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Caspase-11 increases susceptibility to Salmonella infection in the absence of caspase-1
Open accessAbstract
Inflammasomes are cytosolic multiprotein complexes assembled by intracellular nucleotide-binding oligomerization domain (NOD)-like receptors (NLRs) and they initiate innate immune responses to invading pathogens and danger signals by activating caspase-1 (ref. 1). Caspase-1 activation leads to the maturation and release of the pro-inflammatory cytokines interleukin (IL)-1β and IL-18, as well as lytic inflammatory cell death known as pyroptosis. Recently, a new non-canonical inflammasome was described that activates caspase-11, a pro-inflammatory caspase required for lipopolysaccharide-induced lethality. This study also highlighted that previously generated caspase-1 knockout mice lack a functional allele of Casp11 (also known as Casp4), making them functionally Casp1 Casp11 double knockouts. Previous studies have shown that these mice are more susceptible to infections with microbial pathogens, including the bacterial pathogen Salmonella enterica serovar Typhimurium (S. typhimurium), but the individual contributions of caspase-1 and caspase-11 to this phenotype are not known. Here we show that non-canonical caspase-11 activation contributes to macrophage death during S. typhimurium infection. Toll-like receptor 4 (TLR4)-dependent and TIR-domain-containing adaptor-inducing interferon-β (TRIF)-dependent interferon-β production is crucial for caspase-11 activation in macrophages, but is only partially required for pro-caspase-11 expression, consistent with the existence of an interferon-inducible activator of caspase-11. Furthermore, Casp1(-/-) mice were significantly more susceptible to infection with S. typhimurium than mice lacking both pro-inflammatory caspases (Casp1(-/-) Casp11(-/-)). This phenotype was accompanied by higher bacterial counts, the formation of extracellular bacterial microcolonies in the infected tissue and a defect in neutrophil-mediated clearance. These results indicate that caspase-11-dependent cell death is detrimental to the host in the absence of caspase-1-mediated innate immunity, resulting in extracellular replication of a facultative intracellular bacterial pathogen.
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“type I IFN and IFN gamma (IFNG) also contribute to pyroptosis by promoting: (1) the transactivation of CASP11, through an IFNAR1-dependent or IFNGR1-dependent mechanism initiated by TLR4 or IL18 signaling [620, 643, 644]”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [643]
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“A limitation of our study is that the caspase-1–null mice were also found to be deficient in caspase-11 (46,47)”
From Sustained Inflammasome Activity in Macrophages Impairs Wound Healing in Type 2 Diabetic Humans and Mice (2014) · cites this paper as [47]
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Cites
Schroder, K., & Tschopp, J. (2010) · Cell · doi:10.1016/j.cell.2010.01.040 · Cited by 5,475
The family of five: TIR-domain-containing adaptors in Toll-like receptor signalling
O'Neill, L. A. J., & Bowie, A. G. (2007) · Nature Reviews Immunology · doi:10.1038/nri2079 · Cited by 2,667
Non-canonical inflammasome activation targets caspase-11
Kayagaki, N., Warming, S., Lamkanfi, M., Walle, L. V., Louie, S., Dong, J., Newton, K., Qu, Y., Liu, J., Heldens, S., et al. (2011) · Nature · doi:10.1038/nature10558 · Cited by 2,530
Self-citationDifferential 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
Self-citationAltered Cytokine Export and Apoptosis in Mice Deficient in Interleukin-1β Converting Enzyme
Kuida, K., Lippke, J. A., Ku, G., Harding, M. W., Livingston, D. J., Su, M. S. S., & Flavell, R. A. (1995) · Science · doi:10.1126/science.7535475 · Cited by 1,631
Caspase-1-induced pyroptosis is an innate immune effector mechanism against intracellular bacteria
Miao, E. A., Leaf, I. A., Treuting, P. M., Mao, D. P., Dors, M., Sarkar, A., Warren, S. E., Wewers, M. D., & Aderem, A. (2010) · Nature Immunology · doi:10.1038/ni.1960 · Cited by 1,336
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
Franchi, L., Amer, A., Body-Malapel, M., Kanneganti, T.-D., Özören, N., Jagirdar, R., Inohara, N., Vandenabeele, P., Bertin, J., Coyle, A., et al. (2006) · Nature Immunology · doi:10.1038/ni1346 · Cited by 1,131
Cytoplasmic flagellin activates caspase-1 and secretion of interleukin 1β via Ipaf
Miao, E. A., Alpuche-Aranda, C. M., Dors, M., Clark, A. E., Bader, M. W., Miller, S. I., & Aderem, A. (2006) · Nature Immunology · doi:10.1038/ni1344 · Cited by 1,127
Sensing and reacting to microbes through the inflammasomes
Franchi, L., Muñoz-Planillo, R., & Núñez, G. (2012) · Nature Immunology · doi:10.1038/ni.2231 · Cited by 1,046
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Galluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death & Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680
Self-citationCaspase-11 cleaves gasdermin D for non-canonical inflammasome signalling
Kayagaki, N., Stowe, I. B., Lee, B. L., O’Rourke, K., Anderson, K., Warming, S., Cuellar, T., Haley, B., Roose-Girma, M., Phung, Q. T., et al. (2015) · Nature · doi:10.1038/nature15541 · Cited by 3,686
Self-citationThe NLRP3 Inflammasome: an overview of mechanisms of activation and regulation
Kelley, N., Jeltema, D., Duan, Y., & He, Y. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20133328 · Cited by 3,539
Inflammasomes: mechanism of assembly, regulation and signalling
Broz, P., & Dixit, V. M. (2016) · Nature Reviews Immunology · doi:10.1038/nri.2016.58 · Cited by 3,500
Self-citationActivation and regulation of the inflammasomes
Latz, E., Xiao, T. S., & Stutz, A. (2013) · Nature Reviews Immunology · doi:10.1038/nri3452 · Cited by 2,884
Type I interferons in infectious disease
McNab, F., Mayer-Barber, K., Sher, A., Wack, A., & O'Garra, A. (2015) · Nature Reviews Immunology · doi:10.1038/nri3787 · Cited by 2,780
Mechanisms and Functions of Inflammasomes
Lamkanfi, M., & Dixit, V. M. (2014) · Cell · doi:10.1016/j.cell.2014.04.007 · Cited by 2,579
Self-citationPyroptosis: Mechanisms and Diseases
Yu, P., Zhang, X., Liu, N., Tang, L., Peng, C., & Chen, X. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00507-5 · Cited by 2,353
Inflammatory caspases are innate immune receptors for intracellular LPS
Shi, J., Zhao, Y., Wang, Y., Gao, W., Ding, J., Li, P., Hu, L., & Shao, F. (2014) · Nature · doi:10.1038/nature13683 · Cited by 2,285
Toll-like Receptors and the Control of Immunity
Fitzgerald, K. A., & Kagan, J. C. (2020) · Cell · doi:10.1016/j.cell.2020.02.041 · Cited by 2,168
Man, S. M., Karki, R., & Kanneganti, T. (2017) · Immunological Reviews · doi:10.1111/imr.12534 · Cited by 1,684
Noncanonical Inflammasome Activation by Intracellular LPS Independent of TLR4
Kayagaki, N., Wong, M. T., Stowe, I. B., Ramani, S. R., Gonzalez, L. C., Akashi‐Takamura, S., Miyake, K., Zhang, J., Lee, W. P., Muszyński, A., et al. (2013) · Science · doi:10.1126/science.1240248 · Cited by 1,545
Self-citationNeutrophil extracellular traps license macrophages for cytokine production in atherosclerosis
Warnatsch, A., Ιωάννου, Μ., Wang, Q., & Papayannopoulos, V. (2015) · Science · doi:10.1126/science.aaa8064 · Cited by 1,309
Cytoplasmic LPS Activates Caspase-11: Implications in TLR4-Independent Endotoxic Shock
Hagar, J. A., Powell, D. A., Aachoui, Y., Ernst, R. K., & Miao, E. A. (2013) · Science · doi:10.1126/science.1240988 · Cited by 1,261
GSDMD membrane pore formation constitutes the mechanism of pyroptotic cell death
Sborgi, L., Rühl, S., Mulvihill, E., Pipercevic, J., Heilig, R., Stahlberg, H., Farady, C. J., Müller, D. J., Broz, P., & Hiller, S. (2016) · The EMBO Journal · doi:10.15252/embj.201694696 · Cited by 1,152
Inflammasome Complexes: Emerging Mechanisms and Effector Functions
Rathinam, V. A. K., & Fitzgerald, K. A. (2016) · Cell · doi:10.1016/j.cell.2016.03.046 · Cited by 1,130
Pyroptotic cell death defends against intracellular pathogens
Jorgensen, I., & Miao, E. A. (2015) · Immunological Reviews · doi:10.1111/imr.12287 · Cited by 1,021
Caspases in Cell Death, Inflammation, and Pyroptosis
Kesavardhana, S., Malireddi, R. K. S., & Kanneganti, T. (2020) · Annual Review of Immunology · doi:10.1146/annurev-immunol-073119-095439 · Cited by 954
Burdette, B. E., Esparza, A. N., Zhu, H., & Wang, S. (2021) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2021.02.006 · Cited by 721
Converging roles of caspases in inflammasome activation, cell death and innate immunity
Man, S. M., & Kanneganti, T. (2015) · Nature reviews. Immunology · doi:10.1038/nri.2015.7 · Cited by 717
Walsh, J. G., Muruve, D. A., & Power, C. (2014) · Nature Reviews Neuroscience · doi:10.1038/nrn3638 · Cited by 637
Innate immunity to intracellular LPS
Rathinam, V. A. K., Zhao, Y., & Shao, F. (2019) · Nature Immunology · doi:10.1038/s41590-019-0368-3 · Cited by 622
Yang, D., He, Y., Muñoz-Planillo, R., Liu, Q., & Núñez, G. (2015) · Immunity · doi:10.1016/j.immuni.2015.10.009 · Cited by 622
Inflammasome activation and function in liver disease
Szabó, G., & Petrasek, J. (2015) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/nrgastro.2015.94 · Cited by 600
Gurung, P., Anand, P., Malireddi, R. K. S., Walle, L. V., Opdenbosch, N. V., Dillon, C. P., Weinlich, R., Green, D. R., Lamkanfi, M., & Kanneganti, T. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1302839 · Cited by 558
Caspase‐11 activates a canonical NLRP3 inflammasome by promoting K + efflux
Rühl, S., & Brož, P. (2015) · European Journal of Immunology · doi:10.1002/eji.201545772 · Cited by 546
Caspase-11 Protects Against Bacteria That Escape the Vacuole
Aachoui, Y., Leaf, I. A., Hagar, J. A., Fontana, M. F., Campos, C. G., Zak, D. E., Tan, M. H., Cotter, P. A., Vance, R. E., Aderem, A. A., et al. (2013) · Science · doi:10.1126/science.1230751 · Cited by 544
Citrobacter rodentium: infection, inflammation and the microbiota
Collins, J. W., Keeney, K. M., Crepin, V. F., Rathinam, V. A. K., Fitzgerald, K. A., Finlay, B. B., & Frankel, G. M. (2014) · Nature Reviews Microbiology · doi:10.1038/nrmicro3315 · Cited by 536
Salmonellae interactions with host processes
LaRock, D. L., Chaudhary, A., & Miller, S. I. (2015) · Nature Reviews Microbiology · doi:10.1038/nrmicro3420 · Cited by 502
Mechanisms of inflammasome activation: recent advances and novel insights
Vanaja, S. K., Rathinam, V. A. K., & Fitzgerald, K. A. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.12.009 · Cited by 499
Role of pyroptosis in cardiovascular disease
Zeng, Z., Li, G., Wu, S., & Zuo, W. (2018) · Cell Proliferation · doi:10.1111/cpr.12563 · Cited by 500
Caspase-11 activation requires lysis of pathogen-containing vacuoles by IFN-induced GTPases
Meunier, E., Dick, M. S., Dreier, R. F., Schürmann, N., Broz, D. K., Warming, S., Roose-Girma, M., Bumann, D., Kayagaki, N., Takeda, K., et al. (2014) · Nature · doi:10.1038/nature13157 · Cited by 485
Self-citationNewly described pattern recognition receptors team up against intracellular pathogens
Brož, P., & Monack, D. M. (2013) · Nature reviews. Immunology · doi:10.1038/nri3479 · Cited by 481
Self-citationA 360° view of the inflammasome: Mechanisms of activation, cell death, and diseases
Barnett, K. C., Li, S., Liang, K., & Ting, J. P.-Y. (2023) · Cell · doi:10.1016/j.cell.2023.04.025 · Cited by 458
Knodler, L. A., Crowley, S. M., Sham, H. P., Yang, H., Wrande, M., Ma, C., Ernst, R. K., Steele‐Mortimer, O., Celli, J., & Vallance, B. A. (2014) · Cell Host & Microbe · doi:10.1016/j.chom.2014.07.002 · Cited by 430
Inflammasome Activation Triggers Blood Clotting and Host Death through Pyroptosis
Wu, C., Lu, W., Zhang, Y., Zhang, G., Shi, X., Hisada, Y., Grover, S. P., Zhang, X., Li, L., Xiang, B., et al. (2019) · Immunity · doi:10.1016/j.immuni.2019.04.003 · Cited by 422
Mechanisms of NOD-like Receptor-Associated Inflammasome Activation
Wen, H., Miao, E. A., & Ting, J. P. ‐. (2013) · Immunity · doi:10.1016/j.immuni.2013.08.037 · Cited by 415
Recognition of Bacteria by Inflammasomes
von Moltke, J., Ayres, J. S., Kofoed, E. M., Chavarría‐Smith, J., & Vance, R. E. (2012) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032712-095944 · Cited by 420
Recent Advances in Lipopolysaccharide Recognition Systems
Mazgaeen, L., & Gurung, P. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21020379 · Cited by 395
InflammasomesPreprint
de Zoete, M. R., Palm, N. W., Zhu, S., & Flavell, R. A. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016287 · Cited by 399
Man, S. M., Karki, R., Malireddi, R. K. S., Neale, G., Vogel, P., Yamamoto, M., Lamkanfi, M., & Kanneganti, T.-D. (2015) · Nature Immunology · doi:10.1038/ni.3118 · Cited by 380
Baker, P. J., Boucher, D., Bierschenk, D., Tebartz, C., Whitney, P. G., D’Silva, D. B., Tanzer, M. C., Monteleone, M. M., Robertson, A. A. B., Cooper, M. A., et al. (2015) · European Journal of Immunology · doi:10.1002/eji.201545655 · Cited by 370
Pyroptosis in health and disease: mechanisms, regulation and clinical perspective
Liu, Y., Pan, R., Ouyang, Y., Gu, W., Xiao, T., Yang, H., Tang, L. Y., Wang, H., Xiang, B., & Chen, P. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01958-2 · Cited by 391
Signaling pathways and intervention therapies in sepsis
Zhang, Y., & Ning, B. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00816-9 · Cited by 369
Guanylate binding proteins promote caspase-11–dependent pyroptosis in response to cytoplasmic LPS
Pilla, D. M., Hagar, J. A., Haldar, A. K., Mason, A. K., Degrandi, D., Pfeffer, K., Ernst, R. K., Yamamoto, M., Miao, E. A., & Coers, J. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1321700111 · Cited by 357
Structure and function: Lipid A modifications in commensals and pathogens
Steimle, A., Autenrieth, I. B., & Frick, J.-S. (2016) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2016.03.001 · Cited by 373
Pattern recognition receptors: function, regulation and therapeutic potential
Chen, R., Zou, J., Chen, J., Zhong, X. Y., Kang, R., & Tang, D. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02264-1 · Cited by 392
Viganò, E., Diamond, C. E., Spreafico, R., Balachander, A., Sobota, R. M., & Mortellaro, A. (2015) · Nature Communications · doi:10.1038/ncomms9761 · Cited by 367
Meunier, É., Wallet, P., Dreier, R. F., Costanzo, S., Anton, L., Rühl, S., Dussurgey, S., Dick, M. S., Kistner, A., Mélanie, R., et al. (2015) · Nature Immunology · doi:10.1038/ni.3119 · Cited by 366
Caspases Connect Cell-Death Signaling to Organismal Homeostasis
Galluzzi, L., López-Soto, A., Kumar, S., & Kroemer, G. (2016) · Immunity · doi:10.1016/j.immuni.2016.01.020 · Cited by 350
Programmed Necrosis in the Cross Talk of Cell Death and Inflammation
Chan, F. K.-M., Luz, N. F., & Moriwaki, K. (2014) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032414-112248 · Cited by 359
An overview of the non-canonical inflammasome
Downs, K. P., Nguyen, H., Dorfleutner, A., & Stehlik, C. (2020) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2020.100924 · Cited by 338
Pyroptosis, metabolism, and tumor immune microenvironment
Du, T., Gao, J., Li, P., Wang, Y., Qi, Q., Liu, X., Li, J., Wang, C., & Du, L. (2021) · Clinical and Translational Medicine · doi:10.1002/ctm2.492 · Cited by 335
Mirza, R. E., Fang, M. M., Weinheimer-Haus, E. M., Ennis, W. J., & Koh, T. J. (2014) · Diabetes · doi:10.2337/db13-0927 · Cited by 319
“A limitation of our study is that the caspase1–null mice were also found to be deficient in caspase-11 (46,47), and so our bone marrow–transfer experiments do not distinguish the role of these caspases in the impaired healing of wounds in db/db mice.”
BackgroundIRGB10 Liberates Bacterial Ligands for Sensing by the AIM2 and Caspase-11-NLRP3 Inflammasomes
Man, S. M., Karki, R., Sasai, M., Place, D. E., Kesavardhana, S., Temirov, J., Frase, S., Zhu, Q., Malireddi, R. K. S., Kuriakose, T., et al. (2016) · Cell · doi:10.1016/j.cell.2016.09.012 · Cited by 312
The NLRP6 Inflammasome Recognizes Lipoteichoic Acid and Regulates Gram-Positive Pathogen Infection
Hara, H., Seregin, S. S., Yang, D., Fukase, K., Chamaillard, M., Alnemri, E. S., Inohara, N., Chen, G., & Núñez, G. (2018) · Cell · doi:10.1016/j.cell.2018.09.047 · Cited by 315
Inflammasome-mediated pyroptotic and apoptotic cell death, and defense against infection
Aachoui, Y., Sagulenko, V., Miao, E. A., & Stacey, K. J. (2013) · Current Opinion in Microbiology · doi:10.1016/j.mib.2013.04.004 · Cited by 296
Roles of Caspases in Necrotic Cell Death
Yuan, J., Najafov, A., & Py, B. F. (2016) · Cell · doi:10.1016/j.cell.2016.11.047 · Cited by 299
Human GBP1 binds LPS to initiate assembly of a caspase-4 activating platform on cytosolic bacteria
Santos, J. C., Boucher, D., Kapinos, L. E., Demarco, B., Dilucca, M., Shkarina, K., Heilig, R., Chen, K. W., Lim, R. Y. H., & Brož, P. (2020) · Nature Communications · doi:10.1038/s41467-020-16889-z · Cited by 290
The Role of Interferons in Inflammation and Inflammasome Activation
Kopitar-Jerala, N. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00873 · Cited by 260
Casson, C. N., Yu, J. M., Reyes, V. M., Taschuk, F., Yadav, A., Copenhaver, A. M., Nguyen, H. T., Collman, R. G., & Shin, S. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1421699112 · Cited by 281
Caspase-11 stimulates rapid flagellin-independent pyroptosis in response to Legionella pneumophila
Case, C. L., Kohler, L. J., Lima, J. B., Strowig, T., de Zoete, M. R., Flavell, R. A., Zamboni, D. S., & Roy, C. R. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1211521110 · Cited by 276
Non-canonical activation of inflammatory caspases by cytosolic LPS in innate immunity
Yang, J., Zhao, Y., & Shao, F. (2015) · Current Opinion in Immunology · doi:10.1016/j.coi.2015.01.007 · Cited by 269
Harnessing innate immune pathways for therapeutic advancement in cancer
Hu, A.-K., Sun, L., Lin, H., Liao, Y., Yang, H., & Mao, Y. Q. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01765-9 · Cited by 286
Molecular mechanisms of regulated necrosis
Galluzzi, L., Kepp, O., Krautwald, S., Kroemer, G., & Linkermann, A. (2014) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2014.02.006 · Cited by 258
Yi, Y. (2017) · Immunology · doi:10.1111/imm.12787 · Cited by 256
Zamyatina, A., & Heine, H. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.585146 · Cited by 254
Inflammasome Priming in Sterile Inflammatory Disease
Patel, M. N., Carroll, R. G., Galván-Peña, S., Mills, E. L., Olden, R., Triantafilou, M., Wolf, A. I., Bryant, C. E., Triantafilou, K., & Masters, S. L. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2016.12.007 · Cited by 241
Man, S. M., Tourlomousis, P., Hopkins, L., Monie, T. P., Fitzgerald, K. A., & Bryant, C. E. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1301581 · Cited by 239
Regulation of NLRP3 Inflammasome by Phosphorylation
Song, N., & Li, T. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02305 · Cited by 239
Santos, J. C., Dick, M. S., Lagrange, B., Degrandi, D., Pfeffer, K., Yamamoto, M., Meunier, É., Pelczar, P., Henry, T., & Brož, P. (2018) · The EMBO Journal · doi:10.15252/embj.201798089 · Cited by 245
Activation of inflammasome signaling mediates pathology of acute P. aeruginosa pneumonia
Cohen, T. S., & Prince, A. S. (2013) · Journal of Clinical Investigation · doi:10.1172/jci66142 · Cited by 237
Karmakar, M., Katsnelson, M. J., Malak, H. A., Greene, N. G., Howell, S. J., Hise, A. G., Camilli, A., Kadioglu, A., Dubyak, G., & Pearlman, E. M. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1401624 · Cited by 237
NLRP3 tyrosine phosphorylation is controlled by protein tyrosine phosphatase PTPN22
Spalinger, M. R., Kasper, S., Gottier, C., Lang, S., Atrott, K., Vavricka, S. R., Scharl, S., Gutte, P. M., Grütter, M. G., Beer, H., et al. (2016) · Journal of Clinical Investigation · doi:10.1172/jci83669 · Cited by 236
Ullah, M. O., Sweet, M. J., Mansell, A. S., Kellie, S., & Kobe, B. (2016) · Journal of Leukocyte Biology · doi:10.1189/jlb.2ri1115-531r · Cited by 232
Zanoni, I., Tan, Y., Di Gioia, M., Springstead, J. R., & Kagan, J. C. (2017) · Immunity · doi:10.1016/j.immuni.2017.09.010 · Cited by 221
The NLR gene family: from discovery to present day
Chou, W.-C., Jha, S., Linhoff, M. W., & Ting, J. P. ‐. (2023) · Nature reviews. Immunology · doi:10.1038/s41577-023-00849-x · Cited by 232
Pellegrini, C., Antonioli, L., López‐Castejón, G., Blandizzi, C., & Fornai, M. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00036 · Cited by 220
Enteric Nervous System-Derived IL-18 Orchestrates Mucosal Barrier Immunity
Jarret, A. P., Jackson, R. P., Duizer, C., Healy, M. E., Zhao, J., Rone, J. M., Bielecki, P., Sefik, E., Roulis, M., Rice, T., et al. (2020) · Cell · doi:10.1016/j.cell.2019.12.016 · Cited by 211
Kobayashi, T., Ogawa, M., Sanada, T., Mimuro, H., Kim, M., Ashida, H., Akakura, R., Yoshida, M., Kawalec, M., Reichhart, J., et al. (2013) · Cell Host & Microbe · doi:10.1016/j.chom.2013.04.012 · Cited by 203
The NLRP3 Inflammasome: Metabolic Regulation and Contribution to Inflammaging
Meyers, A. K., & Zhu, X. (2020) · Cells · doi:10.3390/cells9081808 · Cited by 207
Chu, L. H., Indramohan, M., Ratsimandresy, R. A., Gangopadhyay, A., Morris, E. P., Monack, D. M., Dorfleutner, A., & Stehlik, C. (2018) · Nature Communications · doi:10.1038/s41467-018-03409-3 · Cited by 200
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Burton, N. A., Schürmann, N., Casse, O., Steeb, A. K., Claudi, B., Zankl, J., Schmidt, A., & Bumann, D. (2014) · Cell Host & Microbe · doi:10.1016/j.chom.2013.12.006 · Cited by 175
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Metadata
- Authors
- Broz, P., Ruby, T., Belhocine, K., Bouley, D. M., Kayagaki, N., Dixit, V. M., & Monack, D. M.
- Affiliations
- Stanford Medicine (US)
- Genentech (US)
- Corresponding author
- Monack, Denise M.
- Venue
- Nature
- Published
- 2012-08-15
- Volume
- 490
- Issue
- 7419
- Pages
- 288-291
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC3470772
- OpenAlex
- W2024591203
- Cited by
- 535
- References
- 23
- Citations by year
- 2026: 13 · 2025: 25 · 2024: 20 · 2023: 35 · 2022: 33 · 2021: 31 · 2020: 47 · 2019: 40 · 2018: 38 · 2017: 40 · 2016: 51 · 2015: 49 · 2014: 53 · 2013: 53 · 2012: 6
- FWCI
- 20.71
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- National Institute of Allergy and Infectious Diseases (F32AI008972, AI095396, R01AI089722, AI08972, R01AI095396)
- 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 › Agricultural and Biological Sciences › Food Science › Salmonella and Campylobacter epidemiology
- Keywords
- caspase-11, caspase-1, Salmonella typhimurium, non-canonical inflammasome, macrophage cell death, pyroptosis, bacterial dissemination, innate immunity, TLR4, TRIF, NOD2, NOD-like receptors, IL-1β, IL-18
- MeSH terms
- Adjuvants, Immunologic, Animals, Cells, Cultured, Disease Susceptibility, Gene Expression Regulation, Interferon-gamma, Lipopolysaccharides, Macrophages, Salmonella Infections, Animal, Salmonella typhimurium, Signal Transduction, Cell Death, Mice, Knockout, Caspases, Mice, Caspases, Initiator, Inflammasomes
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