Cited by 738Inflammasome and immune disordersImmune Response and InflammationIL-33, ST2, and ILC Pathways

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Mechanism of NLRP3 inflammasome activation

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Sutterwala, Fayyaz S., Haasken, Stefanie, Cassel, Suzanne L.·2014·Annals of the New York Academy of Sciences

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Abstract

Inflammasomes continue to generate interest in an increasing number of disciplines owing to their unique ability to integrate a myriad of signals from pathogen- and damage-associated molecular patterns into a proinflammatory response. This potent caspase-1-dependent process is capable of activating the innate immune system, initiating pyroptosis (an inflammatory form of programmed cell death), and shaping adaptive immunity. The NLRP3 inflammasome is the most thoroughly studied of the inflammasome complexes that have been described thus far, perhaps owing to its disparate assortment of agonists. This review highlights our current understanding of the mechanisms of both priming and activation of the NLRP3 inflammasome.

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Martinon, F., Burns, K., & Tschopp, J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00599-3 · Cited by 6,066
A role for mitochondria in nlrp3 inflammasome activation
Zhou, R., Yazdi, A. S., Menu, P., & Tschopp, J. (2011) · Nature · doi:10.1038/nature09663 · Cited by 5,602
Immunological and inflammatory functions of the interleukin-1 family
Dinarello, C. A. (2009) · Annual Review of Immunology · doi:10.1146/annurev.immunol.021908.132612 · Cited by 3,466
Cutting Edge: NF-κB Activating Pattern Recognition and Cytokine Receptors License NLRP3 Inflammasome Activation by Regulating NLRP3 Expression
Bauernfeind, F. G., Horvath, G. L., Stutz, A., Alnemri, E. S., MacDonald, K. L., Speert, D. P., Fernandes‐Alnemri, T., Wu, J., Monks, B. G., Fitzgerald, K. A., et al. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0901363 · Cited by 3,087
Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome
Nakahira, K., Haspel, J. A., Rathinam, V. A. K., Lee, S.-J., Dolinay, T., Lam, H. C., Englert, J. A., Rabinovitch, M., Cernadas, M., Kim, H. P., et al. (2011) · Nature Immunology · doi:10.1038/ni.1980 · Cited by 3,049
Two CD95 (APO‐1/Fas) signaling pathways
Scaffidi, C., Fulda, S., Srinivasan, A., Friesen, C., Li, F., Tomaselli, K. J., Debatin, K., Krammer, P. H., & Peter, M. E. (1998) · The EMBO Journal · doi:10.1093/emboj/17.6.1675 · Cited by 3,000
Activation and regulation of the inflammasomes
Latz, E., Xiao, T. S., & Stutz, A. (2013) · Nature Reviews Immunology · doi:10.1038/nri3452 · Cited by 2,884
AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC
Hornung, V., Ablasser, A., Charrel-Dennis, M., Bauernfeind, F., Horvath, G., Caffrey, D. R., Latz, E., & Fitzgerald, K. A. (2009) · Nature · doi:10.1038/nature07725 · Cited by 2,627
A novel heterodimeric cysteine protease is required for interleukin-1βprocessing in monocytes
Thornberry, N. A., Bull, H. G., Calaycay, J. R., Chapman, K. T., Howard, A. D., Kostura, M. J., Miller, D. K., Molineaux, S. M., Weidner, J. R., Aunins, J. G., et al. (1992) · Nature · doi:10.1038/356768a0 · Cited by 2,613
Oxidized mitochondrial DNA activates the NLRP3 inflammasome during apoptosis
Shimada, K., Crother, T. R., Karlin, J., Dagvadorj, J., Chiba, N., Chen, S., Ramanujan, V. K., Wolf, A. J., Vergnes, L., Ojcius, D. M., et al. (2012) · Immunity · doi:10.1016/j.immuni.2012.01.009 · Cited by 2,282
K+ Efflux Is the Common Trigger of NLRP3 Inflammasome Activation by Bacterial Toxins and Particulate Matter
Muñoz-Planillo, R., Kuffa, P., Martínez-Colón, G. J., Smith, B. L., Rajendiran, T. M., & Núñez, G. (2013) · Immunity · doi:10.1016/j.immuni.2013.05.016 · Cited by 2,167
Loss of the autophagy protein Atg16L1 enhances endotoxin-induced IL-1β production
Saitoh, T., Fujita, N., Jang, M. H., Uematsu, S., Yang, B., Satoh, T., Omori, H., Noda, T., Yamamoto, N., Komatsu, M., et al. (2008) · Nature · doi:10.1038/nature07383 · Cited by 2,064
NLRP6 Inflammasome Regulates Colonic Microbial Ecology and Risk for Colitis
Elinav, E., Strowig, T., Kau, A. L., Henao-Mejia, J., Thaiss, C. A., Booth, C. J., Peaper, D. R., Bertin, J., Eisenbarth, S. C., Gordon, J. I., et al. (2011) · Cell · doi:10.1016/j.cell.2011.04.022 · Cited by 2,024
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
AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA
Fernandes-Alnemri, T., Yu, J.-W., Datta, P., Wu, J., & Alnemri, E. S. (2009) · Nature · doi:10.1038/nature07710 · Cited by 1,831
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
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
Activation of autophagy by inflammatory signals limits IL-1β production by targeting ubiquitinated inflammasomes for destruction
Shi, C.-S., Shenderov, K., Huang, N.-N., Kabat, J., Abu-Asab, M., Fitzgerald, K. A., Sher, A., & Kehrl, J. H. (2012) · Nature Immunology · doi:10.1038/ni.2215 · Cited by 1,367
The NLRC4 inflammasome receptors for bacterial flagellin and type III secretion apparatus
Zhao, Y., Yang, J., Shi, J., Gong, Y., Lu, Q., Xu, H., Liu, L., & Shao, F. (2011) · Nature · doi:10.1038/nature10510 · Cited by 1,310
Regulation of progenitor cell proliferation and granulocyte function by microRNA-223
Johnnidis, J. B., Harris, M. H., Wheeler, R. T., Stehling-Sun, S., Lam, M. H., Kirak, O., Brummelkamp, T. R., Fleming, M. D., & Camargo, F. D. (2008) · Nature · doi:10.1038/nature06607 · Cited by 1,208
Activation of Interferon-γ Inducing Factor Mediated by Interleukin-1β Converting Enzyme
Gu, Y., Kuida, K., Tsutsui, H., Ku, G., Hsiao, K., Fleming, M. A., Hayashi, N., Higashino, K., Okamura, H., Nakanishi, K., et al. (1997) · Science · doi:10.1126/science.275.5297.206 · Cited by 1,159
Caspase-1-dependent pore formation during pyroptosis leads to osmotic lysis of infected host macrophages
Fink, S. L., & Cookson, B. T. (2006) · Cellular Microbiology · doi:10.1111/j.1462-5822.2006.00751.x · Cited by 1,114
An orthogonal proteomic-genomic screen identifies AIM2 as a cytoplasmic DNA sensor for the inflammasome
Bürckstümmer, T., Baumann, C., Blüml, S., Dixit, E., Dürnberger, G., Jahn, H., Planyavsky, M., Bilban, M., Colinge, J., Bennett, K. L., et al. (2009) · Nature Immunology · doi:10.1038/ni.1702 · Cited by 1,091
The calcium-sensing receptor regulates the NLRP3 inflammasome through Ca2+ and cAMP
Lee, G., Subramanian, N., Kim, A. I., Aksentijevich, I. A., Goldbach‐Mansky, R. T., Sacks, D. B., Germain, R. N., Kastner, D. L., & Chae, J. J. (2012) · Nature · doi:10.1038/nature11588 · Cited by 1,077
The pyroptosome: a supramolecular assembly of ASC dimers mediating inflammatory cell death via caspase-1 activation
Fernandes-Alnemri, T., Wu, J., Yu, J.-W., Datta, P., Miller, B., Jankowski, W., Rosenberg, S., Zhang, J., & Alnemri, E. S. (2007) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4402194 · Cited by 1,026
The NLR Gene Family: A Standard Nomenclature
Ting, J. P. ‐., Lovering, R. C., Alnemri, E. S., Bertin, J., Boss, J. M., Davis, B. K., Flavell, R. A., Girardin, S. E., Godzik, A., Harton, J. A., et al. (2008) · Immunity · doi:10.1016/j.immuni.2008.02.005 · Cited by 998
Mitochondrial Cardiolipin Is Required for Nlrp3 Inflammasome Activation
Iyer, S. S., He, Q., Janczy, J. R., Elliott, E. I., Zhong, Z., Olivier, A. K., Sadler, J. J., Knepper-Adrian, V., Han, R., Qiao, L., et al. (2013) · Immunity · doi:10.1016/j.immuni.2013.08.001 · Cited by 968
Critical role for calcium mobilization in activation of the NLRP3 inflammasome
Murakami, T., Öckinger, J., Yu, J., Byles, V., McColl, A., Hofer, A. M., & Horng, T. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1117765109 · Cited by 961
Cytochrome c release from mitochondria proceeds by a two-step process
Ott, M., Robertson, J. D., Gogvadze, V. G., Zhivotovsky, B., & Orrenius, S. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.241655498 · Cited by 955
Inflammasomes and Their Roles in Health and Disease
Lamkanfi, M., & Dixit, V. M. (2012) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-101011-155745 · Cited by 935
Type I Interferon Inhibits Interleukin-1 Production and Inflammasome Activation
Guarda, G., Braun, M., Staehli, F., Tardivel, A., Mattmann, C., Förster, I., Farlik, M., Decker, T., Pasquier, R. D., Romero, P. J., et al. (2011) · Immunity · doi:10.1016/j.immuni.2011.02.006 · Cited by 924
Innate immune recognition of bacterial ligands by NAIPs determines inflammasome specificity
Kofoed, E. M., & Vance, R. E. (2011) · Nature · doi:10.1038/nature10394 · Cited by 894
Microtubule-driven spatial arrangement of mitochondria promotes activation of the NLRP3 inflammasome
Misawa, T., Takahama, M., Kozaki, T., Lee, H., Zou, J., Saitoh, T., & Akira, S. (2013) · Nature Immunology · doi:10.1038/ni.2550 · Cited by 894
Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin
Boyden, E. D., & Dietrich, W. F. (2006) · Nature Genetics · doi:10.1038/ng1724 · Cited by 882
HIN-200 Proteins Regulate Caspase Activation in Response to Foreign Cytoplasmic DNA
Roberts, T. L., Idris, A., Dunn, J. A., Kelly, G., Burnton, C. M., Hodgson, S., Hardy, L., Garceau, V., Sweet, M. J., Ross, I. L., et al. (2009) · Science · doi:10.1126/science.1169841 · Cited by 830
Glyburide inhibits the Cryopyrin/Nalp3 inflammasome
Lamkanfi, M., Mueller, J. L., Vitari, A. C., Misaghi, S., Fedorova, A., Deshayes, K., Lee, W. P., Hoffman, H. M., & Dixit, V. M. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200903124 · Cited by 820
Non-transcriptional Priming and Deubiquitination Regulate NLRP3 Inflammasome Activation
Juliana, C. A., Fernandes‐Alnemri, T., Kang, S., Farias, A., Qin, F., & Alnemri, E. S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.407130 · Cited by 803
De novo CIAS1 mutations, cytokine activation, and evidence for genetic heterogeneity in patients with neonatal‐onset multisystem inflammatory disease (NOMID): A new member of the expanding family of pyrin‐associated autoinflammatory diseases
Aksentijevich, I. A., Nowak, M., Mallah, M., Chae, J. J., Watford, W. T., Hofmann, S. R., Stein, L. D., Russo, R. A. G., Goldsmith, D. P., Dent, P. B., et al. (2002) · Arthritis & Rheumatism · doi:10.1002/art.10688 · Cited by 746
Chronic Infantile Neurological Cutaneous and Articular Syndrome Is Caused by Mutations in CIAS1, a Gene Highly Expressed in Polymorphonuclear Cells and Chondrocytes
Feldmann, J., Prieur, A., Quartier, P., Berquin, P. C., Dogniaux, S., Cortis, E., Hamel‐Teillac, D., Fischer, A., & Basile, G. D. S. (2002) · The American Journal of Human Genetics · doi:10.1086/341357 · Cited by 737
Deubiquitination of NLRP3 by BRCC3 Critically Regulates Inflammasome Activity
Py, B. F., Kim, M.-S., Vakifahmetoglu-Norberg, H., & Yuan, J. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.11.009 · Cited by 718
IFI16 Acts as a Nuclear Pathogen Sensor to Induce the Inflammasome in Response to Kaposi Sarcoma-Associated Herpesvirus Infection
Kerur, N., Veettil, M. V., Sharma-Walia, N., Bottero, V., Sadagopan, S., Otageri, P., & Chandran, B. (2011) · Cell Host & Microbe · doi:10.1016/j.chom.2011.04.008 · Cited by 702
The Adaptor MAVS Promotes NLRP3 Mitochondrial Localization and Inflammasome Activation
Subramanian, N., Natarajan, K., Clatworthy, M. R., Wang, Z., & Germain, R. N. (2013) · Cell · doi:10.1016/j.cell.2013.02.054 · Cited by 692
Cutting Edge: Reactive Oxygen Species Inhibitors Block Priming, but Not Activation, of the NLRP3 Inflammasome
Bauernfeind, F., Bartok, E., Rieger, A., Franchi, L., Núñez, G., & Hornung, V. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1100613 · Cited by 617
Signaling by ROS drives inflammasome activation
Martinon, F. (2010) · European Journal of Immunology · doi:10.1002/eji.200940168 · Cited by 604
Mitochondrial permeability transition in Ca2+-dependent apoptosis and necrosis
Rasola, A., & Bernardi, P. (2011) · Cell Calcium · doi:10.1016/j.ceca.2011.04.007 · Cited by 590
Cutting Edge: TNF-α Mediates Sensitization to ATP and Silica via the NLRP3 Inflammasome in the Absence of Microbial Stimulation
Franchi, L., Eigenbrod, T., & Núñez, G. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0900173 · Cited by 574
Nitric oxide controls the immunopathology of tuberculosis by inhibiting NLRP3 inflammasome–dependent processing of IL-1β
Mishra, B. B., Rathinam, V. A. K., Martens, G. W., Martinot, A. J., Kornfeld, H., Fitzgerald, K. A., & Sassetti, C. M. (2013) · Nature Immunology · doi:10.1038/ni.2474 · Cited by 571
NLRP3 inflammasome activity is negatively controlled by miR-223
Bauernfeind, F., Rieger, A., Schildberg, F. A., Knolle, P. A., Schmid-Burgk, J. L., & Hornung, V. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1201516 · Cited by 544
Recognition of RNA virus by RIG-I results in activation of CARD9 and inflammasome signaling for interleukin 1β production
Poeck, H., Bscheider, M., Groß, O., Finger, K., Roth, S., Rebsamen, M., Hannesschläger, N., Schlee, M., Rothenfußer, S., Barchet, W., et al. (2009) · Nature Immunology · doi:10.1038/ni.1824 · Cited by 534
Extracellular Ca2+ is a danger signal activating the NLRP3 inflammasome through G protein-coupled calcium sensing receptors
Rossol, M., Pierer, M., Raulien, N., Quandt, D., Meusch, U., Rothe, K., Schubert, K. A., Schöneberg, T., Schaefer, M., Krügel, U., et al. (2012) · Nature Communications · doi:10.1038/ncomms2339 · Cited by 506
Inflammasome Activators Induce Interleukin-1α Secretion via Distinct Pathways with Differential Requirement for the Protease Function of Caspase-1
Groß, O., Yazdi, A. S., Thomas, C. J., Masin, M., Heinz, L. X., Guarda, G., Quadroni, M., Drexler, S. K., & Tschopp, J. (2012) · Immunity · doi:10.1016/j.immuni.2012.01.018 · Cited by 479
Gain-of-Function Pyrin Mutations Induce NLRP3 Protein-Independent Interleukin-1β Activation and Severe Autoinflammation in Mice
Chae, J. J., Cho, Y.-H., Lee, G., Cheng, J., Liu, P. P., Feigenbaum, L., Katz, S. I., & Kastner, D. L. (2011) · Immunity · doi:10.1016/j.immuni.2011.02.020 · Cited by 473
Cutting Edge: miR-223 and EBV miR-BART15 Regulate the NLRP3 Inflammasome and IL-1β Production
Haneklaus, M., Gerlic, M., Kurowska‐Stolarska, M., Rainey, A., Pich, D., McInnes, I. B., Hammerschmidt, W., O'Neill, L. A. J., & Masters, S. L. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1200312 · Cited by 466
A crucial function of SGT1 and HSP90 in inflammasome activity links mammalian and plant innate immune responses
Mayor, A., Martinon, F., Smedt, T. D., Pétrilli, V., & Tschopp, J. (2007) · Nature Immunology · doi:10.1038/ni1459 · Cited by 438
Nitric oxide suppresses NLRP3 inflammasome activation and protects against LPS-induced septic shock
Mao, K., Chen, S., Chen, M., Ma, Y., Wang, Y., Huang, B., He, Z., Zeng, Y., Hu, Y., Sun, S., et al. (2013) · Cell Research · doi:10.1038/cr.2013.6 · Cited by 408
Cell Volume Regulation Modulates NLRP3 Inflammasome Activation
Compan, V., Baroja‐Mazo, A., López‐Castejón, G., Gomez, A. I., Martínez, C. M., Angosto-Bazarra, D., Montero, M. T., Herranz, A. S., Bazán, E., Reimers, D., et al. (2012) · Immunity · doi:10.1016/j.immuni.2012.06.013 · Cited by 407
TRPM2 links oxidative stress to NLRP3 inflammasome activation
Zhong, Z., Zhai, Y., Liang, S., Mori, Y., Han, R., Sutterwala, F. S., & Qiao, L. (2013) · Nature Communications · doi:10.1038/ncomms2608 · Cited by 374
Intracellular DNA recognition
Hornung, V., & Latz, E. (2010) · Nature reviews. Immunology · doi:10.1038/nri2690 · Cited by 366
The complement membrane attack complex triggers intracellular Ca2+ fluxes leading to NLRP3 inflammasome activation
Triantafilou, K., Hughes, T. R., Triantafilou, M., & Morgan, B. P. (2013) · Journal of Cell Science · doi:10.1242/jcs.124388 · Cited by 361
An NLRP7-Containing Inflammasome Mediates Recognition of Microbial Lipopeptides in Human Macrophages
Khare, S., Dorfleutner, A., Bryan, N. B., Yun, C., Radian, A. D., de Almeida, L., Rojanasakul, Y., & Stehlik, C. (2012) · Immunity · doi:10.1016/j.immuni.2012.02.001 · Cited by 355
Is mPTP the gatekeeper for necrosis, apoptosis, or both?
Kinnally, K. W., Peixoto, P. M. V., Ryu, S.-Y., & Dejean, L. M. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.09.013 · Cited by 349
Bcl-2 and Bcl-XL Regulate Proinflammatory Caspase-1 Activation by Interaction with NALP1
Bruey, J., Bruey-Sédano, N., Luciano, F., Zhai, D., Balpai, R., Xu, C., Kress, C. L., Bailly‐Maitre, B., Li, X., Osterman, A. L., et al. (2007) · Cell · doi:10.1016/j.cell.2007.01.045 · Cited by 319
Critical functions of priming and lysosomal damage for NLRP3 activation
Hornung, V., & Latz, E. (2010) · European Journal of Immunology · doi:10.1002/eji.200940185 · Cited by 297
Cardiolipin provides an essential activating platform for caspase-8 on mitochondria
Gonzalvez, F., Schug, Z. T., Houtkooper, R. H., MacKenzie, E. D., Brooks, D. G., Wanders, R. J. A., Petit, P. X., Vaz, F. M., & Gottlieb, E. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200803129 · Cited by 296
Mitochondrial protein mitofusin 2 is required for NLRP3 inflammasome activation after RNA virus infection
Ichinohe, T., Yamazaki, T., Koshiba, T., & Yanagi, Y. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1312571110 · Cited by 291
IRAK-1 bypasses priming and directly links TLRs to rapid NLRP3 inflammasome activation
Lin, K.-M., Hu, W., Troutman, T. D., Jennings, M., Brewer, T., Li, X., Nanda, S. K., Cohen, P., Thomas, J. A., & Pasare, C. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1320294111 · Cited by 285
The Mitochondrial Antiviral Protein MAVS Associates with NLRP3 and Regulates Its Inflammasome Activity
Park, S., Juliana, C. A., Hong, S., Datta, P., Hwang, I., Fernandes‐Alnemri, T., Yu, J., & Alnemri, E. S. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1301170 · Cited by 275
T cells dampen innate immune responses through inhibition of NLRP1 and NLRP3 inflammasomes
Guarda, G., Dostert, C., Staehli, F., Cabalzar, K., Castillo, R., Tardivel, A., Schneider, P., & Tschopp, J. (2009) · Nature · doi:10.1038/nature08100 · Cited by 250
Cutting Edge: TLR Signaling Licenses IRAK1 for Rapid Activation of the NLRP3 Inflammasome
Fernandes‐Alnemri, T., Kang, S., Anderson, C., Sagara, J., Fitzgerald, K. A., & Alnemri, E. S. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1301681 · Cited by 243
NALP1 Influences Susceptibility to Human Congenital Toxoplasmosis, Proinflammatory Cytokine Response, and Fate ofToxoplasma gondii-Infected Monocytic Cells
Witola, W. H., Mui, E. J., Hargrave, A. C., Liu, S., Hypolite, M., Montpetit, A., Cavaillès, P., Bisanz, C., Cesbron‐Delauw, M., Fournié, G. J., et al. (2010) · Infection and Immunity · doi:10.1128/iai.00898-10 · Cited by 203
BID is cleaved by caspase-8 within a native complex on the mitochondrial membrane
Schug, Z. T., Gonzalvez, F., Houtkooper, R. H., Vaz, F. M., & Gottlieb, E. (2010) · Cell Death and Differentiation · doi:10.1038/cdd.2010.135 · Cited by 191
Cutting Edge: Mouse NAIP1 Detects the Type III Secretion System Needle Protein
Rayamajhi, M., Zak, D. E., Chavarría‐Smith, J., Vance, R. E., & Miao, E. A. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1301549 · Cited by 191
Acute lipopolysaccharide priming boosts inflammasome activation independently of inflammasome sensor induction
Schroder, K., Sagulenko, V., Zamoshnikova, A., Richards, A. A., Cridland, J. A., Irvine, K. M., Stacey, K. J., & Sweet, M. J. (2012) · Immunobiology · doi:10.1016/j.imbio.2012.07.020 · Cited by 182
Early changes in intramitochondrial cardiolipin distribution during apoptosis.
Garcia‐Fernandez, M. I., Troiano, L., Moretti, L., Nasi, M., Pinti, M., Salvioli, S., Dobrucki, J. W., & Cossarizza, A. (2002) · PubMed · Cited by 181
Cellular Inhibitors of Apoptosis Proteins cIAP1 and cIAP2 Are Required for Efficient Caspase-1 Activation by the Inflammasome
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
Deubiquitinases Regulate the Activity of Caspase-1 and Interleukin-1β Secretion via Assembly of the Inflammasome
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
An Interaction between Bcl-xL and the Voltage-dependent Anion Channel (VDAC) Promotes Mitochondrial Ca2+ Uptake
Huang, H., Hu, X., Eno, C. O., Zhao, G., Li, C., & White, C. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.448290 · Cited by 161
An Update on PYRIN Domain-Containing Pattern Recognition Receptors: From Immunity to Pathology
Ratsimandresy, R. A., Dorfleutner, A., & Stehlik, C. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2013.00440 · Cited by 114
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Authors: Sutterwala, F. S., Haasken, S., & Cassel, S. L.
Affiliations: University of Iowa (US)
Corresponding author: Sutterwala, Fayyaz S.
ORCID: Sutterwala, Fayyaz S.
Venue: Annals of the New York Academy of Sciences
Publisher: Wiley
Published: 2014-05-19
Volume: 1319
Issue: 1
Pages: 82-95
ISSN: 0077-8923 (ISSN-L)
1749-6632
DOI: 10.1111/nyas.12458
PMC: PMC4074217
OpenAlex: W1636793459
Cited by: 736
References: 82
Citations by year: 2026: 25 · 2025: 54 · 2024: 58 · 2023: 68 · 2022: 85 · 2021: 88 · 2020: 81 · 2019: 52 · 2018: 60 · 2017: 57 · 2016: 57 · 2015: 42 · 2014: 8
FWCI: 5.18
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: Annals of the New York Academy of Sciences (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health (AI087630, AI104706, AI007511)
Asthma and Allergy foundation of America
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
Life Sciences › Immunology and Microbiology › Immunology › IL-33, ST2, and ILC Pathways
Keywords: NLRP3 inflammasome, inflammasome activation, inflammasome priming, caspase-1, pyroptosis, innate immunity, damage-associated molecular patterns, pathogen-associated molecular patterns
MeSH terms: NLR Family, Pyrin Domain-Containing 3 Protein, Animals, Carrier Proteins, Cell Survival, Humans, Cell Death, Adaptive Immunity, Inflammasomes

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Mechanism of NLRP3 inflammasome activation

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