The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
In the citing paper
“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]
In the citing paper
“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]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
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
Flagged first, then by citations
Cited by
Sorted by citations
Items 201–300 of 539
Sensing the enemy, containing the threat: cell-autonomous immunity toChlamydia trachomatis
Finethy, R., & Coers, J. (2016) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuw027 · Cited by 68
Chen, S., Yang, D., Wen, Y., Jiang, Z., Zhang, L., Jiang, J., Chen, Y., Hu, T., Wang, Q., Zhang, Y., et al. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1007240 · Cited by 67
Bolívar, B. E., Vogel, T. P., & Bouchier‐Hayes, L. (2019) · FEBS Journal · doi:10.1111/febs.14926 · Cited by 68
Gabrielli, E., Pericolini, E., Luciano, E., Sabbatini, S., Roselletti, E., Perito, S., Kasper, L., Hube, B., & Vecchiarelli, A. (2015) · Infection and Immunity · doi:10.1128/iai.02895-14 · Cited by 67
Błażejewski, A. J., Thiemann, S., Schenk, A., Pils, M. C., Gálvez, E. J. C., Roy, U., Heise, U., de Zoete, M. R., Flavell, R. A., & Strowig, T. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.05.058 · Cited by 67
Inner sensors of endotoxin – implications for sepsis research and therapy
Skirecki, T., & Cavaillon, J. (2019) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuz004 · Cited by 64
Caneparo, V., Landolfo, S., Gariglio, M., & Andrea, M. D. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01180 · Cited by 68
The role of pyroptosis and gasdermin family in tumor progression and immune microenvironment
Li, M., Jiang, P., Yang, Y., Xiong, L., Wei, S., Wang, J., & Li, C. (2023) · Experimental Hematology and Oncology · doi:10.1186/s40164-023-00464-5 · Cited by 65
Irgm2 and Gate‐16 cooperatively dampen Gram‐negative bacteria‐induced caspase‐11 response
Eren, E., Planès, R., Bagayoko, S., Bordignon, P., Chaoui, K., Hessel, A., Santoni, K., Pinilla, M., Lagrange, B., Burlet‐Schiltz, O., et al. (2020) · EMBO Reports · doi:10.15252/embr.202050829 · Cited by 62
Perkins, D. J., Rajaiah, R., Tennant, S. M., Ramachandran, G., Higginson, E. E., Dyson, T., & Vogel, S. N. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1500105 · Cited by 65
Bast, A., Krause, K., Schmidt, I. H. E., Pudla, M., Brakopp, S., Hopf, V., Breitbach, K., & Steinmetz, I. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1003986 · Cited by 62
Regulation Where Autophagy Intersects the Inflammasome
Rodgers, M. A., Bowman, J. W., Liang, Q., & Jung, J. U. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5347 · Cited by 62
Cross talk between intracellular pathogens and cell death
Demarco, B., Chen, K. W., & Brož, P. (2020) · Immunological Reviews · doi:10.1111/imr.12892 · Cited by 62
Interaction of Mycobacteria With Host Cell Inflammasomes
Rastogi, S., & Briken, V. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.791136 · Cited by 64
Inflammasomes as polyvalent cell death platforms
de Vasconcelos, N. M., Opdenbosch, N. V., & Lamkanfi, M. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2204-3 · Cited by 65
Holly, M. K., Han, X., Zhao, E. J., Crowley, S. M., Allaire, J. M., Knodler, L. A., Vallance, B. A., & Smith, J. G. (2020) · Infection and Immunity · doi:10.1128/iai.00017-20 · Cited by 60
Ding, P., Yang, M., Wang, N., Jin, L., Dong, Y., Cai, X., & Chen, L. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.01881 · Cited by 61
Rosadini, C. V., Zanoni, I., Odendall, C., Green, E. R., Paczosa, M. K., Philip, N. H., Brodsky, I. E., Mecsas, J. C., & Kagan, J. C. (2015) · Cell Host & Microbe · doi:10.1016/j.chom.2015.11.006 · Cited by 59
Pyroptotic death storms and cytopenia
Croker, B. A., O’Donnell, J. A., & Gerlic, M. (2013) · Current Opinion in Immunology · doi:10.1016/j.coi.2013.12.002 · Cited by 60
The inflammasome: Learning from bacterial evasion strategies
Shin, S., & Brodsky, I. E. (2015) · Seminars in Immunology · doi:10.1016/j.smim.2015.03.006 · Cited by 59
Molecular Mechanisms Used by Salmonella to Evade the Immune System
Bernal-Bayard, J., & Ramos‐Morales, F. (2017) · Current Issues in Molecular Biology · doi:10.21775/cimb.025.133 · Cited by 59
Emerging Insights into Noncanonical Inflammasome Recognition of Microbes
Russo, A. J., Behl, B., Banerjee, I., & Rathinam, V. A. K. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.10.003 · Cited by 57
Kader, M., Alaoui-El-Azher, M., Vorhauer, J., Kode, B. B., Wells, J. Z., Stolz, D. B., Michalopoulos, G. K., Wells, A. H., Scott, M. J., & Ismail, N. (2017) · PLoS Pathogens · doi:10.1371/journal.ppat.1006644 · Cited by 59
Gain-of-function CEBPE mutation causes noncanonical autoinflammatory inflammasomopathy
Göös, H., Fogarty, C. L., Sahu, B., Plagnol, V., Rajamäki, K., Nurmi, K., Liu, X., Einarsdóttir, E., Jouppila, A., Pettersson, T., et al. (2019) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2019.06.003 · Cited by 57
Glutathione peroxidase 8 negatively regulates caspase‐4/11 to protect against colitis
Hsu, J., Chou, J., Chen, T., Su, F., Su, F., Lan, J., Wu, P., Hu, C., Lee, E. Y., & Lee, W. (2019) · EMBO Molecular Medicine · doi:10.15252/emmm.201809386 · Cited by 56
Ma, X., Li, Y., Shen, W., Oladejo, A. O., Yang, J., Wei, J., Imam, B. H., Wu, X., Ding, X., Yang, Y., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.676088 · Cited by 56
Chen, N., Ou, Z.-B., Zhang, W., Zhu, X., Li, P., & Gong, J. (2018) · Cell Proliferation · doi:10.1111/cpr.12487 · Cited by 55
Caspase-11 promotes renal fibrosis by stimulating IL-1β maturation via activating caspase-1
Miao, N., Xie, H., Xu, D., Yin, J., Wang, Y., Bao, W., Yin, F., Zhou, Z., Cheng, Q., Chen, P., et al. (2018) · Acta Pharmacologica Sinica · doi:10.1038/s41401-018-0177-5 · Cited by 55
Robotic System for Physical Training of Older Adults
Avioz-Sarig, O., Olatunji, S., Sarne‐Fleischmann, V., & Edan, Y. (2020) · International Journal of Social Robotics · doi:10.1007/s12369-020-00697-y · Cited by 55
Meyers, A. K., Wang, Z., Han, W., Zhao, Q., Zabalawi, M., Duan, L., Liu, J., Zhang, Q., Manne, R., Lorenzo, F., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2022.111941 · Cited by 56
A Role for the Inflammasome in Spontaneous Labor at Term with Acute Histologic Chorioamnionitis
Gomez‐Lopez, N., Romero, R. J., Xu, Y., Plazyo, O., Unkel, R., Than, N. G., Chaemsaithong, P., Chaiworapongsa, T., Dong, Z., Tarca, A. L., et al. (2016) · Reproductive Sciences · doi:10.1177/1933719116675058 · Cited by 56
Suppression of Inflammasome Activation by IRF8 and IRF4 in cDCs Is Critical for T Cell Priming
McDaniel, M. M., Kottyan, L. C., Singh, H., & Pasare, C. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107604 · Cited by 57
The crosstalk between immune cells and tumor pyroptosis: advancing cancer immunotherapy strategies
Hu, M., Deng, F., Song, X., Zhao, H., & Yan, F. (2024) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-024-03115-7 · Cited by 57
Inflammasome in Intestinal Inflammation and Cancer
Nunes, T., & de Souza, H. S. P. (2013) · Mediators of Inflammation · doi:10.1155/2013/654963 · Cited by 54
Caspase-11 attenuates gastrointestinal inflammation and experimental colitis pathogenesis
Williams, T. M., Leeth, R. A., Rothschild, D. E., McDaniel, D. K., Coutermarsh‐Ott, S. L., Simmons, A., Kable, K. H., Heid, B., & Allen, I. C. (2014) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00234.2014 · Cited by 53
Dikshit, N., Kale, S. D., Khameneh, H. J., Balamuralidhar, V., Tang, C.-Y., Kumar, P., Lim, T.-P., Tan, T. T., Kwa, A. L., Mortellaro, A., et al. (2017) · Mucosal Immunology · doi:10.1038/mi.2017.50 · Cited by 54
Huang, T., Lai, H., Chen, Y.-B., Chen, L.-G., Wu, Y., Ko, Y., Lu, C., Chang, C., Wu, C.-Y., Martel, J., et al. (2013) · Innate Immunity · doi:10.1177/1753425913507096 · Cited by 53
Manipulation of necroptosis by Porphyromonas gingivalis in periodontitis development
Ke, X., Lei, L., Li, H., Li, H., & Yan, F. (2016) · Molecular Immunology · doi:10.1016/j.molimm.2016.07.010 · Cited by 52
Novel perspectives on non-canonical inflammasome activation
Mortellaro, A., Diamond, C. E., Khameneh, H. J., & Brough, D. (2015) · ImmunoTargets and Therapy · doi:10.2147/itt.s57976 · Cited by 54
Macrophage cell death in microbial infections
Chow, S. H., Deo, P., & Naderer, T. (2016) · Cellular Microbiology · doi:10.1111/cmi.12573 · Cited by 55
Caspase-11 Plays an Essential Role in Methamphetamine-Induced Dopaminergic Neuron Apoptosis
Huang, W., Xie, W., Qiao, D., Qiu, P., Huang, E., Li, B., Chen, C., Liu, C., Wang, Q., Lin, Z., et al. (2015) · Toxicological Sciences · doi:10.1093/toxsci/kfv014 · Cited by 51
NLRP3 Inflammasome Participates in Host Response to Neospora caninum Infection
Wang, X., Gong, P., Zhang, X., Li, S., Lu, X.-Y., Zhao, C., Yu, Q., Wei, Z., Yang, Y., Liu, Q., et al. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01791 · Cited by 51
Viewing Legionella pneumophila Pathogenesis through an Immunological Lens
Liu, X., & Shin, S. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.07.028 · Cited by 53
An update on the role of the inflammasomes in the pathogenesis of kidney diseases
Darisipudi, M. N., & Knauf, F. (2015) · Pediatric Nephrology · doi:10.1007/s00467-015-3153-z · Cited by 49
Evasion and interference: intracellular pathogens modulate caspase-dependent inflammatory responses
Stewart, M. K., & Cookson, B. T. (2016) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2016.50 · Cited by 49
Sun, Y., Abbondante, S., Karmakar, M., Carrion, S. D. J., Che, C., Hise, A. G., & Pearlman, E. M. (2018) · The Journal of Immunology · doi:10.4049/jimmunol.1701195 · Cited by 52
Reduction of Streptolysin O (SLO) Pore-Forming Activity Enhances Inflammasome Activation
Keyel, P. A., Roth, R. A., Yokoyama, W. M., Heuser, J. E., & Salter, R. D. (2013) · Toxins · doi:10.3390/toxins5061105 · Cited by 49
Apoptotic caspase-7 activation inhibits non-canonical pyroptosis by GSDMB cleavage
Li, X., Zhang, T. Y., Kang, L., Xin, R., Sun, M., Chen, Q., Pei, J., Chen, Q., Gao, X., & Lin, Z. (2023) · Cell Death and Differentiation · doi:10.1038/s41418-023-01211-3 · Cited by 48
Rift Valley fever virus infection induces activation of the NLRP3 inflammasome
Ermler, M. E., Traylor, Z., Patel, K., Schattgen, S., Vanaja, S. K., Fitzgerald, K. A., & Hise, A. G. (2013) · Virology · doi:10.1016/j.virol.2013.11.015 · Cited by 48
Noncanonical Roles of Caspase-4 and Caspase-5 in Heme-Driven IL-1β Release and Cell Death
Bolívar, B. E., Brown-Suedel, A. N., Rohrman, B. A., Charendoff, C. I., Yazdani, V., Belcher, J. D., Vercellotti, G. M., Flanagan, J. M., & Bouchier‐Hayes, L. (2021) · The Journal of Immunology · doi:10.4049/jimmunol.2000226 · Cited by 48
Kennelly, J. P., Carlin, S., Ju, T., van der Veen, J. N., Nelson, R. C., Buteau, J., Thiesen, A., Richard, C., Willing, B. P., & Jacobs, R. L. (2020) · Cellular and Molecular Gastroenterology and Hepatology · doi:10.1016/j.jcmgh.2020.11.006 · Cited by 46
Scaling of immune responses against intracellular bacterial infection
Abdullah, Z., & Knolle, P. A. (2014) · The EMBO Journal · doi:10.15252/embj.201489055 · Cited by 49
Cell death programs in Yersinia immunity and pathogenesis
Philip, N. H., & Brodsky, I. E. (2012) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2012.00149 · Cited by 45
Zwack, E. E., Feeley, E. M., Burton, A. R., Hu, B., Yamamoto, M., Kanneganti, T., Bliska, J. B., Coers, J., & Brodsky, I. E. (2017) · Infection and Immunity · doi:10.1128/iai.00778-16 · Cited by 48
Malaria, anemia, and invasive bacterial disease: A neutrophil problem?
Mooney, J. P., Galloway, L. J., & Riley, E. M. (2018) · Journal of Leukocyte Biology · doi:10.1002/jlb.3ri1018-400r · Cited by 45
E3 ubiquitin ligase Nedd4 is a key negative regulator for non-canonical inflammasome activation
Liu, Q., Zhang, S., Sun, Z., Guo, X. P., & Zhou, H. M. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0308-7 · Cited by 45
Selkrig, J., Li, N., Hausmann, A., Mangan, M., Zietek, M., Mateus, A., Bobonis, J., Sueki, A., Imamura, H., Debs, B. E., et al. (2020) · Nature Microbiology · doi:10.1038/s41564-020-0736-7 · Cited by 46
IL-1α and IL-1β-producing macrophages populate lung tumor lesions in mice
Terlizzi, M., Colarusso, C., Popolo, A., Pinto, A., & Sorrentino, R. (2016) · Oncotarget · doi:10.18632/oncotarget.11276 · Cited by 45
Salmonella Bloodstream Infections
Worley, M. J. (2023) · Tropical Medicine and Infectious Disease · doi:10.3390/tropicalmed8110487 · Cited by 44
Wacker, M. A., Teghanemt, A., Weiss, J. P., & Barker, J. H. (2017) · Innate Immunity · doi:10.1177/1753425917695446 · Cited by 47
Host inflammasome defense mechanisms and bacterial pathogen evasion strategies
Brewer, S. M., Brubaker, S. W., & Monack, D. M. (2019) · Current Opinion in Immunology · doi:10.1016/j.coi.2019.05.001 · Cited by 44
Self-citationEvolution-inspired redesign of the LPS receptor caspase-4 into an interleukin-1β–converting enzyme
Devant, P., Cao, A., & Kagan, J. C. (2021) · Science Immunology · doi:10.1126/sciimmunol.abh3567 · Cited by 45
Innate Immune Detection of Flagellin Positively and Negatively Regulates Salmonella Infection
Lai, M. A., Quarles, E. K., López-Yglesias, A. H., Zhao, X., Hajjar, A. M., & Smith, K. D. (2013) · PLoS ONE · doi:10.1371/journal.pone.0072047 · Cited by 46
Interactions between Nod-Like Receptors and Intestinal Bacteria
de Zoete, M. R., & Flavell, R. A. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2013.00462 · Cited by 43
Salmonella-induced inflammasome activation in humans
Bierschenk, D., Boucher, D., & Schroder, K. (2016) · Molecular Immunology · doi:10.1016/j.molimm.2016.11.009 · Cited by 43
Inflammasome activation by Salmonella
Bryant, C. E. (2021) · Current Opinion in Microbiology · doi:10.1016/j.mib.2021.09.004 · Cited by 44
Reconciling Mouse and Human Immunology at the Altar of Genetics
Gros, P., & Casanova, J. (2022) · Annual Review of Immunology · doi:10.1146/annurev-immunol-101721-065201 · Cited by 44
The role of the inflammasome in cardiovascular diseases
Li, X., Deroide, N., & Mallat, Z. (2014) · Journal of Molecular Medicine · doi:10.1007/s00109-014-1144-3 · Cited by 43
Tonnus, W., Gembardt, F., Latk, M., Parmentier, S. P., Hugo, C., Bornstein, S. R., & Linkermann, A. (2018) · Cell Death and Differentiation · doi:10.1038/s41418-018-0193-5 · Cited by 44
Huang, T., Chong, K., Ojcius, D. M., Wu, Y., Ko, Y., Wu, C.-Y., Martel, J., Lu, C., Lai, H., & Young, J. D. (2013) · Scientific Reports · doi:10.1038/srep01374 · Cited by 42
Recognition of Intracellular Bacteria by Inflammasomes
Brož, P. (2019) · Microbiology Spectrum · doi:10.1128/microbiolspec.bai-0003-2019 · Cited by 41
IRF-7 Mediates Type I IFN Responses in Endotoxin-Challenged Mice
Sin, W., Yeong, J. P.-S., Lim, T. J. F., Su, I.-H., Connolly, J. E., & Chin, K.-C. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00640 · Cited by 43
Programmed Cell Death in the Evolutionary Race against Bacterial Virulence FactorsPreprint
Lacey, C. A., & Miao, E. A. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a036459 · Cited by 43
Salmonella and the Inflammasome: Battle for Intracellular Dominance
Crowley, S. M., Knodler, L. A., & Vallance, B. A. (2016) · Current topics in microbiology and immunology · doi:10.1007/978-3-319-41171-2_3 · Cited by 43
Bacterial secretion systems and regulation of inflammasome activation
Ratner, D., Ørning, P., & Lien, E. (2016) · Journal of Leukocyte Biology · doi:10.1189/jlb.4mr0716-330r · Cited by 41
Getting “Inside” Type I IFNs: Type I IFNs in Intracellular Bacterial Infections
Snyder, D. T., Hedges, J. F., & Jutila, M. A. (2017) · Journal of Immunology Research · doi:10.1155/2017/9361802 · Cited by 43
Regulatory roles of ginseng on inflammatory caspases, executioners of inflammasome activation
Yun, M., & Yi, Y. (2019) · Journal of Ginseng Research · doi:10.1016/j.jgr.2019.12.006 · Cited by 40
Inflammasomes in dendritic cells: Friend or foe?
Hatscher, L., Amon, L., Heger, L., & Dudziak, D. (2021) · Immunology Letters · doi:10.1016/j.imlet.2021.04.002 · Cited by 40
Cai, Q., Sun, Z., Xu, S., Jiao, X., Guo, S., Li, Y., Wu, H. G., & Yu, X. (2022) · Renal Failure · doi:10.1080/0886022x.2022.2098764 · Cited by 41
Ratner, D., Ørning, P., Starheim, K. K., Marty-Roix, R., Proulx, M. K., Goguen, J. D., & Lien, E. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.697698 · Cited by 40
Sivick, K. E., Arpaia, N., Reiner, G. L., Lee, B. L., Russell, B. R., & Barton, G. M. (2014) · Cell Host & Microbe · doi:10.1016/j.chom.2014.01.013 · Cited by 40
Jakka, P., Namani, S., Murugan, S., Rai, N., & Radhakrishnan, G. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.815878 · Cited by 39
The interplay between regulated necrosis and bacterial infection
Blériot, C., & Lecuit, M. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2206-1 · Cited by 39
The Role of the Host in Driving Phenotypic Heterogeneity in Salmonella
Tsai, C. N., & Coombes, B. K. (2019) · Trends in Microbiology · doi:10.1016/j.tim.2019.01.004 · Cited by 39
Chen, S., Jin, P., Chen, H., Wu, D., Li, S., Zhang, Y., Liu, Q., & Yang, D. (2021) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2021.104078 · Cited by 39
Yang, Q., Stevenson, H. L., Scott, M. J., & Ismail, N. (2014) · American Journal Of Pathology · doi:10.1016/j.ajpath.2014.10.005 · Cited by 37
An updated view on the structure and function of PYRIN domains
Chu, L. H., Gangopadhyay, A., Dorfleutner, A., & Stehlik, C. (2014) · APOPTOSIS · doi:10.1007/s10495-014-1065-1 · Cited by 38
Interferon-Tau Attenuates Uptake of Nanoparticles and Secretion of Interleukin-1β in Macrophages
Hara, K., Shirasuna, K., Usui, F., Karasawa, T., Mizushina, Y., Kimura, H. J., Kawashima, A., Ohkuchi, A., Matsuyama, S., Kimura, K., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0113974 · Cited by 36
Cirtical role for Salmonella effector SopB in regulating inflammasome activation
Hu, G., Song, P., Chen, W., Qi, S., Yu, S.-X., Du, C., Deng, X., Ouyang, H., & Yang, Y. (2017) · Molecular Immunology · doi:10.1016/j.molimm.2017.07.011 · Cited by 37
Development of an Ex Vivo Tissue Platform To Study the Human Lung Response to Coxiella burnetii
Graham, J. G., Winchell, C. G., Kurten, R. C., & Voth, D. E. (2016) · Infection and Immunity · doi:10.1128/iai.00012-16 · Cited by 35
Inflammasomes and the microbiota–partners in the preservation of mucosal homeostasis
Levy, M., Thaiss, C. A., Katz, M. N., Suez, J., & Elinav, E. (2015) · Seminars in Immunopathology · doi:10.1007/s00281-014-0451-7 · Cited by 34
Pandeya, A., Zhang, Y., Cui, J., Yang, L., Li, J., Zhang, G., Wu, C., Li, Z., & Wei, Y. (2023) · Microbiological Research · doi:10.1016/j.micres.2023.127460 · Cited by 34
Role of toll-like receptor-mediated pyroptosis in sepsis-induced cardiomyopathy
Fan, Y., Guan, B., Xu, J., Zhang, H., Liang, Y., & Yang, Z. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115493 · Cited by 35
Casson, C. N., & Shin, S. (2013) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2013.00111 · Cited by 34
Caspases as the Key Effectors of Inflammatory Responses Against Bacterial Infection
Uchiyama, R., & Tsutsui, H. (2014) · Archivum Immunologiae et Therapiae Experimentalis · doi:10.1007/s00005-014-0301-2 · Cited by 34
Manipulation of the host cell death pathway byShigella
Ashida, H., Kim, M., & Sasakawa, C. (2014) · Cellular Microbiology · doi:10.1111/cmi.12367 · Cited by 38
Ning, W., Acharya, A., Li, S., Schmalz, G., & Huang, S. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.862049 · Cited by 33
Induction of pyroptotic cell death as a potential tool for cancer treatment
Faria, S. S., Fernando, A. J., de Lima, V. C. C., Rossi, A. G., de Carvalho, J. M. A., & Magalhães, K. G. (2022) · Journal of Inflammation · doi:10.1186/s12950-022-00316-9 · Cited by 33
Antimicrobial inflammasomes: unified signalling against diverse bacterial pathogens
Eldridge, M. J. G., & Shenoy, A. R. (2014) · Current Opinion in Microbiology · doi:10.1016/j.mib.2014.10.008 · Cited by 33
Bradley, W. P., Boyer, M. A., Nguyen, H. T., Birdwell, L. D., Yu, J. M., Ribeiro, J. M., Weiss, S. R., Zamboni, D. S., Roy, C. R., & Shin, S. (2016) · Infection and Immunity · doi:10.1128/iai.01536-15 · Cited by 33
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
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