The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
Gout-associated uric acid crystals activate the NALP3 inflammasome
Abstract
Development of the acute and chronic inflammatory responses known as gout and pseudogout are associated with the deposition of monosodium urate (MSU) or calcium pyrophosphate dihydrate (CPPD) crystals, respectively, in joints and periarticular tissues. Although MSU crystals were first identified as the aetiological agent of gout in the eighteenth century and more recently as a 'danger signal' released from dying cells, little is known about the molecular mechanisms underlying MSU- or CPPD-induced inflammation. Here we show that MSU and CPPD engage the caspase-1-activating NALP3 (also called cryopyrin) inflammasome, resulting in the production of active interleukin (IL)-1beta and IL-18. Macrophages from mice deficient in various components of the inflammasome such as caspase-1, ASC and NALP3 are defective in crystal-induced IL-1beta activation. Moreover, an impaired neutrophil influx is found in an in vivo model of crystal-induced peritonitis in inflammasome-deficient mice or mice deficient in the IL-1beta receptor (IL-1R). These findings provide insight into the molecular processes underlying the inflammatory conditions of gout and pseudogout, and further support a pivotal role of the inflammasome in several autoinflammatory diseases.
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In the citing paper
“Colchicine impairs neutrophil adhesion to vascular endothelium and degranulation and blocks activation of the NLRP3 (NOD-, LRR-, and pyrin domaincontaining protein 3) inflammasome, which is required for cleaving caspase-1 leading to the production of IL-1 β and IL-18. 134-136”
From COVID-19, Myocarditis and Pericarditis (2023) · cites this paper as [135]
In the citing paper
“Nucleotide products such as uric acid can also function as DAMPs, presumably by activating the inflammasome in APC, thereby stimulating the production of inflammatory cytokines such as interleukin-1β (IL-1β), IL-18 and IL-33, the secretion of which depends on the inflammasome-mediated activation of caspase-145,46.”
From Immunogenic and tolerogenic cell death (2009) · cites this paper as [46]
In the citing paper
“The secretion of mature IL-1β induced by asbestos was comparable to amounts observed with monosodium urate crystals (MSU), a known potent activator of IL-1β processing (7) (Fig. 1, A and B).”
From Innate Immune Activation Through Nalp3 Inflammasome Sensing of Asbestos and Silica (2008) · cites this paper as [7]
In the citing paper
“In addition to PAMPs, Nalp3 has the extraordinary capacity of sensing endogenous stress-associated danger signals (DAMPs) such as ATP (9) or MSU (7).”
From Innate Immune Activation Through Nalp3 Inflammasome Sensing of Asbestos and Silica (2008) · cites this paper as [7]
In the citing paper
“The Nalp3 inflammasome is implicated in the pathological increase of IL-1β production in autoinflammatory syndromes, such as Muckle-Wells syndrome (22), as well as inflammatory processes, such as gout and pseudogout (7).”
From Innate Immune Activation Through Nalp3 Inflammasome Sensing of Asbestos and Silica (2008) · cites this paper as [7]
In the citing paper
“The NLRP3 inflammasome senses crystalline danger signals that can occur during autoinflammatory diseases, such as gout or atherosclerosis, and environmental diseases, such as silicosis or asbestosis (18, 20, 22).”
From Volcanic Ash Activates the NLRP3 Inflammasome in Murine and Human Macrophages (2018) · cites this paper as [18]
In the citing paper
“Inhalation of crystalline silica can induce inflammation by stimulating the NLRP3 inflammasome, a cytosolic receptor complex that plays a critical role in driving inflammatory immune responses.”
From Volcanic Ash Activates the NLRP3 Inflammasome in Murine and Human Macrophages (2018) · cites this paper as [18]
In the citing paper
“NLRP3 has been shown to respond to sterile stimuli, including asbestos, silica, MSU and CPPD crystals55, cholesterol crystals and β-amyloid fibrils56.”
From Sterile inflammation: sensing and reacting to damage (2010) · cites this paper as [55]
In the citing paper
“Urate and cholesterol crystals, as well as sterile particulates, for example, can bypass the requirement for ATP and P2RX7 for IL-1β production55,59.”
From Sterile inflammation: sensing and reacting to damage (2010) · cites this paper as [55]
In the citing paper
“Consistently, in mouse models of sterile injury, such as gout, asbestosis and silicosis, NLRP3-deficient mice exhibited decreased inflammation with reduced levels of tissue infiltration by neutrophils or macrophages55,57,58.”
From Sterile inflammation: sensing and reacting to damage (2010) · cites this paper as [55]
In the citing paper
“The inflammasome is a multimolecular cytosolic sensor that detects pathogenic microorganisms and sterile stressors and activates caspase-1 during the process of pyroptosis, which, in turn, causes the inactive precursor forms of interleukin-1β and interleukin-18 to become the active forms.”
From Cytokine storm (2020) · cites this paper as [41]
Citations
Cites
Janeway, C. A., & Medzhitov, R. (2002) · Annual Review of Immunology · doi:10.1146/annurev.immunol.20.083001.084359 · Cited by 8,394
Martinon, F., Burns, K., & Tschopp, J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00599-3 · Cited by 6,066
Self-citationThe Danger Model: A Renewed Sense of Self
Matzinger, P. (2002) · Science · doi:10.1126/science.1071059 · Cited by 4,205
Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf
Mariathasan, S., Newton, K., Monack, D. M., Vucic, D., French, D. M., Lee, W. P., Roose-Girma, M., Erickson, S. L., & Dixit, V. M. (2004) · Nature · doi:10.1038/nature02664 · Cited by 1,864
Agostini, L., Martinon, F., Burns, K., McDermott, M. F., Hawkins, P. N., & Tschopp, J. (2004) · Immunity · doi:10.1016/s1074-7613(04)00046-9 · Cited by 1,768
Self-citationMolecular identification of a danger signal that alerts the immune system to dying cells
Shi, Y., Evans, J. E., & Rock, K. L. (2003) · Nature · doi:10.1038/nature01991 · Cited by 1,684
Hoffman, H. M., Mueller, J. L., Broide, D. H., Wanderer, A. A., & Kolodner, R. D. (2001) · Nature Genetics · doi:10.1038/ng756 · Cited by 1,679
Martinon, F., & Tschopp, J. (2004) · Cell · doi:10.1016/j.cell.2004.05.004 · Cited by 957
Self-citationNALPs: a novel protein family involved in inflammation
Tschopp, J., Martinon, F., & Burns, K. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1019 · Cited by 739
Self-citationNLRs join TLRs as innate sensors of pathogens
Martinon, F., & Tschopp, J. (2005) · Trends in Immunology · doi:10.1016/j.it.2005.06.004 · Cited by 673
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Merriman, T. R., & Dalbeth, N. (2010) · Joint Bone Spine · doi:10.1016/j.jbspin.2010.02.027 · Cited by 180
The innate signaling of dangers and the dangers of innate signaling
Sansonetti, P. J. (2006) · Nature Immunology · doi:10.1038/ni1420 · Cited by 185
Review of Hyperuricemia as New Marker for Metabolic Syndrome
Billiet, L., Doaty, S., Katz, J. D., & Velasquez, M. T. (2014) · ISRN Rheumatology · doi:10.1155/2014/852954 · Cited by 180
Autoimmunity vs autoinflammation in Behcet's disease: do we oversimplify a complex disorder?
Di̇reskeneli̇, H. (2006) · Rheumatology · doi:10.1093/rheumatology/kel329 · Cited by 179
Corcoran, S. E., Halai, R., & Cooper, M. A. (2021) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000171 · Cited by 180
Cell biology of inflammasome activation
Pandey, A., Shen, C. X., Feng, S., & Man, S. M. (2021) · Trends in Cell Biology · doi:10.1016/j.tcb.2021.06.010 · Cited by 183
Farrell, G. C., Haczeyni, F., & Chitturi, S. (2018) · Advances in Experimental Medicine and Biology · doi:10.1007/978-981-10-8684-7_3 · Cited by 178
Caspase-11 Activation in Response to Bacterial Secretion Systems that Access the Host Cytosol
Casson, C. N., Copenhaver, A. M., Zwack, E. E., Nguyen, H. T., Strowig, T., Javdan, B., Bradley, W. P., Fung, T. C., Flavell, R. A., Brodsky, I. E., et al. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003400 · Cited by 181
Eucalyptol alleviates inflammation and pain responses in a mouse model of gout arthritis
Yin, C., Liu, B., Wang, P., Li, X., Li, Y., Zheng, X., Tai, Y., Wang, C., & Liu, B. (2019) · British Journal of Pharmacology · doi:10.1111/bph.14967 · Cited by 178
Inflammasomes contributing to inflammation in arthritis
Spel, L., & Martinon, F. (2020) · Immunological Reviews · doi:10.1111/imr.12839 · Cited by 179
Self-citationIL-1 and autoinflammatory disease: biology, pathogenesis and therapeutic targeting
Broderick, L., & Hoffman, H. M. (2022) · Nature Reviews Rheumatology · doi:10.1038/s41584-022-00797-1 · Cited by 182
Gout: state of the art after a decade of developments
Pascart, T., & Lioté, F. (2018) · Rheumatology · doi:10.1093/rheumatology/key002 · Cited by 181
Knight, J. S., Carmona‐Rivera, C., & Kaplan, M. J. (2012) · Frontiers in Immunology · doi:10.3389/fimmu.2012.00380 · Cited by 180
Inflammasome Up-Regulation and Activation in Dysferlin-Deficient Skeletal Muscle
Rawat, R., Cohen, T. V., Ampong, B., Francia, D., Henriques‐Pons, A., Hoffman, E. P., & Nagaraju, K. (2010) · American Journal Of Pathology · doi:10.2353/ajpath.2010.090058 · Cited by 176
Case, C. L., Shin, S., & Roy, C. R. (2009) · Infection and Immunity · doi:10.1128/iai.01382-08 · Cited by 181
Targeting Residual Inflammatory Risk: A Shifting Paradigm for Atherosclerotic Disease
Aday, A. W., & Ridker, P. M. (2019) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2019.00016 · Cited by 178
Kuemmerle-Deschner, J. B., Tyrrell, P. N., Koetter, I., Wittkowski, H., Bialkowski, A., Tzaribachev, N., Lohse, P., Koitschev, A., Deuter, C., Foell, D., et al. (2010) · Arthritis & Rheumatism · doi:10.1002/art.30149 · Cited by 175
How is inflammation initiated? Individual influences of IL-1, IL-18 and HMGB1
Keyel, P. A. (2014) · Cytokine · doi:10.1016/j.cyto.2014.03.007 · Cited by 182
Sun, B., Wang, X., Ji, Z., Wang, M., Liao, Y., Chang, C. H., Li, R., Zhang, H., Nel, A. E., & Xia, T. (2015) · Small · doi:10.1002/smll.201402859 · Cited by 176
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Henao‐Mejia, J., Elinav, E., Thaiss, C. A., & Flavell, R. A. (2013) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021113-170324 · Cited by 176
The cytoskeleton in cell-autonomous immunity: structural determinants of host defence
Mostowy, S., & Shenoy, A. R. (2015) · Nature reviews. Immunology · doi:10.1038/nri3877 · Cited by 190
Lighting the fires within: the cell biology of autoinflammatory diseases
Park, H., Bourla, A. B., Kastner, D. L., Colbert, R. A., & Siegel, R. M. (2012) · Nature reviews. Immunology · doi:10.1038/nri3261 · Cited by 178
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Latz, E., & Duewell, P. (2018) · Seminars in Immunology · doi:10.1016/j.smim.2018.09.001 · Cited by 174
Outcome Domains for Studies of Acute and Chronic Gout
Schumacher, H. R., Taylor, W. J., EDWARDS, L., Grainger, R., Schlesinger, N., Dalbeth, N., Sivera, F., Singh, J. A., Evans, R. R., Waltrip, R. W., et al. (2009) · The Journal of Rheumatology · doi:10.3899/jrheum.090370 · Cited by 174
Recent insights into the molecular mechanisms of the NLRP3 inflammasome activation
Próchnicki, T., Mangan, M., & Latz, E. (2016) · F1000Research · doi:10.12688/f1000research.8614.1 · Cited by 174
Cholesterol crystallization within hepatocyte lipid droplets and its role in murine NASH
Ioannou, G. N., Subramanian, S., Chait, A., Haigh, W. G., Yeh, M. M., Farrell, G. C., Lee, S. P., & Savard, C. E. (2017) · Journal of Lipid Research · doi:10.1194/jlr.m072454 · Cited by 180
NOD-like receptor signaling in inflammation-associated cancers: From functions to targeted therapies
Liu, P., Lu, Z., Liu, L., Li, R., Liang, Z., Shen, M., Han, X., Ren, D., Ji, M., Yuan, S., et al. (2019) · Phytomedicine · doi:10.1016/j.phymed.2019.152925 · Cited by 174
Activation of immune signals during organ transplantation
Li, Q., & Lan, P. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01377-9 · Cited by 175
Mechanism and Regulation of Gasdermin-Mediated Cell DeathPreprint
Xia, S., Hollingsworth, L. R., & Wu, H. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a036400 · Cited by 177
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Alcocer-Gómez, E., Ulecia-Morón, C., Marín-Aguilar, F., Rybkina, T., Casas-Barquero, N., Ruiz-Cabello, J., Ryffel, B., Apetoh, L., Ghiringhelli, F., Bullón, P., et al. (2016) · Molecular Neurobiology · doi:10.1007/s12035-015-9408-7 · Cited by 172
Dorhoi, A., Nouailles, G., Jörg, S., Hagens, K., Heinemann, E., Pradl, L., Oberbeck‐Müller, D., Correa, M. A. D., Reece, S. T., Ruland, J., et al. (2011) · European Journal of Immunology · doi:10.1002/eji.201141548 · Cited by 172
Self-citationIL-1 family cytokines trigger sterile inflammatory disease
Lukens, J. R., Gross, J. M., & Kanneganti, T. (2012) · Frontiers in Immunology · doi:10.3389/fimmu.2012.00315 · Cited by 178
Zeller, M. V., Dias, D., Sebastião, A. M., & Valente, C. A. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-210268 · Cited by 179
Hu, Q., Zhang, X., Pan, Y., Li, Y., & Kong, L. (2012) · Biochemical Pharmacology · doi:10.1016/j.bcp.2012.03.005 · Cited by 174
The intersection of cell death and inflammasome activation
Vince, J. E., & Silke, J. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2205-2 · Cited by 180
Kimball, A., Davis, F. M., denDekker, A. D., Joshi, A., Schaller, M. A., Bermick, J., Xing, X., Burant, C., Obi, A. T., Nysz, D., et al. (2019) · Immunity · doi:10.1016/j.immuni.2019.06.015 · Cited by 172
Inflammation as a Therapeutic Target in Atherosclerosis
Nguyen, M. T., Fernando, S., Schwarz, N., Tan, J. T. M., Bursill, C. A., & Psaltis, P. J. (2019) · Journal of Clinical Medicine · doi:10.3390/jcm8081109 · Cited by 176
Wang, Z., & Xu, J. (2020) · Vaccines · doi:10.3390/vaccines8010128 · Cited by 171
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Menard, C., Martin, F., Apétoh, L., Bouyer, F., & Ghiringhelli, F. (2008) · Cancer Immunology Immunotherapy · doi:10.1007/s00262-008-0505-6 · Cited by 175
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
Silica induces NLRP3 inflammasome activation in human lung epithelial cells
Peeters, P. M., Perkins, T. N., Wouters, E. F. �., Mossman, B. T., & Reynaert, N. L. (2013) · Particle and Fibre Toxicology · doi:10.1186/1743-8977-10-3 · Cited by 170
Inhibition of the NLRP3/IL‐1β axis protects against sepsis‐induced cardiomyopathy
Büsch, K., Kny, M., Huang, N. R., Klassert, T. E., Stock, M., Hahn, A., Graeger, S., Todiraş, M., Schmidt, S., Chamling, B., et al. (2021) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12763 · Cited by 178
Marina–García, N., Franchi, L., Kim, Y., Miller, D., McDonald, C., Boons, G., & Núñez, G. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.6.4050 · Cited by 173
Sokołowska, M., Chen, L., Liu, Y., Martínez‐Antón, A., Qi, H., Logun, C., Alsaaty, S., Park, Y. H., Kastner, D. L., Chae, J. J., et al. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1401343 · Cited by 177
Mitochondrial DNA in the regulation of innate immune responses
Fang, C., Wei, X., & Wei, Y. (2015) · Protein & Cell · doi:10.1007/s13238-015-0222-9 · Cited by 174
Crystal‐induced neutrophil activation
Popa‐Nita, O., & Naccache, P. H. (2009) · Immunology and Cell Biology · doi:10.1038/icb.2009.98 · Cited by 169
Labbè, K., McIntire, C. R., Doiron, K., LeBlanc, P. M., & Saleh, M. (2011) · Immunity · doi:10.1016/j.immuni.2011.10.016 · Cited by 180
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 170
Structure, Activation and Regulation of NLRP3 and AIM2 Inflammasomes
Sharma, M., & de Alba, E. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020872 · Cited by 173
Anti‐inflammatory effects of polyphenols in arthritis
Oliviero, F., Scanu, A., Zamudio-Cuevas, Y. E., Punzi, L., & Spinella, P. (2017) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.8664 · Cited by 168
Oxidative Stress and Renal Fibrosis: Mechanisms and Therapies
Su, H., Wan, C., Song, A., Qiu, Y., Xiong, W., & Zhang, C. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-8871-2_29 · Cited by 168
Keenan, R. T. (2020) · Seminars in Arthritis and Rheumatism · doi:10.1016/j.semarthrit.2020.04.007 · Cited by 172
Sulforaphane inhibits multiple inflammasomes through an Nrf2-independent mechanism
Greaney, A. J., Maier, N. K., Leppla, S. H., & Moayeri, M. (2015) · Journal of Leukocyte Biology · doi:10.1189/jlb.3a0415-155rr · Cited by 167
The Pathology of Orthopedic Implant Failure Is Mediated by Innate Immune System Cytokines
Landgraeber, S., Jäger, M., Jacobs, J. J., & Hallab, N. J. (2014) · Mediators of Inflammation · doi:10.1155/2014/185150 · Cited by 167
Pinkerton, J., Kim, R., Robertson, A. A. B., Hirota, J. A., Wood, L. G., Knight, D. A., Cooper, M. A., O'Neill, L. A. J., Horvat, J. C., & Hansbro, P. M. (2017) · Molecular Immunology · doi:10.1016/j.molimm.2017.01.014 · Cited by 170
Domingo-Fernandéz, R., Coll, R. C., Kearney, J., Breit, S. N., & O'Neill, L. A. J. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.797126 · Cited by 167
Marchetti, C., Swartzwelter, B. J., Koenders, M. I., Azam, T., Tengesdal, I. W., Powers, N. E., de Graaf, D. M., Dinarello, C. A., & Joosten, L. A. B. (2018) · Arthritis Research & Therapy · doi:10.1186/s13075-018-1664-2 · Cited by 167
Shah, A. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01021 · Cited by 169
Lambert, C., Zappia, J., Sanchez, C., Florin, A., Dubuc, J., & Henrotin, Y. E. (2021) · Frontiers in Medicine · doi:10.3389/fmed.2020.607186 · Cited by 167
López‐Castejón, G., Luheshi, N., Compan, V., High, S., Whitehead, R. C., Flitsch, S. L., Kirov, A., Prudovsky, I. A., Swanton, E., & Brough, D. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.422238 · Cited by 175
The inflammasome in pathogen recognition and inflammation
Sutterwala, F. S., Ogura, Y., & Flavell, R. A. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.1206755 · Cited by 166
The CARD plays a critical role in ASC foci formation and inflammasome signalling
Proell, M., Gerlic, M., Mace, P. D., Reed, J. C., & Riedl, S. J. (2012) · Biochemical Journal · doi:10.1042/bj20121198 · Cited by 168
The inflammasome in lung diseases
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Vieira, A. T., Galvão, I., Macia, L., Sernaglia, E. M., Vinolo, M. A. R., Garcia, C. C., Tavares, L. P., Amaral, F. A., Sousa, L. P., Martins, F. S., et al. (2016) · Journal of Leukocyte Biology · doi:10.1189/jlb.3a1015-453rrr · Cited by 167
CXCL1 and CXCL2 Regulate NLRP3 Inflammasome Activation via G-Protein–Coupled Receptor CXCR2
Boro, M., & Balaji, K. N. (2017) · The Journal of Immunology · doi:10.4049/jimmunol.1700129 · Cited by 167
Paugh, S. W., Bonten, E. J., Savic, D., Ramsey, L. B., Thierfelder, W. E., Gurung, P., Malireddi, R. K. S., Actis, M., Mayasundari, A., Min, J., et al. (2015) · Nature Genetics · doi:10.1038/ng.3283 · Cited by 164
NOD1 and NOD2: Beyond Peptidoglycan Sensing
Keestra, A. M., & Tsolis, R. M. (2017) · Trends in Immunology · doi:10.1016/j.it.2017.07.004 · Cited by 170
Caspase-4 Is Required for Activation of Inflammasomes
Sollberger, G., Strittmatter, G. E., Kistowska, M., French, L. E., & Beer, H. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1101620 · Cited by 163
Role of the NOD2 genotype in the clinical phenotype of Blau syndrome and early‐onset sarcoidosis
Okafuji, I., Nishikomori, R., Kanazawa, N., Kambe, N., Fujisawa, A., Yamazaki, S., Saito, M. K., Yoshioka, T., Kawai, T., Sakai, H., et al. (2008) · Arthritis & Rheumatism · doi:10.1002/art.24134 · Cited by 163
Khare, S., Ratsimandresy, R. A., de Almeida, L., Cuda, C. M., Rellick, S. L., Misharin, A. V., Wallin, M., Gangopadhyay, A., Forte, E., Gottwein, E., et al. (2014) · Nature Immunology · doi:10.1038/ni.2829 · Cited by 172
Robertson, S. E. J., Martínez, G. J., Payet, C. A., Barraclough, J., Celermajer, D. S., Bursill, C. A., & Patel, S. (2016) · Clinical Science · doi:10.1042/cs20160090 · Cited by 170
Yazdi, A. S., & Ghoreschi, K. (2016) · Advances in experimental medicine and biology · doi:10.1007/978-94-024-0921-5_2 · Cited by 174
Uric Acid and Chronic Kidney Disease: Still More to Do
Johnson, R. J., Sánchez‐Lozada, L. G., Lanaspa, M. A., Piani, F., & Borghi, C. (2022) · Kidney International Reports · doi:10.1016/j.ekir.2022.11.016 · Cited by 175
Uric Acid nephrolithiasis: recent progress and future directions.
Ngo, T. C., & Assimos, D. G. (2007) · Europe PMC (PubMed Central) · Cited by 162
Applications of nanomaterials as vaccine adjuvants
Zhu, M., Wang, R., & Nie, G. (2014) · Human Vaccines & Immunotherapeutics · doi:10.4161/hv.29589 · Cited by 165
Coban, C., Igari, Y., Yagi, M., Reimer, T., Koyama, S., Aoshi, T., Ohata, K., Tsukui, T., Takeshita, F., Sakurai, K., et al. (2010) · Cell Host & Microbe · doi:10.1016/j.chom.2009.12.003 · Cited by 162
Amyloid‐β oligomers set fire to inflammasomes and induce Alzheimer's pathology
Salminen, A., Ojala, J. O., Suuronen, T., Kaarniranta, K., & Kauppinen, A. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00496.x · Cited by 167
The pathogenesis of bone erosions in gouty arthritis
Schlesinger, N., & Thiele, R. (2010) · Annals of the Rheumatic Diseases · doi:10.1136/ard.2010.128454 · Cited by 163
Deftereos, S., Giannopoulos, G., Papoutsidakis, N., Panagopoulou, V., Kossyvakis, C., Raisakis, K., Cleman, M. W., & Stefanadis, C. (2013) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2013.08.726 · Cited by 161
Hirota, J. A., Hirota, S. A., Warner, S., Stefanowicz, D., Shaheen, F., Beck, P. L., MacDonald, J. A., Hackett, T., Sin, D. D., van Eeden, S. F., et al. (2012) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2011.11.033 · Cited by 161
Fang, R., Tsuchiya, K., Kawamura, I., Shen, Y., Hara, H., Sakai, S., Yamamoto, T., Fernandes‐Alnemri, T., Yang, R., Hernández-Cuellar, E., et al. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1100381 · Cited by 166
Jounai, N., Kobiyama, K., Takeshita, F., & Ishii, K. J. (2013) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2012.00168 · Cited by 169
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Jiang, Y., Wang, M., Huang, K., Zhang, Z., Shao, N., Zhang, Y., Wang, W., & Wang, S. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.07.011 · Cited by 160
Guo, H., Gao, J., Taxman, D. J., Ting, J. P. ‐., & Su, L. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.566620 · Cited by 160
Caspase crosstalk: integration of apoptotic and innate immune signalling pathways
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Chen, W., Gullett, J. M., Tweedell, R. E., & Kanneganti, T. (2023) · European Journal of Immunology · doi:10.1002/eji.202250235 · Cited by 161
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Lancieri, M., Bustaffa, M., Palmeri, S., Prigione, I., Penco, F., Papa, R., Volpi, S., Caorsi, R., & Gattorno, M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24119584 · Cited by 160
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Self-citationCryopyrinopathies: update on pathogenesis and treatment
Neven, B., Prieur, A., & Quartier, P. (2008) · Nature Clinical Practice Rheumatology · doi:10.1038/ncprheum0874 · Cited by 159
Chen, B., Li, H., Ou, G., Ren, L., Yang, X., & Zeng, M. (2019) · Arthritis Research & Therapy · doi:10.1186/s13075-019-1974-z · Cited by 159
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Reyes, A. Z., Hu, K. A., Teperman, J., Muskardin, T. W., Tardif, J., Shah, B., & Pillinger, M. H. (2020) · Annals of the Rheumatic Diseases · doi:10.1136/annrheumdis-2020-219174 · Cited by 161
Francisco, J. J., & Re, D. P. D. (2023) · Antioxidants · doi:10.3390/antiox12111944 · Cited by 165
Rabolli, V., Badissi, A. A., Devosse, R., Uwambayinema, F., Yakoub, Y., Palmai-Pallag, M., Lebrun, A., De Gussem, V., Couillin, I., Ryffel, B., et al. (2014) · Particle and Fibre Toxicology · doi:10.1186/s12989-014-0069-x · Cited by 158
The Therapeutic Potential of Modifying Inflammasomes and NOD-Like Receptors
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Casey, A. M., Ryan, D. G., Prag, H. A., Chowdhury, S. R., Marques, E., Turner, K., Gruszczyk, A. V., Yang, M. H., Wolf, D. M., Miljković, J. L., et al. (2025) · Nature Metabolism · doi:10.1038/s42255-025-01224-x · Cited by 171
Metadata
- Authors
- Martinon, F., Pétrilli, V., Mayor, A., Tardivel, A., & Tschopp, J.
- Affiliations
- University of Lausanne (CH)
- Corresponding author
- Tschopp, Jürg
- Venue
- Nature
- Published
- 2006-01-11
- Volume
- 440
- Issue
- 7081
- Pages
- 237-241
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2009800174
- Cited by
- 5,326
- References
- 31
- Citations by year
- 2026: 227 · 2025: 246 · 2024: 305 · 2023: 310 · 2022: 333 · 2021: 335 · 2020: 340 · 2019: 297 · 2018: 280 · 2017: 248 · 2016: 287 · 2015: 290 · 2014: 271 · 2013: 299 · 2012: 238
- FWCI
- 76.62
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- IRIS (submittedVersion)
- SERVAL (Université de Lausanne) (submittedVersion)
- Funders
- National Science Foundation
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Health Sciences › Medicine › Nephrology › Gout, Hyperuricemia, Uric Acid
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Keywords
- NLRP3 inflammasome, NLRP3, gout, urate crystals, monosodium urate, calcium pyrophosphate dihydrate, pseudogout, caspase-1, IL-1β, IL-18, autoinflammatory disease, innate immunity, crystal-induced inflammation, neutrophil influx, IL-1 receptor, macrophages
- MeSH terms
- NLR Family, Pyrin Domain-Containing 3 Protein, Animals, Calcium Pyrophosphate, Carrier Proteins, Cell Line, Cells, Cultured, Chondrocalcinosis, Colchicine, Disease Models, Animal, Gout, Humans, Inflammation, Interleukin-1, Macrophages, Neutrophils, Peritonitis, Uric Acid, Receptors, Interleukin-1, Caspase 1, Mice
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