Reversible Inhibition of α-Synuclein Fibrillization by Dopaminochrome-mediated Conformational Alterations

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

α-synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies

Spillantini, M. G., Crowther, R. A., Jakes, R., Hasegawa, M., & Goedert, M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6469 · Cited by 2,868

Parkinson's Disease

Lang, A. E., & Lozano, A. M. (1998) · New England Journal of Medicine · doi:10.1056/nejm199810083391506 · Cited by 2,072

The substantia nigra of the human brain

Damier, P., Hirsch, É. C., Agid, Y., & Graybiel, A. M. (1999) · Brain · doi:10.1093/brain/122.8.1437 · Cited by 1,827

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

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 1,622

Aggregation of alpha-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies.

(1998) · Europe PMC (PubMed Central) · Cited by 1,594

Oxidative Damage Linked to Neurodegeneration by Selective α-Synuclein Nitration in Synucleinopathy Lesions

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 1,567

Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy

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 1,559

Neuropathology of Parkinson's Disease

Forno, L. (1996) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199603000-00001 · Cited by 1,556

Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging

Jomova, K., Raptova, R., Alomar, S. Y., Alwasel, S. H., Nepovimova, E., Kuca, K., & Valko, M. (2023) · Archives of Toxicology · doi:10.1007/s00204-023-03562-9 · Cited by 2,638

The Role of Oxidative Stress in Parkinson's Disease

Dias, V., Junn, E., & Mouradian, M. M. (2013) · Journal of Parkinson’s Disease · doi:10.3233/jpd-130230 · Cited by 1,845

The function of α-synuclein

Bendor, J. T., Logan, T. P., & Edwards, R. H. (2013) · Neuron · doi:10.1016/j.neuron.2013.09.004 · Cited by 825

Oxidative Stress and Neurotoxicity

Sayre, L. M., Perry, G. L., & Smith, M. A. (2007) · Chemical Research in Toxicology · doi:10.1021/tx700210j · Cited by 884

Interactions of iron, dopamine and neuromelanin pathways in brain aging and Parkinson's disease

Zucca, F. A., Segura-Aguilar, J., Ferrari, E., Muñoz, P., Paris, I., Sulzer, D., Sarna, T., Casella, L., & Zecca, L. (2017) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.09.012 · Cited by 659

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 660

Parkinson's disease: Mechanisms, translational models and management strategies

Raza, C., Anjum, R., & Shakeel, N. U. A. (2019) · Life Sciences · doi:10.1016/j.lfs.2019.03.057 · Cited by 628

Multiple hit hypotheses for dopamine neuron loss in Parkinson's disease

Sulzer, D. (2007) · Trends in Neurosciences · doi:10.1016/j.tins.2007.03.009 · Cited by 602

α-Synuclein misfolding and aggregation: Implications in Parkinson’s disease pathogenesis

Mehra, S., Sahay, S., & Maji, S. K. (2019) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2019.03.001 · Cited by 536

The Aggregation and Fibrillation of α-Synuclein

Fink, A. L. (2006) · Accounts of Chemical Research · doi:10.1021/ar050073t · Cited by 512

Protective and toxic roles of dopamine in Parkinson's disease

Segura‐Aguilar, J., Paris, I. B., Muñoz, P., Ferrari, E., Zecca, L., & Zucca, F. A. (2014) · Journal of Neurochemistry · doi:10.1111/jnc.12686 · Cited by 517

Mechanisms of Parkinson's Disease Linked to Pathological α-Synuclein: New Targets for Drug Discovery

Lee, V. M. ‐., & Trojanowski, J. Q. (2006) · Neuron · doi:10.1016/j.neuron.2006.09.026 · Cited by 486

Autophagy and neurodegeneration: when the cleaning crew goes on strike

Martínez‐Vicente, M., & Cuervo, A. M. (2007) · The Lancet Neurology · doi:10.1016/s1474-4422(07)70076-5 · Cited by 495

Oxidative Stress in Parkinson's Disease

Zhou, C. H., Huang, Y., & Przedborski, S. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1427.023 · Cited by 460

The two faces of protein misfolding: gain‐ and loss‐of‐function in neurodegenerative diseases

Winklhofer, K. F., Tatzelt, J., & Haass, C. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601930 · Cited by 410

Reduced Vesicular Storage of Dopamine Causes Progressive Nigrostriatal Neurodegeneration

Caudle, W. M., Richardson, J. R., Wang, M. Z., Taylor, T. N., Guillot, T. S., McCormack, A. L., Colebrooke, R. E., Monte, D. A. D., Emson, P. C., & Miller, G. W. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.0319-07.2007 · Cited by 389

Polymorphism in the intermediates and products of amyloid assembly

Kodali, R. B., & Wetzel, R. B. (2007) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2007.01.007 · Cited by 376

Small Molecule Inhibitors of α-Synuclein Filament Assembly

Masuda, M., Suzuki, N., Taniguchi, S., Oikawa, T., Nonaka, T., Iwatsubo, T., Hisanaga, S., Goedert, M., & Hasegawa, M. (2006) · Biochemistry · doi:10.1021/bi0600749 · Cited by 367

Abberant α-Synuclein Confers Toxicity to Neurons in Part through Inhibition of Chaperone-Mediated Autophagy

Xilouri, M., Vogiatzi, T., Vekrellis, K., Park, D. S., & Stefanis, L. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005515 · Cited by 373

Dopamine in Parkinson's disease

Latif, S., Jahangeer, M., Razia, D. E. M., Ashiq, M., Ghaffar, A., Akram, M., Allam, A. E., Bouyahya, A., Garipova, L., Shariati, M. A., et al. (2021) · Clinica Chimica Acta · doi:10.1016/j.cca.2021.08.009 · Cited by 374

MHC-I expression renders catecholaminergic neurons susceptible to T-cell-mediated degeneration

Cebrián, C., Zucca, F. A., Mauri, P., Steinbeck, J. A., Studer, L., Scherzer, C. R., Kanter, E., Budhu, S., Mandelbaum, J., Vonsattel, J. P., et al. (2014) · Nature Communications · doi:10.1038/ncomms4633 · Cited by 338

Pathological Changes in Dopaminergic Nerve Cells of the Substantia Nigra and Olfactory Bulb in Mice Transgenic for Truncated Human α-Synuclein(1–120): Implications for Lewy Body Disorders

Tofaris, G. K., Garcia-Reitboeck, P., Humby, T., Lambourne, S. L., O’Connell, M. T., Ghetti, B. F., Gossage, H., Emson, P. C., Wilkinson, L. S., Goedert, M., et al. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.4965-05.2006 · Cited by 335

Kinetic and Structural Analysis of the Early Oxidation Products of Dopamine

Bisaglia, M., Mammi, S., & Bubacco, L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610893200 · Cited by 303

Oxidative and nitrosative stress in Parkinson's disease

Tsang, A. H. K., & Chung, K. K. K. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.12.006 · Cited by 300

Pathological Unfoldomics of Uncontrolled Chaos: Intrinsically Disordered Proteins and Human Diseases

Uversky, V. N., Davé, V., Iakoucheva, L. M., Malaney, P., Metallo, S. J., Pathak, R. R., & Joerger, A. C. (2014) · Chemical Reviews · doi:10.1021/cr400713r · Cited by 288

Dopamine, Oxidative Stress and Protein–Quinone Modifications in Parkinson's and Other Neurodegenerative Diseases

Monzani, E., Nicolis, S., Dell’Acqua, S., Capucciati, A., Bacchella, C., Zucca, F. A., Mosharov, E. V., Sulzer, D., Zecca, L., & Casella, L. (2018) · Angewandte Chemie International Edition · doi:10.1002/anie.201811122 · Cited by 274

Inhibition of Amyloid Formation

Härd, T., & Lendel, C. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.12.062 · Cited by 277

Dopamine promotes α‐synuclein aggregation into SDS‐resistant soluble oligomers via a distinct folding pathway

Cappai, R., Leck, S., Tew, D. J., Williamson, N. A., Smith, D. P., Galatis, D., Sharpies, R. A., Curtain, C. C., Ali, F. E. A., Cherny, R. A., et al. (2005) · The FASEB Journal · doi:10.1096/fj.04-3437fje · Cited by 254

Aggregation of α-synuclein by DOPAL, the monoamine oxidase metabolite of dopamine

Burke, W. J., Kumar, V. B., Pandey, N., Panneton, W. M., Gan, Q., Franko, M. W., Odell, M., Li, S. W., Pan, Y., Chung, H. D., et al. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0303-9 · Cited by 251

Modulation of Protein–Protein Interactions for the Development of Novel Therapeutics

Πέττα, Ι., Lievens, S., Libert, C., Tavernier, J. H., & Bosscher, K. D. (2015) · Molecular Therapy · doi:10.1038/mt.2015.214 · Cited by 248

Unregulated Cytosolic Dopamine Causes Neurodegeneration Associated with Oxidative Stress in Mice

Chen, L., Ding, Y., Cagniard, B., Laar, A. D. V., Mortimer, A. D., Chi, W., Hastings, T. G., Kang, U. J., & Zhuang, X. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.3602-07.2008 · Cited by 238

Dopamine induces soluble α-synuclein oligomers and nigrostriatal degeneration

Mor, D. E., Tsika, E., Mazzulli, J. R., Gould, N. S., Kim, H., Daniels, M. J., Doshi, S., Gupta, P., Grossman, J., Tan, V. X., et al. (2017) · Nature Neuroscience · doi:10.1038/nn.4641 · Cited by 226

Dopamine Oxidation and Autophagy

Muñoz, P., Huenchuguala, S., Paris, I., & Segura-Aguilar, J. (2012) · Parkinson's Disease · doi:10.1155/2012/920953 · Cited by 214

α-Synuclein structure, posttranslational modification and alternative splicing as aggregation enhancers

Beyer, K. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0104-6 · Cited by 216

Oxidative and nitrative protein modifications in Parkinson's disease

Danielson, S. R., & Andersen, J. K. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.03.005 · Cited by 204

How Epigallocatechin Gallate Can Inhibit α-Synuclein Oligomer Toxicity in Vitro

Lorenzen, N., Nielsen, S. B., Yoshimura, Y., Vad, B. S., Andersen, C. B., Betzer, C., Kaspersen, J. D., Christiansen, G., Pedersen, J. S., Jensen, P. H., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.554667 · Cited by 202

Small Molecule Protein–Protein Interaction Inhibitors as CNS Therapeutic Agents: Current Progress and Future Hurdles

Blazer, L. L., & Neubig, R. R. (2009) · Neuropsychopharmacology · doi:10.1038/npp.2008.151 · Cited by 197

Protein Oxidation in Aging: Does It Play a Role in Aging Progression?

Reeg, S., & Grune, T. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6062 · Cited by 191

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

Post-translational modification of α-synuclein in Parkinson׳s disease

Barrett, P. J., & Greenamyre, J. T. (2015) · Brain Research · doi:10.1016/j.brainres.2015.06.002 · Cited by 175

The Anti-Amyloidogenic Effect Is Exerted against Alzheimer's β-Amyloid Fibrils in Vitro by Preferential and Reversible Binding of Flavonoids to the Amyloid Fibril Structure

Hirohata, M., Hasegawa, K., Tsutsumi, S., Ohhashi, Y., Ookoshi, T., Ono, K., Yamada, M., & Naiki, H. (2007) · Biochemistry · doi:10.1021/bi061540x · Cited by 167

Reprint of: Revisiting oxidative stress and mitochondrial dysfunction in the pathogenesis of Parkinson disease—resemblance to the effect of amphetamine drugs of abuse

Perfeito, R., Cunha‐Oliveira, T., & Rego, A. C. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.05.042 · Cited by 169

Multiple system atrophy: a clinical and neuropathological perspective

Ubhi, K. K., Low, P. A., & Masliah, E. (2011) · Trends in Neurosciences · doi:10.1016/j.tins.2011.08.003 · Cited by 162

The association between Parkinson's disease and melanoma

Pan, T., Li, X., & Jankovic, J. J. (2011) · International Journal of Cancer · doi:10.1002/ijc.25912 · Cited by 158

Oxidative stress-induced posttranslational modifications of alpha-synuclein: Specific modification of alpha-synuclein by 4-hydroxy-2-nonenal increases dopaminergic toxicity

Xiang, W., Schlachetzki, J. C. M., Helling, S., Bussmann, J., Berlinghof, M., Schäffer, T. E., Marcus, K., Winkler, J., Klucken, J., & Becker, C. (2013) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2013.01.004 · Cited by 152

Cytosolic Catechols Inhibit α-Synuclein Aggregation and Facilitate the Formation of Intracellular Soluble Oligomeric Intermediates

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

How specific are the conformation-specific α-synuclein antibodies? Characterization and validation of 16 α-synuclein conformation-specific antibodies using well-characterized preparations of α-synuclein monomers, fibrils and oligomers with distinct structures and morphology

Kumar, S. T., Jagannath, S., François, C., Vanderstichele, H., Stoops, E., & Lashuel, H. A. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.105086 · Cited by 157

Oxidative and nitrative alpha‐synuclein modifications and proteostatic stress: implications for disease mechanisms and interventions in synucleinopathies

Schildknecht, S., Gerding, H. R., Karreman, C., Drescher, M., Lashuel, H. A., Outeiro, T. F., Di Monte, D. A., & Leist, M. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12226 · Cited by 148

Oxidative modifications, mitochondrial dysfunction, and impaired protein degradation in Parkinson's disease: how neurons are lost in the Bermuda triangle

Malkus, K. A., Tsika, E., & Ischiropoulos, H. (2009) · Molecular Neurodegeneration · doi:10.1186/1750-1326-4-24 · Cited by 144

Tyrosinase-Expressing Neuronal Cell Line as in Vitro Model of Parkinson’s Disease

Hasegawa, T. (2010) · International Journal of Molecular Sciences · doi:10.3390/ijms11031082 · Cited by 146

Entacapone and Tolcapone, Two Catechol O-Methyltransferase Inhibitors, Block Fibril Formation of α-Synuclein and β-Amyloid and Protect against Amyloid-induced Toxicity

Giovanni, S. D., Eleuteri, S., Paleologou, K. E., Yin, G., Zweckstetter, M., Carrupt, P., & Lashuel, H. A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.080390 · Cited by 137

E46K Human α-Synuclein Transgenic Mice Develop Lewy-like and Tau Pathology Associated with Age-dependent, Detrimental Motor Impairment

Emmer, K. L., Waxman, E. A., Covy, J. P., & Giasson, B. I. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.247965 · Cited by 138

Are Dopamine Oxidation Metabolites Involved in the Loss of Dopaminergic Neurons in the Nigrostriatal System in Parkinson’s Disease?

Herrera, A., Muñoz, P., Steinbusch, H. W. M., & Segura‐Aguilar, J. (2017) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00034 · Cited by 138

Oxidative Stress and Neuroinflammation in Parkinson’s Disease: The Role of Dopamine Oxidation Products

Chakrabarti, S., & Bisaglia, M. (2023) · Antioxidants · doi:10.3390/antiox12040955 · Cited by 145

Models of α-synuclein aggregation in Parkinson’s disease

Giráldez‐Pérez, R. M., Antolín‐Vallespín, M., Muñoz, M.-D., & Sánchez‐Capelo, A. (2014) · Acta Neuropathologica Communications · doi:10.1186/s40478-014-0176-9 · Cited by 140

Impact of Dopamine Oxidation on Dopaminergic Neurodegeneration

Zhang, S., Wang, R., & Wang, G. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00454 · Cited by 133

Viral vector-mediated overexpression of α-synuclein as a progressive model of Parkinson’s disease

Ulusoy, A., Decressac, M., Kirik, D., & Björklund, A. (2010) · Progress in brain research · doi:10.1016/s0079-6123(10)84005-1 · Cited by 141

Impact of Plant-Derived Flavonoids on Neurodegenerative Diseases

Costa, S. L., da Silva, V. D. A., Souza, C. D. S., dos Santos, C. C., Paris, I. B., Muñoz, P., & Segura‐Aguilar, J. (2016) · Neurotoxicity Research · doi:10.1007/s12640-016-9600-1 · Cited by 130

Molecular Mechanisms Underlying the Flavonoid-Induced Inhibition of α-Synuclein Fibrillation

Meng, X., Munishkina, L. A., Fink, A. L., & Uversky, V. N. (2009) · Biochemistry · doi:10.1021/bi900506b · Cited by 132

Interactions between Hsp70 and the Hydrophobic Core of α-Synuclein Inhibit Fibril Assembly

Luk, K. C., Mills, I. P., Trojanowski, J. Q., & Lee, V. M. ‐. (2008) · Biochemistry · doi:10.1021/bi801475r · Cited by 137

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

A Potential Role for Cyclized Quinones Derived from Dopamine, DOPA, and 3,4-Dihydroxyphenylacetic Acid in Proteasomal Inhibition

Zafar, K. S., Siegel, D. M., & Ross, D. (2006) · Molecular Pharmacology · doi:10.1124/mol.106.024703 · Cited by 120

Physiological and pathological properties of α-synuclein

Tofaris, G. K., & Spillantini, M. G. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7217-5 · Cited by 117

Inhibition of α-Synuclein Fibrillization by Dopamine Is Mediated by Interactions with Five C-Terminal Residues and with E83 in the NAC Region

Herrera, F. E., Chesi, A., Paleologou, K. E., Schmid, A. W., Munoz, A., Vendruscolo, M., Gustincich, S., Lashuel, H. A., & Carloni, P. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003394 · Cited by 118

Altered vesicular dopamine storage in Parkinson's disease: a premature demise

Caudle, W. M., Colebrooke, R. E., Emson, P. C., & Miller, G. W. (2008) · Trends in Neurosciences · doi:10.1016/j.tins.2008.02.010 · Cited by 119

Suppression of autophagy precipitates neuronal cell death following low doses of methamphetamine

Castino, R., Lazzeri, G., Lenzi, P., Bellio, N., Follo, C., Ferrucci, M., Fornai, F., & Isidoro, C. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05488.x · Cited by 115

Formation of dopamine-mediated α-synuclein-soluble oligomers requires methionine oxidation

Leong, S. L., Pham, C. L. L., Galatis, D., Fodero‐Tavoletti, M. T., Perez, K. A., Hill, A. F., Masters, C. L., Ali, F. E. A., Barnham, K. J., & Cappai, R. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.02.009 · Cited by 114

A critical evaluation of the ubiquitin–proteasome system in Parkinson's disease

Cook, C. N., & Petrucelli, L. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.01.012 · Cited by 119

VMAT2-Deficient Mice Display Nigral and Extranigral Pathology and Motor and Nonmotor Symptoms of Parkinson's Disease

Taylor, T. N., Caudle, W. M., & Miller, G. W. (2011) · Parkinson s Disease · doi:10.4061/2011/124165 · Cited by 113

Interactions between misfolded protein oligomers and membranes: A central topic in neurodegenerative diseases?

Andreasen, M., Lorenzen, N., & Otzen, D. E. (2015) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2015.01.018 · Cited by 109

Structural and mechanistic basis behind the inhibitory interaction of PcTS on α-synuclein amyloid fibril formation

Lamberto, G. R., Binolfi, A., Orcellet, M. L., Bertoncini, C. W., Zweckstetter, M., Griesinger, C., & Fernández, C. O. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0902603106 · Cited by 113

Modulation of α-Synuclein Aggregation by Dopamine: A Review

Leong, S. L., Cappai, R., Barnham, K. J., & Pham, C. L. L. (2009) · Neurochemical Research · doi:10.1007/s11064-009-9986-8 · Cited by 110

Characterization of Hydrophobic Residue Requirements for α-Synuclein Fibrillization

Waxman, E. A., Mazzulli, J. R., & Giasson, B. I. (2009) · Biochemistry · doi:10.1021/bi900539p · Cited by 110

Revisiting oxidative stress and mitochondrial dysfunction in the pathogenesis of Parkinson disease—resemblance to the effect of amphetamine drugs of abuse

Perfeito, R., Cunha‐Oliveira, T., & Rego, A. C. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.08.569 · Cited by 109

Mechanistic aspects of Parkinson’s disease: α-synuclein and the biomembrane

Beyer, K. (2007) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-007-0014-9 · Cited by 104

The usual suspects, dopamine and alpha‐synuclein, conspire to cause neurodegeneration

Mor, D. E., Daniels, M. J., & Ischiropoulos, H. (2019) · Movement Disorders · doi:10.1002/mds.27607 · Cited by 107

Distinct Region-Specific α-Synuclein Oligomers in A53T Transgenic Mice: Implications for Neurodegeneration

Tsika, E., Moysidou, M., Guo, J., Cushman-Nick, M., Gannon, P. J., Sandaltzopoulos, R., Giasson, B. I., Krainc, D., Ischiropoulos, H., & Mazzulli, J. R. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.4977-09.2010 · Cited by 98

Interaction of alpha-synuclein and dopamine metabolites in the pathogenesis of Parkinson’s disease: a case for the selective vulnerability of the substantia nigra

Galvin, J. E. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0096-2 · Cited by 98

Dopamine and the Dopamine Oxidation Product 5,6-Dihydroxylindole Promote Distinct On-Pathway and Off-Pathway Aggregation of α-Synuclein in a pH-Dependent Manner

Pham, C. L. L., Leong, S. L., Ali, F. E. A., Kenche, V. B., Hill, A. F., Gras, S. L., Barnham, K. J., & Cappai, R. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.02.007 · Cited by 99

The structure of dopamine induced α-synuclein oligomers

Rekas, A., Knott, R. B., Sokolova, A. V., Barnham, K. J., Perez, K. A., Masters, C. L., Drew, S. C., Cappai, R., Curtain, C. C., & Pham, C. L. L. (2010) · European Biophysics Journal · doi:10.1007/s00249-010-0595-x · Cited by 95

The Anti-Parkinsonian Drug Selegiline Delays the Nucleation Phase of α-Synuclein Aggregation Leading to the Formation of Nontoxic Species

Braga, C. A. C. A., Follmer, C., Palhano, F. L., Khattar, E., de Freitas, M. S., Romão, L. F., Giovanni, S. D., Lashuel, H. A., Silva, J. L., & Foguel, D. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.10.027 · Cited by 94

Dopamine quinones interact with α-synuclein to form unstructured adducts

Bisaglia, M., Tosatto, L., Munari, F., Tessari, I., de Laureto, P. P., Mammi, S., & Bubacco, L. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.03.044 · Cited by 94

Cellular Oligomerization of α-Synuclein Is Determined by the Interaction of Oxidized Catechols with a C-terminal Sequence

Mazzulli, J. R., Armakola, M., Bridi, M., Parastatidis, I., & Ischiropoulos, H. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704737200 · Cited by 93

Regulatory Activities of Dopamine and Its Derivatives toward Metal-Free and Metal-Induced Amyloid-β Aggregation, Oxidative Stress, and Inflammation in Alzheimer’s Disease

Nam, E., Derrick, J. S., Lee, S., Kang, J., Han, J., Lee, S. J. C., Chung, S. W., & Lim, M. H. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00122 · Cited by 89

Aminochrome Induces Disruption of Actin, Alpha-, and Beta-Tubulin Cytoskeleton Networks in Substantia-Nigra-Derived Cell Line

Paris, I. B., Perez-Pastene, C., Cárdenas, S., Iturra, P., Muñoz, P., Couve, E., Caviedes, P. A., & Segura‐Aguilar, J. (2010) · Neurotoxicity Research · doi:10.1007/s12640-009-9148-4 · Cited by 89

Characterization of α-Synuclein Interactions with Selected Aggregation-Inhibiting Small Molecules

Rao, J. N., Dua, V., & Ulmer, T. S. (2008) · Biochemistry · doi:10.1021/bi8002378 · Cited by 85

Molecular Insights into Parkinson's Disease

Rochet, J., Hay, B. A., & Guo, M. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-385883-2.00011-4 · Cited by 87

γ-Synuclein: Seeding of α-Synuclein Aggregation and Transmission between Cells

Surgucheva, I. G., Sharov, V. S., & Surguchov, A. P. (2012) · Biochemistry · doi:10.1021/bi300478w · Cited by 86

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Bisaglia, M., Filograna, R., Beltramini, M., & Bubacco, L. (2014) · Ageing Research Reviews · doi:10.1016/j.arr.2013.12.009 · Cited by 81

DT-Diaphorase Prevents Aminochrome-Induced Alpha-Synuclein Oligomer Formation and Neurotoxicity

Muñoz, P., Cárdenas, S., Huenchuguala, S., Briceño, A., Couve, E., Paris, I. B., & Segura‐Aguilar, J. (2015) · Toxicological Sciences · doi:10.1093/toxsci/kfv016 · Cited by 80

Post translational changes to α-synuclein control iron and dopamine trafficking; a concept for neuron vulnerability in Parkinson’s disease

Duce, J. A., Wong, B. X. W., Durham, H., Devedjian, J.-C., Smith, D. P., & Devos, D. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0186-8 · Cited by 81

Inhibition of VMAT-2 and DT-Diaphorase Induce Cell Death in a Substantia Nigra-Derived Cell LineAn Experimental Cell Model for Dopamine Toxicity Studies

Fuentes, P., Paris, I. B., Nassif, M., Caviedes, P. A., & Segura‐Aguilar, J. (2007) · Chemical Research in Toxicology · doi:10.1021/tx600325u · Cited by 77

The Chemistry of Neurodegeneration: Kinetic Data and Their Implications

Pavlin, M., Repič, M., Vianello, R., & Mavri, J. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9284-1 · Cited by 75

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Biosa, A., Outeiro, T. F., Bubacco, L., & Bisaglia, M. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1025-9 · Cited by 74

Autophagy protects against aminochrome-induced cell death in substantia nigra-derived cell line.

Paris, I., Muñoz, P., Huenchuguala, S., Couve, E., Sanders, L. H., Greenamyre, J., Caviedes, P., & Segura-Aguilar, J. (2011) · Toxicological Sciences · doi:10.1093/toxsci/kfr060 · Cited by 69

Neurotoxin Mechanisms and Processes Relevant to Parkinson’s Disease: An Update

Segura‐Aguilar, J., & Kostrzewa, R. M. (2015) · Neurotoxicity Research · doi:10.1007/s12640-015-9519-y · Cited by 74

The Drosophila vesicular monoamine transporter reduces pesticide-induced loss of dopaminergic neurons

Lawal, H. O., Chang, H.-Y., Terrell, A. N., Brooks, E. S., Pulido, D., Simon, A. F., & Krantz, D. E. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.05.008 · Cited by 77

Quinone-induced protein handling changes: Implications for major protein handling systems in quinone-mediated toxicity

Xiong, R., Siegel, D. M., & Ross, D. (2014) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2014.08.014 · Cited by 72

Copper·Dopamine Complex Induces Mitochondrial Autophagy Preceding Caspase-independent Apoptotic Cell Death

Paris, I. B., Perez-Pastene, C., Couve, E., Caviedes, P. A., LeDoux, S. P., & Segura‐Aguilar, J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m900323200 · Cited by 71

Glutathione transferase mu 2 protects glioblastoma cells against aminochrome toxicity by preventing autophagy and lysosome dysfunction

Huenchuguala, S., Muñoz, P., Figueroa, P. Z., Villa, M., Cuevas, C. M., Ahumada-Castro, U., Graumann, R., Nore, B. F., Couve, E., Mannervik, B., et al. (2014) · Autophagy · doi:10.4161/auto.27720 · Cited by 73

At Low Concentrations, 3,4-Dihydroxyphenylacetic Acid (DOPAC) Binds Non-Covalently to α-Synuclein and Prevents Its Fibrillation

Zhou, W., Gallagher, A., Hong, D.-P., Long, C., Fink, A. L., & Uversky, V. N. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.03.053 · Cited by 58

Inhibition of α-Synuclein Fibrillization by Dopamine Is Mediated by Interactions with Five C-Terminal Residues and with E83 in the NAC Region

Herrera, F. E., Chesi, A., Paleologou, K. E., Schmid, A. W., Munoz, A., Vendruscolo, M., Gustincich, S., Lashuel, H. A., & Carloni, P. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003394 · Cited by 118

Inhibition of α‐synuclein fibrillization by dopamine analogs via reaction with the amino groups of α‐synuclein

Li, H., Lin, D., Luo, X., Zhang, F., Ji, L., Du, H., Song, G., Hu, J., Zhou, J., & Hu, H. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04792.x · Cited by 117

Dopamine-Induced Conformational Changes in Alpha-Synuclein

Outeiro, T. F., Klucken, J., Bercury, K. K., Tetzlaff, J. E., Putcha, P., Oliveira, L. M. A., Quintas, A., McLean, P. J., & Hyman, B. T. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006906 · Cited by 66

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