The DOI matches its Crossref record; 54 of the 54 references it cites were found in a registry or an index.
Differential Requirement of P2X7 Receptor and Intracellular K+ for Caspase-1 Activation Induced by Intracellular and Extracellular Bacteria
Open accessAbstract
Interleukin-1beta (IL-1beta) is a pro-inflammatory cytokine that plays an important role in host defense and inflammatory diseases. The maturation and secretion of IL-1beta are mediated by caspase-1, a protease that processes pro-IL-1beta into biologically active IL-1beta. The activity of caspase-1 is controlled by the inflammasome, a multiprotein complex formed by NLR proteins and the adaptor ASC, that induces the activation of caspase-1. The current model proposes that changes in the intracellular concentration of K(+) potentiate caspase-1 activation induced by the recognition of bacterial products. However, the roles of P2X7 receptor and intracellular K(+) in IL-1beta secretion induced by bacterial infection remain unknown. Here we show that, in response to Toll-like receptor agonists such as lipopolysaccharide or infection with extracellular bacteria Staphylococcus aureus and Escherichia coli, efficient caspase-1 activation is only triggered by addition of ATP, a signal that promotes caspase-1 activation through depletion of intracellular K(+) caused by stimulation of the purinergic P2X7 receptor. In contrast, activation of caspase-1 that relies on cytosolic sensing of flagellin or intracellular bacteria did not require ATP stimulation or depletion of cytoplasmic K(+). Consistently, caspase-1 activation induced by intracellular Salmonella or Listeria was unimpaired in macrophages deficient in P2X7 receptor. These results indicate that, unlike caspase-1 induced by Toll-like receptor agonists and ATP, activation of the inflammasome by intracellular bacteria and cytosolic flagellin proceeds normally in the absence of P2X7 receptor-mediated cytoplasmic K(+) perturbations.
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
“In favour of the latter assumption is the recent finding that potassium (K + ) efflux, lowering intracellular K + levels, is a requirement for Nalp3 inflammasome activation triggered by all known activators including MSU (13)(14)(15).”
From Innate Immune Activation Through Nalp3 Inflammasome Sensing of Asbestos and Silica (2008) · cites this paper as [14]
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
Martinon, F., Burns, K., & Tschopp, J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00599-3 · Cited by 6,066
Cryopyrin activates the inflammasome in response to toxins and ATP
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. (2006) · Nature · doi:10.1038/nature04515 · Cited by 3,080
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
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 1,822
The Cytolytic P 2Z Receptor for Extracellular ATP Identified as a P 2X Receptor (P2X 7 )
Surprenant, A., Rassendren, F., Kawashima, E., North, R. A., & Buell, G. (1996) · Science · doi:10.1126/science.272.5262.735 · Cited by 1,739
Altered 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
Pannexin‐1 mediates large pore formation and interleukin‐1β release by the ATP‐gated P2X7 receptor
Pelegrı́n, P., & Surprenant, A. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601378 · Cited by 1,490
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
Nod1 responds to peptidoglycan delivered by the Helicobacter pylori cag pathogenicity island
Viala, J., Chaput, C., Boneca, I. G., Cardona, A., Girardin, S. E., Moran, A. P., Athman, R., Mémet, S., Huerre, M., Coyle, A. J., et al. (2004) · Nature Immunology · doi:10.1038/ni1131 · Cited by 1,221
Bacterial RNA and small antiviral compounds activate caspase-1 through cryopyrin/Nalp3
Kanneganti, T., Özören, N., Body–Malapel, M., Amer, A. O., Park, J., Franchi, L., Whitfield, J. R., Barchet, W., Colonna, M., Vandenabeele, P., et al. (2006) · Nature · doi:10.1038/nature04517 · Cited by 1,149
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Items 101–200 of 356
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
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
NLRP3 Inflammasome: Checkpoint Connecting Innate and Adaptive Immunity in Autoimmune Diseases
Zhang, Y., Yang, W., Li, W., & Zhao, Y. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.732933 · Cited by 142
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
Qu, Y., & Dubyak, G. (2009) · Purinergic Signalling · doi:10.1007/s11302-009-9132-8 · Cited by 130
Self-citationModulation of three key innate immune pathways for the most common retinal degenerative diseases
Akhtar‐Schäfer, I., Wang, L., Krohne, T. U., Xu, H., & Langmann, T. (2018) · EMBO Molecular Medicine · doi:10.15252/emmm.201708259 · Cited by 129
Cheng, W., Shivshankar, P., Li, Z., Chen, L., Yeh, I., & Zhong, G. (2007) · Infection and Immunity · doi:10.1128/iai.01064-07 · Cited by 128
The NLRP3 inflammasome renders cell death pro-inflammatory
Gaidt, M. M., & Hornung, V. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.11.013 · Cited by 124
Sun, B., Pokhrel, S., Dunphy, D. R., Zhang, H., Ji, Z., Wang, X., Wang, M., Liao, Y., Chang, C. H., Dong, J. I., et al. (2015) · ACS Nano · doi:10.1021/acsnano.5b03443 · Cited by 124
Sater, A. A. A., Koo, E., Häcker, G. A., & Ojcius, D. M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.026823 · Cited by 122
Palová-Jelínková, L., Dáňová, K., Drašarová, H., Dvořák, M., Funda, D. P., Fundová, P., Kotrbová-Kozak, A., Černá, M., Kamanová, J., Martin, S. F., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0062426 · Cited by 117
Inflammasome-mediated GSDMD activation facilitates escape of Candida albicans from macrophages
Ding, X., Kambara, H., Guo, R., Kanneganti, A., Acosta-Zaldívar, M., Li, J., Liu, F., Bei, T., Qi, W., Xie, X., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-27034-9 · Cited by 115
Kaminski, J. J., Schattgen, S. A., Tzeng, T.-C., Bode, C., Klinman, D. M., & Fitzgerald, K. A. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1300530 · Cited by 112
Tsuchiya, K., Hara, H., Kawamura, I., Nomura, T., Yamamoto, T., Daim, S. J., Dewamitta, S. R., Shen, Y., Fang, R., & Mitsuyama, M. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1001058 · Cited by 113
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
ENTPD-1 disrupts inflammasome IL-1β–driven venous thrombosis
Yadav, V., Chi, L., Zhao, R., Tourdot, B. E., Yalavarthi, S., Jacobs, B. N., Banka, A. L., Liao, H., Koonse, S., Anyanwu, A. C., et al. (2019) · Journal of Clinical Investigation · doi:10.1172/jci124804 · Cited by 109
Hamon, M. A., & Cossart, P. (2011) · Infection and Immunity · doi:10.1128/iai.01243-10 · Cited by 105
Nakamura, Y., Franchi, L., Kambe, N., Meng, G., Strober, W., & Núñez, G. (2012) · Immunity · doi:10.1016/j.immuni.2012.04.013 · Cited by 107
Self-citationInnate Defense against Fungal PathogensPreprint
Drummond, R. A., Gaffen, S. L., Hise, A. G., & Brown, G. D. (2014) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a019620 · Cited by 102
Increasing complexity of NLRP3 inflammasome regulation
Moretti, J., & Blander, J. M. (2020) · Journal of Leukocyte Biology · doi:10.1002/jlb.3mr0520-104rr · Cited by 107
Choi, C. H., Spooner, R., DeGuzman, J., Koutouzis, T., Ojcius, D. M., & Yilmaz, Ö. (2012) · Cellular Microbiology · doi:10.1111/cmi.12089 · Cited by 104
The Role of Potassium in Inflammasome Activation by Bacteria
Arlehamn, C. S. L., Pétrilli, V., Groß, O., Tschopp, J., & Evans, T. J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.067298 · Cited by 101
Winter, S., Thiennimitr, P., Nuccio, S., Haneda, T., Winter, M. G., Wilson, R. P., Russell, J. M., Henry, T., Tran, Q. T., Lawhon, S. D., et al. (2009) · Infection and Immunity · doi:10.1128/iai.01341-08 · Cited by 101
BAX/BAK-Induced Apoptosis Results in Caspase-8-Dependent IL-1β Maturation in Macrophages
Chauhan, D., Bartok, E., Gaidt, M. M., Bock, F. J., Herrmann, J. E., Seeger, J. M., Brož, P., Beckmann, R., Kashkar, H., Tait, S. W. G., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.10.087 · Cited by 103
Rae, C. S., Geissler, A. L., Adamson, P. C., & Portnoy, D. A. (2011) · Infection and Immunity · doi:10.1128/iai.00077-11 · Cited by 98
Ozkurede, U., & Franchi, L. (2011) · Clinical & Experimental Immunology · doi:10.1111/j.1365-2249.2011.04535.x · Cited by 94
Self-citationZheng, Y., Lilo, S., Brodsky, I. E., Zhang, Y., Medzhitov, R. M., Marcu, K. B., & Bliska, J. B. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002026 · Cited by 90
The Inflammasome Mediates Hyperoxia-Induced Alveolar Cell Permeability
Kolliputi, N., Shaik, R. S., & Waxman, A. B. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0902766 · Cited by 93
Activation of inflammasomes in adipose tissue of women with gestational diabetes
Lappas, M. (2013) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2013.09.011 · Cited by 96
Sater, A. A. A., Sadier, N. S., Padilla, E. V., & Ojcius, D. M. (2010) · Microbes and Infection · doi:10.1016/j.micinf.2010.04.008 · Cited by 88
Witte, C. E., Archer, K. A., Rae, C. S., Sauer, J., Woodward, J. J., & Portnoy, D. A. (2012) · Advances in immunology · doi:10.1016/b978-0-12-394590-7.00002-6 · Cited by 90
Ion channels in regulated cell death
Kunzelmann, K. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2208-z · Cited by 93
Wang, H., Lv, C., Wang, S., Ying, H., Weng, Y., & Yu, W. (2018) · Inflammation · doi:10.1007/s10753-018-0780-0 · Cited by 91
Pirzada, R. H., Javaid, N., & Choi, S. (2020) · Genes · doi:10.3390/genes11020131 · Cited by 84
Tkaczyk, C., Hamilton, M. M., Datta, V., Yang, X. P., Hilliard, J. J., Stephens, G. L., Sadowska, A., Hua, L., O’Day, T. L., Suzich, J., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0075103 · Cited by 82
Desirable cell death during anticancer chemotherapy
Locher, C., Conforti, R., Aymeric, L., Ma, Y., Yamazaki, T., Rusakiewicz, S., Tesnière, A., Ghiringhelli, F., Apétoh, L., Morel, Y., et al. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05763.x · Cited by 84
Shridas, P., de Beer, M. C., & Webb, N. R. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.002428 · Cited by 84
Inflammasome and cytokine blocking strategies in autoinflammatory disorders
Moll, M., & Kuemmerle-Deschner, J. B. (2013) · Clinical Immunology · doi:10.1016/j.clim.2013.04.008 · Cited by 85
Naseer, N., Egan, M. S., Ruiz, V. M. R., Scott, W. P., Hunter, E. N., Demissie, T., Rauch, I., Brodsky, I. E., & Shin, S. (2022) · PLoS Pathogens · doi:10.1371/journal.ppat.1009718 · Cited by 86
Inflammasomes and Their Activation
Khare, S., Luc, N., Dorfleutner, A., & Stehlik, C. (2010) · Critical Reviews in Immunology · doi:10.1615/critrevimmunol.v30.i5.50 · Cited by 77
Reber, L. L., Marichal, T., Sokolove, J. B., Starkl, P. M., Gaudenzio, N., Iwakura, Y., Karasuyama, H., Schwartz, L. B., Robinson, W. H., Tsai, M. M., et al. (2014) · Arthritis & Rheumatology · doi:10.1002/art.38747 · Cited by 80
Toll like receptor-5: protecting the gut from enteric microbes
Vijay–Kumar, M., Aitken, J. D., & Gewirtz, A. T. (2007) · Seminars in Immunopathology · doi:10.1007/s00281-007-0100-5 · Cited by 75
The rhapsody of NLRPs: master players of inflammation … and a lot more
Zambetti, L. P., Laudisi, F., Licandro, G., Ricciardi‐Castagnoli, P., & Mortellaro, A. (2012) · Immunologic Research · doi:10.1007/s12026-012-8272-z · Cited by 75
Inflammasomes in the pathophysiology of autoinflammatory syndromes
Tartey, S., & Kanneganti, T. (2019) · Journal of Leukocyte Biology · doi:10.1002/jlb.3mir0919-191r · Cited by 77
Self-citationDifferential role of the NLRP 3 inflammasome in infection and tumorigenesis
Tartey, S., & Kanneganti, T. (2019) · Immunology · doi:10.1111/imm.13046 · Cited by 74
Self-citationInterplay between redox status and inflammasome activation
Rubartelli, A., Gattorno, M., Netea, M. G., & Dinarello, C. A. (2011) · Trends in Immunology · doi:10.1016/j.it.2011.08.005 · Cited by 73
Wang, X., Sun, B., Liu, S., & Xia, T. (2016) · NanoImpact · doi:10.1016/j.impact.2016.08.002 · Cited by 72
Role of Inflammasomes in Intestinal Inflammation and Crohnʼs Disease
Opipari, A. W., & Franchi, L. (2014) · Inflammatory Bowel Diseases · doi:10.1097/mib.0000000000000230 · Cited by 75
Self-citationStaphylococcus aureus Activates the NLRP3 Inflammasome in Human and Rat Conjunctival Goblet Cells
McGilligan, V., Gregory-Ksander, M. S., Li, D., Moore, J. E., Hodges, R. R., Gilmore, M. S., Moore, T., & Dartt, D. A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0074010 · Cited by 72
Cole, J., Aberdein, J., Jubrail, J., & Dockrell, D. H. (2014) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/bs.ampbs.2014.08.004 · Cited by 71
NOD-Like Receptors in Lung Diseases
Chaput, C., Sander, L. E., Suttorp, N., & Opitz, B. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2013.00393 · Cited by 75
Nod-Like Receptors: Cytosolic Watchdogs for Immunity against Pathogens
Sirard, J., Vignal, C., Dessein, R., & Chamaillard, M. (2007) · PLoS Pathogens · doi:10.1371/journal.ppat.0030152 · Cited by 72
NLRP3 Inflammasome Activation Is Essential for Paraquat-Induced Acute Lung Injury
Liu, Z., Zhao, H., Liu, W., Li, T., Wang, Y., & Zhao, M. (2014) · Inflammation · doi:10.1007/s10753-014-0048-2 · Cited by 66
Naseer, N., Zhang, J., Bauer, R., Constant, D. A., Nice, T. J., Brodsky, I. E., Rauch, I., & Shin, S. (2022) · Infection and Immunity · doi:10.1128/iai.00663-21 · Cited by 67
Ruwona, T. B., Xu, H., Li, X., Taylor, A. N., Shi, Y.-C., & Cui, Z. (2016) · Vaccine · doi:10.1016/j.vaccine.2016.04.081 · Cited by 64
Activation and Inhibition of the NLRP3 Inflammasome by RNA Viruses
Choudhury, S. M., Ma, X., Abdullah, S. W., & Zheng, H. (2021) · Journal of Inflammation Research · doi:10.2147/jir.s295706 · Cited by 66
Trendelenburg, G. (2008) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/sj.jcbfm.9600609 · Cited by 64
Loria, J. R. D., Rohmann, K., Droemann, D., Kujath, P., Rupp, J., Goldmann, T., & Dalhoff, K. (2013) · PLoS ONE · doi:10.1371/journal.pone.0066818 · Cited by 63
The Dual Role of Nod-Like Receptors in Mucosal Innate Immunity and Chronic Intestinal Inflammation
Corridoni, D., Arseneau, K. O., Cifone, M. G., & Cominelli, F. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00317 · Cited by 66
Morimoto, N., Kono, T., Sakai, M., & Hikima, J.-I. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094389 · Cited by 62
Patankar, Y. R., Lovewell, R. R., Poynter, M. E., Jyot, J., Kazmierczak, B. I., & Berwin, B. L. (2013) · Infection and Immunity · doi:10.1128/iai.00054-13 · Cited by 65
Kurenuma, T., Kawamura, I., Hara, H., Uchiyama, R., Daim, S. J., Dewamitta, S. R., Sakai, S., Tsuchiya, K., Nomura, T., & Mitsuyama, M. (2009) · Infection and Immunity · doi:10.1128/iai.00015-09 · Cited by 62
Shamaa, O. R., Mitra, S., Gavrilin, M. A., & Wewers, M. D. (2015) · PLoS ONE · doi:10.1371/journal.pone.0142203 · Cited by 62
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
Skeldon, A. M., & Saleh, M. (2011) · Frontiers in Microbiology · doi:10.3389/fmicb.2011.00015 · Cited by 62
Cytoadherence‐dependent induction of inflammatory responses by Mycoplasma pneumoniae
Shimizu, T., Kida, Y., & Kuwano, K. (2011) · Immunology · doi:10.1111/j.1365-2567.2011.03408.x · Cited by 57
P2X7R: A potential key regulator of acute gouty arthritis
Tao, J., Zhang, Y., & Li, X.-P. (2013) · Seminars in Arthritis and Rheumatism · doi:10.1016/j.semarthrit.2013.04.007 · Cited by 55
Sensing intracellular pathogens—NOD-like receptors
Rietdijk, S. T., Burwell, T., Bertin, J., & COYLE, A. (2008) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2008.04.003 · Cited by 58
Heiss, K., Jänner, N., Mähnß, B., Schumacher, V., Koch-Nolte, F., Haag, F., & Mittrücker, H. (2008) · Journal of Immunology · doi:10.4049/jimmunol.181.6.3861 · Cited by 58
Silica-induced inflammasome activation in macrophages: role of ATP and P2X7 receptor
Luna-Gomes, T., Santana, P. T., & Coutinho‐Silva, R. (2015) · Immunobiology · doi:10.1016/j.imbio.2015.05.004 · Cited by 54
Hara, H., Tsuchiya, K., Nomura, T., Kawamura, I., Shoma, S., & Mitsuyama, M. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.12.7859 · Cited by 54
Human and mouse NAIP/NLRC4 inflammasome responses to bacterial infection
Egan, M. S., Zhang, J., & Shin, S. (2023) · Current Opinion in Microbiology · doi:10.1016/j.mib.2023.102298 · Cited by 55
Immune and Inflammatory Reponses to Staphylococcus aureus Skin Infections
Liu, Q., Mazhar, M., & Miller, L. S. (2018) · Current Dermatology Reports · doi:10.1007/s13671-018-0235-8 · Cited by 58
Innate Immune Recognition and Inflammasome Activation in Listeria Monocytogenes Infection
Eitel, J., Suttorp, N., & Opitz, B. (2011) · Frontiers in Microbiology · doi:10.3389/fmicb.2010.00149 · Cited by 51
Mechanisms of NLRP3 inflammasome activation and the development of peptide inhibitors
Tao, Y., Tao, W., Chen, X.-Y., Jiang, C., Di, B., & Xu, L. (2023) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2023.09.007 · Cited by 55
A clear and present danger: inflammasomes DAMPing down disorders of pregnancy
Khan, R. N., & Hay, D. P. (2014) · Human Reproduction Update · doi:10.1093/humupd/dmu059 · Cited by 49
Cooper, Z. A., Ghosh, A., Gupta, A., Maity, T. K., Benjamin, I. J., Vogel, S. N., Hasday, J. D., & Singh, I. S. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00346.2009 · Cited by 50
Pathways of IL-1β secretion by macrophages infected with clinical Mycobacterium tuberculosis strains
Krishnan, N., Robertson, B. D., & Thwaites, G. E. (2013) · Tuberculosis · doi:10.1016/j.tube.2013.05.002 · Cited by 50
Deplano, S., Cook, H. T., Russell, R. F., Franchi, L., Schneiter, S., Bhangal, G., Unwin, R. J., Pusey, C. D., Tam, F. W. K., & Behmoaras, J. V. (2012) · Journal of Leukocyte Biology · doi:10.1189/jlb.0612284 · Cited by 52
Self-citationIntracellular pattern-recognition receptors☆
Dostert, C., Meylan, E., & Tschopp, J. (2008) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2007.12.003 · Cited by 50
Role of Connexin/Pannexin containing channels in infectious diseases
Eugenín, E. A. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.01.030 · Cited by 48
Ion flux in the lung: virus-induced inflammasome activation
Triantafilou, K., & Triantafilou, M. (2014) · Trends in Microbiology · doi:10.1016/j.tim.2014.06.002 · Cited by 47
Swartz, T. H., Esposito, A. M., Durham, N. D., Hartmann, B., & Chen, B. K. (2014) · Journal of Virology · doi:10.1128/jvi.01158-14 · Cited by 48
NLRP3 Inflammasome and Its Critical Role in Gynecological Disorders and Obstetrical Complications
Fang, X., Wang, Y., Zhang, Y. L., Li, Y., Kwak-Kim, J. Y.-H., & Wu, L. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2020.555826 · Cited by 46
Voronova, V., Vislobokova, A., Mutig, K., Samsonov, M., Peskov, K. V., Sekacheva, M. I., Materenchuk, M. Y., Bunyatyan, N. D., & Lebedeva, S. A. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.1035884 · Cited by 47
Inflammasomes bridge signaling between pathogen identification and the immune response.
Sater, A. A. A., Sadier, N. S., Ojcius, D. M., Yilmaz, Ö., & Kelly, K. A. (2009) · PubMed · Cited by 44
Shibata, K. (2018) · Molecular Oral Microbiology · doi:10.1111/omi.12217 · Cited by 38
The zebrafish: A research model to understand the evolution of vertebrate immunity
García‐Moreno, D., Tyrkalska, S. D., Valera, A., Gómez‐Abenza, E., Pérez‐Oliva, A. B., & Mulero, V. (2019) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2019.04.067 · Cited by 47
ATP-induced apoptosis involves a Ca2+-independent phospholipase A2 and 5-lipoxygenase in macrophages
Costa‐Junior, H. M., Mendes, A. N., Davis, G. H. N. G., da Cruz, C. M., Ventura, A. L. M., Serezani, C. H., Faccioli, L. H., Nomizo, A., Freire-de-Lima, C. G., Bisaggio, R. D. C., et al. (2008) · Prostaglandins & Other Lipid Mediators · doi:10.1016/j.prostaglandins.2008.09.004 · Cited by 42
Toll-Like Receptors in Bacterial Meningitis
Koedel, U. (2009) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-00549-7_2 · Cited by 43
Jamilloux, Y., & Henry, T. (2013) · médecine/sciences · doi:10.1051/medsci/20132911013 · Cited by 42
Research Progress of Metabolomics in Asthma
Wang, C., Jiang, S., Zhang, S., Ouyang, Z., Wang, G., & Wang, F. (2021) · Metabolites · doi:10.3390/metabo11090567 · Cited by 42
Huang, L. S., Anas, M., Xu, J., Zhou, B., Tóth, P. T., Krishnan, Y., Di, A., & Malik, A. B. (2023) · eLife · doi:10.7554/elife.83842 · Cited by 41
Huang, T., Ojcius, D. M., Young, J. D., Wu, Y., Ko, Y., Wong, T.-Y., Wu, C.-Y., Lu, C., & Lai, H. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041383 · Cited by 40
IL-27 enhances LPS-induced IL-1β in human monocytes and murine macrophages
Petes, C., Wynick, C., Guzzo, C., Mehta, D., Logan, S., Banfield, B. W., Basta, S., Cooper, A. M., & Gee, K. (2017) · Journal of Leukocyte Biology · doi:10.1189/jlb.3a0316-098r · Cited by 41
ATP as a Pathophysiologic Mediator of Bacteria-Host Crosstalk in the Gastrointestinal Tract
Inami, A., Kiyono, H., & Kurashima, Y. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19082371 · Cited by 40
Autophagy and the Immune Response to TB
Harris, J., Hope, J. C., & Lavelle, E. C. (2009) · Transboundary and Emerging Diseases · doi:10.1111/j.1865-1682.2009.01069.x · Cited by 38
Soare, A. Y., Durham, N. D., Gopal, R., Tweel, B. C., Hoffman, K. W., Brown, J. A., O’Brien, M., Bhardwaj, N., Lim, J. K., Chen, B. K., et al. (2018) · Journal of Virology · doi:10.1128/jvi.01186-18 · Cited by 36
Lappas, M. (2013) · American Journal of Reproductive Immunology · doi:10.1111/aji.12174 · Cited by 37
Metadata
- Authors
- Franchi, L., Kanneganti, T.-D., Dubyak, G. R., & Núñez, G.
- Affiliations
- University of Michigan (US)
- Case Western Reserve University (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2007-06
- Volume
- 282
- Issue
- 26
- Pages
- 18810-18818
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2012576192
- Cited by
- 356
- References
- 54
- Citations by year
- 2026: 6 · 2025: 10 · 2024: 7 · 2023: 20 · 2022: 12 · 2021: 15 · 2020: 9 · 2019: 8 · 2018: 16 · 2017: 9 · 2016: 16 · 2015: 23 · 2014: 28 · 2013: 29 · 2012: 23
- FWCI
- 12.46
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Arthritis Foundation
- Pfizer
- National Institutes of Health (AI063331)
- Takeda Oncology
- National Institute of General Medical Sciences (GM-36387, R01GM036387)
- National Institute of Allergy and Infectious Diseases (AI 064748, AI063331, R01AI064748)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (AR 051790)
- 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 › Biochemistry, Genetics and Molecular Biology › Physiology › Adenosine and Purinergic Signaling
- Keywords
- P2X7 receptor, intracellular potassium, caspase-1 activation, inflammasome, interleukin-1β secretion, ATP, TLR agonists, lipopolysaccharide, Staphylococcus aureus, Escherichia coli, flagellin, intracellular bacteria, Salmonella, Listeria, macrophages, purinergic signaling
- MeSH terms
- Adenosine Triphosphate, Animals, Bacterial Infections, Calcium-Binding Proteins, Cytosol, Escherichia coli Infections, Extracellular Space, Flagellin, Lipopolysaccharides, Listeriosis, Macrophages, Mice, Mutant Strains, Potassium, Salmonella Infections, Salmonella typhimurium, Staphylococcal Infections, Staphylococcus aureus, Receptors, Purinergic P2, Caspase 1, Apoptosis Regulatory Proteins, Mice, Receptors, Purinergic P2X7
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