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An endogenous caspase-11 ligand elicits interleukin-1 release from living dendritic cells
Open accessAbstract
Immune activation in context: Dendritic cells (DCs) initiate protective immunity upon binding molecules derived from microbes or released from dying cells. Zanoni et al. examined how microbial and endogenous signals interact to shape the course of the ensuing immune response (see the Perspective by Napier and Monack). They found that oxPAPC, an oxidized phospholipid released from dying cells, binds to a protein called caspase-11 in DCs, activating an inflammatory program in these cells. Whereas caspase-11 binding to oxPAPC and bacterial lipopolysaccharide causes DCs to produce the cytokine interleukin-1 (IL-1) and undergo cell death, binding to oxPAPC alone triggers DCs to secrete IL-1 and induce strong adaptive immunity. Thus, context-dependent signals can shape the ensuing immune response. Science , this issue p. 1232 ; see also p. 1173
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“at least in some cell types including DCs, CASP11 activation can drive IL-1β secretion in the absence of cell death [628].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [628]
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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-citationMartinon, F., Burns, K., & Tschopp, J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00599-3 · Cited by 6,066
Caspase-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
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
Self-citationControl of adaptive immunity by the innate immune system
Iwasaki, A., & Medzhitov, R. (2015) · Nature Immunology · doi:10.1038/ni.3123 · Cited by 2,160
How dying cells alert the immune system to danger
Kono, H., & Rock, K. L. (2008) · Nature Reviews Immunology · doi:10.1038/nri2215 · Cited by 1,737
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
The IL-1 family: regulators of immunity
Sims, J. E., & Smith, D. E. (2010) · Nature reviews. Immunology · doi:10.1038/nri2691 · Cited by 1,459
Imai, Y., Kuba, K., Neely, G. G., Yaghubian-Malhami, R., Perkmann, T., van Loo, G., Ermolaeva, M., Veldhuizen, R., Leung, Y. H. C., Wang, H., et al. (2008) · Cell · doi:10.1016/j.cell.2008.02.043 · Cited by 1,356
Pyroptotic cell death defends against intracellular pathogens
Jorgensen, I., & Miao, E. A. (2015) · Immunological Reviews · doi:10.1111/imr.12287 · Cited by 1,021
Flagged first, then by citations
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Items 101–200 of 593
Carty, M., Kearney, J., Shanahan, K. A., Hams, E., Sugisawa, R., Connolly, D. J., Doran, C. G., Muñoz‐Wolf, N., Gürtler, C., Fitzgerald, K. A., et al. (2019) · Immunity · doi:10.1016/j.immuni.2019.04.005 · Cited by 147
Sharygin, D. A., Koniaris, L. G., Wells, C. D., Zimmers, T. A., & Hamidi, T. (2023) · Immunology · doi:10.1111/imm.13634 · Cited by 147
The gasdermin family: emerging therapeutic targets in diseases
Zhu, C., Xu, S., Jiang, R., Yu, Y., Bian, J., & Zou, Z. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01801-8 · Cited by 149
Context-Dependent Role of Oxidized Lipids and Lipoproteins in Inflammation
Miller, Y. I., & Shyy, J. Y.-J. (2016) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2016.11.002 · Cited by 141
Intracellular Lipopolysaccharide Sensing as a Potential Therapeutic Target for Sepsis
Pfalzgraff, A., & Weindl, G. (2019) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2019.01.001 · Cited by 139
Recent Insights on Inflammasomes, Gasdermin Pores, and PyroptosisPreprint
de Vasconcelos, N. M., & Lamkanfi, M. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a036392 · Cited by 139
Inflammasome biology, molecular pathology and therapeutic implications
Awad, F., Assrawi, E., Louvrier, C., Jumeau, C., Georgin‐Lavialle, S., Grateau, G., Amselem, S., Giurgea, I., & Karabina, S. (2018) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2018.02.011 · Cited by 138
RIPK3 collaborates with GSDMD to drive tissue injury in lethal polymicrobial sepsis
Chen, H., Li, Y., Wu, J., Li, G., Tao, X., Lai, K., Yuan, Y., Zhang, X., Zou, Z., & Xu, Y. (2020) · Cell Death and Differentiation · doi:10.1038/s41418-020-0524-1 · Cited by 138
DAMPs in the immunogenicity of cell death
Chen, R., Zou, J., Liu, J., Kang, R., & Tang, D. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.09.007 · Cited by 141
Caspase-11-mediated tubular epithelial pyroptosis underlies contrast-induced acute kidney injury
Zhang, Z., Shao, X., Jiang, N., Mou, S., Gu, L., Li, S., Lin, Q., He, Y., Zhang, M., Zhou, W., et al. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-1023-x · Cited by 133
Cellular context of IL-33 expression dictates impact on anti-helminth immunity
Hung, L., Tanaka, Y., Herbine, K., Pastore, C., Singh, B. K., Ferguson, A. A., Vora, N., Douglas, B. B., Zullo, K. M., Behrens, E. M., et al. (2020) · Science Immunology · doi:10.1126/sciimmunol.abc6259 · Cited by 131
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Dri, E., Lampas, E., Lazaros, G. A., Lazarou, E., Theofilis, P., Tsioufis, C. P., & Tousoulis, D. (2023) · Life · doi:10.3390/life13061420 · Cited by 132
Innate immunity, cytokine storm, and inflammatory cell death in COVID-19
Karki, R., & Kanneganti, T. (2022) · Journal of Translational Medicine · doi:10.1186/s12967-022-03767-z · Cited by 131
Pleiotropic effects of oxidized phospholipids
Bochkov, V. N., Gesslbauer, B., Mauerhofer, C., Philippova, M., Erné, P., & Oskolkova, O. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.12.034 · Cited by 129
Russo, A. J., Vasudevan, S. O., Méndez‐Huergo, S. P., Kumari, P. H., Ménoret, A., Duduskar, S. N., Wang, C., Sáez, J. M. P., Fettis, M. M., Li, C., et al. (2021) · Nature Immunology · doi:10.1038/s41590-020-00844-7 · Cited by 132
Self-citationInnate immune detection of lipid oxidation as a threat assessment strategy
Zhivaki, D., & Kagan, J. C. (2021) · Nature reviews. Immunology · doi:10.1038/s41577-021-00618-8 · Cited by 129
Self-citationEpithelial Gasdermin D shapes the host-microbial interface by driving mucus layer formation
Zhang, J., Yu, Q., Jiang, D., Kang, Y., Yu, W., Chi, Z., Chen, S., Li, M., Yang, D., Wang, Z., et al. (2022) · Science Immunology · doi:10.1126/sciimmunol.abk2092 · Cited by 126
Alternative inflammasome activation enables IL-1β release from living cells
Gaidt, M. M., & Hornung, V. (2016) · Current Opinion in Immunology · doi:10.1016/j.coi.2016.10.007 · Cited by 124
Molecular mechanism for NLRP6 inflammasome assembly and activation
Shen, C., Lu, A. Z., Xie, W. J., Ruan, J., Negro, R., Egelman, E. H., Fu, T., & Wu, H. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1817221116 · Cited by 124
Self-citationKnocking ’em Dead: Pore-Forming Proteins in Immune Defense
Liu, X., & Lieberman, J. (2020) · Annual Review of Immunology · doi:10.1146/annurev-immunol-111319-023800 · Cited by 114
The discontinuity theory of immunity
Pradeu, T., & Vivier, É. (2016) · Science Immunology · doi:10.1126/sciimmunol.aag0479 · Cited by 111
The intra‐ and extracellular functions of ASC specks
Franklin, B. S., Latz, E., & Schmidt, F. I. (2017) · Immunological Reviews · doi:10.1111/imr.12611 · Cited by 112
Liu, P., Zhang, Z., & Yao, L. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.603416 · Cited by 112
Stressing out the mitochondria: Mechanistic insights into NLRP3 inflammasome activation
Yabal, M., Calleja, D. J., Simpson, D. S., & Lawlor, K. E. (2018) · Journal of Leukocyte Biology · doi:10.1002/jlb.mr0318-124r · Cited by 110
Inflammasome activation in acute lung injury
McVey, M. J., Steinberg, B. E., & Goldenberg, N. M. (2020) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00303.2020 · Cited by 108
The lipid basis of cell death and autophagy
Lin, Z., Long, F., Kang, R., Klionsky, D. J., Yang, M., & Tang, D. (2023) · Autophagy · doi:10.1080/15548627.2023.2259732 · Cited by 107
O’Donnell, V. B., Aldrovandi, M., Murphy, R. C., & Krönke, G. (2019) · Science Signaling · doi:10.1126/scisignal.aau2293 · Cited by 105
Gasdermin and MLKL necrotic cell death effectors: Signaling and diseases
Lawlor, K. E., Murphy, J. M., & Vince, J. E. (2024) · Immunity · doi:10.1016/j.immuni.2024.02.011 · Cited by 108
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Wu, K. K.-L., Cheung, S. W. M., & Cheng, K. K. Y. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21114184 · Cited by 105
Normalization of cholesterol metabolism in spinal microglia alleviates neuropathic pain
Pelaez, J. M. N., Choi, S., Capettini, L. D. S. A., Xia, Y., Gonen, A., Agatisa-Boyle, C., Delay, L., dos Santos, G. G., Catroli, G. F., Kim, J., et al. (2021) · The Journal of Experimental Medicine · doi:10.1084/jem.20202059 · Cited by 104
Beyond inflammasomes: emerging function of gasdermins during apoptosis and NETosis
Chen, K. W., Demarco, B., & Brož, P. (2019) · The EMBO Journal · doi:10.15252/embj.2019103397 · Cited by 103
Cell death is not essential for caspase-1-mediated interleukin-1β activation and secretion
Conos, S. A., Lawlor, K. E., Vaux, D. L., Vince, J. E., & Lindqvist, L. (2016) · Cell Death and Differentiation · doi:10.1038/cdd.2016.69 · Cited by 102
Correction of age-associated defects in dendritic cells enables CD4+ T cells to eradicate tumors
Zhivaki, D., Kennedy, S. N., Park, J., Borriello, F., Devant, P., Cao, A., Bahleda, K. M., Murphy, S. M., Aubin, C., Evavold, C. L., et al. (2024) · Cell · doi:10.1016/j.cell.2024.05.026 · Cited by 102
Self-citationThe NLRP1 Inflammasome in Human Skin and Beyond
Fenini, G., Karakaya, T., Hennig, P., Filippo, M. D., & Beer, H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21134788 · Cited by 99
Programmed Cell Death in Sepsis Associated Acute Kidney Injury
Wu, Z., Deng, J., Zhou, H., Tan, W., Lin, L., & Yang, J. (2022) · Frontiers in Medicine · doi:10.3389/fmed.2022.883028 · Cited by 99
Dubey, S. R., Turnbull, C., Pandey, A., Zhao, A., Kurera, M., Al-Zidan, R. N., Shen, C. X., Gautam, M., Mahajan, S., Jadhav, P. S., et al. (2025) · Cellular and Molecular Immunology · doi:10.1038/s41423-025-01354-y · Cited by 101
Fite, B. Z., Wang, J., Kare, A. J., Ilovitsh, A., Chavez, M., Ilovitsh, T., Zhang, N., Chen, W., Robinson, E. R., Zhang, H., et al. (2021) · Scientific Reports · doi:10.1038/s41598-020-80135-1 · Cited by 96
Multifaceted role of CD14 in innate immunity and tissue homeostasis
Na, K., Oh, B., & Jung, Y. (2023) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2023.08.008 · Cited by 98
Ion homeostasis and ion channels in NLRP3 inflammasome activation and regulation
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Nadendla, E. K., Tweedell, R. E., Kasof, G. M., & Kanneganti, T. (2025) · Cell Discovery · doi:10.1038/s41421-025-00791-3 · Cited by 95
Inflammasome activation and Th17 responses
Deng, J. P., Yu, X., & Wang, P. (2019) · Molecular Immunology · doi:10.1016/j.molimm.2018.12.024 · Cited by 94
The Regulation and Modification of GSDMD Signaling in Diseases
Li, Z., Ji, S., Jiang, M., Xu, Y., & Zhang, C. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.893912 · Cited by 95
Inflammasome-Dependent Coagulation Activation in Sepsis
Wu, R., Wang, N., Comish, P. B., Tang, D., & Kang, R. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.641750 · Cited by 89
Activation and Function of NLRP3 Inflammasome in Bone and Joint-Related Diseases
Murakami, T., Nakaminami, Y., Takahata, Y., Hata, K., & Nishimura, R. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23105365 · Cited by 89
Uncoupled pyroptosis and IL-1β secretion downstream of inflammasome signaling
Li, Y., & Jiang, Q. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1128358 · Cited by 92
Inflammasome: structure, biological functions, and therapeutic targets
Dai, Y., Zhou, J., & Shi, C. (2023) · MedComm · doi:10.1002/mco2.391 · Cited by 89
Advances in the molecular mechanisms of NLRP3 inflammasome activators and inactivators
Liu, D., Zeng, X., Li, X., Cui, C., Hou, R., Guo, Z., Mehta, J. L., & Wang, X. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.113863 · Cited by 88
Li, C., Wang, W., Xie, S.-S., Ma, W., Fan, Q.-W., Chen, Y., He, Y., Wang, J.-N., Yang, Q., Li, H.-D., et al. (2021) · Frontiers in Medicine · doi:10.3389/fmed.2021.796724 · Cited by 86
Yi, Y. (2019) · Immunology · doi:10.1111/imm.13134 · Cited by 85
Caspase-11–mediated enteric neuronal pyroptosis underlies Western diet–induced colonic dysmotility
Ye, L., Li, G., Goebel, A. M., Raju, A. V., Kong, F., Lv, Y., Li, K., Zhu, Y., Raja, S. M., He, P., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci130176 · Cited by 84
Pereira, M. C. A., Liang, J. J., Edwards-Hicks, J., Meadows, A. M., Hinz, C., Liggi, S., Hepprich, M., Mudry, J. M., Han, K., Griffin, J. L., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.113700 · Cited by 85
Angosto-Bazarra, D., Alarcón‐Vila, C., Hurtado‐Navarro, L., Baños, M. C., Rivers‐Auty, J., & Pelegrı́n, P. (2022) · BMC Biology · doi:10.1186/s12915-021-01220-z · Cited by 83
Caspase-11 promotes allergic airway inflammation
Zasłona, Z., Flis, E., Wilk, M. M., Carroll, R. G., Pålsson‐McDermott, E. M., Hughes, M. M., Diskin, C., Banahan, K., Ryan, D. G., Hooftman, A., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-14945-2 · Cited by 83
Lipid and Non-lipid Factors Affecting Macrophage Dysfunction and Inflammation in Atherosclerosis
Gibson, M. S., Domingues, N. S., & Vieira, O. V. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00654 · Cited by 82
Recent insights into the regulatory networks of NLRP3 inflammasome activation
Weber, A. N. R., Bittner, Z., Shankar, S., Liu, X., Chang, T.-H., Jin, T., & Tapia‐Abellán, A. (2020) · Journal of Cell Science · doi:10.1242/jcs.248344 · Cited by 85
Du, S., Qiao, D., Chen, C., Chen, S., Liu, C., Lin, Z., Wang, H., & Xie, W. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00409 · Cited by 82
Linking vaccine adjuvant mechanisms of action to function
Ben‐Akiva, E., Chapman, A. P., Mao, T., & Irvine, D. J. (2025) · Science Immunology · doi:10.1126/sciimmunol.ado5937 · Cited by 83
The effect of oxidized phospholipids on phenotypic polarization and function of macrophages
Serbulea, V., DeWeese, D. E., & Leitinger, N. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.02.035 · Cited by 79
Inhibition of Neuroinflammation by AIBP: Spinal Effects upon Facilitated Pain States
Woller, S. A., Choi, S.-H., An, E. J., Low, H., Schneider, D. A., Ramachandran, R., Kim, J., Bae, Y. S., Sviridov, D., Corr, M., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.04.110 · Cited by 79
Lipid regulation of NLRP3 inflammasome activity through organelle stress
Liang, J. J., Fraser, I. D. C., & Bryant, C. E. (2021) · Trends in Immunology · doi:10.1016/j.it.2021.07.005 · Cited by 79
Drummer, C., Saaoud, F., Jhala, N. C., Cueto, R., Sun, Y., Xu, K., Shao, Y., Lu, Y., Shen, H., Yang, L., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1113883 · Cited by 78
Lorey, M. B., Rossi, K., Eklund, K. K., Nyman, T. A., & Matikainen, S. (2017) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m116.064840 · Cited by 78
Inflammasome-Mediated Immunogenicity of Clinical and Experimental Vaccine Adjuvants
Reinke, S., Thakur, A., Gartlan, C., Bezbradica, J. S., & Milicic, A. (2020) · Vaccines · doi:10.3390/vaccines8030554 · Cited by 77
Ross, C. M., Chan, A. H., von Pein, J. B., Boucher, D., & Schroder, K. (2018) · Life Science Alliance · doi:10.26508/lsa.201800237 · Cited by 78
Cell-Specific Roles of NLRP3 Inflammasome in Myocardial Infarction
Takahashi, M. (2019) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0000000000000709 · Cited by 77
Irmscher, S., Brix, S. R., Zipfel, S. L. H., Halder, L. D., Mutlutürk, S., Wulf, S., Girdauskas, E., Reichenspurner, H. C., Stahl, R. A. K., Jungnickel, B., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-10766-0 · Cited by 76
Caspase-11-Gasdermin D-Mediated Pyroptosis Is Involved in the Pathogenesis of Atherosclerosis
Jiang, M., Sun, X., Liu, S., Tang, Y. J., Shi, Y., Bai, Y., Wang, Y., Yang, Q., Yang, Q., Jiang, W., et al. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.657486 · Cited by 75
Regulation of Lytic and Non-Lytic Functions of Gasdermin Pores
Rühl, S., & Broz, P. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167246 · Cited by 74
Caution, K., Young, N. A., Robledo-Avila, F. H., Krause, K., Khweek, A. A., Hamilton, K., Badr, A., Vaidya, A., Daily, K. P., Gosu, H., et al. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02519 · Cited by 74
Serbulea, V., Upchurch, C. M., Ahern, K. W., Bories, G. F. P., Voigt, P. E., DeWeese, D. E., Meher, A. K., Harris, T. E., & Leitinger, N. (2017) · Molecular Metabolism · doi:10.1016/j.molmet.2017.11.002 · Cited by 74
Pattern recognition receptor‐mediated inflammation in diabetic vascular complications
Wang, X., Antony, V., Wang, Y., Wu, G., & Liang, G. (2020) · Medicinal Research Reviews · doi:10.1002/med.21711 · Cited by 73
Dubyak, G., Miller, B. A., & Pearlman, E. M. (2023) · Immunological Reviews · doi:10.1111/imr.13186 · Cited by 73
The gasdermin protein family: emerging roles in gastrointestinal health and disease
Privitera, G., Rana, N., Armuzzi, A., & Pizarro, T. T. (2023) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/s41575-023-00743-w · Cited by 72
Regulatory Roles of the Caspase-11 Non-Canonical Inflammasome in Inflammatory Diseases
Yi, Y. (2018) · Immune Network · doi:10.4110/in.2018.18.e41 · Cited by 71
Regulation, Activation and Function of Caspase-11 during Health and Disease
Agnew, A., Nulty, C., & Creagh, E. M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22041506 · Cited by 70
Saturated fatty acids activate caspase-4/5 in human monocytes, triggering IL-1β and IL-18 release
Pillon, N. J., Chan, K. L., Zhang, S., Mejdani, M., Jacobson, M. R., Ducos, A., Bilan, P. J., Niu, W., & Klip, A. (2016) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00296.2016 · Cited by 70
Sitia, R., & Rubartelli, A. (2018) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2018.03.011 · Cited by 70
Oxidized phospholipids as novel mediators of neurodegeneration
Dong, Y., & Yong, V. W. (2022) · Trends in Neurosciences · doi:10.1016/j.tins.2022.03.002 · Cited by 69
NLRP3 and cancer: Pathogenesis and therapeutic opportunities
Tengesdal, I. W., Dinarello, C. A., & Marchetti, C. (2023) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2023.108545 · Cited by 70
Yang, M., Du, Q., Goswami, J., Varley, P. R., Chen, B., Wang, R., Morelli, A. E., Stolz, D. B., Billiar, T. R., Li, J., et al. (2017) · Hepatology · doi:10.1002/hep.29605 · Cited by 68
Posttranslational and Therapeutic Control of Gasdermin-Mediated Pyroptosis and Inflammation
Fischer, F. A., Chen, K. W., & Bezbradica, J. S. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.661162 · Cited by 71
NLRP3-mediated pyroptosis in diabetic nephropathy
Wan, J., Liu, D., Pan, S., Zhou, S., & Liu, Z. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.998574 · Cited by 66
NLRP3 inflammasome in cognitive impairment and pharmacological properties of its inhibitors
Xu, Y., Yang, Y., Chen, X., Jiang, D., Zhang, F., Guo, Y., Hu, B., Xu, G., Peng, S., Wu, L., et al. (2023) · Translational Neurodegeneration · doi:10.1186/s40035-023-00381-x · Cited by 65
Inflammatory pain control by blocking oxidized phospholipid-mediated TRP channel activation
Oehler, B., Kistner, K., Martin, C., Schiller, J., Mayer, R., Mohammadi, M., Sauer, R., Filipović, M. R., Nieto, F. R., Kloka, J. A., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-05348-3 · Cited by 64
Eltobgy, M. M., Zani, A., Kenney, A. D., Estfanous, S. Z. K., Kim, E., Badr, A., Carafice, C., Daily, K. P., Whitham, O. D., Pietrzak, M., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2202012119 · Cited by 62
NLRP3 Inflammasome: A central player in renal pathologies and nephropathy
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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
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Metadata
- Authors
- Zanoni, I., Tan, Y., Di Gioia, M., Broggi, A., Ruan, J., Shi, J., Donado, C. A., Shao, F., Wu, H., Springstead, J. R., & Kagan, J. C.
- Affiliations
- Boston Children's Hospital (US)
- Harvard Medical School and Division of Gastroenterology, Boston Children’s Hospital, Boston, MA, USA.
- Harvard University (US)
- National Institute of Biological Sciences, Beijing (CN)
- Western Michigan University (US)
- Corresponding author
- Kagan, Jonathan C.
- ORCID
- Venue
- Science
- Published
- 2016-06-03
- Volume
- 352
- Issue
- 6290
- Pages
- 1232-1236
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC5111085
- OpenAlex
- W2340046691
- Cited by
- 583
- References
- 30
- Citations by year
- 2026: 34 · 2025: 69 · 2024: 58 · 2023: 76 · 2022: 69 · 2021: 62 · 2020: 61 · 2019: 51 · 2018: 49 · 2017: 38 · 2016: 14
- FWCI
- 26.34
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- BOA (University of Milano-Bicocca) (submittedVersion)
- Funders
- Mead Johnson & Company
- Burroughs Wellcome Fund
- Harvard Digestive Diseases Center (P30 DK34854)
- Cariplo Foundation
- Jane Coffin Childs Fund
- NIH (AI093589, AI072955, P30 DK34854, 1R01AI121066-01A1, 1R15HL121770-01A1)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Immunology and Microbiology › Immunology › Immunotherapy and Immune Responses
- Keywords
- caspase-11, dendritic cells, OxPAPC, lipopolysaccharide, pyroptosis, inflammasome, dendritic cell activation, pattern recognition receptors, innate immunity, adaptive immune response
- MeSH terms
- NLR Family, Pyrin Domain-Containing 3 Protein, Animals, Carrier Proteins, Dendritic Cells, Immunity, Innate, Lipopolysaccharides, Phospholipids, Cell Death, Mice, Knockout, Caspases, Receptors, Pattern Recognition, Toll-Like Receptor 4, Mice, Caspases, Initiator, Interleukin-1beta, Adaptive Immunity, Inflammasomes
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