Caspase-1 causes truncation and aggregation of the Parkinson’s disease-associated protein α-synuclein

Chronic traumatic encephalopathy in athletes: Progressive tauopathy after repetitive head injury

McKee, A. C., Cantu, R. C., Nowinski, C. J., Hedley-Whyte, E. T., Gavett, B. E., Budson, A. E., Santini, V. E., Lee, H.-S., Kubilus, C. A., & Stern, R. A. (2009) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181a9d503 · Cited by 2,295

Rotenone, Paraquat, and Parkinson’s Disease

Tanner, C. M., Kamel, F., Ross, G. W., Hoppin, J. A., Goldman, S. M., Korell, M., Marras, C., Bhudhikanok, G. S., Kasten, M., Chade, A. R., et al. (2011) · Environmental Health Perspectives · doi:10.1289/ehp.1002839 · Cited by 1,565

Parkinson's disease. Second of two parts.

Lang, A., & Lozano, A. (1998) · New England Journal of Medicine · doi:10.1056/nejm199810153391607 · Cited by 1,193

Tumor necrosis factor-α (TNF-α) increases both in the brain and in the cerebrospinal fluid from parkinsonian patients

Mogi, M., Harada, M., Riederer, P., Narabayashi, H., Fujita, K., & Nagatsu, T. (1994) · Neuroscience Letters · doi:10.1016/0304-3940(94)90746-3 · Cited by 986

Interleukin-1β, interleukin-6, epidermal growth factor and transforming growth factor-α are elevated in the brain from parkinsonian patients

Mogi, M., Harada, M., Kondo, T., Riederer, P., Inagaki, H., Minami, M., & Nagatsu, T. (1994) · Neuroscience Letters · doi:10.1016/0304-3940(94)90508-8 · Cited by 855

Yeast Cells Provide Insight into Alpha-Synuclein Biology and Pathobiology

Outeiro, T. F., & Lindquist, S. L. (2003) · Science · doi:10.1126/science.1090439 · Cited by 811

Interleukin-1β and interleukin-6 are elevated in the cerebrospinal fluid of Alzheimer's and de novo Parkinson's disease patients

Blum-Degena, D., Müller, T., Kuhn, W., Gerlach, M., Przuntek, H., & Riederer, P. (1995) · Neuroscience Letters · doi:10.1016/0304-3940(95)12192-7 · Cited by 801

Minocycline Prevents Nigrostriatal Dopaminergic Neurodegeneration in the MPTP Model of Parkinson’s Disease

Du, Y., Ma, Z., Lin, S., Dodel, R. C., Gao, F., Bales, K. R., Triarhou, L. C., Chernet, E., Perry, K. W., Nelson, D. L. G., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.251341998 · Cited by 789

Inflammation and neurodegeneration in Parkinson's disease

McGeer, P. L., & McGeer, E. G. (2004) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2004.01.005 · Cited by 632

Interleukin (IL)-1β, IL-2, IL-4, IL-6 and transforming growth factor-α levels are elevated in ventricular cerebrospinal fluid in juvenile parkinsonism and Parkinson's disease

Mogi, M., Harada, M., Narabayashi, H., Inagaki, H., Minami, M., & Nagatsu, T. (1996) · Neuroscience Letters · doi:10.1016/0304-3940(96)12706-3 · Cited by 545

Ageing as a risk factor for neurodegenerative disease

Hou, Y., Dan, X., Babbar, M., Wei, Y., Hasselbalch, S. G., Croteau, D. L., & Bohr, V. A. (2019) · Nature Reviews Neurology · doi:10.1038/s41582-019-0244-7 · Cited by 3,310

Role of neuroinflammation in neurodegeneration development

Zhang, W., Xiao, D., Mao, Q., & Xia, H. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01486-5 · Cited by 1,668

T cells from patients with Parkinson’s disease recognize α-synuclein peptides

Sulzer, D., Alcalay, R. N., Garretti, F., Cote, L., Kanter, E., Agin-Liebes, J., Liong, C., McMurtrey, C., Hildebrand, W. H., Mao, X., et al. (2017) · Nature · doi:10.1038/nature22815 · Cited by 866

Inflammasome signalling in brain function and neurodegenerative disease

Heneka, M. T., McManus, R. M., & Latz, E. (2018) · Nature Reviews Neuroscience · doi:10.1038/s41583-018-0055-7 · Cited by 836

Inflammasomes in neuroinflammatory and neurodegenerative diseases

Voet, S., Srinivasan, S., Lamkanfi, M., & van Loo, G. (2019) · EMBO Molecular Medicine · doi:10.15252/emmm.201810248 · Cited by 761

Cryo-EM structure of alpha-synuclein fibrils

Guerrero-Ferreira, R., Taylor, N. M. I., Mona, D., Ringler, P., Lauer, M. E., Riek, R., Britschgi, M., & Stahlberg, H. (2018) · eLife · doi:10.7554/elife.36402 · Cited by 615

Analysis of Gut Microbiota in Patients with Parkinson’s Disease

Petrov, V. A., Saltykova, I. V., Zhukova, I. A., Alifirova, V. M., Zhukova, N. G., Dorofeeva, Y. B., Tyakht, A. V., Kovarsky, B. A., Alekseev, D. G., Kostryukova, E. S., et al. (2017) · Bulletin of Experimental Biology and Medicine · doi:10.1007/s10517-017-3700-7 · Cited by 487

Parkinson disease and the immune system - Associations, mechanisms and therapeutics

Tan, E.-K., Chao, Y.-X., West, A., Chan, L.-L., Poewe, W., & Jankovic, J. (2020) · Nature Reviews Neurology · doi:10.1038/s41582-020-0344-4 · Cited by 457

Poly(ADP-ribose) drives pathologic α-synuclein neurodegeneration in Parkinson’s disease

Kam, T.-I., Mao, X., Park, H., Chou, S.-C., Karuppagounder, S. S., Umanah, G. E., Yun, S. P., Brahmachari, S., Panicker, N., Chen, R., et al. (2018) · Science · doi:10.1126/science.aat8407 · Cited by 476

The endotoxin hypothesis of neurodegeneration

Brown, G. C. (2019) · Journal of Neuroinflammation · doi:10.1186/s12974-019-1564-7 · Cited by 457

MPTP-driven NLRP3 inflammasome activation in microglia plays a central role in dopaminergic neurodegeneration

Lee, E., Hwang, I., Park, S., Hong, S., Hwang, B., Cho, Y., Son, J., & Yu, J.-W. (2019) · Cell Death & Differentiation · doi:10.1038/s41418-018-0124-5 · Cited by 431

The microbiome–gut–brain axis in Parkinson disease — from basic research to the clinic

Tan, A. H., Lim, S. Y., & Lang, A. E. (2022) · Nature Reviews Neurology · doi:10.1038/s41582-022-00681-2 · Cited by 392

Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy

Guerrero-Ferreira, R., Taylor, N. M. I., Arteni, A., Kumari, P., Mona, D., Ringler, P., Britschgi, M., Lauer, M. E., Makky, A., Verasdonck, J., et al. (2019) · eLife · doi:10.7554/elife.48907 · Cited by 345

Fiery Cell Death: Pyroptosis in the Central Nervous System

McKenzie, B., Dixit, V. M., & Power, C. (2019) · Trends in Neurosciences · doi:10.1016/j.tins.2019.11.005 · Cited by 341

Multiple system atrophy

Poewe, W. H., Stanković, I., Halliday, G. M., Meissner, W. G., Wenning, G. K., Pellecchia, M. T., Seppi, K., Palma, J., & Kaufmann, H. (2022) · Nature Reviews Disease Primers · doi:10.1038/s41572-022-00382-6 · Cited by 295

The vermiform appendix impacts the risk of developing Parkinson’s disease

Killinger, B. A., Madaj, Z., Sikora, J. W., Rey, N. L., Haas, A. J., Vepa, Y., Lindqvist, D., Chen, H., Thomas, P. M., Brundin, P., et al. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aar5280 · Cited by 287

Periphery and brain, innate and adaptive immunity in Parkinson’s disease

Harms, A. S., Ferreira, S. A., & Romero‐Ramos, M. (2021) · Acta Neuropathologica · doi:10.1007/s00401-021-02268-5 · Cited by 291

The Ageing Brain: Molecular and Cellular Basis of Neurodegeneration

Azam, S., Haque, M. E., Balakrishnan, R., Kim, I., & Choi, D. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.683459 · Cited by 273

Targeting the Microglial NLRP3 Inflammasome and Its Role in Parkinson's Disease

Haque, M. E., Akther, M., Jakaria, M., Kim, I., Azam, S., & Choi, D. (2019) · Movement Disorders · doi:10.1002/mds.27874 · Cited by 251

A20 critically controls microglia activation and inhibits inflammasome-dependent neuroinflammation

Voet, S., Mc Guire, C., Hagemeyer, N., Martens, A., Schroeder, A., Wieghofer, P., Daems, C., Staszewski, O., Vande Walle, L., Jordao, M. J. C., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-04376-5 · Cited by 227

Neuronal NLRP3 is a parkin substrate that drives neurodegeneration in Parkinson’s disease

Panicker, N., Kam, T., Wang, H., Neifert, S., Chou, S.-C., Kumar, M., Brahmachari, S., Jhaldiyal, A., Hinkle, J. T., Akkentli, F., et al. (2022) · Neuron · doi:10.1016/j.neuron.2022.05.009 · Cited by 222

Microglia Response During Parkinson’s Disease: Alpha-Synuclein Intervention

Ferreira, S. A., & Romero‐Ramos, M. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00247 · Cited by 227

Stool Immune Profiles Evince Gastrointestinal Inflammation in Parkinson's Disease

Houser, M. C., Chang, J., Factor, S. A., Molho, E., Zabetian, C. P., Hill‐Burns, E. M., Payami, H., Hertzberg, V., & Tansey, M. G. (2018) · Movement Disorders · doi:10.1002/mds.27326 · Cited by 204

Asparagine endopeptidase cleaves α-synuclein and mediates pathologic activities in Parkinson's disease

Zhang, Z., Kang, S. S., Liu, X., Ahn, E. H., Zhang, Z., He, L., Iuvone, P. M., Duong, D. M., Seyfried, N. T., Benskey, M. J., et al. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3433 · Cited by 201

Neurodegenerative Disease and the NLRP3 Inflammasome

Holbrook, J. A., Jarosz-Griffiths, H., Caseley, E. A., Reyna, S. J. L., Poulter, J. A., Williams‐Gray, C. H., Peckham, D. G., & McDermott, M. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.643254 · Cited by 201

Novel Approaches for the Treatment of Alzheimer’s and Parkinson’s Disease

Bulck, M. V., Sierra‐Magro, A., Alarcón-Gil, J., Pérez‐Castillo, A., & Morales-Garcia, J. A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20030719 · Cited by 186

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

Mitochondrial damage by α-synuclein causes cell death in human dopaminergic neurons

Ganjam, G. K., Bolte, K., Matschke, L. A., Neitemeier, S., Dolga, A. M., Höllerhage, M., Höglinger, G. U., Adamczyk, A., Decher, N., Oertel, W. H., et al. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-2091-2 · Cited by 187

The subcellular arrangement of alpha-synuclein proteoforms in the Parkinson’s disease brain as revealed by multicolor STED microscopy

Moors, T. E., Maat, C. A., Niedieker, D., Mona, D., Petersen, D., Huisman, E., Kole, J., El‐Mashtoly, S. F., Spycher, L., Zago, W. M., et al. (2021) · Acta Neuropathologica · doi:10.1007/s00401-021-02329-9 · Cited by 155

Redox Mechanisms in Neurodegeneration: From Disease Outcomes to Therapeutic Opportunities

Sbodio, J. I., Snyder, S. H., & Paul, B. D. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7321 · Cited by 149

NLRP3 inflammasome in neurodegenerative disease

Anderson, F. L., Biggs, K. E., Rankin, B. E., & Havrda, M. C. (2022) · Translational research · doi:10.1016/j.trsl.2022.08.006 · Cited by 154

Genetics and Therapies for GM2 Gangliosidosis

Cachón-González, M. B., Zaccariotto, E., & Cox, T. M. (2018) · Current Gene Therapy · doi:10.2174/1566523218666180404162622 · Cited by 141

Mitochondria at the interface between neurodegeneration and neuroinflammation

Bader, V., & Winklhofer, K. F. (2019) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2019.05.028 · Cited by 135

α‐Synuclein evokes NLRP3 inflammasome‐mediated IL ‐1β secretion from primary human microglia

Pike, A. F., Varanita, T., Herrebout, M. A. C., Plug, B. C., Kole, J., Musters, R. J. P., Teunissen, C. E., Hoozemans, J. J. M., Bubacco, L., & Veerhuis, R. (2021) · Glia · doi:10.1002/glia.23970 · Cited by 136

Reactive microglia enhance the transmission of exosomal α-synuclein via toll-like receptor 2

Xia, Y., Zhang, G., Kou, L., Yin, S., Han, C., Hu, J., Wan, F., Sun, Y., Wu, J., Li, Y., et al. (2021) · Brain · doi:10.1093/brain/awab122 · Cited by 123

Dopamine signaling modulates microglial NLRP3 inflammasome activation: implications for Parkinson’s disease

Pike, A. F., Longhena, F., Faustini, G., van Eik, J.-M., Gombert, I., Herrebout, M. A. C., Fayed, M. M. H. E., Sandre, M., Varanita, T., Teunissen, C. E., et al. (2022) · Journal of Neuroinflammation · doi:10.1186/s12974-022-02410-4 · Cited by 124

Neurodegeneration by α-synuclein-specific T cells in AAV-A53T-α-synuclein Parkinson’s disease mice

Karikari, A. A., McFleder, R. L., Ribechini, E., Blum, R., Bruttel, V., Knorr, S., Gehmeyr, M., Volkmann, J., Brotchie, J. M., Ahsan, F., et al. (2022) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2022.01.007 · Cited by 116

Reducing C-terminal truncation mitigates synucleinopathy and neurodegeneration in a transgenic model of multiple system atrophy

Bassil, F., Fernagut, P., Bézard, E., Pruvost, A., Lesté-Lasserre, T., Hoang, Q. Q., Ringe, D., Petsko, G. A., & Meissner, W. G. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1609291113 · Cited by 111

Immunomodulatory Effects of Dopamine in Inflammatory Diseases

Feng, Y., & Lü, Y. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.663102 · Cited by 113

SGK1 inhibition in glia ameliorates pathologies and symptoms in Parkinson disease animal models

Kwon, O., Song, J., Yang, Y., Kim, S., Kim, J. Y., Seok, M., Hwang, I., Yu, J., Karmacharya, J., Maeng, H., et al. (2021) · EMBO Molecular Medicine · doi:10.15252/emmm.202013076 · Cited by 110

A novel role of NLRP3-generated IL-1β in the acute-chronic transition of peripheral lipopolysaccharide-elicited neuroinflammation: implications for sepsis-associated neurodegeneration

Zhao, Z., Wang, Y., Zhou, R., Li, Y., Gao, Y., Tu, D., Wilson, B., Song, S., Feng, J., Hong, J.-S., et al. (2020) · Journal of Neuroinflammation · doi:10.1186/s12974-020-1728-5 · Cited by 109

New insights on the structure of alpha-synuclein fibrils using cryo-electron microscopy

Guerrero-Ferreira, R., Kováčik, Ľ., Ni, D., & Stahlberg, H. (2020) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2020.01.014 · Cited by 109

Temporal evolution of microglia and α-synuclein accumulation following foetal grafting in Parkinson’s disease

Olanow, C. W., Savolainen, M., Chu, Y., Halliday, G. M., & Kordower, J. H. (2019) · Brain · doi:10.1093/brain/awz104 · Cited by 112

Phytochemicals as Novel Therapeutic Strategies for NLRP3 Inflammasome-Related Neurological, Metabolic, and Inflammatory Diseases

Pellegrini, C., Fornai, M., Antonioli, L., Blandizzi, C., & Calderone, V. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20122876 · Cited by 113

Peripheral innate immune and bacterial signals relate to clinical heterogeneity in Parkinson’s disease

Wijeyekoon, R., Kronenberg‐Versteeg, D., Scott, K. M., Hayat, S., Kuan, W., Evans, J., Breen, D. P., Cummins, G. A., Jones, J., Clatworthy, M. R., et al. (2020) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2020.01.018 · Cited by 105

α-Synuclein pathology as a target in neurodegenerative diseases

Park, H.-J., Kam, T., Dawson, V. L., & Dawson, T. M. (2024) · Nature Reviews Neurology · doi:10.1038/s41582-024-01043-w · Cited by 121

C-terminal truncation of α-synuclein promotes amyloid fibril amplification at physiological pH

van der Wateren, I. M., Knowles, T. P. J., Buell, A. K., Dobson, C. M., & Galvagnion, C. (2018) · Chemical Science · doi:10.1039/c8sc01109e · Cited by 98

NLRP3 Inflammasome-Mediated Neuroinflammation and Related Mitochondrial Impairment in Parkinson’s Disease

Han, Q.-Q., & Le, W. (2023) · Neuroscience Bulletin · doi:10.1007/s12264-023-01023-y · Cited by 106

Pre-symptomatic Caspase-1 inhibitor delays cognitive decline in a mouse model of Alzheimer disease and aging

Flores, J., Noël, A., Foveau, B., Beauchet, O., & LeBlanc, A. C. (2020) · Nature Communications · doi:10.1038/s41467-020-18405-9 · Cited by 103

Aggregation of Disordered Proteins Associated with Neurodegeneration

Tsoi, P. S., Quan, M. D., Ferreon, J. C., & Ferreon, A. C. M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24043380 · Cited by 103

The N terminus of α-synuclein dictates fibril formation

McGlinchey, R., Ni, X., Shadish, J. A., Jiang, J.-S., & Lee, J. C. (2021) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.2023487118 · Cited by 89

Caspase‐1 inhibition prevents neuronal death by targeting the canonical inflammasome pathway of pyroptosis in a murine model of cerebral ischemia

Li, J., Hao, J., Yao, D., Li, R., Li, X. X., Yu, Z., Luo, X., Liu, X., Wang, M., & Wang, W. (2020) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.13384 · Cited by 89

Key Mechanisms and Potential Targets of the NLRP3 Inflammasome in Neurodegenerative Diseases

Guan, Y., & Han, F. (2020) · Frontiers in Integrative Neuroscience · doi:10.3389/fnint.2020.00037 · Cited by 90

Role of NLRP3 Inflammasome in Parkinson’s Disease and Therapeutic Considerations

Nguyen, L. T. N., Nguyễn, H. Đ., Kim, Y. J., Nguyen, T. T., Lai, T. T., Lee, Y. K., Ma, H., & Kim, Y. E. (2022) · Journal of Parkinson s Disease · doi:10.3233/jpd-223290 · Cited by 90

The effect of truncation on prion-like properties of α-synuclein

Terada, M., Suzuki, G., Nonaka, T., Kametani, F., Tamaoka, A., & Hasegawa, M. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.001862 · Cited by 85

Targeting NLRP3 Inflammasome With Nrf2 Inducers in Central Nervous System Disorders

Tastan, B., Arioz, B. I., & Genç, Ş. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.865772 · Cited by 87

Plasma-borne indicators of inflammasome activity in Parkinson’s disease patients

Anderson, F. L., von Herrmann, K. M., Andrew, A. S., Kuras, Y. I., Young, A. L., Scherzer, C. R., Hickey, W. F., Lee, S., & Havrda, M. C. (2021) · npj Parkinson s Disease · doi:10.1038/s41531-020-00147-6 · Cited by 89

Inflammasome assembly in neurodegenerative diseases

Singh, J., Habean, M. L., & Panicker, N. (2023) · Trends in Neurosciences · doi:10.1016/j.tins.2023.07.009 · Cited by 83

C-terminal α-synuclein truncations are linked to cysteine cathepsin activity in Parkinson’s disease

McGlinchey, R. P., Lacy, S. M., Huffer, K., Tayebi, N., Sidransky, E., & Lee, J. C. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.008930 · Cited by 79

Cannabinoids as Key Regulators of Inflammasome Signaling: A Current Perspective

Suryavanshi, S. V., Kovalchuk, I., & Kovalchuk, O. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2020.613613 · Cited by 87

Understanding the involvement of innate immunity and the Nrf2-NLRP3 axis on mitochondrial health in Parkinson's disease

Rajan, S., Tryphena, K. P., Khan, S. S., Vora, L. K., Srivastava, S., Singh, S. B., & Khatri, D. K. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101915 · Cited by 84

The Endotoxin Hypothesis of Parkinson's Disease

Brown, G. C., Camacho, M., & Williams‐Gray, C. H. (2023) · Movement Disorders · doi:10.1002/mds.29432 · Cited by 85

Alpha-Synuclein as a Prominent Actor in the Inflammatory Synaptopathy of Parkinson’s Disease

Cardinale, A., Calabrese, V., de Iure, A., & Picconi, B. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126517 · Cited by 79

Role of Inflammasomes in Neuroimmune and Neurodegenerative Diseases: A Systematic Review

Lang, Y., Chu, F., Shen, D., Zhang, W., Zheng, C., Zhu, J., & Cui, L. (2018) · Mediators of Inflammation · doi:10.1155/2018/1549549 · Cited by 80

Targeting α-Synuclein for PD Therapeutics: A Pursuit on All Fronts

Teil, M., Arotçarena, M.-L., Faggiani, E., Laferrière, F., Bézard, E., & Dehay, B. (2020) · Biomolecules · doi:10.3390/biom10030391 · Cited by 80

C-terminal truncation exacerbates the aggregation and cytotoxicity of α-Synuclein: A vicious cycle in Parkinson's disease

Ma, L., Yang, C., Zhang, X., Li, Y., Wang, S. L., Zheng, L., & Huang, K. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.10.003 · Cited by 78

Berberine Protects Against NLRP3 Inflammasome via Ameliorating Autophagic Impairment in MPTP-Induced Parkinson’s Disease Model

Huang, S., Liu, H., Lin, Y., Liu, M., Lǐ, Y., Mao, H., Zhang, Z., Zhang, Y., Ye, P., Ding, L., et al. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.618787 · Cited by 80

Inflammasomes: Mechanisms of Action and Involvement in Human Diseases

Bulté, D., Rigamonti, C., Romano, A., & Mortellaro, A. (2023) · Cells · doi:10.3390/cells12131766 · Cited by 83

NLRP3 Inflammasomes in Parkinson’s disease and their Regulation by Parkin

Yan, Y., Fang, Y., Zheng, R., Pu, J., & Zhang, B. (2020) · Neuroscience · doi:10.1016/j.neuroscience.2020.08.004 · Cited by 72

Roles of α‑synuclein in gastrointestinal microbiome dysbiosis‑related Parkinson's disease progression (Review)

Lei, Q., Wu, T., Wu, J., Hu, X., Guan, Y., Wang, Y., Yan, J., & Shi, G. (2021) · Molecular Medicine Reports · doi:10.3892/mmr.2021.12374 · Cited by 74

Altered ceramide metabolism is a feature in the extracellular vesicle-mediated spread of alpha-synuclein in Lewy body disorders

Kurzawa‐Akanbi, M., Tammireddy, S. R., Fabrik, I., Gliaudelytė, L., Doherty, M. K., Heap, R. E., Matečko‐Burmann, I., Burmann, B. M., Trost, M., Lucocq, J. M., et al. (2021) · Acta Neuropathologica · doi:10.1007/s00401-021-02367-3 · Cited by 71

Alpha-Synuclein Contribution to Neuronal and Glial Damage in Parkinson’s Disease

Saramowicz, K., Siwecka, N., Galita, G., Kucharska-Lusina, A., Rozpędek‐Kamińska, W., & Majsterek, I. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms25010360 · Cited by 79

An Update on the Critical Role of α-Synuclein in Parkinson’s Disease and Other Synucleinopathies: from Tissue to Cellular and Molecular Levels

Serratos, I. N., Hernández‐Pérez, E., Campos, C., Aschner, M., & Santamarı́a, A. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02596-3 · Cited by 70

Therapeutic functions of astrocytes to treat α-synuclein pathology in Parkinson’s disease

Yang, Y., Song, J., Choi, Y. R., Kim, S. H., Seok, M., Wulansari, N., Darsono, W. H. W., Kwon, O., Chang, M., Park, S. M., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2110746119 · Cited by 61

Total Synthesis of (±)-Berkeleyone A

Elkin, M., Szewczyk, S. M., Scruse, A. C., & Newhouse, T. R. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.6b12914 · Cited by 63

Effects of α-Synuclein-Associated Post-Translational Modifications in Parkinson’s Disease

He, S., Wang, F., Yung, K. K. L., Zhang, S., & Qu, S. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00028 · Cited by 62

Neuroprotective Effects of Betulin in Pharmacological and Transgenic Caenorhabditis elegans Models of Parkinson’s Disease

Tsai, C.-W., Tsai, R.-T., Liu, S., Chen, C., Tsai, M.-C., Chien, S.-H., Hung, H., Lin, S., Shyu, W., & Fu, R. (2017) · Cell Transplantation · doi:10.1177/0963689717738785 · Cited by 64

Microglia Pyroptosis: A Candidate Target for Neurological Diseases Treatment

Wu, X., Wan, T., Gao, X., Fu, M., Duan, Y., Shen, X., & Guo, W. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.922331 · Cited by 64

MLKL deficiency alleviates neuroinflammation and motor deficits in the α-synuclein transgenic mouse model of Parkinson’s disease

Geng, L., Gao, W., Saiyin, H., Li, Y., Zeng, Y., Zhang, Z., Liu, Z., Liu, Z., Gao, Q., An, P., et al. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00686-5 · Cited by 66

The Interplay Between Beta-Amyloid 1–42 (Aβ1–42)-Induced Hippocampal Inflammatory Response, p-tau, Vascular Pathology, and Their Synergistic Contributions to Neuronal Death and Behavioral Deficits

Guzmán, B. C., Chaffey, T. E., Palpagama, T. H., Waters, S., Boix, J., Tate, W. P., Peppercorn, K., Dragunow, M., Waldvogel, H. J., Faull, R. L. M., et al. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.552073 · Cited by 63

Crosstalk Between the NLRP3 Inflammasome/ASC Speck and Amyloid Protein Aggregates Drives Disease Progression in Alzheimer’s and Parkinson’s Disease

Hulse, J. P., & Bhaskar, K. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.805169 · Cited by 63

C-terminal truncation modulates α-Synuclein’s cytotoxicity and aggregation by promoting the interactions with membrane and chaperone

Zhang, C., Pei, Y., Zhang, Z., Xu, L., Liu, X., Jiang, L., Pielak, G. J., Zhou, X., Liu, M., & Li, C. (2022) · Communications Biology · doi:10.1038/s42003-022-03768-0 · Cited by 57

Looking at the recent advances in understanding α-synuclein and its aggregation through the proteoform prism

Uversky, V. N. (2017) · F1000Research · doi:10.12688/f1000research.10536.1 · Cited by 59

Targeting the NLRP3 Inflammasome in Neuroinflammation: Health Promoting Effects of Dietary Phytochemicals in Neurological Disorders

Hung, W., Ho, C., & Pan, M. (2019) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201900550 · Cited by 57

Progress in the molecular pathogenesis and nucleic acid therapeutics for Parkinson's disease in the precision medicine era

Li, D., Mastaglia, F. L., Fletcher, S., & Wilton, S. D. (2020) · Medicinal Research Reviews · doi:10.1002/med.21718 · Cited by 59

Baicalin exerts neuroprotective actions by regulating the Nrf2-NLRP3 axis in toxin-induced models of Parkinson's disease

Huang, J., Zhang, X., Yang, X., Yv, Q., Ye, F., Chen, S., Cui, Y., Gu, L., Zhu, M., & Li, W. (2023) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2023.110820 · Cited by 53

Nicotine slows down oligomerisation of α-synuclein and ameliorates cytotoxicity in a yeast model of Parkinson's disease

Kardani, J., Sethi, R., & Roy, I. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.02.002 · Cited by 51

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Han, D., Zheng, W., Wang, X., & Chen, Z. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.00045 · Cited by 55

Neurons and Glia Interplay in α-Synucleinopathies

Mavroeidi, P., & Xilouri, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094994 · Cited by 55

Therapeutic Role of Inflammasome Inhibitors in Neurodegenerative Disorders

Lahooti, B., Chhibber, T., Bagchi, S., Varahachalam, S. P., & Jayant, R. D. (2021) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2020.11.004 · Cited by 50

The potential convergence of NLRP3 inflammasome, potassium, and dopamine mechanisms in Parkinson’s disease

Pike, A. F., Szabó, I., Veerhuis, R., & Bubacco, L. (2022) · npj Parkinson s Disease · doi:10.1038/s41531-022-00293-z · Cited by 50

Inflammasome Activation in Parkinson’s Disease

Jewell, S. L., Herath, A. M., & Gordon, R. (2022) · Journal of Parkinson s Disease · doi:10.3233/jpd-223338 · Cited by 53

The NLRP3 inflammasome: a new player in neurological diseases

Eren, E., & Özören, N. (2019) · TURKISH JOURNAL OF BIOLOGY · doi:10.3906/biy-1909-31 · Cited by 54

Role of the NLRP3 inflammasome in neurodegenerative diseases and therapeutic implications

Duan, Y., Kelley, N., & He, Y. (2020) · Neural Regeneration Research · doi:10.4103/1673-5374.272576 · Cited by 50

Phytochemical inhibitors of the NLRP3 inflammasome for the treatment of inflammatory diseases

Özenver, N., & Efferth, T. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105710 · Cited by 54

Modulation of the Interactions Between α-Synuclein and Lipid Membranes by Post-translational Modifications

Bell, R., & Vendruscolo, M. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2021.661117 · Cited by 52

Inflammasomes: An Emerging Mechanism Translating Environmental Toxicant Exposure Into Neuroinflammation in Parkinson’s Disease

Anderson, F. L., Coffey, M., Berwin, B. L., & Havrda, M. C. (2018) · Toxicological Sciences · doi:10.1093/toxsci/kfy219 · Cited by 48

The making of a Lewy body: the role of alpha-synuclein post-fibrillization modifications in regulating the formation and the maturation of pathological inclusions.Preprint

Mahul‐Mellier, A., Altay, M. F., Burtscher, J., Maharjan, N., Ait‐Bouziad, N., Chiki, A., Vingill, S., Wade‐Martins, R., Holton, J. L., Strand, C., et al. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/500058 · Cited by 45

Brain region-specific microglial and astrocytic activation in response to systemic lipopolysaccharides exposure

Brandi, E., Torres-Garcia, L., Svanbergsson, A., Haikal, C., Liu, D., Li, W., & Li, J. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.910988 · Cited by 48

ASC specks exacerbate α‑synuclein pathology via amplifying NLRP3 inflammasome activities

Zheng, R., Yan, Y., Dai, S., Ruan, Y., Chen, Y., Hu, C., Lin, Z., Xue, N., Song, Z., Liu, Y. F., et al. (2023) · Journal of Neuroinflammation · doi:10.1186/s12974-023-02709-w · Cited by 50

C-terminal truncation exacerbates the aggregation and cytotoxicity of α-Synuclein: A vicious cycle in Parkinson's disease

Ma, L., Yang, C., Zhang, X., Li, Y., Wang, S. L., Zheng, L., & Huang, K. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.10.003 · Cited by 78

Triggering of inflammasome by aggregated α-synuclein, an inflammatory response in synucleinopathies

Codolo, G., Plotegher, N., Pozzobon, T., Brucale, M., Tessari, I., Bubacco, L., & de Bernard, M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055375 · Cited by 585

Alpha-Synuclein Aggregates Activate the Nlrp3 Inflammasome Following Vesicle Rupture

Cedillos, R. O. (2013) · Loyola eCommons (Loyola University of Chicago) · Cited by 4

α-synuclein promotes progression of Parkinson's disease by upregulating autophagy signaling pathway to activate NLRP3 inflammasome

Wang, X., Chi, J., Huang, D., Ding, L., Zhao, X., Jiang, L., Yu, Y., & Gao, F. (2019) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2019.8297 · Cited by 61

IC100 blocks inflammasome activation induced by α-synuclein aggregates and ASC specks

Cyr, B. S., Vontell, R., Hadad, R., Vaccari, J. P. D. R., & Keane, R. W. (2025) · npj Parkinson s Disease · doi:10.1038/s41531-025-00963-8 · Cited by 11