Cited by 3,080Inflammasome and immune disordersImmune Response and InflammationAutoimmune and Inflammatory Disorders Research

The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.

Cryopyrin activates the inflammasome in response to toxins and ATP

Mariathasan, Sanjeev, Weiss, David S., Newton, Kim, McBride, Jacqueline, O'Rourke, Karen, Roose-Girma, Meron, Lee, Wyne P., Weinrauch, Yvette, Monack, Denise M., Dixit, Vishva M.·2006·Nature

DOI 10.1038/nature04515

Open this paper in CoChat — free account

Abstract

A crucial part of the innate immune response is the assembly of the inflammasome, a cytosolic complex of proteins that activates caspase-1 to process the proinflammatory cytokines interleukin (IL)-1beta and IL-18. The adaptor protein ASC is essential for inflammasome function, binding directly to caspase-1 (refs 3, 4), but the triggers of this interaction are less clear. ASC also interacts with the adaptor cryopyrin (also known as NALP3 or CIAS1). Activating mutations in cryopyrin are associated with familial cold autoinflammatory syndrome, Muckle-Wells syndrome and neonatal onset multisystem inflammatory disease, diseases that are characterized by excessive production of IL-1beta. Here we show that cryopyrin-deficient macrophages cannot activate caspase-1 in response to Toll-like receptor agonists plus ATP, the latter activating the P2X7 receptor to decrease intracellular K+ levels. The release of IL-1beta in response to nigericin, a potassium ionophore, and maitotoxin, a potent marine toxin, was also found to be dependent on cryopyrin. In contrast to Asc-/- macrophages, cells deficient in the gene encoding cryopyrin (Cias1-/-) activated caspase-1 and secreted normal levels of IL-1beta and IL-18 when infected with Gram-negative Salmonella typhimurium or Francisella tularensis. Macrophages exposed to Gram-positive Staphylococcus aureus or Listeria monocytogenes, however, required both ASC and cryopyrin to activate caspase-1 and secrete IL-1beta. Therefore, cryopyrin is essential for inflammasome activation in response to signalling pathways triggered specifically by ATP, nigericin, maitotoxin, S. aureus or L. monocytogenes.

Integrity signals

Registry

Crossref · 10.1038/nature04515

Cites

26 of 26 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

Defective LPS Signaling in C3H/HeJ and C57BL/10ScCr Mice: Mutations in Tlr4 Gene
Poltorak, A., He, X., Smirnova, I., Liu, M.-Y., Huffel, C. V., Du, X., Birdwell, D., Alejos, E., Silva, M., Galanos, C., et al. (1998) · Science · doi:10.1126/science.282.5396.2085 · Cited by 7,631
The Inflammasome
Martinon, F., Burns, K., & Tschopp, J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00599-3 · Cited by 6,066
Nod2 Is a General Sensor of Peptidoglycan through Muramyl Dipeptide (MDP) Detection
Girardin, S. E., Boneca, I. G., Viala, J., Chamaillard, M., Labigne-Roussel, A., Thomas, G. D., Philpott, D. J., & Sansonetti, P. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200651200 · Cited by 2,397
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
Nod2-Dependent Regulation of Innate and Adaptive Immunity in the Intestinal Tract
Kobayashi, K. S., Chamaillard, M., Ogura, Y., Henegariu, O., Inohara, N., Núñez, G., & Flavell, R. A. (2005) · Science · doi:10.1126/science.1104911 · Cited by 1,834
NALP3 Forms an IL-1β-Processing Inflammasome with Increased Activity in Muckle-Wells Autoinflammatory Disorder
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
Mutation of a new gene encoding a putative pyrin-like protein causes familial cold autoinflammatory syndrome and Muckle–Wells syndrome
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
Mice deficient in IL-1β-converting enzyme are defective in production of mature IL-1β and resistant to endotoxic shock
Li, P., Allen, H., Banerjee, S., Franklin, S., Herzog, L., Johnston, C. G., McDowell, J., Paskind, M. P., Rodman, L., Salfeld, J. G., et al. (1995) · Cell · doi:10.1016/0092-8674(95)90490-5 · Cited by 1,408
Altered Cytokine Production in Mice Lacking P2X7Receptors
Solle, M., Labasi, J. M., Perregaux, D. G., Stam, E. J., Petrushova, N., Koller, B. H., Griffiths, R., & Gabel, C. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006781200 · Cited by 924
Interleukin-1 beta maturation and release in response to ATP and nigericin. Evidence that potassium depletion mediated by these agents is a necessary and common feature of their activity.
Perregaux, D. G., & Gabel, C. A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36591-2 · Cited by 775

Flagged first, then by citations

Show all 26 references

Sorted by citations

Items 701–800 of 1,021

Inflammasomes: Their Role in Normal and Complicated Pregnancies
Gomez‐Lopez, N., Motomura, K., Miller, D., Garcia‐Flores, V., Galaz, J., & Romero, R. J. (2019) · The Journal of Immunology · doi:10.4049/jimmunol.1900901 · Cited by 136
Palmitoylation of the P2X7 receptor, an ATP‐gated channel, controls its expression and association with lipid rafts
Gonnord, P., Delarasse, C., Auger, R., Benihoud, K., Prigent, M., Cuif, M., Lamaze, C., & Kanellopoulos, J. (2008) · The FASEB Journal · doi:10.1096/fj.08-114637 · Cited by 138
Antimicrobial Cathelicidin Peptide LL-37 Inhibits the LPS/ATP-Induced Pyroptosis of Macrophages by Dual Mechanism
Hu, Z., Murakami, T., Suzuki, K., Tamura, H., Kuwahara‐Arai, K., Iba, T., & Nagaoka, I. (2014) · PLoS ONE · doi:10.1371/journal.pone.0085765 · Cited by 142
Cutting Edge: Proteolytic Inactivation of Poly(ADP-Ribose) Polymerase 1 by the Nlrp3 and Nlrc4 Inflammasomes
Malireddi, R. K. S., Ippagunta, S. K., Lamkanfi, M., & Kanneganti, T. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1001512 · Cited by 139
NLRP3 inflammasome in neurodegenerative disease
Anderson, F. L., Biggs, K. E., Rankin, B. E., & Havrda, M. C. (2022) · Translational research · doi:10.1016/j.trsl.2022.08.006 · Cited by 154
Sterile inflammatory responses mediated by the NLRP3 inflammasome
Cassel, S. L., & Sutterwala, F. S. (2010) · European Journal of Immunology · doi:10.1002/eji.200940207 · Cited by 142
Aging-Associated TNF Production Primes Inflammasome Activation and NLRP3-Related Metabolic Disturbances
Bauernfeind, F., Niepmann, S., Knolle, P. A., & Hornung, V. (2016) · The Journal of Immunology · doi:10.4049/jimmunol.1501336 · Cited by 137
Quantitative Subcellular Proteome and Secretome Profiling of Influenza A Virus-Infected Human Primary Macrophages
Lietzén, N., Öhman, T., Rintahaka, J., Julkunen, I., Aittokallio, T., Matikainen, S., & Nyman, T. A. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1001340 · Cited by 137
Toll-like receptor signaling in the lysosomal pathways
Sanjuan, M. A., Milasta, S., & Green, D. R. (2009) · Immunological Reviews · doi:10.1111/j.1600-065x.2008.00732.x · Cited by 137
Activation of P2X7 Promotes Cerebral Edema and Neurological Injury after Traumatic Brain Injury in Mice
Kimbler, D. E., Shields, J., Yanasak, N. E., Vender, J. R., & Dhandapani, K. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041229 · Cited by 137
The Cytokine Release Inhibitory Drug CRID3 Targets ASC Oligomerisation in the NLRP3 and AIM2 Inflammasomes
Coll, R. C., & O'Neill, L. A. J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0029539 · Cited by 142
Caspase-1 Has Both Proinflammatory and Regulatory Properties in Helicobacter Infections, Which Are Differentially Mediated by Its Substrates IL-1β and IL-18
Hitzler, I., Sayi‐Yazgan, A., Kohler, E., Engler, D. B., Koch, K. N., Hardt, W., & Mueller, A. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1103212 · Cited by 138
Chronic inflammation within the vascular wall in pulmonary arterial hypertension: more than a spectator
Huertas, A., Tu, L., Humbert, M. J. C., & Guignabert, C. (2019) · Cardiovascular Research · doi:10.1093/cvr/cvz308 · Cited by 141
The Inflammasomes
Lamkanfi, M., & Dixit, V. M. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000510 · Cited by 139
Innate Immunity and Biomaterials at the Nexus: Friends or Foes
Christo, S. N., Diener, K. R., Bachhuka, A., Vasilev, K. A., & Hayball, J. D. (2015) · BioMed Research International · doi:10.1155/2015/342304 · Cited by 138
Biochemical regulation of the inflammasome
Dowling, J. K., & O'Neill, L. A. J. (2012) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2012.694844 · Cited by 139
Activation of NLRP 3 and AIM2 inflammasomes in Kupffer cells in hepatic ischemia/reperfusion
Kim, H.-Y., Kim, S., & Lee, S. (2014) · FEBS Journal · doi:10.1111/febs.13123 · Cited by 137
The Stroke-Induced Blood-Brain Barrier Disruption: Current Progress of Inspection Technique, Mechanism, and Therapeutic Target
Okada, T., Suzuki, H., Travis, Z. D., & Zhang, J. H. (2020) · Current Neuropharmacology · doi:10.2174/1570159x18666200528143301 · Cited by 141
Intracellular innate immune receptors: Life inside the cell
Kanneganti, T. (2020) · Immunological Reviews · doi:10.1111/imr.12912 · Cited by 145
Coordinated Host Responses during Pyroptosis: Caspase-1–Dependent Lysosome Exocytosis and Inflammatory Cytokine Maturation
Bergsbaken, T., Fink, S. L., den Hartigh, A. B., Loomis, W. P., & Cookson, B. T. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1100477 · Cited by 138
Inflammasomes and Metabolic Disease
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
Inflammasome biology, molecular pathology and therapeutic implications
Awad, F., Assrawi, E., Louvrier, C., Jumeau, C., Georgin‐Lavialle, S., Grateau, G., Amselem, S., Giurgea, I., & Karabina, S. (2018) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2018.02.011 · Cited by 138
NOD-like receptors: major players (and targets) in the interface between innate immunity and cancer
Velloso, F. J., Trombetta-Lima, M., Anschau, V., Sogayar, M. C., & Correa, R. G. (2019) · Bioscience Reports · doi:10.1042/bsr20181709 · Cited by 133
Listeria monocytogenes engineered to activate the Nlrc4 inflammasome are severely attenuated and are poor inducers of protective immunity
Sauer, J., Pereyre, S., Archer, K. A., Burke, T., Hanson, B., Lauer, P., & Portnoy, D. A. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1019041108 · Cited by 130
Detection of immune danger signals by NALP3
Martinon, F. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.0607362 · Cited by 140
An NLRP3 inflammasome-triggered cytokine storm contributes to Streptococcal toxic shock-like syndrome (STSLS)
Lin, L., Xu, L., Lv, W., Han, L., Xiang, Y., Fu, L., Jin, M., Zhou, R., Chen, H., & Zhang, A. (2019) · PLoS Pathogens · doi:10.1371/journal.ppat.1007795 · Cited by 131
Staphylococcus aureus Leukocidin A/B (LukAB) Kills Human Monocytes via Host NLRP3 and ASC when Extracellular, but Not Intracellular
Melehani, J. H., James, D. B. A., Dumont, A., Torres, V. J., & Duncan, J. A. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1004970 · Cited by 135
Post-Translational Control of IL-1β via the Human Papillomavirus Type 16 E6 Oncoprotein: A Novel Mechanism of Innate Immune Escape Mediated by the E3-Ubiquitin Ligase E6-AP and p53
Niebler, M., Qian, X., Höfler, D., Kogosov, V., Kaewprag, J., Kaufmann, A. M., Ly, R., Böhmer, G., Zawatzky, R., Rösl, F., et al. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003536 · Cited by 133
Nanomaterial-based vaccine adjuvants
Sun, B., & Xia, T. (2016) · Journal of Materials Chemistry B · doi:10.1039/c6tb01131d · Cited by 136
NLRC4 inflammasomopathies
Romberg, N. D., Vogel, T. P., & Canna, S. (2017) · Current Opinion in Allergy and Clinical Immunology · doi:10.1097/aci.0000000000000396 · Cited by 135
PANoptosome signaling and therapeutic implications in infection: central role for ZBP1 to activate the inflammasome and PANoptosis
Karki, R., & Kanneganti, T. (2023) · Current Opinion in Immunology · doi:10.1016/j.coi.2023.102348 · Cited by 138
Crystals of monosodium urate monohydrate enhance lipopolysaccharide-induced release of interleukin 1β by mononuclear cells through a caspase 1-mediated process
Giamarellos‐Bourboulis, E. J., Mouktaroudi, M., Bodar, E. J., van der Ven, J., Kullberg, B.-J., Netea, M. G., & van der Meer, J. W. M. (2008) · Annals of the Rheumatic Diseases · doi:10.1136/ard.2007.082222 · Cited by 132
NLR-mediated control of inflammasome assembly in the host response against bacterial pathogens
Brodsky, I. E., & Monack, D. M. (2009) · Seminars in Immunology · doi:10.1016/j.smim.2009.05.007 · Cited by 132
Innate instruction of adaptive immunity revisited: the inflammasome
Eisenbarth, S. C., & Flavell, R. A. (2009) · EMBO Molecular Medicine · doi:10.1002/emmm.200900014 · Cited by 135
Macrophage activation and polarization modify P2X7 receptor secretome influencing the inflammatory process
de Torre‐Minguela, C., Barberà-Cremades, M., Gómez, A. I., Martín‐Sánchez, F., & Pelegrı́n, P. (2016) · Scientific Reports · doi:10.1038/srep22586 · Cited by 135
A multicomponent toxin from Bacillus cereus incites inflammation and shapes host outcome via the NLRP3 inflammasome
Mathur, A., Feng, S., Hayward, J. A., Ngo, C., Fox, D., Atmosukarto, I. I., Price, J. D., Schauer, K., Märtlbauer, E. P., Robertson, A. A. B., et al. (2018) · Nature Microbiology · doi:10.1038/s41564-018-0318-0 · Cited by 134
SERPINB1-mediated checkpoint of inflammatory caspase activation
Choi, Y. J., Kim, S., Choi, Y., Nielsen, T. B., Yan, J., Lu, A. Z., Ruan, J., Lee, H.-R., Wu, H., Spellberg, B. J., et al. (2019) · Nature Immunology · doi:10.1038/s41590-018-0303-z · Cited by 139
SQSTM1-dependent autophagic degradation of PKM2 inhibits the production of mature IL1B/IL-1β and contributes to LIPUS-mediated anti-inflammatory effect
Zhang, B., Chen, H., Ouyang, J., Xie, Y., Chen, L., Tan, Q., Du, X., Su, N. Y., Ni, Z., & Chen, L. (2019) · Autophagy · doi:10.1080/15548627.2019.1664705 · Cited by 135
COPs and POPs: modulators of inflammasome activity
Stehlik, C., & Dorfleutner, A. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.12.7993 · Cited by 130
P2X7 receptors regulate multiple types of membrane trafficking responses and non-classical secretion pathways
Qu, Y., & Dubyak, G. (2009) · Purinergic Signalling · doi:10.1007/s11302-009-9132-8 · Cited by 130
Subversion of Host Recognition and Defense Systems by Francisella spp
Jones, C. L., Napier, B. A., Sampson, T. R., Llewellyn, A. C., Schroeder, M. R., & Weiss, D. S. (2012) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.05027-11 · Cited by 135
A recurrent intragenic genomic duplication, other novel mutations in NLRP7 and imprinting defects in recurrent biparental hydatidiform moles
Kou, Y.-C., Shao, L., Peng, H., Rosetta, R., del Gaudio, D., Wagner, A. F., Al-Hussaini, T. K., & den Veyver, I. B. V. (2007) · Molecular Human Reproduction · doi:10.1093/molehr/gam079 · Cited by 130
Inflammasomes as therapeutic targets for A lzheimer's disease
White, C., Lawrence, C. B., Brough, D., & Rivers‐Auty, J. (2016) · Brain Pathology · doi:10.1111/bpa.12478 · Cited by 136
Regulation and Function of the Nucleotide Binding Domain Leucine-Rich Repeat-Containing Receptor, Pyrin Domain-Containing-3 Inflammasome in Lung Disease
Lee, S., Suh, G. Y., Ryter, S. W., & Choi, A. M. K. (2015) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2015-0231tr · Cited by 130
Dangerous attraction: phagocyte recruitment and danger signals of apoptotic and necrotic cells
Peter, C., Wesselborg, S., i, M. H., & Lauber, K. (2010) · APOPTOSIS · doi:10.1007/s10495-010-0472-1 · Cited by 136
Interleukin-1β has trophic effects in microglia and its release is mediated by P2X7R pore
Monif, M., Reid, C. A., Powell, K. L., Drummond, K., O’Brien, T. J., & Williams, D. A. (2016) · Journal of Neuroinflammation · doi:10.1186/s12974-016-0621-8 · Cited by 126
PTPN22 regulates NLRP3-mediated IL1B secretion in an autophagy-dependent manner
Spalinger, M. R., Lang, S., Gottier, C., Dai, X., Rawlings, D. J., Chan, A. C., Rogler, G., & Scharl, M. M. (2017) · Autophagy · doi:10.1080/15548627.2017.1341453 · Cited by 136
Caspase-8 Collaborates with Caspase-11 to Drive Tissue Damage and Execution of Endotoxic Shock
Mandal, P., Feng, Y., Lyons, J. D., Berger, S. B., Otani, S., DeLaney, A. A., Tharp, G. K., Maner-Smith, K. M., Burd, E. M., Schaeffer, M. C., et al. (2018) · Immunity · doi:10.1016/j.immuni.2018.06.011 · Cited by 131
Cardamonin from a medicinal herb protects against LPS-induced septic shock by suppressing NLRP3 inflammasome
Wang, Z., Xu, G., Gao, Y., Zhan, X., Qin, N., Fu, S., Li, R., Niu, M., Wang, J., Liu, Y., et al. (2019) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2019.02.003 · Cited by 129
Role of Toll-like receptors, NOD-like receptors and RIG-I-like receptors in endothelial cells and systemic infections
Eitel, J., Meixenberger, K., Suttorp, N., & Opitz, B. (2009) · Thrombosis and Haemostasis · doi:10.1160/th09-05-0323 · Cited by 133
The Inflammasome — A Linebacker of Innate Defense
Drenth, J. P. H., & van der Meer, J. W. M. (2006) · New England Journal of Medicine · doi:10.1056/nejmcibr063500 · Cited by 130
Pyrin Levels in Human Monocytes and Monocyte-Derived Macrophages Regulate IL-1β Processing and Release
Seshadri, S., Duncan, M., Hart, J., Gavrilin, M. A., & Wewers, M. D. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.2.1274 · Cited by 128
Unsolved Mysteries in NLR Biology
Lupfer, C. R., & Kanneganti, T. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2013.00285 · Cited by 130
Danger Signals in the Initiation of the Inflammatory Response after Myocardial Infarction
de Haan, J. J., Smeets, M. B., Pasterkamp, G., & Arslan, F. (2013) · Mediators of Inflammation · doi:10.1155/2013/206039 · Cited by 139
Diabetes and Alzheimer Disease, Two Overlapping Pathologies with the Same Background: Oxidative Stress
Rosales‐Corral, S., Tan, D., Manchester, L. C., & Reiter, R. J. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/985845 · Cited by 134
Natural Compounds as Regulators of NLRP3 Inflammasome-Mediated IL-1 β Production
Tőzsér, J., & Benkő, S. (2016) · Mediators of Inflammation · doi:10.1155/2016/5460302 · Cited by 129
Therapeutic potential of garlic chive-derived vesicle-like nanoparticles in NLRP3 inflammasome-mediated inflammatory diseases
Liu, B., Li, X., Yu, H. V., Shi, X., Zhou, Y., Alvarez, S., Naldrett, M. J., Kachman, S. D., Ro, S., Sun, X., et al. (2021) · Theranostics · doi:10.7150/thno.60265 · Cited by 137
Specific inhibition of the NLRP3 inflammasome suppresses immune overactivation and alleviates COVID-19 like pathology in mice
Zeng, J., Xie, X., Feng, X., Xu, L., Han, J.-B., Yu, D., Zou, Q., Liu, Q., Li, X., Ma, G., et al. (2021) · EBioMedicine · doi:10.1016/j.ebiom.2021.103803 · Cited by 130
Sporadic colorectal cancer: microbial contributors to disease prevention, development and therapy
Drewes, J. L., Housseau, F., & Sears, C. L. (2016) · British Journal of Cancer · doi:10.1038/bjc.2016.189 · Cited by 121
Chrysophanol Inhibits NALP3 Inflammasome Activation and Ameliorates Cerebral Ischemia/Reperfusion in Mice
Zhang, N., Zhang, X., Liu, X., Wang, H., Xue, J., Yu, J., Kang, N., & Wang, X. (2014) · Mediators of Inflammation · doi:10.1155/2014/370530 · Cited by 126
Cutting Edge: Necrosis Activates the NLRP3 Inflammasome
Li, H., Ambade, A., & Re, F. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0901080 · Cited by 127
IL-1 family cytokines in inflammation and immunity
Garlanda, C., Ceglie, I. D., & Jaillon, S. (2025) · Cellular and Molecular Immunology · doi:10.1038/s41423-025-01358-8 · Cited by 153
Canonical Inflammasomes Drive IFN-γ to Prime Caspase-11 in Defense against a Cytosol-Invasive Bacterium
Aachoui, Y., Kajiwara, Y., Leaf, I. A., Mao, D., Ting, J. P.-Y., Coers, J., Aderem, A., Buxbaum, J. D., & Miao, E. A. (2015) · Cell Host & Microbe · doi:10.1016/j.chom.2015.07.016 · Cited by 125
Stress-evoked sterile inflammation, danger associated molecular patterns (DAMPs), microbial associated molecular patterns (MAMPs) and the inflammasome
Fleshner, M. (2013) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2012.08.012 · Cited by 126
Reciprocal Regulation between Enterovirus 71 and the NLRP3 Inflammasome
Wang, H., Lei, X., Xiao, X., Yang, C., Lu, W., Huang, Z. W., Leng, Q., Jin, Q., He, B., Meng, G., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.05.047 · Cited by 126
Caspase-1 autoproteolysis is differentially required for NLRP1b and NLRP3 inflammasome function
Guey, B., Bodnar‐Wachtel, M., Manié, S. N., Tardivel, A., & Pétrilli, V. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1415756111 · Cited by 129
Double-walled carbon nanotubes trigger IL-1β release in human monocytes through Nlrp3 inflammasome activation
Meunier, É., Coste, A., Olagnier, D. P., Authier, H., Lefèvre, L., Dardenne, C., Bernad, J., Béraud, M., Emmanuel Flahaut, B., & Pipy, B. (2011) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2011.11.004 · Cited by 126
Mycobacterial EST12 activates a RACK1–NLRP3–gasdermin D pyroptosis–IL-1β immune pathway
Qu, Z., Zhou, J., Zhou, Y., Xie, Y., Jiang, Y., Wu, J., Luo, Z., Liu, G., Yin, L., & Zhang, X. (2020) · Science Advances · doi:10.1126/sciadv.aba4733 · Cited by 129
MCC950 attenuates doxorubicin-induced myocardial injury in vivo and in vitro by inhibiting NLRP3-mediated pyroptosis
Zhang, L., Jiang, Y.-H., Fan, C., Zhang, Q., Jiang, Y.-H., Li, Y., & Xue, Y. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.112133 · Cited by 129
NF-κB activation by the Toll-IL-1 receptor domain protein MyD88 adapter-like is regulated by caspase-1
Miggin, S. M., Pålsson‐McDermott, E. M., Dunne, A., Jefferies, C. A., Pinteaux, E., Banahan, K., Murphy, C., Moynagh, P. N., Yamamoto, M., Akira, S., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608100104 · Cited by 126
Intracellular sensing of microbes and danger signals by the inflammasomes
Horvath, G. L., Schrum, J. E., Nardo, C. M. D., & Latz, E. (2011) · Immunological Reviews · doi:10.1111/j.1600-065x.2011.01050.x · Cited by 127
The NLRP3 Inflammasome Is Required for the Development of Hypoxemia in LPS/Mechanical Ventilation Acute Lung Injury
Jones, H. D., Crother, T. R., González-Villalobos, R. A., Jupelli, M., Chen, S., Dagvadorj, J., Arditi, M., & Shimada, K. (2013) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2013-0087oc · Cited by 125
Constitutively Activated NLRP3 Inflammasome Causes Inflammation and Abnormal Skeletal Development in Mice
Bonar, S. L., Brydges, S., Mueller, J., McGeough, M. D., Peña, C., Chen, D., Grimston, S., Hickman-Brecks, C. L., Ravindran, S., McAlinden, A., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0035979 · Cited by 130
Genome Editing of Human Primary Keratinocytes by CRISPR/Cas9 Reveals an Essential Role of the NLRP1 Inflammasome in UVB Sensing
Fenini, G., Grossi, S., Contassot, E., Biedermann, T., Reichmann, E., French, L. E., & Beer, H.-D. (2018) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2018.07.016 · Cited by 125
Roles of mitochondrial ROS and NLRP3 inflammasome in multiple ozone-induced lung inflammation and emphysema
Li, F., Xu, M., Wang, M., Wang, L., Wang, H., Zhang, H., Chen, Y., Gong, J., Zhang, J. J., Adcock, I. M., et al. (2018) · Respiratory Research · doi:10.1186/s12931-018-0931-8 · Cited by 125
The impact of endogenous triggers on trauma-associated inflammation
Zedler, S., & Faist, E. (2006) · Current Opinion in Critical Care · doi:10.1097/mcc.0b013e3280106806 · Cited by 125
NLRP3 Inflammasome and MS/EAE
Inoue, M., & Shinohara, M. L. (2013) · Autoimmune Diseases · doi:10.1155/2013/859145 · Cited by 123
NLRP3 Inflammasome and Host Protection against Bacterial Infection
Kim, J.-J., & Jo, E. (2013) · Journal of Korean Medical Science · doi:10.3346/jkms.2013.28.10.1415 · Cited by 124
Opposing roles of LTB4 and PGE2 in regulating the inflammasome-dependent scorpion venom-induced mortality
Zoccal, K. F., Sorgi, C. A., Hori, J. I., Paula‐Silva, F. W. G., Arantes, E. C., Serezani, C. H., Zamboni, D. S., & Faccioli, L. H. (2016) · Nature Communications · doi:10.1038/ncomms10760 · Cited by 128
Attenuation of mechanical pain hypersensitivity by treatment with Peptide5, a connexin-43 mimetic peptide, involves inhibition of NLRP3 inflammasome in nerve-injured mice
Tonkin, R. S., Bowles, C., Perera, C. J., Keating, B. A., Makker, P. G. S., Duffy, S. S., Lees, J. G., Tran, C., Don, A. S., Fath, T., et al. (2017) · Experimental Neurology · doi:10.1016/j.expneurol.2017.10.016 · Cited by 124
Leishmania Lipophosphoglycan Triggers Caspase-11 and the Non-canonical Activation of the NLRP3 Inflammasome
de Carvalho, R. A., Andrade, W. A., Lima-Junior, D. S., Dilucca, M., de Oliveira, C. V., Wang, K., Nogueira, P. M., Rugani, J. M. N., Soares, R. P., Beverley, S. M., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2018.12.047 · Cited by 122
Pyroptosis in the Initiation and Progression of Atherosclerosis
Qian, Z., Zhao, Y., Wan, C., Deng, Y., Zhuang, Y., Xu, Y., Zhu, Y., Lu, S., & Bao, Z. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.652963 · Cited by 127
Novel cellular and molecular mechanisms of induction of immune responses by aluminum adjuvants
Aimanianda, V., Haensler, J., Lacroix‐Desmazes, S., Kaveri, S. V., & Bayry, J. (2009) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2009.03.005 · Cited by 126
Metabolic signals and innate immune activation in obesity and exercise
Ringseis, R., Eder, K., Mooren, F. C., & Krüger, K. (2026) · PubMed · doi:10.22029/eir.2015.1696 · Cited by 120
Cryopyrin-associated periodic syndromes and autoinflammation
Shinkai, K., McCalmont, T. H., & Leslie, K. S. (2007) · Clinical and Experimental Dermatology · doi:10.1111/j.1365-2230.2007.02540.x · Cited by 123
ILr1β production is dependent on the activation of purinergic receptors and NLRP3 pathway in human macrophages
Gicquel, T., Robert, S., Loyer, P., Victoni, T., Bodin, A., Ribault, C., Gléonnec, F., Couillin, I., Boichot, E., & Lagente, V. (2015) · The FASEB Journal · doi:10.1096/fj.14-267393 · Cited by 133
NLRP3 controls Trypanosoma cruzi infection through a caspase-1-dependent IL-1R-independent NO production
Gonçalves, V. M., Matteucci, K. C., Buzzo, C. L., Miollo, B. H., Ferrante, D., Torrecilhas, A. C., Rodrigues, M. M., Alvarez, J. M., & Bortoluci, K. R. (2013) · PLoS Neglected Tropical Diseases · doi:10.1371/journal.pntd.0002469 · Cited by 123
NLRP3 Inflammasome: A Possible Link Between Obesity-Associated Low-Grade Chronic Inflammation and Colorectal Cancer Development
Ahechu, P., Zozaya, G., Martí, P., Hernández-Lizoáin, J. L., Baixauli, J., Unamuno, X., Frühbeck, G., & Catalán, V. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02918 · Cited by 131
Mechanisms of NLRP3 Inflammasome Activation: Its Role in the Treatment of Alzheimer’s Disease
Zhang, Y., Zhao, Y., Zhang, J., & Yang, G. (2020) · Neurochemical Research · doi:10.1007/s11064-020-03121-z · Cited by 127
Distinct Molecular Mechanisms Underlying Potassium Efflux for NLRP3 Inflammasome Activation
Xu, Z., Chen, Z.-M., Wu, X., Zhang, L., Cao, Y., & Zhou, P. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.609441 · Cited by 127
A Key Role for Redox Signaling in Rapid P2X7 Receptor-Induced IL-1β Processing in Human Monocytes
Hewinson, J., Moore, S., Glover, C., Watts, A. G., & Mackenzie, A. B. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.12.8410 · Cited by 123
The PYRIN Domain-only Protein POP1 Inhibits Inflammasome Assembly and Ameliorates Inflammatory Disease
de Almeida, L., Khare, S., Misharin, A. V., Patel, R., Ratsimandresy, R. A., Wallin, M., Perlman, H., Greaves, D. R., Hoffman, H. M., Dorfleutner, A., et al. (2015) · Immunity · doi:10.1016/j.immuni.2015.07.018 · Cited by 132
HMGB1 release by inflammasomes
Walle, L. V., Kanneganti, T., & Lamkanfi, M. (2011) · Virulence · doi:10.4161/viru.2.2.15480 · Cited by 122
Ambiguities in NLRP3 inflammasome regulation: Is there a role for mitochondria?
Lawlor, K. E., & Vince, J. E. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.08.014 · Cited by 124
Co-Localization of Glia Maturation Factor with NLRP3 Inflammasome and Autophagosome Markers in Human Alzheimer’s Disease Brain
Ahmed, M. E., Iyer, S. S., Thangavel, R., Kempuraj, D., Selvakumar, G. P., Raikwar, S. P., Zaheer, S. A., & Zaheer, A. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170634 · Cited by 120
Pyroptosis-Induced Inflammation and Tissue Damage
Wei, Y., Yang, L., Pandeya, A., Cui, J., Zhang, Y., & Li, Z. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167301 · Cited by 130
It’s All in the PAN: Crosstalk, Plasticity, Redundancies, Switches, and Interconnectedness Encompassed by PANoptosis Underlying the Totality of Cell Death-Associated Biological Effects
Gullett, J. M., Tweedell, R. E., & Kanneganti, T. (2022) · Cells · doi:10.3390/cells11091495 · Cited by 129
Lipopolysaccharide induces and activates the Nalp3 inflammasome in the liver
Ganz, M. (2011) · World Journal of Gastroenterology · doi:10.3748/wjg.v17.i43.4772 · Cited by 122
NLRP3 inflammasome signalling in Alzheimer's disease
McManus, R. M., & Latz, E. (2024) · Neuropharmacology · doi:10.1016/j.neuropharm.2024.109941 · Cited by 136
The inflammatory caspases: guardians against infections and sepsis
Scott, A., & Saleh, M. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402026 · Cited by 119

Authors: 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.
Affiliations: Genentech (US)
Stanford Medicine (US)
New York University (US)
Corresponding author: Dixit, Vishva M.
ORCID: Mariathasan, Sanjeev
Weiss, David S.
Newton, Kim
McBride, Jacqueline
Roose-Girma, Meron
Lee, Wyne P.
Monack, Denise M.
Dixit, Vishva M.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2006-01-11
Volume: 440
Issue: 7081
Pages: 228-232
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature04515
OpenAlex: W2090859543
Cited by: 3,080
References: 26
Citations by year: 2026: 90 · 2025: 101 · 2024: 129 · 2023: 121 · 2022: 150 · 2021: 152 · 2020: 160 · 2019: 161 · 2018: 155 · 2017: 164 · 2016: 184 · 2015: 179 · 2014: 180 · 2013: 189 · 2012: 173
FWCI: 62.33
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)
Funders: National Institutes of Health
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
Health Sciences › Medicine › Hematology › Autoimmune and Inflammatory Disorders Research
Keywords: NLRP3, inflammasome, caspase-1, IL-1β, IL-18, ATP, P2X7 receptor, bacterial toxins, maitotoxin, nigericin, bacterial RNA, R837, R848, urate crystals, autoinflammatory disease, innate immunity
MeSH terms: NLR Family, Pyrin Domain-Containing 3 Protein, Polyether Toxins, Adenosine Triphosphate, Animals, Carrier Proteins, Cytoskeletal Proteins, Enzyme Activation, Inflammation, Interleukin-1, Listeria monocytogenes, Macrophages, Marine Toxins, Nigericin, Staphylococcus aureus, Toxins, Biological, Signal Transduction, NF-kappa B, Caspase 1, Oxocins, Multiprotein Complexes, Intracellular Signaling Peptides and Proteins, Extracellular Signal-Regulated MAP Kinases, Apoptosis Regulatory Proteins, Toll-Like Receptors, Mice, CARD Signaling Adaptor Proteins, Nod2 Signaling Adaptor Protein

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

Cryopyrin activates the inflammasome in response to toxins and ATP

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks