manifestations

Yang, W., & Yu, S. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2411-y · Cited by 49 · see citing works

Randomized Phase I Trial of the α‐Synuclein Antibody Lu AF82422

Vesterager, L. B., Wiedemann, J., Larsen, F., Alaya‐Fourati, F. B., Kallunki, P., Ditlevsen, D. K., Sørensen, M. H., & Meulien, D. (2024) · Movement Disorders · doi:10.1002/mds.29784 · Cited by 48 · see citing works

Overview of therapeutic targets in management of dementia

Malik, R., Kalra, S., Bhatia, S., Al‐Harrasi, A., Singh, G., Mohan, S., Makeen, H. A., Albratty, M., Meraya, A. M., Bahar, B., et al. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113168 · Cited by 48 · see citing works

Altered α‐synuclein, parkin, and synphilin isoform levels in multiple system atrophy brains

Brudek, T., Winge, K., Rasmussen, N. B., Bahl, J. M. C., Tanassi, J. T., Agander, T. K., Hyde, T. M., & Pakkenberg, B. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13392 · Cited by 48 · see citing works

Extracellular Alpha-Synuclein: Mechanisms for Glial Cell Internalization and Activation

Chavarría, C., Ivagnes, R., & Souza, J. M. (2022) · Biomolecules · doi:10.3390/biom12050655 · Cited by 47 · see citing works

Native-state proteomics of Parvalbumin interneurons identifies unique molecular signatures and vulnerabilities to early Alzheimer’s pathology

Kumar, P., Goettemoeller, A. M., Espinosa‐García, C., Tobin, B. R., Tfaily, A., Nelson, R. S., Natu, A., Dammer, E. B., Santiago, J. V., Malepati, S., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-47028-7 · Cited by 48 · see citing works

LRRK2 variation and dementia with Lewy bodies

Heckman, M. G., Soto‐Ortolaza, A. I., Sánchez-Contreras, M., Murray, M. E., Pedraza, O., Diehl, N. N., Walton, R. L., Labbé, C., Lorenzo‐Betancor, O., Uitti, R. J., et al. (2016) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2016.07.015 · Cited by 46 · see citing works

Large-scale network dysfunction in α-Synucleinopathy: A meta-analysis of resting-state functional connectivity

Tang, S., Wang, Y., Liu, Y., Chau, S. W. H., Chan, J. W. Y., Chu, C. W., Abrigo, J., Mok, V., & Wing, Y. K. (2022) · EBioMedicine · doi:10.1016/j.ebiom.2022.103915 · Cited by 46 · see citing works

Genome sequence analyses identify novel risk loci for multiple system atrophy

Chia, R., Ray, A., Shah, Z., Ding, J., Ruffo, P., Fujita, M., Menon, V., Sáez-Atiénzar, S., Reho, P., Kaivola, K., et al. (2024) · Neuron · doi:10.1016/j.neuron.2024.04.002 · Cited by 45 · see citing works

Alpha-Synuclein and the Endolysosomal System in Parkinson’s Disease: Guilty by Association

Teixeira, M., Sheta, R., Idi, W., & Oueslati, A. (2021) · Biomolecules · doi:10.3390/biom11091333 · Cited by 43 · see citing works

Alpha‐synuclein‐associated changes in PINK1‐PRKN‐mediated mitophagy are disease context dependent

Hou, X., Chen, T. H., Koga, S., Bredenberg, J. M., Faroqi, A. H., Delenclos, M., Bu, G., Wszołek, Z. K., Carr, J. A., Ross, O. A., et al. (2023) · Brain Pathology · doi:10.1111/bpa.13175 · Cited by 42 · see citing works

Nrf2 activation attenuates the early suppression of mitochondrial respiration due to the α-synuclein overexpression

Fu, M., Wu, C., Lee, Y., Hung, C., Chen, I., & Wu, K. L. H. (2018) · Biomedical Journal · doi:10.1016/j.bj.2018.02.005 · Cited by 42 · see citing works

Diagnostic challenges in rapidly progressive dementia

Zerr, I., & Hermann, P. (2018) · Expert Review of Neurotherapeutics · doi:10.1080/14737175.2018.1519397 · Cited by 42 · see citing works

Overexpression of alpha-synuclein promotes both cell proliferation and cell toxicity in human SH-SY5Y neuroblastoma cells

Rodríguez-Losada, N., de la Rosa, J., Larriva, M., Wendelbo, R., Aguirre, J. A., Castresana, J. S., & Ballaz, S. (2020) · Journal of Advanced Research · doi:10.1016/j.jare.2020.01.009 · Cited by 42 · see citing works

LRRK2 mutant knock-in mouse models: therapeutic relevance in Parkinson's disease

Chang, E. E. S., Ho, P. W., Liu, H., Pang, S. Y.-Y., Leung, C.-T., Malki, Y., Choi, Z. Y.-K., Ramsden, D. B., & Ho, S. (2022) · Translational Neurodegeneration · doi:10.1186/s40035-022-00285-2 · Cited by 44 · see citing works

Nortriptyline inhibits aggregation and neurotoxicity of alpha-synuclein by enhancing reconfiguration of the monomeric form

Collier, T. J., Srivastava, K. R., Justman, C. J., Grammatopoulous, T., Hutter‐Paier, B., Prokesch, M., Havas, D., Rochet, J., Liu, F., Jock, K., et al. (2017) · Neurobiology of Disease · doi:10.1016/j.nbd.2017.07.007 · Cited by 41 · see citing works

Neuropathology underlying clinical variability in patients with synucleinopathies

Halliday, G. M., Holton, J. L., Révész, T., & Dickson, D. W. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0852-9 · Cited by 426 · see citing works

Structural variations in αSyn fibrils of Parkinson’s disease and related disorders

Ikenaka, K., Aguirre, C., Araki, K., So, M., Kakuda, K., Nagano, S., & Hideki, M. (2017) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2017.08.995 · Cited by 1 · see citing works

Alpha-Synuclein and synuceinopathies as related to Parkinson's disease

Anyanwu, F. E. (2017) · BIBSYS Brage (BIBSYS (Norway))

Section II: Genetics

(2007) · CRC Press eBooks · doi:10.3109/9781420019223-8

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

Graves, N. J., Gambin, Y., & Sierecki, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241512134 · Cited by 34 · see citing works