Triggering of inflammasome by aggregated α-synuclein, an inflammatory response in synucleinopathies
Open accessAbstract
Parkinson's disease (PD) is one of the most common neurodegenerative diseases. It is characterized by the loss of dopaminergic neurons in the substantia nigra pars compacta of the brain. Another feature is represented by the formation in these cells of inclusions called Lewy bodies (LB), principally constituted by fibrillar α-synuclein (αSyn). This protein is considered a key element in the aetiology of a group of neurodegenerative disorders termed synucleinopathies, which include PD, but the cellular and molecular mechanisms involved are not completely clear. It is established that the inflammatory process plays a crucial role in the pathogenesis and/or progression of PD; moreover, it is known that aggregated αSyn, released by neurons, activates microglia cells to produce pro-inflammatory mediators, such as IL-1β. IL-1β is one of the strongest pro-inflammatory cytokines; it is produced as an inactive mediator, and its maturation and activation requires inflammasome activation. In particular, the NLRP3 inflammasome is activated by a wide variety of stimuli, among which are crystallized and particulate material. In this work, we investigated the possibility that IL-1β production, induced by fibrillar αSyn, is involved the inflammasome activation. We demonstrated the competence of monomeric and fibrillar αSyn to induce synthesis of IL-1β, through TLR2 interaction; we found that the secretion of the mature cytokine was a peculiarity of the fibrillated protein. Moreover, we observed that the secretion of IL-1β involves NLRP3 inflammasome activation. The latter relies on the phagocytosis of fibrillar αSyn, followed by increased ROS production and cathepsin B release into the cytosol. Taken together, our data support the notion that fibrillar αSyn, likely released by neuronal degeneration, acts as an endogenous trigger inducing a strong inflammatory response in PD.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In an in vitro experiment, both monomeric and fibrillary α-synuclein can stimulate TLR2 and induce expression of pro-IL-1β, but only fibrillary α-synuclein can activate NLRP3 inflammasome, resulting in secretion of active IL-1β.
“In an in vitro experiment, both monomeric and fibrillary α-synuclein can stimulate TLR2 and induce the expression of pro-IL-1β, but only fibrillary α-synuclein can activate the NLRP3 inflammasome, resulting in the secretion of active IL-1β.358”
From Role of neuroinflammation in neurodegeneration development (2023) · cites this paper as [358]
The Introduction and Discussion report that both monomeric and fibrillar α-synuclein induce pro-IL-1β through TLR2, while only fibrils induce inflammasome-dependent secretion of mature IL-1β. The Results section on IL-1β maturation says the data *suggest* that NLRP3 is the inflammasome mainly involved; it does not establish the claim’s more definite statement that fibrils activate NLRP3. (LLM, conf=0.83)
Experimental — accuracy not yet measuredTargeting caspase-1 decreases secretion of IL-1β and attenuates susceptibility of dopaminergic neurons.
“Targeting caspase-1, a downstream molecule of NLRP3, is another promising method, which was found to decrease the secretion of IL-1β and attenuate the susceptibility of dopaminergic neurons.358”
From Role of neuroinflammation in neurodegeneration development (2023) · cites this paper as [358]
The Results section reports that a caspase-1 inhibitor impaired IL-1β secretion from human monocytes exposed to fibrillar α-synuclein. The Discussion describes how inflammation may harm dopaminergic neurons, but the paper does not show that inhibiting caspase-1 attenuates their susceptibility. Page numbers were not available in our copy. (LLM, conf=0.88)
Experimental — accuracy not yet measuredFibrillar, but not monomeric, α-synuclein induced NLRP3- and caspase-1-mediated IL-1β secretion in human monocytes and BV2 microglial cell line, or via TLR-2 signaling in rodent microglial cells.
“The fibrillar, but not monomeric, form of α-synuclein induced NLRP3- and caspase-1–mediated IL-1β secretion in human monocytes and BV2 microglial cell line (238), or via TLR-2 signaling pathway in rodents microglial cells (250).”
From The gut-brain axis: how microbiota and host inflammasome influence brain physiology and pathology (2020) · cites this paper as [238]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Analysis of Relative Gene Expression Data Using Real-Time Quantitative PCR and the 2−ΔΔCT Method
Livak, K. J., & Schmittgen, T. D. (2001) · Methods · doi:10.1006/meth.2001.1262 · Cited by 180,860 · see citing works
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
Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease
Polymeropoulos, M. H., Lavedan, C., Leroy, E., Ide, S. E., Dehejia, A., Dutra, A., Pike, B., Root, H., Rubenstein, J., Boyer, R., et al. (1997) · Science · doi:10.1126/science.276.5321.2045 · Cited by 8,240 · see citing works
Protein Misfolding, Functional Amyloid, and Human Disease
Chiti, F., & Dobson, C. M. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.123901 · Cited by 6,435 · see citing works
Martinon, F., Burns, K., & Tschopp, J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00599-3 · Cited by 6,066 · see citing works
Schroder, K., & Tschopp, J. (2010) · Cell · doi:10.1016/j.cell.2010.01.040 · Cited by 5,475 · see citing works
Gout-associated uric acid crystals activate the NALP3 inflammasome
Martinon, F., Pétrilli, V., Mayor, A., Tardivel, A., & Tschopp, J. (2006) · Nature · doi:10.1038/nature04516 · Cited by 5,326 · see citing works
Microglia-mediated neurotoxicity: uncovering the molecular mechanisms
Block, M. L., Zecca, L., & Hong, J.-S. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2038 · Cited by 4,110 · see citing works
AlaSOPro mutation in the gene encoding α-synuclein in Parkinson's disease
Krüger, R., Kuhn, W., Müller, T., Woitalla, D., Graeber, M., Kösel, S., Przuntek, H., Epplen, J. T., Schols, L., & Riess, O. (1998) · Nature Genetics · doi:10.1038/ng0298-106 · Cited by 3,836 · see citing works
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 3,151 · see citing works
Cryopyrin activates the inflammasome in response to toxins and ATP
Mariathasan, S., Weiss, D. S., Newton, K., McBride, J., O'Rourke, K., Roose-Girma, M., Lee, W. P., Weinrauch, Y., Monack, D. M., & Dixit, V. M. (2006) · Nature · doi:10.1038/nature04515 · Cited by 3,080 · see citing works
Hornung, V., Bauernfeind, F., Halle, A., Samstad, E. O., Kono, H., Rock, K. L., Fitzgerald, K. A., & Latz, E. (2008) · Nature Immunology · doi:10.1038/ni.1631 · Cited by 3,065 · see citing works
McGeer, P. L., Itagaki, S., Boyes, B. E., & McGeer, E. G. (1988) · Neurology · doi:10.1212/wnl.38.8.1285 · Cited by 2,990 · see citing works
The new mutation, E46K, of α‐synuclein causes parkinson and Lewy body dementia
Zarranz, J. J., Alegre, J., Gómez‐Esteban, J. C., Lezcano, E., Ros, R., Ampuero, I., Vidal, L., Hoenicka, J., Rodriguez, O., Atarés, B., et al. (2004) · Annals of Neurology · doi:10.1002/ana.10795 · Cited by 2,737 · see citing works
Thioredoxin-interacting protein links oxidative stress to inflammasome activation
Zhou, R., Tardivel, A., Thorens, B., Choi, I., & Tschopp, J. (2010) · Nature Immunology · doi:10.1038/ni.1831 · Cited by 2,708 · see citing works
Innate Immune Activation Through Nalp3 Inflammasome Sensing of Asbestos and Silica
Dostert, C., Pétrilli, V., Van Bruggen, R., Steele, C., Mossman, B. T., & Tschopp, J. (2008) · Science · doi:10.1126/science.1156995 · Cited by 2,658 · see citing works
The NALP3 inflammasome is involved in the innate immune response to amyloid-β
Halle, A., Hornung, V., Petzold, G. C., Stewart, C. R., Monks, B. G., Reinheckel, T., Fitzgerald, K. A., Latz, E., Moore, K. J., & Golenbock, D. T. (2008) · Nature Immunology · doi:10.1038/ni.1636 · Cited by 2,441 · see citing works
LeVine, H. (1993) · Protein Science · doi:10.1002/pro.5560020312 · Cited by 2,268 · see citing works
Inflammasomes in health and disease
Strowig, T., Henao-Mejia, J., Elinav, E., & Flavell, R. (2012) · Nature · doi:10.1038/nature10759 · Cited by 2,230 · see citing works
Li, J.-Y., Englund, E., Holton, J. L., Soulet, D., Hagell, P., Lees, A. J., Lashley, T., Quinn, N. P., Rehncrona, S., Björklund, A., et al. (2008) · Nature Medicine · doi:10.1038/nm1746 · Cited by 1,845 · see citing works
MyD88 is an adaptor protein in the hToll/IL-1 receptor family signaling pathways.
Medzhitov, R., Preston-Hurlburt, P., Kopp, E., Stadlen, A., Chen, C.-Q., Ghosh, S., & Janeway, C. (1998) · Molecules and Cells · doi:10.1016/s1097-2765(00)80136-7 · Cited by 1,783 · see citing works
Activation of the NALP3 inflammasome is triggered by low intracellular potassium concentration
Pétrilli, V, Papin, S., Dostert, C., Mayor, A., Martinon, F., & Tschopp, J. (2007) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4402195 · Cited by 1,445 · see citing works
Masters, S. L., Dunne, A., Subramanian, S. L., Hull, R. L., Tannahill, G. M., Sharp, F. A., Becker, C., Franchi, L., Yoshihara, E., Chen, Z., et al. (2010) · Nature Immunology · doi:10.1038/ni.1935 · Cited by 1,330 · see citing works
Zhang, W., Wang, T., Pei, Z., Miller, D. S., Wu, X., Block, M. L., Wilson, B., Zhang, W., Zhou, Y., Hong, J.-S., et al. (2005) · The FASEB Journal · doi:10.1096/fj.04-2751com · Cited by 1,265 · see citing works
In vivo imaging of microglial activation with [11C](R)-PK11195 PET in idiopathic Parkinson's disease
Gerhard, A., Pavese, N., Hotton, G., Turkheimer, F., Es, M., Hammers, A., Eggert, K., Oertel, W., Banati, R. B., & Brooks, D. J. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.08.002 · Cited by 1,200 · see citing works
Molecular Cloning of the Interleukin-1β Converting Enzyme
Cerretti, D. P., Kozlosky, C. J., Mosley, B., Nelson, N. C., Ness, K. V., Greenstreet, T. A., March, C. J., Kronheim, S. R., Druck, T., Cannizzaro, L. A., et al. (1992) · Science · doi:10.1126/science.1373520 · Cited by 1,147 · see citing works
Rajamäki, K., Lappalainen, J., Öörni, K., Välimäki, E., Matikainen, S., Kovanen, P. T., & Eklund, K. K. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011765 · Cited by 1,039 · see citing works
Active Caspase-1 Is a Regulator of Unconventional Protein Secretion
Keller, M., Rüegg, A., Werner, S., & Beer, H. (2008) · Cell · doi:10.1016/j.cell.2007.12.040 · Cited by 851 · see citing works
El‐Agnaf, O. M. A., Salem, S. A., Paleologou, K. E., Curran, M. D., Gibson, M. J., Court, J. A., Schlossmacher, M. G., & Allsop, D. (2006) · The FASEB Journal · doi:10.1096/fj.03-1449com · Cited by 715 · see citing works
El-Agnaf, O. M. A., Salem, S. A., Paleologou, K. E., Cooper, L. J., Fullwood, N. J., Gibson, M. J., Curran, M. D., Court, J. A., Mann, D. M. A., Ikeda, S.-I., et al. (2003) · The FASEB Journal · doi:10.1096/fj.03-0098fje · Cited by 590 · see citing works
de Rijk, M. C., Launer, L. J., Berger, K., Breteler, M. M. B., Dartigues, J. F., Baldereschi, M., Fratiglioni, L., Lobo, A., Martinez-Lage, J., Trenkwalder, C., et al. (2000) · PubMed · Cited by 528 · see citing works
Endogenous ligands of TLR2 and TLR4: agonists or assistants?
Erridge, C. (2010) · Journal of Leukocyte Biology · doi:10.1189/jlb.1209775 · Cited by 518 · see citing works
Molecular Mechanism of NLRP3 Inflammasome Activation
Jin, C., & Flavell, R. A. (2010) · Journal of Clinical Immunology · doi:10.1007/s10875-010-9440-3 · Cited by 440 · see citing works
Tokuda, T., Salem, S. A., Allsop, D., Mizuno, T., Nakagawa, M., Qureshi, M. M., Locascio, J. J., Schlossmacher, M. G., & El-Agnaf, O. M. A. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.08.024 · Cited by 425 · see citing works
Croisier, E., Moran, L. B., Dexter, D. T., Pearce, R. K., & Graeber, M. B. (2005) · Journal of Neuroinflammation · doi:10.1186/1742-2094-2-14 · Cited by 414 · see citing works
Theodore, S., Cao, S., McLean, P. J., & Standaert, D. G. (2008) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31818e5e99 · Cited by 367 · see citing works
Borghi, R., Marchese, R., Negro, A., Marinelli, L., Forloni, G., Zaccheo, D., Abbruzzese, G., & Tabaton, M. (2000) · Neuroscience Letters · doi:10.1016/s0304-3940(00)01153-8 · Cited by 363 · see citing works
Getts, D. R., Terry, R. L., Getts, M. T., Müller, M., Rana, S., Shrestha, B., Radford, J., Van Rooijen, N., Campbell, I. L., & King, N. J. C. (2008) · The Journal of Experimental Medicine · doi:10.1084/jem.20080421 · Cited by 360 · see citing works
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 · see citing works
IL‐1: Discoveries, controversies and future directions
Dinarello, C. A. (2010) · European Journal of Immunology · doi:10.1002/eji.201040319 · Cited by 270 · see citing works
Lee, E.-J., Woo, M.-S., Moon, P., Baek, M., Choi, I.-Y., Kim, W.-K., Junn, E., & Kim, H.-S. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0903480 · Cited by 267 · see citing works
The plasma alpha-synuclein levels in patients with Parkinson’s disease and multiple system atrophy
Lee, P. H., Lee, G., Park, H. J., Bang, O. Y., Joo, I. S., & Huh, K. (2006) · Journal of Neural Transmission · doi:10.1007/s00702-005-0427-9 · Cited by 242 · see citing works
Ferrari, C. C., Pott Godoy, M. C., Tarelli, R., Chertoff, M., Depino, A. M., & Pitossi, F. J. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.06.013 · Cited by 235 · see citing works
(2000) · Neurology · doi:10.1212/wnl.54.5.21a · Cited by 209 · see citing works
α-Synuclein Alters Toll-Like Receptor Expression
Béraud, D., Twomey, M. A., Bloom, B., Mittereder, A., Ton, V., Neitzke, K., Chasovskikh, S., Mhyre, T. R., & Maguire‐Zeiss, K. A. (2011) · Frontiers in Neuroscience · doi:10.3389/fnins.2011.00080 · Cited by 199 · see citing works
Alpha-synuclein release by neurons activates the inflammatory response in a microglial cell line
Alvarez‐Erviti, L., Couch, Y., Richardson, J. C., Cooper, J. A. D., & Wood, M. J. A. (2011) · Neuroscience Research · doi:10.1016/j.neures.2010.12.020 · Cited by 193 · see citing works
Genetics of Parkinsonʼs disease
Gasser, T. (2005) · Current Opinion in Neurology · doi:10.1097/01.wco.0000170951.08924.3d · Cited by 191 · see citing works
Djukic, M. (2006) · Brain · doi:10.1093/brain/awl206 · Cited by 186 · see citing works
A new method for purification of recombinant human α-synuclein in Escherichia coli
Huang, C., Ren, G., Zhou, H., & Wang, C.-C. (2005) · Protein Expression and Purification · doi:10.1016/j.pep.2005.02.014 · Cited by 183 · see citing works
Béraud, D., Hathaway, H. A., Trecki, J., Chasovskikh, S., Johnson, D. A., Johnson, J. A., Federoff, H. J., Shimoji, M., Mhyre, T. R., & Maguire‐Zeiss, K. A. (2012) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-012-9401-0 · Cited by 175 · see citing works
Origins and Effects of Extracellular α-synuclein: Implications in Parkinson’s Disease
Lee, S. (2007) · Journal of Molecular Neuroscience · doi:10.1007/s12031-007-0012-9 · Cited by 159 · see citing works
Structured Regions of α-Synuclein Fibrils Include the Early-Onset Parkinson's Disease Mutation Sites
Comellas, G., Lemkau, L., Nieuwkoop, A. J., Kloepper, K. D., Ladror, D. T., Ebisu, R., Woods, W. S., Lipton, A. S., George, J. M., & Rienstra, C. M. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.06.026 · Cited by 149 · see citing works
Mutant α-Synuclein Overexpression Mediates Early Proinflammatory Activity
Su, X., Federoff, H. J., & Maguire-Zeiss, K. A. (2009) · Neurotoxicity Research · doi:10.1007/s12640-009-9053-x · Cited by 145 · see citing works
Tassi, S., Carta, S., Delfino, L., Caorsi, R., Martini, A., Gattorno, M., & Rubartelli, A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1000779107 · Cited by 141 · see citing works
Misfolded α-synuclein and toll-like receptors: therapeutic targets for Parkinson's disease
Béraud, D., & Maguire‐Zeiss, K. A. (2011) · Parkinsonism & Related Disorders · doi:10.1016/s1353-8020(11)70008-6 · Cited by 135 · see citing works
Nitrated Alpha-Synuclein and Microglial Neuroregulatory Activities
Reynolds, A. D., Kadiu, I., Garg, S. K., Glanzer, J. G., Nordgren, T. M., Ciborowski, P. S., Banerjee, R. V., & Gendelman, H. E. (2008) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-008-9100-z · Cited by 128 · see citing works
Immunological features of α‐synuclein in Parkinson's disease
Roodveldt, C., Christodoulou, J. C., & Dobson, C. M. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00450.x · Cited by 95 · see citing works
Inflammatory Mechanisms of Neurodegeneration in Toxin-Based Models of Parkinson's Disease
Litteljohn, D., Mangano, E. N., Clarke, M., Bobyn, J., Moloney, K., & Hayley, S. P. (2010) · Parkinson s Disease · doi:10.4061/2011/713517 · Cited by 94 · see citing works
Hafner‐Bratkovič, I., Benčina, M., Fitzgerald, K. A., Golenbock, D. T., & Jerala, R. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1140-0 · Cited by 92 · see citing works
Palokangas, H., Metsikkö, K., & Väänänen, K. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32480-8 · Cited by 77 · see citing works
van Raaij, M. E., van Gestel, J., Segers‐Nolten, I. M. J., de Leeuw, S. W., & Subramaniam, V. (2008) · Biophysical Journal · doi:10.1529/biophysj.107.127464 · Cited by 68 · see citing works
Mankan, A. K., Kubarenko, A. V., & Hornung, V. (2011) · Clinical & Experimental Immunology · doi:10.1111/j.1365-2249.2011.04534.x · Cited by 55 · see citing works
Su, E. R., Bell, M. J., Wisniewski, S. R., Adelson, P. D., Janesko‐Feldman, K. L., Salonia, R., Clark, R. S. B., Kochanek, P. M., Kagan, V. E., & Bayır, H. (2010) · Developmental Neuroscience · doi:10.1159/000321342 · Cited by 55 · see citing works
Future directions for immune modulation in neurodegenerative disorders: focus on Parkinson’s disease
Maguire‐Zeiss, K. A., & Federoff, H. J. (2010) · Journal of Neural Transmission · doi:10.1007/s00702-010-0431-6 · Cited by 44 · see citing works
Cognet, I., de Coignac, A. B., Magistrelli, G., Jeannin, P., Aubry, J., Maisnier-Patin, K., Caron, G., Chevalier, S., Humbert, F., Nguyen, T. N., et al. (2003) · Journal of Immunological Methods · doi:10.1016/s0022-1759(02)00506-9 · Cited by 43 · see citing works
A Statistical-Mechanical Theory of Fibril Formation in Dilute Protein Solutions
van Gestel, J., & de Leeuw, S. W. (2006) · Biophysical Journal · doi:10.1529/biophysj.105.076000 · Cited by 28 · see citing works
Translocation of α-Synuclein Expressed in Escherichia coli
Ren, G., Wang, X., Hao, S., Hu, H., & Wang, C.-C. (2007) · Journal of Bacteriology · doi:10.1128/jb.01406-06 · Cited by 22 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
The NLRP3 Inflammasome: an overview of mechanisms of activation and regulation
Kelley, N., Jeltema, D., Duan, Y., & He, Y. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20133328 · Cited by 3,539 · see citing works
Inflammasomes: mechanism of action, role in disease, and therapeutics
Guo, H., Callaway, J. B., & Ting, J. P.-Y. (2015) · Nature Medicine · doi:10.1038/nm.3893 · Cited by 3,340 · see citing works
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 · see citing works
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 · see citing works
Microglia in physiology and disease
Wolf, S. A., Boddeke, H. W. G. M., & Kettenmann, H. (2017) · Annual Review of Physiology · doi:10.1146/annurev-physiol-022516-034406 · Cited by 1,426 · see citing works
Inflammation and immune dysfunction in Parkinson disease
Tansey, M. G., Wallings, R. L., Houser, M. C., Herrick, M. K., Keating, C. E., & Joers, V. (2022) · Nature Reviews Immunology · doi:10.1038/s41577-022-00684-6 · Cited by 1,382 · see citing works
Innate immune activation in neurodegenerative disease
Heneka, M. T., Kummer, M. P., & Latz, E. (2014) · Nature Reviews Immunology · doi:10.1038/nri3705 · Cited by 1,437 · see citing works
Dopamine controls systemic inflammation through inhibition of NLRP3 inflammasome
Yan, Y., Jiang, W., Liu, L., Wang, X., Ding, C., Tian, Z., & Zhou, R. (2015) · Cell · doi:10.1016/j.cell.2014.11.047 · Cited by 1,014 · see citing works
The Continuum of Aging and Age-Related Diseases: Common Mechanisms but Different Rates
Franceschi, C., Garagnani, P., Morsiani, C., Conte, M., Santoro, A., Grignolio, A., Monti, D., Capri, M., & Salvioli, S. (2018) · Frontiers in Medicine · doi:10.3389/fmed.2018.00061 · Cited by 945 · see citing works
Inflammasome inhibition prevents α-synuclein pathology and dopaminergic neurodegeneration in mice
Gordon, R., Albornoz, E. A., Christie, D. C., Langley, M. R., Kumar, V., Mantovani, S., Robertson, A. A. B., Butler, M. S., Rowe, D. B., O’Neill, L. A., et al. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aah4066 · Cited by 897 · see citing works
Neuroinflammation in Parkinson's disease and its potential as therapeutic target
Wang, Q., Liu, Y., & Zhou, J. (2015) · Translational Neurodegeneration · doi:10.1186/s40035-015-0042-0 · Cited by 884 · see citing works
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 · see citing works
The gut-brain axis: how microbiota and host inflammasome influence brain physiology and pathology
Rutsch, A., Kantsjö, J. B., & Ronchi, F. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.604179 · Cited by 821 · see citing works
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 · see citing works
Walsh, J. G., Muruve, D. A., & Power, C. (2014) · Nature Reviews Neuroscience · doi:10.1038/nrn3638 · Cited by 637 · see citing works
Microglia in Neuroinflammation and Neurodegeneration: From Understanding to Therapy
Muzio, L., Viotti, A., & Martino, G. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.742065 · Cited by 581 · see citing works
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 · see citing works
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 · see citing works
Stancu, I.-C., Cremers, N., Vanrusselt, H., Couturier, J., Vanoosthuyse, A., Kessels, S., Lodder, C., Brône, B., Huaux, F., Octave, J.-N., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-018-01957-y · Cited by 447 · see citing works
A 360° view of the inflammasome: Mechanisms of activation, cell death, and diseases
Barnett, K. C., Li, S., Liang, K., & Ting, J. P.-Y. (2023) · Cell · doi:10.1016/j.cell.2023.04.025 · Cited by 458 · see citing works
Zhou, Y., Lu, M., Du, R.-H., Qiao, C., Jiang, C.-Y., Zhang, K.-Z., Ding, J.-H., & Hu, G. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0094-3 · Cited by 455 · see citing works
The mechanisms of NLRP3 inflammasome/pyroptosis activation and their role in Parkinson's disease
Wang, S., Yuan, Y., Chen, N., & Wang, H. (2018) · International Immunopharmacology · doi:10.1016/j.intimp.2018.12.019 · Cited by 447 · see citing works
Healthy Effects of Plant Polyphenols: Molecular Mechanisms
Leri, M., Scuto, M. C., Ontario, M. L., Calabrese, V., Calabrese, E. J., Bucciantini, M., & Stefani, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21041250 · Cited by 440 · see citing works
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 · see citing works
Progress towards therapies for disease modification in Parkinson's disease
Vijiaratnam, N., Simuni, T., Bandmann, O., Morris, H. R., & Foltynie, T. (2021) · The Lancet Neurology · doi:10.1016/s1474-4422(21)00061-2 · Cited by 427 · see citing works
Han, X., Sun, S., Sun, Y., Song, Q., Zhu, J., Song, N., Chen, M., Sun, T., Xia, M., Ding, J., et al. (2019) · Autophagy · doi:10.1080/15548627.2019.1596481 · Cited by 408 · 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
NLR members NLRC4 and NLRP3 mediate sterile inflammasome activation in microglia and astrocytes
Freeman, L., Guo, H., David, C. N., Brickey, W. J., Jha, S., & Ting, J. P.-Y. (2017) · Journal of Experimental Medicine · doi:10.1084/jem.20150237 · Cited by 397 · see citing works
Microglia Mediated Neuroinflammation in Parkinson’s Disease
Işık, S., Yeman-Kıyak, B., Akbayır, R., Şeyhali-Abutayeh, R., & Arpaci, T. (2023) · Cells · doi:10.3390/cells12071012 · Cited by 402 · see citing works
Mitochondria-associated membranes (MAMs) and inflammation
Missiroli, S., Patergnani, S., Caroccia, N., Pedriali, G., Perrone, M., Previati, M., Wieckowski, M. R., & Giorgi, C. (2018) · Cell Death and Disease · doi:10.1038/s41419-017-0027-2 · Cited by 389 · see citing works
Ubiquitin signalling in neurodegeneration: mechanisms and therapeutic opportunities
Schmidt, M. F., Gan, Z. Y., Komander, D., & Dewson, G. (2021) · Cell Death and Differentiation · doi:10.1038/s41418-020-00706-7 · Cited by 373 · see citing works
NLRP3 inflammasome is expressed and functional in mouse brain microglia but not in astrocytes
Gustin, A., Kirchmeyer, M., Koncina, E., Felten, P., Losciuto, S., Heurtaux, T., Tardivel, A., Heuschling, P., & Dostert, C. (2015) · PLoS ONE · doi:10.1371/journal.pone.0130624 · Cited by 369 · see citing works
Drugging the NLRP3 inflammasome: from signalling mechanisms to therapeutic targets
Walle, L. V., & Lamkanfi, M. (2023) · Nature Reviews Drug Discovery · doi:10.1038/s41573-023-00822-2 · Cited by 376 · see citing works
Calabrese, V., Santoro, A., Monti, D., Crupi, R., Di Paola, R., Latteri, S., Cuzzocrea, S., Zappia, M., Giordano, J., Calabrese, E. J., et al. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.10.379 · Cited by 356 · see citing works
Microbiome-Gut-Brain Axis and Toll-Like Receptors in Parkinson’s Disease
Caputi, V., & Giron, M. C. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19061689 · Cited by 338 · see citing works
Sacino, A. N., Brooks, M., Thomas, M. A., McKinney, A. B., Lee, S., Regenhardt, R. W., McGarvey, N. H., Ayers, J. I., Notterpek, L. M., Borchelt, D., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1321785111 · Cited by 328 · see citing works
Ferroptosis and cell death mechanisms in Parkinson's disease
Guiney, S. J., Adlard, P. A., Bush, A. I., Finkelstein, D. I., & Ayton, S. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.01.004 · Cited by 337 · see citing works
Innate Immunity and Neurodegeneration
Labzin, L. I., Heneka, M. T., & Latz, E. (2018) · Annual Review of Medicine · doi:10.1146/annurev-med-050715-104343 · Cited by 319 · see citing works
Daniele, S. G., Béraud, D., Davenport, C., Cheng, K., Yin, H., & Maguire-Zeiss, K. A. (2015) · Science Signaling · doi:10.1126/scisignal.2005965 · Cited by 303 · see citing works
Focus on the Role of NLRP3 Inflammasome in Diseases
Fusco, R., Siracusa, R., Genovese, T., Cuzzocrea, S., & Paola, R. D. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21124223 · Cited by 292 · see citing works
TLR Agonists as Vaccine Adjuvants Targeting Cancer and Infectious Diseases
Luchner, M., Reinke, S., & Milicic, A. (2021) · Pharmaceutics · doi:10.3390/pharmaceutics13020142 · Cited by 287 · see citing works
DAMPs as mediators of sterile inflammation in aging-related pathologies
Feldman, N., Rotter-Maskowitz, A., & Okun, E. (2015) · Ageing Research Reviews · doi:10.1016/j.arr.2015.01.003 · Cited by 283 · see citing works
The role of Toll-like receptors and neuroinflammation in Parkinson’s disease
Heidari, A., Yazdanpanah, N., & Rezaei, N. (2022) · Journal of Neuroinflammation · doi:10.1186/s12974-022-02496-w · Cited by 275 · see citing works
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 279 · see citing works
Immune aging, dysmetabolism, and inflammation in neurological diseases
Deleidi, M., Jäggle, M., & Rubino, G. (2015) · Frontiers in Neuroscience · doi:10.3389/fnins.2015.00172 · Cited by 260 · see citing works
Fyn kinase regulates misfolded α-synuclein uptake and NLRP3 inflammasome activation in microglia
Panicker, N., Sarkar, S., Harischandra, D. S., Neal, M. P., Kam, T., Jin, H., Saminathan, H., Langley, M. R., Charli, A., Samidurai, M., et al. (2019) · The Journal of Experimental Medicine · doi:10.1084/jem.20182191 · Cited by 255 · see citing works
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 257 · see citing works
Doorn, K. J., Moors, T., Drukarch, B., van de Berg, W. D., Lucassen, P. J., & van Dam, A.-M. (2014) · Acta Neuropathologica Communications · doi:10.1186/s40478-014-0090-1 · Cited by 254 · see citing works
Uchihara, T., & Giasson, B. I. (2016) · Acta Neuropathologica · doi:10.1007/s00401-015-1485-1 · Cited by 249 · see citing works
microRNA-155 Regulates Alpha-Synuclein-Induced Inflammatory Responses in Models of Parkinson Disease
Thome, A. D., Harms, A. S., Volpicelli‐Daley, L. A., & Standaert, D. G. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.3900-15.2016 · Cited by 249 · see citing works
Role of α-Synuclein in Inducing Innate and Adaptive Immunity in Parkinson Disease
Allen Reish, H. E., & Standaert, D. G. (2015) · Journal of Parkinson’s Disease · doi:10.3233/jpd-140491 · Cited by 244 · see citing works
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 248 · see citing works
Ma, Q. (2023) · Pharmacological Reviews · doi:10.1124/pharmrev.122.000629 · Cited by 255 · see citing works
The microglial NLRP3 inflammasome is activated by amyotrophic lateral sclerosis proteins
Deora, V., Lee, J. D., Albornoz, E. A., McAlary, L., Jagaraj, C. J., Robertson, A. A. B., Atkin, J. D., Cooper, M. A., Schroder, K., Yerbury, J. J., et al. (2020) · Glia · doi:10.1002/glia.23728 · Cited by 245 · see citing works
Inflammasome Priming in Sterile Inflammatory Disease
Patel, M. N., Carroll, R. G., Galván-Peña, S., Mills, E. L., Olden, R., Triantafilou, M., Wolf, A. I., Bryant, C. E., Triantafilou, K., & Masters, S. L. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2016.12.007 · Cited by 241 · see citing works
Wang, D., Zhang, J., Jiang, W., Cao, Z., Zhao, F., Cai, T., Aschner, M., & Luo, W. (2017) · Autophagy · doi:10.1080/15548627.2017.1293766 · Cited by 236 · see citing works
Targeting Microglial α-Synuclein/TLRs/NF-kappaB/NLRP3 Inflammasome Axis in Parkinson’s Disease
Li, Y., Xia, Y., Yin, S., Wan, F., Hu, J., Kou, L., Sun, Y., Wu, J., Zhou, Q., Huang, J., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.719807 · Cited by 230 · see citing works
Inflammasomes as therapeutic targets in human diseases
Li, Y., Huang, H., Liu, B., Zhang, Y. L., Pan, X., Yu, X., Shen, Z., & Song, Y. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00650-z · Cited by 235 · see citing works
Inflammation is genetically implicated in Parkinson’s disease
Dzamko, N., Geczy, C. L., & Halliday, G. M. (2015) · Neuroscience · doi:10.1016/j.neuroscience.2014.10.028 · Cited by 222 · see citing works
Fan, Z., Pan, Y.-T., Zhang, Z.-Y., Yang, H., Yu, S.-Y., Zheng, Y., Ma, J.-H., & Wang, X.-M. (2020) · Journal of Neuroinflammation · doi:10.1186/s12974-019-1670-6 · Cited by 228 · see citing works
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 220 · see citing works
Microglia and CNS Interleukin-1: Beyond Immunological Concepts
Liu, X., & Quan, N. (2018) · Frontiers in Neurology · doi:10.3389/fneur.2018.00008 · Cited by 214 · see citing works
Transcriptional and epigenetic decoding of the microglial aging process
Li, X., Li, Y., Jin, Y., Zhang, Y., Wu, J., Xu, Z., Huang, Y., Cai, L., Gao, S., Liu, T., et al. (2023) · Nature Aging · doi:10.1038/s43587-023-00479-x · Cited by 225 · see citing works
Rimessi, A., Previati, M., Nigro, F., Wieckowski, M. R., & Pinton, P. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.06.015 · Cited by 210 · see citing works
Mitochondria and the NLRP3 inflammasome: physiological and pathological relevance
Yu, J., & Lee, M. (2016) · Archives of Pharmacal Research · doi:10.1007/s12272-016-0827-4 · Cited by 207 · see citing works
Bordt, E. A., & Polster, B. M. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.07.033 · Cited by 202 · see citing works
The role of lysosomal cysteine cathepsins in NLRP3 inflammasome activation
Campden, R. I., & Zhang, Y. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.02.015 · Cited by 203 · see citing works
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 197 · see citing works
Wu, A., Zhou, X., Qiao, G., Yu, L., Tang, Y., Yan, L., Qiu, W., Pan, R., Yu, C., Law, B. Y. K., et al. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101202 · Cited by 193 · see citing works
Mitophagy: a balance regulator of NLRP3 inflammasome activation
Kim, M., Yoon, J., & Ryu, J.-H. (2016) · BMB Reports · doi:10.5483/bmbrep.2016.49.10.115 · Cited by 195 · see citing works
Updated insights into the molecular networks for NLRP3 inflammasome activation
Paik, S., Kim, J. K., Shin, H. J., Park, E., Kim, I. S., & Jo, E. (2025) · Cellular and Molecular Immunology · doi:10.1038/s41423-025-01284-9 · Cited by 207 · see citing works
Neuroinflammation and Parkinson’s Disease—From Neurodegeneration to Therapeutic Opportunities
Araújo, B., Caridade-Silva, R., Soares-Guedes, C., Martins‐Macedo, J., Gomes, E. D., Monteiro, S., & Teixeira, F. G. (2022) · Cells · doi:10.3390/cells11182908 · Cited by 197 · see citing works
von Herrmann, K. M., Salas, L. A., Martinez, E. M., Young, A. L., Howard, J. M., Feldman, M. S., Christensen, B. C., Wilkins, O. M., Lee, S., Hickey, W. F., et al. (2018) · npj Parkinson s Disease · doi:10.1038/s41531-018-0061-5 · Cited by 185 · see citing works
Amyloid fibrils are the molecular trigger of inflammation in Parkinson's disease
Gustot, A., Gallea, J. I., Sarroukh, R., Celej, M. S., Ruysschaert, J., & Raussens, V. (2015) · Biochemical Journal · doi:10.1042/bj20150617 · Cited by 183 · see citing works
Recent Advances of the NLRP3 Inflammasome in Central Nervous System Disorders
Zhou, K., Shi, L., Wang, Y., Chen, S., & Zhang, J. (2016) · Journal of Immunology Research · doi:10.1155/2016/9238290 · Cited by 175 · see citing works
Corcoran, S. E., Halai, R., & Cooper, M. A. (2021) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000171 · Cited by 179 · see citing works
Hughes, C. D., Choi, M. L., Ryten, M., Hopkins, L., Drews, A., Botía, J. A., Iljina, M., Rodrigues, M., Gagliano, S. A., Gandhi, S., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-018-1907-y · Cited by 177 · see citing works
Haslund‐Vinding, J., McBean, G., Jaquet, V, & Vilhardt, F. (2017) · British Journal of Pharmacology · doi:10.1111/bph.13425 · Cited by 169 · see citing works
Rui, W., Li, S., Xiao, H., Xiao, M., & Shi, J. (2020) · The International Journal of Neuropsychopharmacology · doi:10.1093/ijnp/pyaa060 · Cited by 175 · see citing works
The relation between α-synuclein and microglia in Parkinson’s disease: Recent developments
Sánchez-Guajardo, V., Tentillier, N., & Romero‐Ramos, M. (2015) · Neuroscience · doi:10.1016/j.neuroscience.2015.02.008 · Cited by 171 · see citing works
Ortiz‐Virumbrales, M., Moreno, C. L., Kruglikov, I., Marazuela, P., Sproul, A. A., Jacob, S., Zimmer, M., Paull, D. J., Zhang, B., Schadt, E. E., et al. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0475-z · Cited by 176 · see citing works
Sarkar, S., Rokad, D., Malovic, E., Luo, J., Harischandra, D. S., Jin, H., Anantharam, V., Huang, X., Lewis, M., Kanthasamy, A., et al. (2019) · Science Signaling · doi:10.1126/scisignal.aat9900 · Cited by 171 · see citing works
Inflammasomes link vascular disease with neuroinflammation and brain disorders
Lénárt, N., Brough, D., & Dénes, Á. (2016) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x16662043 · Cited by 169 · see citing works
Inflammasomes in neurological diseases: emerging pathogenic and therapeutic concepts
Mamik, M. K., & Power, C. (2017) · Brain : a journal of neurology · doi:10.1093/brain/awx133 · Cited by 151 · see citing works
NLRP3 inflammasome activation is associated with proliferative diabetic retinopathy
Loukovaara, S., Piippo, N., Kinnunen, K., Hytti, M., Kaarniranta, K., & Kauppinen, A. (2017) · Acta Ophthalmologica · doi:10.1111/aos.13427 · Cited by 160 · see citing works
NADPH oxidases in Parkinson’s disease: a systematic review
Bélarbi, K., Cuvelier, E., Destée, A., Gressier, B., & Chartier‐Harlin, M. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0225-5 · Cited by 158 · see citing works
The NLRP3 Inflammasome is Involved in the Pathogenesis of Parkinson’s Disease in Rats
Mao, Z., Liu, C., Ji, S., Yang, Q., Ye, H., Han, H., & Xue, Z. (2017) · Neurochemical Research · doi:10.1007/s11064-017-2185-0 · Cited by 155 · see citing works
Mouton‐Liger, F., Rosazza, T., Sepulveda‐Diaz, J., Ieang, A., Hassoun, S., Claire, E., Mangone, G., Brice, A., Michel, P. P., Corvol, J., et al. (2018) · Glia · doi:10.1002/glia.23337 · Cited by 160 · see citing works
Glycosphingolipids and Neuroinflammation in Parkinson’s Disease
Belarbi, K., Cuvelier, E., Bonte, M.-A., Desplanque, M., Gressier, B., Devos, D., & Chartier-Harlin, M.-C. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00408-1 · Cited by 155 · see citing works
Manganese exposure induces neuroinflammation by impairing mitochondrial dynamics in astrocytes
Sarkar, S., Malovic, E., Harischandra, D. S., Ngwa, H. A., Ghosh, A., Hogan, C., Rokad, D., Zenitsky, G. D., Jin, H., Anantharam, V., et al. (2017) · NeuroToxicology · doi:10.1016/j.neuro.2017.05.009 · Cited by 151 · see citing works
Mulay, S. R., & Anders, H. (2016) · New England Journal of Medicine · doi:10.1056/nejmra1601611 · Cited by 148 · see citing works
Toll-like receptors and their therapeutic potential in Parkinson’s disease and α-synucleinopathies
Kouli, A., Horne, C. B., & Williams-Gray, C. H. (2019) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2019.06.042 · Cited by 143 · see citing works
Fu, P., Gao, M., & Yung, K. K. L. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00607 · Cited by 145 · see citing works
Diet in Parkinson’s Disease: Critical Role for the Microbiome
Jackson, A., Forsyth, C. B., Shaikh, M., Voigt, R. M., Engen, P. A., Ramirez, V., & Keshavarzian, A. (2019) · Frontiers in Neurology · doi:10.3389/fneur.2019.01245 · Cited by 145 · see citing works
The Role of the Inflammasome in Neurodegenerative Diseases
Piancone, F., La Rosa, F., Marventano, I., Saresella, M., & Clerici, M. (2021) · Molecules · doi:10.3390/molecules26040953 · Cited by 144 · see citing works
Alpha-Synuclein Pathology and the Role of the Microbiota in Parkinson’s Disease
Fitzgerald, E., Murphy, S. A., & Martinson, H. A. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00369 · Cited by 148 · see citing works
The immune system in Parkinson's disease: what we know so far
Roodveldt, C., Bernardino, L. I., Çakmak, Ö. Ö., Dragić, M., Fladmark, K. E., Ertan, S., Aktaş, B., Pita, C., Ciglar, L., Garraux, G., et al. (2024) · Brain · doi:10.1093/brain/awae177 · Cited by 148 · see citing works
Campolo, M., Paterniti, I., Siracusa, R., Filippone, A., Esposito, E., & Cuzzocrea, S. (2018) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2018.12.003 · Cited by 143 · see citing works
Sacino, A. N., Brooks, M., McKinney, A. B., Thomas, M. A., Shaw, G., Golde, T. E., & Giasson, B. I. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.2102-14.2014 · Cited by 141 · see citing works
MicroRNA-30e regulates neuroinflammation in MPTP model of Parkinson’s disease by targeting Nlrp3
Li, D., Yang, H., Ma, J., Luo, S., Chen, S., & Gu, Q. (2017) · Human Cell · doi:10.1007/s13577-017-0187-5 · Cited by 140 · see citing works
- Authors
- Codolo, G., Plotegher, N., Pozzobon, T., Brucale, M., Tessari, I., Bubacco, L., & de Bernard, M.
- Affiliations
- University of Padua (IT)
- Veneto Institute of Molecular Medicine (IT)
- Institute of Nanostructured Materials (IT)
- Corresponding author
- Bubacco, Luigi
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2013-01-31
- Volume
- 8
- Issue
- 1
- Pages
- e55375
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC3561263
- OpenAlex
- W2015283405
- Cited by
- 585
- References
- 67
- Citations by year
- 2026: 23 · 2025: 38 · 2024: 56 · 2023: 59 · 2022: 68 · 2021: 65 · 2020: 58 · 2019: 53 · 2018: 48 · 2017: 31 · 2016: 27 · 2015: 30 · 2014: 23 · 2013: 5
- FWCI
- 12.83
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS ONE (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, other-oa)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Padua Research Archive (University of Padova) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- Funders
- Fondazione Cariplo (2011-0485)
- Università degli Studi di Padova
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- alpha-synuclein aggregation, NLRP3 inflammasome, IL-1β, Parkinson's disease, synucleinopathies, TLR2, microglial activation, phagocytosis, reactive oxygen species, cathepsin B, Lewy bodies, neuroinflammation, neurodegeneration
- MeSH terms
- NLR Family, Pyrin Domain-Containing 3 Protein, Analysis of Variance, Carrier Proteins, Humans, Inflammation, Neurons, Parkinson Disease, Phagocytosis, Spectrometry, Fluorescence, Spectrophotometry, Ultraviolet, Thiazoles, Blotting, Western, Lewy Bodies, DNA Primers, Microscopy, Confocal, Microscopy, Atomic Force, Microscopy, Electron, Transmission, Toll-Like Receptor 2, alpha-Synuclein, Benzothiazoles, Interleukin-1beta, Chromatography, Reverse-Phase, Inflammasomes, Real-Time Polymerase Chain Reaction
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review