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Inhibitor of Apoptosis Proteins Limit RIP3 Kinase-Dependent Interleukin-1 Activation
Open accessAbstract
Interleukin-1β (IL-1β) is a potent inflammatory cytokine that is usually cleaved and activated by inflammasome-associated caspase-1. To determine whether IL-1β activation is regulated by inhibitor of apoptosis (IAP) proteins, we treated macrophages with an IAP-antagonist "Smac mimetic" compound or genetically deleted the genes that encode the three IAP family members cIAP1, cIAP2, and XIAP. After Toll-like receptor priming, IAP inhibition triggered cleavage of IL-1β that was mediated not only by the NLRP3-caspase-1 inflammasome, but also by caspase-8 in a caspase-1-independent manner. In the absence of IAPs, rapid and full generation of active IL-1β by the NLRP3-caspase-1 inflammasome, or by caspase-8, required the kinase RIP3 and reactive oxygen species production. These results demonstrate that activation of the cell death-inducing ripoptosome platform and RIP3 can generate bioactive IL-1β and implicate them as additional targets for the treatment of pathological IL-1-driven inflammatory responses.
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“Importantly, multiple components of the molecular machinery for necroptosis—including ZBP1, RIPK3, MLKL, and TNFR1 (mainly via NF-κB)—impinge on the control of the so-called “inflammasome”, a supramolecular platform for the activation of CASP1 and consequent secretion of mature interleukin 1 beta (IL1B; best known as IL-1β) and IL18 [524–529].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [526]
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Cites
A role for mitochondria in nlrp3 inflammasome activation
Zhou, R., Yazdi, A. S., Menu, P., & Tschopp, J. (2011) · Nature · doi:10.1038/nature09663 · Cited by 5,602
Self-citationSchroder, K., & Tschopp, J. (2010) · Cell · doi:10.1016/j.cell.2010.01.040 · Cited by 5,475
Self-citationBauernfeind, F. G., Horvath, G. L., Stutz, A., Alnemri, E. S., MacDonald, K. L., Speert, D. P., Fernandes‐Alnemri, T., Wu, J., Monks, B. G., Fitzgerald, K. A., et al. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0901363 · Cited by 3,087
Hornung, V., Bauernfeind, F., Halle, A., Samstad, E. O., Kono, H., Rock, K. L., Fitzgerald, K. A., & Latz, E. (2008) · Nature Immunology · doi:10.1038/ni.1631 · Cited by 3,065
Nakahira, K., Haspel, J. A., Rathinam, V. A. K., Lee, S.-J., Dolinay, T., Lam, H. C., Englert, J. A., Rabinovitch, M., Cernadas, M., Kim, H. P., et al. (2011) · Nature Immunology · doi:10.1038/ni.1980 · Cited by 3,049
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 NALP3 inflammasome is involved in the innate immune response to amyloid-β
Halle, A., Hornung, V., Petzold, G. C., Stewart, C. R., Monks, B. G., Reinheckel, T., Fitzgerald, K. A., Latz, E., Moore, K. J., & Golenbock, D. T. (2008) · Nature Immunology · doi:10.1038/ni.1636 · Cited by 2,441
Cho, Y., Challa, S., Moquin, D., Genga, R., Ray, T. D., Guildford, M., & Chan, F. K.-M. (2009) · Cell · doi:10.1016/j.cell.2009.05.037 · Cited by 2,435
Molecular mechanisms of necroptosis: an ordered cellular explosion
Vandenabeele, P., Galluzzi, L., Vanden Berghe, T., & Kroemer, G. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2970 · Cited by 2,382
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
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Items 101–200 of 491
Inflammasomes and host defenses against bacterial infections
Vladimer, G. I., Marty-Roix, R., Ghosh, S., Weng, D., & Lien, E. (2013) · Current Opinion in Microbiology · doi:10.1016/j.mib.2012.11.008 · Cited by 173
Murakami, Y., Matsumoto, H., Roh, M., Suzuki, J., Hisatomi, T., Ikeda, Y., Miller, J. W., & Vavvas, D. G. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1206937109 · Cited by 174
IL-1 family cytokines trigger sterile inflammatory disease
Lukens, J. R., Gross, J. M., & Kanneganti, T. (2012) · Frontiers in Immunology · doi:10.3389/fimmu.2012.00315 · Cited by 178
The Diversification of Cell Death and Immunity: Memento Mori
Legrand, A. J., Konstantinou, M., Goode, E., & Meier, P. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.09.006 · Cited by 181
The intersection of cell death and inflammasome activation
Vince, J. E., & Silke, J. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2205-2 · Cited by 180
Self-citationFueling the Fire: Inflammatory Forms of Cell Death and Implications for Cancer Immunotherapy
Rosenbaum, S. R., Wilski, N. A., & Aplin, A. E. (2021) · Cancer Discovery · doi:10.1158/2159-8290.cd-20-0805 · Cited by 177
López‐Castejón, G., Luheshi, N., Compan, V., High, S., Whitehead, R. C., Flitsch, S. L., Kirov, A., Prudovsky, I. A., Swanton, E., & Brough, D. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.422238 · Cited by 175
Caspase-8-Dependent Inflammatory Responses Are Controlled by Its Adaptor, FADD, and Necroptosis
Tummers, B., Mari, L., Guy, C. S., Heckmann, B. L., Rodríguez, D. A., Rühl, S., Moretti, J., Crawford, J. C., Fitzgerald, P., Kanneganti, T., et al. (2020) · Immunity · doi:10.1016/j.immuni.2020.04.010 · Cited by 166
Structure, Activation and Regulation of NLRP3 and AIM2 Inflammasomes
Sharma, M., & de Alba, E. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020872 · Cited by 173
Necroptosis, in vivo detection in experimental disease models
Jouan-Lanhouet, S., Riquet, F. B., Duprez, L., Berghe, T. V., Takahashi, N., & Vandenabeele, P. (2014) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2014.08.010 · Cited by 166
Polykratis, A., Martens, A., Eren, R. O., Shirasaki, Y., Yamagishi, M., Yamaguchi, Y., Uemura, S., Miura, M., Holzmann, B., Kollias, G. A., et al. (2019) · Nature Cell Biology · doi:10.1038/s41556-019-0324-3 · Cited by 162
Schwarzer, R., Laurien, L., & Pasparakis, M. (2020) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2020.02.004 · Cited by 162
Caspase crosstalk: integration of apoptotic and innate immune signalling pathways
Creagh, E. M. (2014) · Trends in Immunology · doi:10.1016/j.it.2014.10.004 · Cited by 164
A RIPK3–Caspase 8 Complex Mediates Atypical Pro–IL-1β Processing
Moriwaki, K., Bertin, J., Gough, P. J., & Chan, F. K.-M. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1402167 · Cited by 164
Wong, W. W.-L., Vince, J. E., Lalaoui, N., Lawlor, K. E., Chau, D., Bankovacki, A., Anderton, H., Metcalf, D., O’Reilly, L. A., Jost, P. J., et al. (2014) · Blood · doi:10.1182/blood-2013-06-510743 · Cited by 159
Self-citationThe pathological features of regulated necrosis
Tonnus, W., Meyer, C., Paliege, A., Belavgeni, A., von Mäßenhausen, A., Bornstein, S. R., Hugo, C., Becker, J. U., & Linkermann, A. (2019) · The Journal of Pathology · doi:10.1002/path.5248 · Cited by 168
Protective Roles for Caspase-8 and cFLIP in Adult Homeostasis
Weinlich, R., Oberst, A., Dillon, C. P., Janke, L. J., Milasta, S., Lukens, J. R., Rodriguez, D. A., Gurung, P., Savage, C., Kanneganti, T. D., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.08.045 · Cited by 157
Shenderov, K., Riteau, N., Yip, R. H. N., Mayer-Barber, K. D., Oland, S., Hieny, S. E., Fitzgerald, P., Oberst, A., Dillon, C. P., Green, D. R., et al. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1302549 · Cited by 156
Staying Alive: Cell Death in Antiviral Immunity
Upton, J. W., & Chan, F. K.-M. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.01.027 · Cited by 160
XIAP variants in male Crohn's disease
Zeißig, Y., Petersen, B., Milutinovic, S., Bosse, E., Mayr, G., Peuker, K., Hartwig, J., Keller, A., Kohl, M., Laass, M. W., et al. (2014) · Gut · doi:10.1136/gutjnl-2013-306520 · Cited by 156
A RIPK2 inhibitor delays NOD signalling events yet prevents inflammatory cytokine production
Nachbur, U., Stafford, C. A., Bankovacki, A., Zhan, Y., Lindqvist, L., Fiil, B. K., Khakham, Y., Ko, H., Sandow, J. J., Falk, H., et al. (2015) · Nature Communications · doi:10.1038/ncomms7442 · Cited by 148
Self-citationCondon, S. M., Mitsuuchi, Y., Deng, Y., LaPorte, M. G., Rippin, S. R., Haimowitz, T., Alexander, M. D., Kumar, P. T., Hendi, M. S., Lee, Y.-H., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm500176w · Cited by 156
Self-citationViral modulation of programmed necrosis
Kaiser, W. J., Upton, J. W., & Mocarski, E. S. (2013) · Current Opinion in Virology · doi:10.1016/j.coviro.2013.05.019 · Cited by 151
Modulation of immune signalling by inhibitors of apoptosis
Beug, S. T., Cheung, H. H., LaCasse, E. C., & Korneluk, R. G. (2012) · Trends in Immunology · doi:10.1016/j.it.2012.06.004 · Cited by 156
The Role of Inflammasome-Dependent and Inflammasome-Independent NLRP3 in the Kidney
Kim, Y., Kim, S., Kim, K., Lee, S.-H., & Moon, J.-Y. (2019) · Cells · doi:10.3390/cells8111389 · Cited by 157
Disease‐causing mutations in the XIAP BIR2 domain impair NOD2‐dependent immune signalling
Damgaard, R. B., Fiil, B. K., Speckmann, C., Yabal, M., Stadt, U. Z., Bekker‐Jensen, S., Jost, P. J., Ehl, S. R., Mailand, N., & Gyrd‐Hansen, M. (2013) · EMBO Molecular Medicine · doi:10.1002/emmm.201303090 · Cited by 152
The walking dead: macrophage inflammation and death in atherosclerosis
Kavurma, M. M., Rayner, K. J., & Karunakaran, D. (2017) · Current Opinion in Lipidology · doi:10.1097/mol.0000000000000394 · Cited by 146
XIAP deficiency syndrome in humans
Latour, S., & Aguilar, C. (2015) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2015.01.015 · Cited by 148
Control of the inflammasome by the ubiquitin system
López‐Castejón, G. (2019) · FEBS Journal · doi:10.1111/febs.15118 · Cited by 146
Future Therapeutic Directions for Smac-Mimetics
Morrish, E., Brumatti, G., & Silke, J. (2020) · Cells · doi:10.3390/cells9020406 · Cited by 151
Self-citationCell death in chronic inflammation: breaking the cycle to treat rheumatic disease
Anderton, H., Wicks, I. P., & Silke, J. (2020) · Nature Reviews Rheumatology · doi:10.1038/s41584-020-0455-8 · Cited by 152
Self-citationSimpson, D. S., Pang, J., Weir, A. L., Kong, I. Y., Fritsch, M., Rashidi, M., Cooney, J. P., Davidson, K. C., Speir, M., Djajawi, T. M., et al. (2022) · Immunity · doi:10.1016/j.immuni.2022.01.003 · Cited by 146
Self-citationLinear ubiquitination in immunity
Shimizu, Y., Taraborrelli, L., & Walczak, H. (2015) · Immunological Reviews · doi:10.1111/imr.12309 · Cited by 139
Lawlor, K. E., Feltham, R., Yabal, M., Conos, S. A., Chen, K. W., Ziehe, S., Graß, C., Zhan, Y., Nguyen, T. A., Hall, C. M., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.06.073 · Cited by 139
Self-citationOpdenbosch, N. V., Gorp, H. V., Verdonckt, M., Saavedra, P. H. V., de Vasconcelos, N. M., Gonçalves, A. C., Walle, L. V., Demon, D., Matusiak, M., Hauwermeiren, F. V., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.11.088 · Cited by 137
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
IAP proteins as targets for drug development in oncology
Dubrez, L., Berthelet, J., & Glorian, V. (2013) · OncoTargets and Therapy · doi:10.2147/ott.s33375 · Cited by 143
The Two Faces of Receptor Interacting Protein Kinase-1
Weinlich, R., & Green, D. R. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.11.001 · Cited by 132
An outline of necrosome triggers
Berghe, T. V., Hassannia, B., & Vandenabeele, P. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2189-y · Cited by 134
Activation of necroptosis in human and experimental cholestasis
Afonso, M. B., Rodrigues, P. M., Simão, A. L., Ofengeim, D., Carvalho, T., Amaral, J. D., Gaspar, M. M., Cortez‐Pinto, H., Castro, R. E., Yuan, J., et al. (2016) · Cell Death and Disease · doi:10.1038/cddis.2016.280 · Cited by 129
Ganesan, S., Rathinam, V. A. K., Bossaller, L., Army, K., Kaiser, W. J., Mocarski, E. S., Dillon, C. P., Green, D. R., Mayadas, T. N., Levitz, S. M., et al. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1400276 · Cited by 134
Latour, S., & Fischer, A. (2019) · Immunological Reviews · doi:10.1111/imr.12791 · Cited by 135
Retinal Inflammation, Cell Death and Inherited Retinal Dystrophies
Olivares‐González, L., Velasco, S., Campillo, I., & Rodrigo, R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22042096 · Cited by 135
IAP Family of Cell Death and Signaling Regulators
Silke, J., & Vucic, D. (2014) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-801430-1.00002-0 · Cited by 138
Self-citationNew Dawn for Atherosclerosis: Vascular Endothelial Cell Senescence and Death
Bu, L.-L., Yuan, H., Xie, L., Guo, M.-H., Liao, D., & Zheng, X. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242015160 · Cited by 133
A long-awaited merger of the pathways mediating host defence and programmed cell death
Blander, J. M. (2014) · Nature reviews. Immunology · doi:10.1038/nri3720 · Cited by 127
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Gaidt, M. M., & Hornung, V. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.11.013 · Cited by 124
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Feltham, R., Vince, J. E., & Lawlor, K. E. (2017) · Clinical & Translational Immunology · doi:10.1038/cti.2016.83 · Cited by 124
Self-citationAmbiguities in NLRP3 inflammasome regulation: Is there a role for mitochondria?
Lawlor, K. E., & Vince, J. E. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.08.014 · Cited by 124
Self-citationLatour, S., & Winter, S. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01103 · Cited by 119
Antonopoulos, C. H., Sanadi, C. E. E., Kaiser, W. J., Mocarski, E. S., & Dubyak, G. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1300645 · Cited by 115
Wang, W., Dernst, A., Martin, B., Lorenzi, L., Cadefau-Fabregat, M., Phulphagar, K. M., Wagener, A., Budden, C. F., Stair, N., Wagner, T. M., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114736 · Cited by 116
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Dhillon, B., Aleithan, F., Sater, Z. A., & Sater, A. A. A. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00104 · Cited by 123
Redox control of NLRP3 inflammasome activation in health and disease
Rubartelli, A. (2012) · Journal of Leukocyte Biology · doi:10.1189/jlb.0512265 · Cited by 114
Schmidt, S. V., Seibert, S., Walch‐Rückheim, B., Vicinus, B., Kamionka, E.-M., Pahne‐Zeppenfeld, J., Solomayer, E., Kim, Y.-J., Bohle, R. M., & Smola, S. (2015) · Oncotarget · doi:10.18632/oncotarget.3249 · Cited by 112
Cong, H., Xu, L., Wu, Y., Qu, Z., Bian, T., Zhang, W., Xing, C., & Zhuang, C. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01668 · Cited by 119
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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
Self-citationZinc depletion regulates the processing and secretion of IL-1β
Summersgill, H. R., England, H., López‐Castejón, G., Lawrence, C. B., Luheshi, N., Pahle, J., Mendes, P., & Brough, D. (2014) · Cell Death and Disease · doi:10.1038/cddis.2013.547 · Cited by 112
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Pedersen, J., LaCasse, E. C., Seidelin, J. B., Coskun, M., & Nielsen, O. H. (2014) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2014.09.006 · Cited by 105
Aguilar, C., & Latour, S. (2015) · Journal of Clinical Immunology · doi:10.1007/s10875-015-0141-9 · Cited by 104
Necroptosis induced by RIPK3 requires MLKL but not Drp1
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The Inflammatory Signal Adaptor RIPK3: Functions Beyond Necroptosis
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RIP3 dependent NLRP3 inflammasome activation is implicated in acute lung injury in mice
Chen, J., Wang, S., Fu, R., Zhou, M., Zhang, T., Pan, W., Yang, N., & Huang, Y. (2018) · Journal of Translational Medicine · doi:10.1186/s12967-018-1606-4 · Cited by 105
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Self-citationCell 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
Self-citationProgrammed necrosis in microbial pathogenesis
Sridharan, H., & Upton, J. W. (2014) · Trends in Microbiology · doi:10.1016/j.tim.2014.01.005 · Cited by 103
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Greaney, A. J., Leppla, S. H., & Moayeri, M. (2015) · Frontiers in Immunology · doi:10.3389/fimmu.2015.00570 · Cited by 101
IAPs, regulators of innate immunity and inflammation
Estornes, Y., & Bertrand, M. J. M. (2014) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2014.03.035 · Cited by 106
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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
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
Regulation of Cell Death and Immunity by XIAPPreprint
Jost, P. J., & Vucic, D. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a036426 · Cited by 98
Necroptosis-independent signaling by the RIP kinases in inflammation
Moriwaki, K., & Chan, F. K.-M. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2203-4 · Cited by 99
Necroptosis promotes autophagy-dependent upregulation of DAMP and results in immunosurveillance
Lin, S., Hsieh, S., Fan, Y.-T., Wei, W., Hsiao, P., Tsai, D.-H., Wu, T., & Yang, N. (2017) · Autophagy · doi:10.1080/15548627.2017.1386359 · Cited by 96
NLRP3 Ubiquitination—A New Approach to Target NLRP3 Inflammasome Activation
Akther, M., Haque, M. E., Park, J., Kang, T., & Lee, K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22168780 · Cited by 95
Zhang, X., Fan, C., Zhang, H., Zhao, Q., Liu, Y., Xu, C., Xie, Q., Wu, X., Yu, X., Zhang, J., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.06.103 · Cited by 93
Khan, N. R., Lawlor, K. E., Murphy, J. M., & Vince, J. E. (2013) · Current Opinion in Immunology · doi:10.1016/j.coi.2013.10.017 · Cited by 93
Self-citationEvolution of Our Understanding of XIAP Deficiency
Mudde, A. C. A., Booth, C., & Marsh, R. A. (2021) · Frontiers in Pediatrics · doi:10.3389/fped.2021.660520 · Cited by 92
The role of caspase-8 in inflammatory signalling and pyroptotic cell death
Pang, J., & Vince, J. E. (2023) · Seminars in Immunology · doi:10.1016/j.smim.2023.101832 · Cited by 90
Self-citationVijayaraj, S. L., Feltham, R., Rashidi, M., Frank, D. O., Liu, Z., Simpson, D. S., Ebert, G., Vince, A. J., Herold, M. J., Kueh, A. J., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-22979-3 · Cited by 88
Self-citationRecent advances in understanding inhibitor of apoptosis proteins
Lalaoui, N., & Vaux, D. L. (2018) · F1000Research · doi:10.12688/f1000research.16439.1 · Cited by 88
Loss of XIAP facilitates switch to TNFα-induced necroptosis in mouse neutrophils
Wicki, S., Gurzeler, U., Wong, W. W.-L., Jost, P. J., Bachmann, D., & Kaufmann, T. (2016) · Cell Death and Disease · doi:10.1038/cddis.2016.311 · Cited by 85
Self-citationNecrosis-dependent and independent signaling of the RIP kinases in inflammation
Moriwaki, K., & Chan, F. K.-M. (2013) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2013.12.013 · Cited by 84
Regulation and Function of the Caspase-1 in an Inflammatory Microenvironment
Lee, D.-J., Du, F., Chen, S., Nakasaki, M., Rana, I., Shih, V. F.-S., Hoffmann, A., & Jamora, C. (2015) · Journal of Investigative Dermatology · doi:10.1038/jid.2015.119 · Cited by 82
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Wang, L., Wang, T., Li, H., Liu, Q. L., Zhang, Z., Xie, W., Feng, Y., Socorburam, T., Wu, G., Xia, Z., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0155723 · Cited by 80
Hu, Z., Murakami, T., Tamura, H., Reich, J., Kuwahara‐Arai, K., Iba, T., Tabe, Y., & Nagaoka, I. (2017) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2017.2870 · Cited by 79
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Speir, M., & Lawlor, K. E. (2020) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2020.07.011 · Cited by 78
Self-citationLiu, Z.-M., Chen, Q., Chen, Z., Tian, D., Li, M., Wang, J., Wang, L., Liu, B., Zhang, S., Li, F., et al. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.02.150 · Cited by 78
Hughes, S. A., Lin, M., Weir, A. L., Huang, B., Xiong, L., Chua, N. K., Pang, J., Santavanond, J. P., Tixeira, R., Doerflinger, M., et al. (2023) · The EMBO Journal · doi:10.15252/embj.2021110468 · Cited by 75
Self-citationKataoka, K., Matsumoto, H., Kaneko, H., Notomi, S., Takeuchi, K., Sweigard, J. H., Atik, A., Murakami, Y., Connor, K. M., Terasaki, H., et al. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.73 · Cited by 75
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Vandenabeele, P., & Bertrand, M. J. M. (2012) · Nature reviews. Immunology · doi:10.1038/nri3325 · Cited by 75
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Tonnus, W., Belavgeni, A., Beuschlein, F., Eisenhofer, G., Faßnacht, M., Kroiß, M., Krone, N. P., Reincke, M., Bornstein, S. R., & Linkermann, A. (2021) · Nature Reviews Endocrinology · doi:10.1038/s41574-021-00499-w · Cited by 74
Monie, T. P., & Bryant, C. E. (2015) · Immunological Reviews · doi:10.1111/imr.12284 · Cited by 74
Shutinoski, B., Alturki, N. A., Rijal, D., Bertin, J., Gough, P. J., Schlossmacher, M. G., & Sad, S. (2016) · Cell Death and Differentiation · doi:10.1038/cdd.2016.51 · Cited by 71
Metadata
- Authors
- Vince, J. E., Wong, W. W.-L., Gentle, I., Lawlor, K. E., Allam, R., O'Reilly, L., Mason, K., Gross, O., Ma, S., Guarda, G., Anderton, H., Castillo, R., Häcker, G., Silke, J., & Tschopp, J.
- Affiliations
- University of Lausanne (CH)
- The University of Melbourne (AU)
- University of Freiburg (DE)
- Corresponding author
- Vince, James E.
- ORCID
- Venue
- Immunity
- Publisher
- Elsevier BV
- Published
- 2012-02
- Volume
- 36
- Issue
- 2
- Pages
- 215-227
- ISSN
- 1074-7613 (ISSN-L)
- OpenAlex
- W2087968540
- Cited by
- 491
- References
- 62
- Citations by year
- 2026: 9 · 2025: 22 · 2024: 22 · 2023: 22 · 2022: 33 · 2021: 28 · 2020: 37 · 2019: 28 · 2018: 40 · 2017: 33 · 2016: 41 · 2015: 43 · 2014: 73 · 2013: 38 · 2012: 20
- FWCI
- 22.39
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 532 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Immunity (publishedVersion)
- PubMed (publishedVersion)
- Zurich Open Repository and Archive (University of Zurich) (acceptedVersion, other-oa)
- IRIS (submittedVersion)
- mediaTUM – the media and publications repository of the Technical University Munich (Technical University Munich) (submittedVersion)
- SERVAL (Université de Lausanne) (submittedVersion)
- Zurich Open Repository and Archive (University of Zurich) (submittedVersion, other-oa)
- Zurich Open Repository and Archive (University of Zurich)
- Funders
- Australian Government
- State Government of Victoria
- Deutsche Krebshilfe
- National Health and Medical Research Council
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Keywords
- inhibitor of apoptosis proteins, caspase-8, NLRP3 inflammasome, caspase-1, IAP antagonists, cIAP1, cIAP2, XIAP, ripoptosome, reactive oxygen species, macrophages, Toll-like receptors, inflammatory cytokines
- MeSH terms
- NLR Family, Pyrin Domain-Containing 3 Protein, Baculoviral IAP Repeat-Containing 3 Protein, Animals, Carrier Proteins, Macrophages, Apoptosis, Reactive Oxygen Species, Mice, Knockout, Molecular Mimicry, Caspase 1, Mitochondrial Proteins, Ubiquitin-Protein Ligases, Apoptosis Regulatory Proteins, Inhibitor of Apoptosis Proteins, Mice, X-Linked Inhibitor of Apoptosis Protein, Receptor-Interacting Protein Serine-Threonine Kinases, Interleukin-1beta, Inflammasomes
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