Inflammasome-mediated pyroptotic and apoptotic cell death, and defense against infection

Pyroptosis: host cell death and inflammation

Bergsbaken, T., Fink, S. L., & Cookson, B. T. (2009) · Nature Reviews Microbiology · doi:10.1038/nrmicro2070 · Cited by 3,185 · see citing works

AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC

Hornung, V., Ablasser, A., Charrel-Dennis, M., Bauernfeind, F., Horvath, G., Caffrey, D. R., Latz, E., & Fitzgerald, K. A. (2009) · Nature · doi:10.1038/nature07725 · Cited by 2,627 · see citing works

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 · see citing works

AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA

Fernandes-Alnemri, T., Yu, J.-W., Datta, P., Wu, J., & Alnemri, E. S. (2009) · Nature · doi:10.1038/nature07710 · Cited by 1,831 · see citing works

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 · see citing works

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 1,273 · see citing works

Caspase‐1‐induced pyroptotic cell death

Miao, E. A., Rajan, J. V., & Aderem, A. A. (2011) · Immunological Reviews · doi:10.1111/j.1600-065x.2011.01044.x · Cited by 1,139 · see citing works

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 · see citing works

An orthogonal proteomic-genomic screen identifies AIM2 as a cytoplasmic DNA sensor for the inflammasome

Bürckstümmer, T., Baumann, C., Blüml, S., Dixit, E., Dürnberger, G., Jahn, H., Planyavsky, M., Bilban, M., Colinge, J., Bennett, K. L., et al. (2009) · Nature Immunology · doi:10.1038/ni.1702 · Cited by 1,091 · see citing works

Innate immune recognition of bacterial ligands by NAIPs determines inflammasome specificity

Kofoed, E. M., & Vance, R. E. (2011) · Nature · doi:10.1038/nature10394 · Cited by 894 · see citing works

HIN-200 Proteins Regulate Caspase Activation in Response to Foreign Cytoplasmic DNA

Roberts, T. L., Idris, A., Dunn, J. A., Kelly, G., Burnton, C. M., Hodgson, S., Hardy, L., Garceau, V., Sweet, M. J., Ross, I. L., et al. (2009) · Science · doi:10.1126/science.1169841 · Cited by 830 · see citing works

Innate immune detection of the type III secretion apparatus through the NLRC4 inflammasome

Miao, E. A., Mao, D. P., Yudkovsky, N., Bonneau, R., Lorang, C. G., Warren, S. E., Leaf, I. A., & Aderem, A. A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913087107 · Cited by 800 · see citing works

TRIF Licenses Caspase-11-Dependent NLRP3 Inflammasome Activation by Gram-Negative Bacteria

Rathinam, V. A. K., Vanaja, S. K., Waggoner, L., Sokolovska, A., Becker, C., Stuart, L. M., Leong, J. M., & Fitzgerald, K. A. (2012) · Cell · doi:10.1016/j.cell.2012.07.007 · Cited by 729 · see citing works

Murine Caspase-11, an ICE-Interacting Protease, Is Essential for the Activation of ICE

Wang, S., Miura, M., Jung, Y., Zhu, H., Li, E., & Yuan, J. (1998) · Cell · doi:10.1016/s0092-8674(00)80943-5 · Cited by 699 · see citing works

Differential Requirement for Caspase-1 Autoproteolysis in Pathogen-Induced Cell Death and Cytokine Processing

Brož, P., von Moltke, J., Jones, J. W. M., Vance, R. E., & Monack, D. M. (2010) · Cell Host & Microbe · doi:10.1016/j.chom.2010.11.007 · Cited by 614 · see citing works

Melioidosis: insights into the pathogenicity of Burkholderia pseudomallei

Wiersinga, W. J., van der Poll, T., White, N. J., Day, N., & Peacock, S. J. (2006) · Nature Reviews Microbiology · doi:10.1038/nrmicro1385 · Cited by 586 · see citing works

Caspase-11 Protects Against Bacteria That Escape the Vacuole

Aachoui, Y., Leaf, I. A., Hagar, J. A., Fontana, M. F., Campos, C. G., Zak, D. E., Tan, M. H., Cotter, P. A., Vance, R. E., Aderem, A. A., et al. (2013) · Science · doi:10.1126/science.1230751 · Cited by 544 · see citing works

ASC, a Novel 22-kDa Protein, Aggregates during Apoptosis of Human Promyelocytic Leukemia HL-60 Cells

Masumoto, J., Taniguchi, S., Ayukawa, K., Sarvotham, H., Kishino, T., Niikawa, N., Hidaka, E., Katsuyama, T., Higuchi, T., & Sagara, J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.48.33835 · Cited by 542 · see citing works

Caspase-11 increases susceptibility to Salmonella infection in the absence of caspase-1

Broz, P., Ruby, T., Belhocine, K., Bouley, D. M., Kayagaki, N., Dixit, V. M., & Monack, D. M. (2012) · Nature · doi:10.1038/nature11419 · Cited by 535 · see citing works

AIM2 and NLRP3 inflammasomes activate both apoptotic and pyroptotic death pathways via ASC

Sagulenko, V., Thygesen, S. J., Sester, D. P., Idris, A., Cridland, J. A., Vajjhala, P. R., Roberts, T. L., Schroder, K., Vince, J. E., Hill, J. M., et al. (2013) · Cell Death and Differentiation · doi:10.1038/cdd.2013.37 · Cited by 511 · see citing works

Gain-of-Function Pyrin Mutations Induce NLRP3 Protein-Independent Interleukin-1β Activation and Severe Autoinflammation in Mice

Chae, J. J., Cho, Y.-H., Lee, G., Cheng, J., Liu, P. P., Feigenbaum, L., Katz, S. I., & Kastner, D. L. (2011) · Immunity · doi:10.1016/j.immuni.2011.02.020 · Cited by 473 · see citing works

Cutting Edge: Caspase-1 Independent IL-1β Production Is Critical for Host Resistance to Mycobacterium tuberculosis and Does Not Require TLR Signaling In Vivo

Mayer-Barber, K. D., Barber, D. L., Shenderov, K., White, S., Wilson, M. S., Cheever, A. W., Kugler, D. G., Hieny, S. E., Caspar, P., Núñez, G., et al. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0904189 · Cited by 472 · see citing works

Inflammasome-Dependent Release of the Alarmin HMGB1 in Endotoxemia

Lamkanfi, M., Sarkar, A., Walle, L. V., Vitari, A. C., Amer, A. O., Wewers, M. D., Tracey, K. J., Kanneganti, T., & Dixit, V. M. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1000803 · Cited by 468 · see citing works

Manipulation of Host Cell Death Pathways during Microbial Infections

Lamkanfi, M., & Dixit, V. M. (2010) · Cell Host & Microbe · doi:10.1016/j.chom.2010.06.007 · Cited by 450 · see citing works

Recognition of Bacteria by Inflammasomes

von Moltke, J., Ayres, J. S., Kofoed, E. M., Chavarría‐Smith, J., & Vance, R. E. (2012) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032712-095944 · Cited by 414 · see citing works

Many stimuli pull the necrotic trigger, an overview

Vanlangenakker, N., Berghe, T. V., & Vandenabeele, P. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.164 · Cited by 407 · see citing works

Innate immunity against Francisella tularensis is dependent on the ASC/caspase-1 axis

Mariathasan, S., Weiss, D. S., Dixit, V. M., & Monack, D. M. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20050977 · Cited by 402 · see citing works

Cell death and infection: A double-edged sword for host and pathogen survival

Ashida, H., Mimuro, H., Ogawa, M., Kobayashi, T., Sanada, T., Kim, M., & Sasakawa, C. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201108081 · Cited by 361 · see citing works

NLRP1 Inflammasome Activation Induces Pyroptosis of Hematopoietic Progenitor Cells

Masters, S. L., Gerlic, M., Metcalf, D., Preston, S., Pellegrini, M., O’Donnell, J. A., McArthur, K., Baldwin, T. M., Chevrier, S., Nowell, C. J., et al. (2012) · Immunity · doi:10.1016/j.immuni.2012.08.027 · Cited by 309 · see citing works

Caspase-11 stimulates rapid flagellin-independent pyroptosis in response to Legionella pneumophila

Case, C. L., Kohler, L. J., Lima, J. B., Strowig, T., de Zoete, M. R., Flavell, R. A., Zamboni, D. S., & Roy, C. R. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1211521110 · Cited by 272 · see citing works

AIM2/ASC triggers caspase-8-dependent apoptosis in Francisella-infected caspase-1-deficient macrophages

Pierini, R., Juruj, C., Perret, M., Jones, C., Mangeot, P.-E., Weiss, D. S., & Henry, T. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.51 · Cited by 268 · see citing works

Caspase-1-Mediated Activation of Interleukin-1β (IL-1β) and IL-18 Contributes to Innate Immune Defenses againstSalmonella entericaSerovar Typhimurium Infection

Raupach, B., Peuschel, S.-K., Monack, D. M., & Zychlinsky, A. (2006) · Infection and Immunity · doi:10.1128/iai.00417-06 · Cited by 255 · see citing works

Toll or Interleukin-1 Receptor (TIR) Domain-containing Adaptor Inducing Interferon-β (TRIF)-mediated Caspase-11 Protease Production Integrates Toll-like Receptor 4 (TLR4) Protein- and Nlrp3 Inflammasome-mediated Host Defense against Enteropathogens

Gurung, P., Malireddi, R. K. S., Anand, P., Demon, D., Walle, L. V., Liu, Z., Vogel, P., Lamkanfi, M., & Kanneganti, T. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.401406 · Cited by 239 · see citing works

C/EBP Homologous Protein (CHOP) Is Crucial for the Induction of Caspase-11 and the Pathogenesis of Lipopolysaccharide-Induced Inflammatio

Endo, M., Mori, M., Akira, S., & Gotoh, T. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.10.6245 · Cited by 221 · see citing works

Modulation of Inflammasome Pathways by Bacterial and Viral Pathogens

Lamkanfi, M., & Dixit, V. M. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1100229 · Cited by 217 · see citing works

CLEC5A is critical for dengue virus–induced inflammasome activation in human macrophages

Wu, M., Chen, S.-T., Yang, A., Lin, W., Lin, Y., Chen, N., Tsai, I.-S., Li, L., & Hsieh, S.-L. E. (2012) · Blood · doi:10.1182/blood-2012-05-430090 · Cited by 212 · see citing works

ASC is an activating adaptor for NF-κB and caspase-8-dependent apoptosis

Masumoto, J., Dowds, T. A., Schaner, P. E., Chen, F. F., Ogura, Y., Li, M., Li, Z., Katsuyama, T., Sagara, J., Taniguchi, S., et al. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00309-7 · Cited by 209 · see citing works

Inflammasome-dependent Pyroptosis and IL-18 Protect against Burkholderia pseudomallei Lung Infection while IL-1β Is Deleterious

Ceballos‐Olvera, I., Sahoo, M., Miller, M. A., del Barrio, L., & Re, F. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002452 · Cited by 208 · see citing works

The Yersinia Virulence Effector YopM Binds Caspase-1 to Arrest Inflammasome Assembly and Processing

LaRock, C. N., & Cookson, B. T. (2012) · Cell Host & Microbe · doi:10.1016/j.chom.2012.10.020 · Cited by 207 · see citing works

Caspase-11 Promotes the Fusion of Phagosomes Harboring Pathogenic Bacteria with Lysosomes by Modulating Actin Polymerization

Akhter, A., Caution, K., Khweek, A. A., Tazi, M., Abdulrahman, B., Abdelaziz, D. H., Voss, O. H., Doseff, A. I., Hassan, H., Azad, A. K., et al. (2012) · Immunity · doi:10.1016/j.immuni.2012.05.001 · Cited by 185 · see citing works

Adenovirus Membrane Penetration Activates the NLRP3 Inflammasome

Barlan, A., Griffin, T., McGuire, K. A., & Wiethoff, C. M. (2010) · Journal of Virology · doi:10.1128/jvi.01265-10 · Cited by 181 · see citing works

Caspase-11 Gene Expression in Response to Lipopolysaccharide and Interferon-γ Requires Nuclear Factor-κB and Signal Transducer and Activator of Transcription (STAT) 1

Schauvliege, R., Vanrobaeys, J., Schotte, P., & Beyaert, R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207852200 · Cited by 162 · see citing works

Granuloma Formation and Host Defense in Chronic Mycobacterium tuberculosis Infection Requires PYCARD/ASC but Not NLRP3 or Caspase-1

McElvania, E., Allen, I. C., Hulseberg, P. D., Sullivan, J. T., McCann, J. R., Sándor, M., Braunstein, M., & Ting, J. P. ‐. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012320 · Cited by 155 · see citing works

Caspase-1 Regulates Escherichia coli Sepsis and Splenic B Cell Apoptosis Independently of Interleukin-1β and Interleukin-18

Sarkar, A., Hall, M. W., Exline, M. C., Hart, J., Knatz, N. L., Gatson, N. T., & Wewers, M. D. (2006) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200604-546oc · Cited by 150 · see citing works

Listeria monocytogenes engineered to activate the Nlrc4 inflammasome are severely attenuated and are poor inducers of protective immunity

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 · see citing works

Roles of caspase-1 in Listeria infection in mice

Tsuji, N. M. (2004) · International Immunology · doi:10.1093/intimm/dxh041 · Cited by 120 · see citing works

Evolution of inflammasome functions in vertebrates: Inflammasome and caspase-1 trigger fish macrophage cell death but are dispensable for the processing of IL-1β

Angosto-Bazarra, D., López‐Castejón, G., López‐Muñoz, A., Sepulcre, M. P., Arizcún, M., Meseguer, J., & Mulero, V. (2012) · Innate Immunity · doi:10.1177/1753425912441956 · Cited by 91 · see citing works

Molecular cell death platforms and assemblies

Mace, P. D., & Riedl, S. J. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2010.08.004 · Cited by 90 · see citing works

Asc Modulates the Function of NLRC4 in Response to Infection of Macrophages by Legionella pneumophila

Case, C. L., & Roy, C. R. (2011) · mBio · doi:10.1128/mbio.00117-11 · Cited by 85 · see citing works

Inflammasomes and viruses: cellular defence versus viral offence

Gram, A. M., Frenkel, J., & Ressing, M. E. (2012) · Journal of General Virology · doi:10.1099/vir.0.042978-0 · Cited by 74 · see citing works

Caspase-1 activity is required to bypass macrophage apoptosis upon Salmonella infection

Puri, A. W., Brož, P., Shen, A., Monack, D. M., & Bogyo, M. S. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.1023 · Cited by 66 · see citing works

Hypoxic induction of caspase-11/caspase-1/interleukin-1β in brain microglia

Kim, N.-G., Lee, H., Son, E., Kwon, O.-Y., Park, J., Park, J.-H., Cho, G. J., Choi, W. S., & Suk, K. (2003) · Molecular Brain Research · doi:10.1016/s0169-328x(03)00135-9 · Cited by 59 · see citing works

Viral strategies for the evasion of immunogenic cell death

Galluzzi, L., Kepp, O., Morselli, E., Vitale, I., Senovilla, L., Pinti, M., Zitvogel, L., & Kroemer, G. (2010) · Journal of Internal Medicine · doi:10.1111/j.1365-2796.2010.02223.x · Cited by 58 · see citing works

Induction of caspase‐11 by inflammatory stimuli in rat astrocytes: lipopolysaccharide induction through p38 mitogen‐activated protein kinase pathway

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Asc-Dependent and Independent Mechanisms Contribute to Restriction of Legionella Pneumophila Infection in Murine Macrophages

Abdelaziz, D. H., Gavrilin, M. A., Akhter, A., Caution, K., Kotrange, S., Khweek, A. A., Abdulrahman, B., Hassan, Z. A., El-Sharkawi, F., Bedi, S., et al. (2011) · Frontiers in Microbiology · doi:10.3389/fmicb.2011.00018 · Cited by 41 · see citing works

Generation of a Listeria vaccine strain by enhanced caspase‐1 activation

Warren, S. E., Duong, H., Mao, D. P., Armstrong, A. M., Rajan, J. V., Miao, E. A., & Aderem, A. A. (2011) · European Journal of Immunology · doi:10.1002/eji.201041214 · Cited by 35 · see citing works

A Recombination Hotspot in a Schizophrenia-Associated Region of GABRB2

Ng, S.-K., Lo, W.-S., Pun, F. W., Zhao, C., Yu, Z., Chen, J., Tong, K.-L., Xu, Z., Tsang, S., Yang, Q., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009547 · Cited by 31 · see citing works

Activation of ASC induces apoptosis or necrosis, depending on the cell type, and causes tumor eradication

Motani, K., Kawase, K., Imamura, R., Kinoshita, T., Kushiyama, H., & Suda, T. (2010) · Cancer Science · doi:10.1111/j.1349-7006.2010.01610.x · Cited by 26 · see citing works

Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018.

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Pyroptosis: 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 · see citing works

Cell death: a review of the major forms of apoptosis, necrosis and autophagy

D'Arcy, M. (2019) · Cell Biology International · doi:10.1002/cbin.11137 · Cited by 2,324 · see citing works

Pyroptosis: A new frontier in cancer

Fang, Y., Tian, S., Pan, Y., Li, W., Wang, Q., Tang, Y. R., Yu, T., Wu, X., Shi, Y., Ma, P., et al. (2019) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2019.109595 · Cited by 1,055 · see citing works

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 1,014 · see citing works

Guidelines for the use of flow cytometry and cell sorting in immunological studies (second edition)

Cossarizza, A., Chang, H., Radbruch, A., Acs, A., Adam, D., Adam‐Klages, S., Agace, W. W., Aghaeepour, N., Akdiş, M., Allez, M., et al. (2019) · European Journal of Immunology · doi:10.1002/eji.201970107 · Cited by 982 · see citing works

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 815 · see citing works

Gasdermin D in pyroptosis

Burdette, B. E., Esparza, A. N., Zhu, H., & Wang, S. (2021) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2021.02.006 · Cited by 710 · see citing works

Statins: a repurposed drug to fight cancer

Jiang, W., Hu, J.-W., He, X.-R., Jin, W.-L., & He, X.-Y. (2021) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-021-02041-2 · Cited by 417 · see citing works

Apoptosis, Pyroptosis, and Necroptosis—Oh My! The Many Ways a Cell Can Die

Ketelut-Carneiro, N., & Fitzgerald, K. A. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167378 · Cited by 418 · see citing works

Recent Insights into the Molecular Mechanisms Underlying Pyroptosis and Gasdermin Family Functions

Aglietti, R. A., & Dueber, E. C. (2017) · Trends in Immunology · doi:10.1016/j.it.2017.01.003 · Cited by 409 · see citing works

NLRP3 Inflammasome Activation‐Mediated Pyroptosis Aggravates Myocardial Ischemia/Reperfusion Injury in Diabetic Rats

Qiu, Z., Lei, S., Zhao, B., Wu, Y., Su, W., Liu, M., Meng, Q., Zhou, B., Leng, Y., & Xia, Z. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/9743280 · Cited by 351 · see citing works

Diversity and complexity of cell death: a historical review

Park, W., Wei, S., Kim, B., Kim, B., Bae, S., Chae, Y. C., Ryu, D., & Ha, K. (2023) · Experimental & Molecular Medicine · doi:10.1038/s12276-023-01078-x · Cited by 364 · see citing works

Pyroptosis and its relationship to atherosclerosis

Xu, Y., Zheng, L., Hu, Y., & Wang, Q. (2017) · Clinica Chimica Acta · doi:10.1016/j.cca.2017.11.005 · Cited by 322 · see citing works

Cell Death in Liver Diseases: A Review

Shojaie, L., Iorga, A., & Dara, L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249682 · Cited by 299 · see citing works

Focus on the Role of NLRP3 Inflammasome in Diseases

Fusco, R., Siracusa, R., Genovese, T., Cuzzocrea, S., & Paola, R. D. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21124223 · Cited by 292 · see citing works

K+ Efflux Agonists Induce NLRP3 Inflammasome Activation Independently of Ca2+ Signaling

Katsnelson, M. J., Rucker, L. G., Russo, H. M., & Dubyak, G. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1402658 · Cited by 278 · see citing works

Mechanism and regulation of pyroptosis-mediated in cancer cell death

Ruan, J., Wang, S., & Wang, J. (2020) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2020.109052 · Cited by 274 · see citing works

Role of pyroptosis in cardiovascular diseases

Jia, C., Chen, H. A., Zhang, J., Zhou, K., Zhuge, Y., Niu, C., Qiu, J., Rong, X., Shi, Z., Xiao, J., et al. (2018) · International Immunopharmacology · doi:10.1016/j.intimp.2018.12.028 · Cited by 268 · see citing works

Mechanism of membrane pore formation by human gasdermin‐D

Mulvihill, E., Sborgi, L., Mari, S. A., Pfreundschuh, M., Hiller, S., & Müller, D. J. (2018) · The EMBO Journal · doi:10.15252/embj.201798321 · Cited by 263 · see citing works

Emerging insights into molecular mechanisms underlying pyroptosis and functions of inflammasomes in diseases

Lu, F., Lan, Z., Xin, Z., He, C., Guo, Z., Xia, X., & Hu, T. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.29268 · Cited by 248 · see citing works

Inflammasome-Mediated Inflammation in Liver Ischemia-Reperfusion Injury

Jiménez‐Castro, M. B., Cornide‐Petronio, M. E., Gracia‐Sancho, J., & Peralta, C. (2019) · Cells · doi:10.3390/cells8101131 · Cited by 243 · see citing works

Role of pyroptosis in spinal cord injury and its therapeutic implications

Mamun, A. A., Wu, Y., Monalisa, I., Jia, C., Zhou, K., Munir, F., & Xiao, J. (2020) · Journal of Advanced Research · doi:10.1016/j.jare.2020.08.004 · Cited by 230 · see citing works

Ischemia-reperfusion induces renal tubule pyroptosis via the CHOP-caspase-11 pathway

Yang, J., Yao, F.-H., Zhang, J., Ji, Z.-Y., Li, K., Zhan, J., Tong, Y., Lin, L.-R., & He, Y. (2013) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00117.2013 · Cited by 226 · see citing works

Canonical and Non-Canonical Activation of NLRP3 Inflammasome at the Crossroad between Immune Tolerance and Intestinal Inflammation

Pellegrini, C., Antonioli, L., López‐Castejón, G., Blandizzi, C., & Fornai, M. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00036 · Cited by 212 · see citing works

Metabolic Remodeling, Inflammasome Activation, and Pyroptosis in Macrophages Stimulated by Porphyromonas gingivalis and Its Outer Membrane Vesicles

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Betulinic acid inhibits pyroptosis in spinal cord injury by augmenting autophagy via the AMPK-mTOR-TFEB signaling pathway

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