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Inflammatory caspases are innate immune receptors for intracellular LPS
Abstract
The murine caspase-11 non-canonical inflammasome responds to various bacterial infections. Caspase-11 activation-induced pyroptosis, in response to cytoplasmic lipopolysaccharide (LPS), is critical for endotoxic shock in mice. The mechanism underlying cytosolic LPS sensing and the responsible pattern recognition receptor are unknown. Here we show that human monocytes, epithelial cells and keratinocytes undergo necrosis upon cytoplasmic delivery of LPS. LPS-induced cytotoxicity was mediated by human caspase-4 that could functionally complement murine caspase-11. Human caspase-4 and the mouse homologue caspase-11 (hereafter referred to as caspase-4/11) and also human caspase-5, directly bound to LPS and lipid A with high specificity and affinity. LPS associated with endogenous caspase-11 in pyroptotic cells. Insect-cell purified caspase-4/11 underwent oligomerization upon LPS binding, resulting in activation of the caspases. Underacylated lipid IVa and lipopolysaccharide from Rhodobacter sphaeroides (LPS-RS) could bind to caspase-4/11 but failed to induce their oligomerization and activation. LPS binding was mediated by the CARD domain of the caspase. Binding-deficient CARD-domain point mutants did not respond to LPS with oligomerization or activation and failed to induce pyroptosis upon LPS electroporation or bacterial infections. The function of caspase-4/5/11 represents a new mode of pattern recognition in immunity and also an unprecedented means of caspase activation.
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In the citing paper
“Further experimental observations confirmed that CASP11, CASP4, and CASP5 trigger pyroptosis upon sensing cytosolic LPS [609 622–624], in monocytes as well as in other cell types [609, 625].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [609]
In the citing paper
“LPS-induced pyroptosis involves the physical interaction of LPS (or its lipid moiety) with the CARD domain of CASP11, CASP4, or CASP5, a highly specific binding resulting in caspase oligomerization and consequent activation [609].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [609]
In the citing paper
“(2) can also occur in cell types other than cells from the monocytic lineage [609]”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [609]
In the citing paper
“Thus, CASP11, CASP4, and CASP5 act as bona fide PRRs for cytosolic LPS.”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [609]
Citations
Cites
RNA-Guided Human Genome Engineering via Cas9
Mali, P., Yang, L., Esvelt, K. M., Aach, J., Guell, M., DiCarlo, J. E., Norville, J. E., & Church, G. M. (2013) · Science · doi:10.1126/science.1232033 · Cited by 9,210
Caspase Functions in Cell Death and DiseasePreprint
McIlwain, D. R., Berger, T., & Mak, T. W. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008656 · Cited by 2,702
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
The structural basis of lipopolysaccharide recognition by the TLR4–MD-2 complex
Park, B. S., Song, D. H., Kim, H. M., Choi, B., Lee, H., & Lee, J. (2009) · Nature · doi:10.1038/nature07830 · Cited by 2,513
Receptor Interacting Protein Kinase-3 Determines Cellular Necrotic Response to TNF-α
He, S., Wang, L., Miao, L., Wang, T., Du, F., Zhao, L., & Wang, X. (2009) · Cell · doi:10.1016/j.cell.2009.05.021 · Cited by 2,214
Molecular mechanisms of caspase regulation during apoptosis
Riedl, S. J., & Shi, Y. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1496 · Cited by 1,933
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
Mechanisms of caspase activation
Boatright, K. M., & Salvesen, G. S. (2003) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2003.10.009 · Cited by 1,374
Lipid A Modification Systems in Gram-Negative Bacteria
Raetz, C. R. H., Reynolds, C. M., Trent, M. S., & Bishop, R. E. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.010307.145803 · Cited by 1,371
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
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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
Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell death
Shi, J., Zhao, Y., Wang, K., Shi, X., Wang, Y., Huang, H., Zhuang, Y., Cai, T., Wang, F., & Shao, F. (2015) · Nature · doi:10.1038/nature15514 · Cited by 6,659
Self-citationThe NLRP3 inflammasome: molecular activation and regulation to therapeutics
Swanson, K. V., Deng, M., & Ting, J. P.-Y. (2019) · Nature Reviews Immunology · doi:10.1038/s41577-019-0165-0 · Cited by 4,884
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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
The 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
Inflammasomes: mechanism of action, role in disease, and therapeutics
Guo, H., Callaway, J. B., & Ting, J. P.-Y. (2015) · Nature Medicine · doi:10.1038/nm.3893 · Cited by 3,340
Chemotherapy drugs induce pyroptosis through caspase-3 cleavage of a gasdermin
Wang, Y., Gao, W., Shi, X., Ding, J., Liu, W., He, H., Wang, K., & Shao, F. (2017) · Nature · doi:10.1038/nature22393 · Cited by 3,199
Self-citationPyroptosis: Gasdermin-Mediated Programmed Necrotic Cell Death
Shi, J., Gao, W., & Shao, F. (2017) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.10.004 · Cited by 3,088
Self-citationPore-forming activity and structural autoinhibition of the gasdermin family
Ding, J., Wang, K., Liu, W., She, Y., Sun, Q., Shi, J., Sun, H., Wang, D.-C., & Shao, F. (2016) · Nature · doi:10.1038/nature18590 · Cited by 2,771
Self-citationMechanism and Regulation of NLRP3 Inflammasome Activation
He, Y., Hara, H., & Núñez, G. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.09.002 · Cited by 2,759
The molecular machinery of regulated cell death
Tang, D., Kang, R., Berghe, T. V., Vandenabeele, P., & Kroemer, G. (2019) · Cell Research · doi:10.1038/s41422-019-0164-5 · Cited by 2,675
Gasdermin D is an executor of pyroptosis and required for interleukin-1β secretion
He, W.-T., Wan, H., Hu, L., Chen, P., Wang, X., Huang, Z., Yang, Z.-H., Zhong, C.-Q., & Han, J. (2015) · Cell Research · doi:10.1038/cr.2015.139 · Cited by 2,517
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
Necroptosis, pyroptosis and apoptosis: an intricate game of cell death
Bertheloot, D., Latz, E., & Franklin, B. S. (2021) · Cellular and Molecular Immunology · doi:10.1038/s41423-020-00630-3 · Cited by 2,297
Man, S. M., Karki, R., & Kanneganti, T. (2017) · Immunological Reviews · doi:10.1111/imr.12534 · Cited by 1,684
NLRP3 inflammasome activation and cell death
Huang, Y., Xu, W., & Zhou, R. (2021) · Cellular & Molecular Immunology · doi:10.1038/s41423-021-00740-6 · Cited by 1,527
Rogers, C., Fernandes-Alnemri, T., Mayes, L., Alnemri, D., Cingolani, G., & Alnemri, E. S. (2017) · Nature Communications · doi:10.1038/ncomms14128 · Cited by 1,510
Granzyme A from cytotoxic lymphocytes cleaves GSDMB to trigger pyroptosis in target cells
Zhou, Z., He, H., Wang, K., Shi, X., Wang, Y., Su, Y., Wang, Y., Li, D., Liu, W., Zhang, Y., et al. (2020) · Science · doi:10.1126/science.aaz7548 · Cited by 1,317
Self-citationRecent advances in the mechanisms of NLRP3 inflammasome activation and its inhibitors
Yang, Y., Wang, H., Kouadir, M., Song, H., & Shi, F. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1413-8 · Cited by 1,326
Old, new and emerging functions of caspases
Shalini, S., Dorstyn, L., Dawar, S., & Kumar, S. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2014.216 · Cited by 1,267
Caspases in Cell Death, Inflammation, and Disease
Opdenbosch, N. V., & Lamkanfi, M. (2019) · Immunity · doi:10.1016/j.immuni.2019.05.020 · Cited by 1,272
Inflammation and atherosclerosis: signaling pathways and therapeutic intervention
Kong, P., Cui, Z.-Y., Huang, X.-F., Zhang, D.-D., Guo, R.-J., & Han, M. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-00955-7 · Cited by 1,183
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
Regulation of inflammasome activation
Man, S. M., & Kanneganti, T. (2015) · Immunological Reviews · doi:10.1111/imr.12296 · Cited by 1,088
Pyroptosis versus necroptosis: similarities, differences, and crosstalk
Frank, D., & Vince, J. E. (2019) · Cell Death & Differentiation · doi:10.1038/s41418-018-0212-6 · Cited by 1,062
Inflammasome activation and regulation: toward a better understanding of complex mechanisms
Zheng, D., Liwinski, T., & Elinav, E. (2020) · Cell Discovery · doi:10.1038/s41421-020-0167-x · Cited by 1,078
Newton, K., Strasser, A., Kayagaki, N., & Dixit, V. M. (2024) · Cell · doi:10.1016/j.cell.2023.11.044 · Cited by 1,068
Pyroptotic cell death defends against intracellular pathogens
Jorgensen, I., & Miao, E. A. (2015) · Immunological Reviews · doi:10.1111/imr.12287 · Cited by 1,021
Programmed cell death as a defence against infection
Jørgensen, I., Rayamajhi, M., & Miao, E. A. (2017) · Nature reviews. Immunology · doi:10.1038/nri.2016.147 · Cited by 1,057
Emerging connectivity of programmed cell death pathways and its physiological implications
Bedoui, S., Herold, M. J., & Strasser, A. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0270-8 · Cited by 1,027
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Re, D. P. D., Amgalan, D., Linkermann, A., Liu, Q., & Kitsis, R. N. (2019) · Physiological Reviews · doi:10.1152/physrev.00022.2018 · Cited by 994
Hou, J., Zhao, R., Xia, W., Chang, C.-W. M., You, Y., Hsu, J.-M., Nie, L., Chen, Y., Wang, Y.-C., Liu, C., et al. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-0575-z · Cited by 979
Self-citationNLRP3 Inflammasome and the IL-1 Pathway in Atherosclerosis
Grebe, A., Hoss, F., & Latz, E. (2018) · Circulation Research · doi:10.1161/circresaha.118.311362 · Cited by 926
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
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Aglietti, R. A., Estevez, A., Gupta, A., Ramirez, M. G., Liu, P. S., Kayagaki, N., Ciferri, C., Dixit, V. M., & Dueber, E. C. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1607769113 · Cited by 898
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Hwang, H. S., & Kim, H. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms161125943 · Cited by 902
Tong, X., Tang, R., Xiao, M., Xu, J., Wang, W., Zhang, B., Liu, J., Yu, X., & Shi, S. (2022) · Journal of Hematology & Oncology · doi:10.1186/s13045-022-01392-3 · Cited by 883
The role of pyroptosis in cancer: pro-cancer or pro-“host”?
Xia, X., Wang, X., Cheng, Z., Qin, W., Lei, L., Jiang, J., & Hu, J. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1883-8 · Cited by 856
Rogers, C., Erkes, D. A., Nardone, A., Aplin, A. E., Fernandes‐Alnemri, T., & Alnemri, E. S. (2019) · Nature Communications · doi:10.1038/s41467-019-09397-2 · Cited by 844
Julien, O., & Wells, J. A. (2017) · Cell Death & Differentiation · doi:10.1038/cdd.2017.44 · Cited by 816
Pyroptosis in inflammatory diseases and cancer
Rao, Z., Zhu, Y., Yang, P., Chen, Z., Xia, Y., Qiao, C., Liu, W., Deng, H., Li, J., Ning, P., et al. (2022) · Theranostics · doi:10.7150/thno.71086 · Cited by 835
Human Monocytes Engage an Alternative Inflammasome Pathway
Gaidt, M. M., Ebert, T. S., Chauhan, D., Schmidt, T., Schmid-Burgk, J. L., Rapino, F. A., Robertson, A. A. B., Cooper, M. A., Graf, T., & Hornung, V. (2016) · Immunity · doi:10.1016/j.immuni.2016.01.012 · Cited by 808
Co-operation of TLR4 and raft proteins in LPS-induced pro-inflammatory signaling
Płóciennikowska, A., Hromada‐Judycka, A., Borzęcka-Solarz, K., & Kwiatkowska, K. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1762-5 · Cited by 792
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Sollberger, G., Choidas, A., Burn, G. L., Habenberger, P., Lucrezia, R. D., Kordes, S., Menninger, S., Eickhoff, J., Nußbaumer, P., Klebl, B., et al. (2018) · Science Immunology · doi:10.1126/sciimmunol.aar6689 · Cited by 779
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Amarante-Mendes, G. P., Adjemian, S., Branco, L. M., Zanetti, L. C., Weinlich, R., & Bortoluci, K. R. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02379 · Cited by 802
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Wang, K., Sun, Q., Zhong, X., Zeng, M., Zeng, H., Shi, X., Li, Z., Wang, Y., Zhao, Q., Shao, F., et al. (2020) · Cell · doi:10.1016/j.cell.2020.02.002 · Cited by 755
Self-citationESCRT-dependent membrane repair negatively regulates pyroptosis downstream of GSDMD activation
Rühl, S., Shkarina, K., Demarco, B., Heilig, R., Santos, J. C., & Brož, P. (2018) · Science · doi:10.1126/science.aar7607 · Cited by 770
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Sharma, D., & Kanneganti, T. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201602089 · Cited by 754
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Vanaja, S. K., Russo, A. J., Behl, B., Banerjee, I., Yankova, M. P., Deshmukh, S. D., & Rathinam, V. A. K. (2016) · Cell · doi:10.1016/j.cell.2016.04.015 · Cited by 750
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Xue, Q., Kang, R., Klionsky, D. J., Tang, D., Liu, J., & Chen, X. (2023) · Autophagy · doi:10.1080/15548627.2023.2200554 · Cited by 731
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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
Targeting Inflammation Driven by HMGB1
Yang, H., Wang, H., & Andersson, U. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00484 · Cited by 662
Noncanonical inflammasome signaling elicits gasdermin D–dependent neutrophil extracellular traps
Chen, K. W., Monteleone, M. M., Boucher, D., Sollberger, G., Ramnath, D., Condon, N. D., von Pein, J. B., Brož, P., Sweet, M. J., & Schroder, K. (2018) · Science Immunology · doi:10.1126/sciimmunol.aar6676 · Cited by 657
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Post-Translational Modification Control of Innate Immunity
Liu, J., Qian, C., & Cao, X. (2016) · Immunity · doi:10.1016/j.immuni.2016.06.020 · Cited by 641
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Lipid Peroxidation Drives Gasdermin D-Mediated Pyroptosis in Lethal Polymicrobial Sepsis
Kang, R., Zeng, L., Zhu, S., Xie, Y., Liu, J., Wen, Q., Cao, L., Xie, M., Ran, Q., Kroemer, G., et al. (2018) · Cell Host & Microbe · doi:10.1016/j.chom.2018.05.009 · Cited by 627
Pyroptosis and Apoptosis Pathways Engage in Bidirectional Crosstalk in Monocytes and Macrophages
Taabazuing, C. Y., Okondo, M. C., & Bachovchin, D. A. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2017.03.009 · Cited by 630
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Biasizzo, M., & Kopitar‐Jerala, N. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.591803 · Cited by 636
Walle, L. V., & Lamkanfi, M. (2016) · Current Biology · doi:10.1016/j.cub.2016.02.019 · Cited by 628
The role of interleukin-1 in general pathology
Kaneko, N., Kurata, M., Yamamoto, T., Morikawa, S., & Masumoto, J. (2019) · Inflammation and Regeneration · doi:10.1186/s41232-019-0101-5 · Cited by 650
Interleukin‐18: Biological properties and role in disease pathogenesis
Kaplanski, G. (2017) · Immunological Reviews · doi:10.1111/imr.12616 · Cited by 621
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
Self-citationYang, D., He, Y., Muñoz-Planillo, R., Liu, Q., & Núñez, G. (2015) · Immunity · doi:10.1016/j.immuni.2015.10.009 · Cited by 622
Marchetti, C., Swartzwelter, B. J., Gamboni, F., Neff, C. P., Richter, K., Azam, T., Carta, S., Tengesdal, I. W., Nemkov, T. G., D’Alessandro, A., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1716095115 · Cited by 605
Zheng, M., & Kanneganti, T. (2020) · Immunological Reviews · doi:10.1111/imr.12909 · Cited by 602
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Deng, M., Tang, Y., Li, W., Wang, X., Zhang, R., Zhang, X., Zhao, X. S., Liu, J., Tang, C. W., Liu, Z., et al. (2018) · Immunity · doi:10.1016/j.immuni.2018.08.016 · Cited by 596
Blevins, H. M., Xu, Y., Biby, S., & Zhang, S. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.879021 · Cited by 587
Polymicrobial synergy and dysbiosis in inflammatory disease
Lamont, R. J., & Hajishengallis, G. (2015) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2014.11.004 · Cited by 585
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Zanoni, I., Tan, Y., Di Gioia, M., Broggi, A., Ruan, J., Shi, J., Donado, C. A., Shao, F., Wu, H., Springstead, J. R., et al. (2016) · Science · doi:10.1126/science.aaf3036 · Cited by 583
Self-citationKlebsiella pneumoniae infection biology: living to counteract host defences
Bengoechea, J. A., & Sá‐Pessoa, J. (2018) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuy043 · Cited by 605
PKM2-dependent glycolysis promotes NLRP3 and AIM2 inflammasome activation
Xie, M., Yu, Y., Kang, R., Zhu, S., Yang, L., Zeng, L., Sun, X., Yang, M., Billiar, T. R., Wang, H., et al. (2016) · Nature Communications · doi:10.1038/ncomms13280 · Cited by 579
The Coming Decade of Cell Death Research: Five Riddles
Green, D. R. (2019) · Cell · doi:10.1016/j.cell.2019.04.024 · Cited by 575
Programmed necrosis in inflammation: Toward identification of the effector molecules
Wallach, D., Kang, T., Dillon, C. P., & Green, D. R. (2016) · Science · doi:10.1126/science.aaf2154 · Cited by 555
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Rühl, S., & Brož, P. (2015) · European Journal of Immunology · doi:10.1002/eji.201545772 · Cited by 546
Wang, Y., & Kanneganti, T.-D. (2021) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2021.07.038 · Cited by 545
Self-citationCaspase-6 Is a Key Regulator of Innate Immunity, Inflammasome Activation, and Host Defense
Zheng, M., Karki, R., Vogel, P., & Kanneganti, T. (2020) · Cell · doi:10.1016/j.cell.2020.03.040 · Cited by 539
Linking cellular stress responses to systemic homeostasis
Galluzzi, L., Yamazaki, T., & Kroemer, G. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0068-0 · Cited by 556
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Nagata, S., & Tanaka, M. (2017) · Nature reviews. Immunology · doi:10.1038/nri.2016.153 · Cited by 540
Emerging Activators and Regulators of Inflammasomes and Pyroptosis
Xue, Y., Tuipulotu, D. E., Tan, W. H., Kay, C., & Man, S. M. (2019) · Trends in Immunology · doi:10.1016/j.it.2019.09.005 · Cited by 517
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Salmonellae interactions with host processes
LaRock, D. L., Chaudhary, A., & Miller, S. I. (2015) · Nature Reviews Microbiology · doi:10.1038/nrmicro3420 · Cited by 502
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Tsuchiya, K., Nakajima, S., Hosojima, S., Nguyen, D. T., Hattori, T., Le, T. M., Hori, O., Mahib, M. R., Yamaguchi, Y., Miura, M., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09753-2 · Cited by 512
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
Hsu, S., Li, C., Lin, I., Syue, W.-J., Chen, Y., Cheng, K., Teng, Y., Lin, Y., Yen, C., & Chiu, C. (2021) · Theranostics · doi:10.7150/thno.62521 · Cited by 502
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Yu, J., Li, S., Qi, J., Chen, Z., Wu, Y., Guo, J., Wang, K., Sun, X., & Zheng, J. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1441-4 · Cited by 481
Platnich, J. M., & Muruve, D. A. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.02.008 · Cited by 491
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Lancaster, G. I., Langley, K. G., Berglund, N. A., Kammoun, H. L., Reibe, S., Estévez, E., Weir, J. M., Mellett, N. A., Pernes, G., Conway, J. R. W., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.03.014 · Cited by 488
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Malik, A., & Kanneganti, T. (2017) · Journal of Cell Science · doi:10.1242/jcs.207365 · Cited by 459
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Wang, S., Yuan, Y., Chen, N., & Wang, H. (2018) · International Immunopharmacology · doi:10.1016/j.intimp.2018.12.019 · Cited by 452
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Arroyo, V., Moreau, R., Kamath, P. S., Jalan, R., Ginès, P., Nevens, F., Fernández, J., To, U. K., García–Tsao, G., & Schnabl, B. (2016) · Nature Reviews Disease Primers · doi:10.1038/nrdp.2016.41 · Cited by 450
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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
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Evavold, C. L., Hafner‐Bratkovič, I., Devant, P., D’Andrea, J. M., Ngwa, E. M., Boršić, E., Doench, J. G., LaFleur, M. W., Sharpe, A. H., Thiagarajah, J. R., et al. (2021) · Cell · doi:10.1016/j.cell.2021.06.028 · Cited by 426
Metadata
- Authors
- Shi, J., Zhao, Y., Wang, Y., Gao, W., Ding, J., Li, P., Hu, L., & Shao, F.
- Affiliations
- Peking University (CN)
- National Institute of Biological Sciences, Beijing (CN)
- Chinese Academy of Sciences (CN)
- Corresponding author
- Shao, Feng
- Venue
- Nature
- Published
- 2014-08-06
- Volume
- 514
- Issue
- 7521
- Pages
- 187-192
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2068619092
- Cited by
- 2,285
- References
- 41
- Citations by year
- 2026: 190 · 2025: 205 · 2024: 231 · 2023: 277 · 2022: 254 · 2021: 227 · 2020: 193 · 2019: 162 · 2018: 158 · 2017: 131 · 2016: 128 · 2015: 103 · 2014: 23
- FWCI
- 52.72
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Rare & Special e-Zone (The Hong Kong University of Science and Technology) (submittedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- Tsinghua University
- University of British Columbia
- National Key Research and Development Program of China
- 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 › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- caspase-4, caspase-5, non-canonical inflammasome, pyroptosis, pattern recognition receptors, CARD domain, lipid A, endotoxic shock, intracellular bacterial infection, innate immunity, inflammatory cell death
- MeSH terms
- Animals, Cells, Cultured, Enzyme Activation, Epithelial Cells, Genetic Complementation Test, Humans, Immunity, Innate, Inflammation, Lipid A, Lipopolysaccharides, Macrophages, Necrosis, Protein Binding, Rhodobacter sphaeroides, Substrate Specificity, Keratinocytes, Cell Death, Caspases, Surface Plasmon Resonance, Mutant Proteins, Mice, Caspases, Initiator, Protein Multimerization
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