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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Pennisi, M., Crupi, R., Di Paola, R., Ontario, M. L., Bella, R., Calabrese, E. J., Crea, R., Cuzzocrea, S., & Calabrese, V. (2017) · Journal of Neuroscience Research · doi:10.1002/jnr.23986 · Cited by 157
Engagement of CD14 Mediates the Inflammatory Potential of Monosodium Urate Crystals
Scott, P., Ma, H., Viriyakosol, S., Terkeltaub, R. A., & Liu‐Bryan, R. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.9.6370 · Cited by 157
Danger‐associated molecular patterns ( DAMPs ) in acute lung injury
Tolle, L. B., & Standiford, T. J. (2013) · The Journal of Pathology · doi:10.1002/path.4124 · Cited by 157
Kerur, N., Hirano, Y., Tarallo, V., Fowler, B. J., Bastos-Carvalho, A., Yasuma, T. R., Yasuma, R., Kim, Y., Hinton, D. R., Kirschning, C. J., et al. (2013) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.13-12500 · Cited by 163
Bracey, N. A., Gershkovich, B., Chun, J., Vilaysane, A., Meijndert, H. C., Wright, J. R., Fedak, P. W. M., Beck, P. L., Muruve, D. A., & Duff, H. J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.550624 · Cited by 156
Monosodium urate crystals in inflammation and immunity
Shi, Y., Mucsi, A. D., & Ng, G. (2009) · Immunological Reviews · doi:10.1111/j.0105-2896.2009.00851.x · Cited by 163
Synovial mast cells: role in acute and chronic arthritis
Nigrovic, P. A., & Lee, D. M. (2007) · Immunological Reviews · doi:10.1111/j.1600-065x.2007.00506.x · Cited by 157
Activation of the NLRP3 Inflammasome by Group B Streptococci
Costa, A., Gupta, R., Signorino, G., Malara, A., Cardile, F., Biondo, C., Midiri, A., Galbo, R., Trieu‐Cuot, P., Papasergi, S., et al. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1102543 · Cited by 162
He, X., Mekasha, S., Mavrogiorgos, N. C., Fitzgerald, K. A., Lien, E., & Ingalls, R. R. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0903937 · Cited by 160
Inflammasomes: Threat-Assessment Organelles of the Innate Immune System
Evavold, C. L., & Kagan, J. C. (2019) · Immunity · doi:10.1016/j.immuni.2019.08.005 · Cited by 159
ZDHHC5-mediated NLRP3 palmitoylation promotes NLRP3-NEK7 interaction and inflammasome activation
Zheng, S., Que, X., Wang, S., Zhou, Q., Xing, X., Liang, C., Hou, C., Ma, J., An, P., Peng, Y., et al. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.11.015 · Cited by 165
Hyperuricaemia and gout: time for a new staging system?
Dalbeth, N., & Stamp, L. K. (2014) · Annals of the Rheumatic Diseases · doi:10.1136/annrheumdis-2014-205304 · Cited by 155
Deregulated inflammasome signaling in disease
Lamkanfi, M., Walle, L. V., & Kanneganti, T. (2011) · Immunological Reviews · doi:10.1111/j.1600-065x.2011.01042.x · Cited by 154
The NLRP3 inflammasome: an emerging therapeutic target for chronic pain
Chen, R., Yin, C., Fang, J., & Liu, B. (2021) · Journal of Neuroinflammation · doi:10.1186/s12974-021-02131-0 · Cited by 158
Curcumin suppresses NLRP3 inflammasome activation and protects against LPS‐induced septic shock
Gong, Z., Zhou, J., Li, H., Gao, Y., Xu, C., Zhao, S., Chen, Y., Cai, W., & Wu, J. (2015) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201500316 · Cited by 154
Dalbeth, N., Smith, T., Nicolson, B., Clark, B., Callon, K. E., Naot, D., Haskard, D. O., McQueen, F. M., Reid, I. R., & Cornish, J. (2008) · Arthritis & Rheumatism · doi:10.1002/art.23488 · Cited by 157
The role of tissue resident cells in neutrophil recruitment
Kim, N. D., & Luster, A. D. (2015) · Trends in Immunology · doi:10.1016/j.it.2015.07.007 · Cited by 161
The microbial and danger signals that activate Nod-like receptors
Benkő, S., Philpott, D. J., & Girardin, S. E. (2008) · Cytokine · doi:10.1016/j.cyto.2008.07.013 · Cited by 156
Morishige, T., Yoshioka, Y., Inakura, H., Tanabe, A., Yao, X., Narimatsu, S., Monobe, Y., Imazawa, T., Tsunoda, S., Tsutsumi, Y. M., et al. (2010) · Biomaterials · doi:10.1016/j.biomaterials.2010.05.036 · Cited by 155
Inflammasome-IL-1-Th17 response in allergic lung inflammation
Besnard, A., Togbe, D., Couillin, I., Tan, Z., Zheng, S. G., Erard, F., Bert, M. L., Quesniaux, V. F. J., & Ryffel, B. (2011) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjr042 · Cited by 155
Tailoring inorganic nanoadjuvants towards next-generation vaccines
Li, X., Wang, X., & Ito, A. (2018) · Chemical Society Reviews · doi:10.1039/c8cs00028j · Cited by 153
TIR, CARD and PYRIN: three domains for an antimicrobial triad
Werts, C., Girardin, S. E., & Philpott, D. J. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401890 · Cited by 156
Francesco, P. N. D., Mucci, J. M., Ceci, R., Fossati, C. A., & Rozenfeld, P. A. (2013) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2013.02.003 · Cited by 152
Treating to target: a strategy to cure gout
Pérez-Ruiz, F. (2009) · Rheumatology · doi:10.1093/rheumatology/kep087 · Cited by 154
Bauer, C. A., Duewell, P., Lehr, H., Endres, S., & Schnurr, M. M. (2012) · Digestive Diseases · doi:10.1159/000341681 · Cited by 152
Stress molecules in sepsis and systemic inflammatory response syndrome
Adib‐Conquy, M., & Cavaillon, J. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.03.074 · Cited by 152
Differential roles of caspase-1 and caspase-11 in infection and inflammation
Man, S. M., Karki, R., Briard, B., Burton, A. R., Gingras, S., Pelletier, S. W., & Kanneganti, T. (2017) · Scientific Reports · doi:10.1038/srep45126 · Cited by 155
Komada, T., Chung, H., Lau, A. N., Platnich, J. M., Beck, P. L., Benediktsson, H., Duff, H. J., Jenne, C. N., & Muruve, D. A. (2018) · Journal of the American Society of Nephrology · doi:10.1681/asn.2017080863 · Cited by 152
Strategies for Targeting the NLRP3 Inflammasome in the Clinical and Preclinical Space
Schwaid, A. G., & Spencer, K. B. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01307 · Cited by 154
Tapia‐Abellán, A., Angosto-Bazarra, D., Alarcón‐Vila, C., Baños, M. C., Hafner‐Bratkovič, I., Oliva, B., & Pelegrín, P. (2021) · Science Advances · doi:10.1126/sciadv.abf4468 · Cited by 155
Therapeutic potential of colchicine in cardiovascular medicine: a pharmacological review
Zhang, F.-S., He, Q.-Z., Qin, C. X., Little, P. J., Weng, J., & Xu, S. (2022) · Acta Pharmacologica Sinica · doi:10.1038/s41401-021-00835-w · Cited by 156
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Leaf, I. A., Nakagawa, S., Johnson, B. G., Cha, J. J., Mittelsteadt, K., Guckian, K. M., Gomez, I. G., Altemeier, W. A., & Duffield, J. S. (2016) · Journal of Clinical Investigation · doi:10.1172/jci87532 · Cited by 151
Saito, M. K., Nishikomori, R., Kambe, N., Fujisawa, A., Tanizaki, H., Takeichi, K., Imagawa, T., Iehara, T., Takada, H., Matsubayashi, T., et al. (2007) · Blood · doi:10.1182/blood-2007-06-094201 · Cited by 151
Inflammasomes in Intestinal Inflammation and Cancer
Chen, G., & Núñez, G. (2011) · Gastroenterology · doi:10.1053/j.gastro.2011.10.002 · Cited by 158
Pattern‐recognition receptors in human eosinophils
Kvarnhammar, A. M., & Cardell, L. (2012) · Immunology · doi:10.1111/j.1365-2567.2012.03556.x · Cited by 160
Müller, K. H., Motskin, M., Philpott, A. J., Routh, A. F., Shanahan, C. M., Duer, M. J., & Skepper, J. N. (2013) · Biomaterials · doi:10.1016/j.biomaterials.2013.10.041 · Cited by 152
Sun, Y., Zhao, Y., Yao, J., Zhao, L., Wu, Z., Wang, Y., Pan, D., Miao, H., Guo, Q., & Lu, N. (2015) · Biochemical Pharmacology · doi:10.1016/j.bcp.2015.02.002 · Cited by 150
Drexler, S. K., Bonsignore, L., Masin, M., Tardivel, A., Jackstadt, R., Hermeking, H., Schneider, P., Groß, O., Tschopp, J., & Yazdi, A. S. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1209171109 · Cited by 154
Self-citationA2E Induces IL-1ß Production in Retinal Pigment Epithelial Cells via the NLRP3 Inflammasome
Anderson, O. A., Finkelstein, A., & Shima, D. T. (2013) · PLoS ONE · doi:10.1371/journal.pone.0067263 · Cited by 152
Johnson, R. J., Lanaspa, M. A., & Gaucher, E. A. (2011) · Seminars in Nephrology · doi:10.1016/j.semnephrol.2011.08.002 · Cited by 151
Li, X., Thome, S., Ma, X., Amrute‐Nayak, M., Finigan, A. J., Kitt, L., Masters, L. M., James, J. R., Shi, Y., Meng, G., et al. (2017) · Nature Communications · doi:10.1038/ncomms15986 · Cited by 160
Libby, P. (2021) · Cells · doi:10.3390/cells10040951 · Cited by 158
Gut microbiota remodeling: A promising therapeutic strategy to confront hyperuricemia and gout
Wang, Z., Li, Y., Liao, W., Huang, J., Liu, Y., Li, Z., & Tang, J. (2022) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2022.935723 · Cited by 154
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Wang, R.-F., Miyahara, Y., & Wang, H. Y. (2008) · Oncogene · doi:10.1038/sj.onc.1210906 · Cited by 151
Toll or Toll-Free Adjuvant Path Toward the Optimal Vaccine Development
Ishii, K. J., & Akira, S. (2007) · Journal of Clinical Immunology · doi:10.1007/s10875-007-9087-x · Cited by 149
Lin, Y., Huang, D.-Y., Wang, J.-S., Lin, Y., Hsieh, S.-L. E., Huang, K., & Lin, W. (2015) · Journal of Leukocyte Biology · doi:10.1189/jlb.3hi0814-371rr · Cited by 148
Control of infection by pyroptosis and autophagy: role of TLR and NLR
Bortoluci, K. R., & Medzhitov, R. M. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0335-5 · Cited by 150
Torres, R., Macdonald, L. E., Croll, S. D., Reinhardt, J., Dore, A. T., Stevens, S. G., Hylton, D., Rudge, J. S., Liu‐Bryan, R., Terkeltaub, R. A., et al. (2009) · Annals of the Rheumatic Diseases · doi:10.1136/ard.2009.109355 · Cited by 148
NLRP3 recruitment by NLRC4 during Salmonella infection
Qu, Y., Misaghi, S., Newton, K., Maltzman, A., Izrael-Tomasevic, A., Arnott, D. P., & Dixit, V. M. (2016) · The Journal of Experimental Medicine · doi:10.1084/jem.20132234 · Cited by 148
Mulay, S. R., & Anders, H. (2016) · New England Journal of Medicine · doi:10.1056/nejmra1601611 · Cited by 154
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Bernabei, I., So, A. K.-L., Busso, N., & Nasi, S. (2022) · Nature Reviews Rheumatology · doi:10.1038/s41584-022-00875-4 · Cited by 150
Abais, J. M., Zhang, C., Xia, M., Liu, Q., Gehr, T. W. B., Boini, K. M., & Li, P. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4666 · Cited by 148
Interactions of tumor cells with dendritic cells: balancing immunity and tolerance
Dhodapkar, M. V., Dhodapkar, K. M., & Palucka, A. K. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402247 · Cited by 154
Gut mucosal DAMPs in IBD: from mechanisms to therapeutic implications
Boyapati, R. K., Rossi, A. G., Satsangi, J., & Ho, G. (2016) · Mucosal Immunology · doi:10.1038/mi.2016.14 · Cited by 150
Maruzuru, Y., Ichinohe, T., Sato, R., Miyake, K., Okano, T., Suzuki, T., Koshiba, T., Koyanagi, N., Tsuda, S., Watanabe, M., et al. (2018) · Cell Host & Microbe · doi:10.1016/j.chom.2017.12.014 · Cited by 150
Zhang, X., Xu, A., Lv, J., Zhang, Q., Ran, Y., Wei, C., & Wu, J. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.111822 · Cited by 148
Sellmayr, M., Petzsche, M. R. H., Ma, Q., Krüger, N., Liapis, H., Brink, A., Lenz, B. F., Angelotti, M. L., Gnemmi, V., Kuppe, C., et al. (2020) · Journal of the American Society of Nephrology · doi:10.1681/asn.2020040523 · Cited by 147
Innate recognition of intracellular bacteria
Delbridge, L. M., & O’Riordan, M. X. (2006) · Current Opinion in Immunology · doi:10.1016/j.coi.2006.11.005 · Cited by 147
Yilmaz, Ö., Sater, A. A. A., Yao, L., Koutouzis, T., Pettengill, M. A., & Ojcius, D. M. (2009) · Cellular Microbiology · doi:10.1111/j.1462-5822.2009.01390.x · Cited by 146
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Ea, H., Nguyen, C., Bazin, D. C., Bianchi, A., Guicheux, J., Reboul, P., Daudon, M., & Lioté, F. (2010) · Arthritis & Rheumatism · doi:10.1002/art.27761 · Cited by 146
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McGonagle, D. G., Tan, A. L., Shankaranarayana, S., Madden, J. M., Emery, P., & McDermott, M. (2007) · Annals of the Rheumatic Diseases · doi:10.1136/ard.2007.073759 · Cited by 146
Marques-da-Silva, C., Chaves, M. M., Castro, N. G., Coutinho‐Silva, R., & Guimaraes, M. (2011) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2011.01254.x · Cited by 145
Sensors of the innate immune system: their mode of action
Baccalà, R., González‐Quintial, R., Lawson, B. R., Stern, M. E., Kono, D. H., Beutler, B., & Theofilopoulos, A. N. (2009) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2009.136 · Cited by 145
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Cronstein, B. N., & Sunkureddi, P. R. (2013) · JCR Journal of Clinical Rheumatology · doi:10.1097/rhu.0b013e31827d8790 · Cited by 145
Nile, S. H., Ko, E. Y., Kim, D. H., & Keum, Y. (2015) · Revista Brasileira de Farmacognosia · doi:10.1016/j.bjp.2015.08.013 · Cited by 145
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Lv, D., Cao, X., Li, Z. A., Dong, Y., Xu, Z., Rong, Y., Xu, H., Wang, Z., Yang, H., Yin, R. H., et al. (2023) · Cell Reports Medicine · doi:10.1016/j.xcrm.2023.101129 · Cited by 149
MDP-induced interleukin-1β processing requires Nod2 and CIAS1/NALP3
Pan, Q., Mathison, J. C., Fearns, C., Kravchenko, V. V., Correia, J. D. S., Hoffman, H. M., Kobayashi, K. S., Bertin, J., Grant, E. P., Coyle, A. J., et al. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.1006627 · Cited by 145
Gout: new insights into an old disease
Martinon, F. (2006) · Journal of Clinical Investigation · doi:10.1172/jci29404 · Cited by 145
Self-citationNLRC5 regulates MHC class I antigen presentation in host defense against intracellular pathogens
Yao, Y., Wang, Y., Chen, F., Huang, Y., Zhu, S., Leng, Q., Wang, H., Shi, Y., & Qian, Y. (2012) · Cell Research · doi:10.1038/cr.2012.56 · Cited by 145
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Xue, Z., Xi, Q., Liu, H., Guo, X., Zhang, J., Zhang, Z., Li, Y., Yang, G., Zhou, D., Yang, H., et al. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1713-z · Cited by 147
Simpson, D. S., Pang, J., Weir, A. L., Kong, I. Y., Fritsch, M., Rashidi, M., Cooney, J. P., Davidson, K. C., Speir, M., Djajawi, T. M., et al. (2022) · Immunity · doi:10.1016/j.immuni.2022.01.003 · Cited by 146
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Di Micco, A., Frera, G., Lugrin, J., Jamilloux, Y., Hsu, E.-T., Tardivel, A., De Gassart, A., Zaffalon, L., Bujisic, B., Siegert, S., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1602419113 · Cited by 143
Self-citationBerthet, J., Damien, P., Hamzeh‐Cognasse, H., Arthaud, C., Eyraud, M., Zéni, F., Pozzetto, B., McNicol, A., Garraud, O., & Cognasse, F. (2012) · Clinical Immunology · doi:10.1016/j.clim.2012.09.004 · Cited by 143
Progress in understanding adjuvant immunotoxicity mechanisms
Batista-Duharte, A., Lindblad, E. B., & Oviedo‐Orta, E. (2011) · Toxicology Letters · doi:10.1016/j.toxlet.2011.03.001 · Cited by 143
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Mitroulis, I., Kambas, K., & Ritis, K. (2013) · Seminars in Immunopathology · doi:10.1007/s00281-013-0361-0 · Cited by 146
Frey, B., Rubner, Y., Wunderlich, R., Weiss, E., Pockley, A. G., Fietkau, R., & Gaipl, U. S. (2012) · Current Medicinal Chemistry · doi:10.2174/092986712800099811 · Cited by 149
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Farasat, S., Aksentijevich, I. A., & Toro, J. R. (2008) · Archives of Dermatology · doi:10.1001/archderm.144.3.392 · Cited by 143
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Kim, M. L., Chae, J. J., Park, Y. H., Nardo, D. D., Stirzaker, R. A., Ko, H., Tye, H., Cengia, L. H., DiRago, L., Metcalf, D., et al. (2015) · The Journal of Experimental Medicine · doi:10.1084/jem.20142384 · Cited by 147
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Chu, J., Thomas, L. M., Watkins, S. C., Franchi, L., Núñez, G., & Salter, R. D. (2009) · Journal of Leukocyte Biology · doi:10.1189/jlb.0309164 · Cited by 142
Toma, C., Higa, N., Koizumi, Y., Nakasone, N., Ogura, Y., McCoy, A. J., Franchi, L., Uematsu, S., Sagara, J., Taniguchi, S., et al. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0903536 · Cited by 145
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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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