Inhibitor of Apoptosis Proteins Limit RIP3 Kinase-Dependent Interleukin-1 Activation
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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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Multiple components of molecular machinery for necroptosis-including ZBP1, RIPK3, MLKL, and TNFR1 (mainly via NF-κB)-impinge on control of inflammasome, a supramolecular platform for activation of CASP1 and consequent secretion of mature IL1B and IL18.
“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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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 · see citing works
Self-citationSchroder, K., & Tschopp, J. (2010) · Cell · doi:10.1016/j.cell.2010.01.040 · Cited by 5,475 · see citing works
Self-citationHornung, 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 · see citing works
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 · see citing works
Bauernfeind, 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 3,006 · 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
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Identification of RIP1 kinase as a specific cellular target of necrostatins
Degterev, A., Hitomi, J., Germscheid, M., Ch'en, I. L., Korkina, O., Teng, X., Abbott, D., Cuny, G. D., Yuan, C., Wagner, G., et al. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.83 · Cited by 2,059 · see citing works
RIP3, an Energy Metabolism Regulator That Switches TNF-Induced Cell Death from Apoptosis to Necrosis
Zhang, D.-W., Shao, J., Lin, J., Zhang, N., Lu, B.-J., Lin, S.-C., Dong, M.-Q., & Han, J. (2009) · Science · doi:10.1126/science.1172308 · Cited by 1,931 · see citing works
Ghiringhelli, F., Apetoh, L., Tesniere, A., Aymeric, L., Ma, Y., Ortiz, C., Vermaelen, K., Panaretakis, T., Mignot, G., Ullrich, E., et al. (2009) · Nature Medicine · doi:10.1038/nm.2028 · Cited by 1,898 · see citing works
Self-citationCrucial role for the Nalp3 inflammasome in the immunostimulatory properties of aluminium adjuvants
Eisenbarth, S. C., Colegio, O. R., O’Connor, W., Sutterwala, F. S., & Flavell, R. A. (2008) · Nature · doi:10.1038/nature06939 · Cited by 1,542 · see citing works
NF-κB activation by reactive oxygen species: Fifteen years later
Gloire, G., Legrand-Poels, S., & Piette, J. G. (2006) · Biochemical Pharmacology · doi:10.1016/j.bcp.2006.04.011 · Cited by 1,540 · see citing works
Varfolomeev, E., Schuchmann, M., Luria, V., Chiannilkulchai, N., Beckmann, J., Mett, I., Rebrikov, D., Brodianski, V. M., Kemper, O., Kollet, O., et al. (1998) · Immunity · doi:10.1016/s1074-7613(00)80609-3 · Cited by 1,332 · see citing works
Catalytic activity of the caspase-8–FLIPL complex inhibits RIPK3-dependent necrosis
Oberst, A., Dillon, C. P., Weinlich, R., McCormick, L. L., Fitzgerald, P., Pop, C., Hakem, R., Salvesen, G. S., & Green, D. R. (2011) · Nature · doi:10.1038/nature09852 · Cited by 1,278 · cited 1× · see citing works
“Caspase-8 inhibits RIP3 signaling, that if left unchecked causes embryonic lethality (Kaiser et al., 2011; Oberst et al., 2011).”
BackgroundIAP Antagonists Induce Autoubiquitination of c-IAPs, NF-κB Activation, and TNFα-Dependent Apoptosis
Varfolomeev, E., Blankenship, J. W., Wayson, S. M., Fedorova, A. V., Kayagaki, N., Garg, P., Zobel, K., Dynek, J. N., Elliott, L. O., Wallweber, H. J. A., et al. (2007) · Cell · doi:10.1016/j.cell.2007.10.030 · Cited by 1,218 · see citing works
Intravascular Danger Signals Guide Neutrophils to Sites of Sterile Inflammation
McDonald, B., Pittman, K., Menezes, G. B., Hirota, S. A., Slaba, I., Waterhouse, C. C. M., Beck, P. L., Muruve, D. A., & Kubes, P. (2010) · Science · doi:10.1126/science.1195491 · Cited by 1,210 · see citing works
IAP Antagonists Target cIAP1 to Induce TNFα-Dependent Apoptosis
Vince, J. E., Wong, W. W.-L., Khan, N. R., Feltham, R., Chau, D., Ahmed, A. U., Benetatos, C. A., Chunduru, S. K., Condon, S. M., McKinlay, M. A., et al. (2007) · Cell · doi:10.1016/j.cell.2007.10.037 · Cited by 1,061 · see citing works
Self-citationRIP3 mediates the embryonic lethality of caspase-8-deficient mice
Kaiser, W. J., Upton, J. W., Long, A. B., Livingston-Rosanoff, D., Daley-Bauer, L. P., Hakem, R., Caspary, T., & Mocarski, E. S. (2011) · Nature · doi:10.1038/nature09857 · Cited by 1,057 · see citing works
The Sterile Inflammatory Response
Rock, K. L., Latz, E., Ontiveros, F., & Kono, H. (2010) · Annual Review of Immunology · doi:10.1146/annurev-immunol-030409-101311 · Cited by 865 · see citing works
Feoktistova, M., Geserick, P., Kellert, B., Panayotova‐Dimitrova, D., Langlais, C., Hupe, M., Cain, K., MacFarlane, M., Häcker, G. A., & Leverkus, M. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.06.011 · Cited by 855 · see citing works
Self-citationCleavage of the death domain kinase RIP by Caspase-8 prompts TNF-induced apoptosisPreprint
Lin, Y., Devin, A., Rodriguez, Y., & Liu, Z.-G. (1999) · Genes & Development · doi:10.1101/gad.13.19.2514 · Cited by 835 · see citing works
Glyburide inhibits the Cryopyrin/Nalp3 inflammasome
Lamkanfi, M., Mueller, J. L., Vitari, A. C., Misaghi, S., Fedorova, A., Deshayes, K., Lee, W. P., Hoffman, H. M., & Dixit, V. M. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200903124 · Cited by 820 · see citing works
Tenev, T., Bianchi, K., Darding, M., Broemer, M., Langlais, C., Wållberg, F., Zachariou, A., Lopez, J. S., MacFarlane, M., Cain, K., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.06.006 · Cited by 818 · see citing works
IAPs: from caspase inhibitors to modulators of NF-κB, inflammation and cancer
Gyrd-Hansen, M., & Meier, P. (2010) · Nature Reviews Cancer · doi:10.1038/nrc2889 · Cited by 790 · see citing works
He, S., Liang, Y., Shao, F., & Wang, X. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1116302108 · Cited by 725 · see citing works
Necrotic cells trigger a sterile inflammatory response through the Nlrp3 inflammasome
Iyer, S. S., Pulskens, W. P., Sadler, J. J., Butter, L. M., Teske, G. J., Ulland, T. K., Eisenbarth, S. C., Florquin, S., Flavell, R. A., Leemans, J. C., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908698106 · Cited by 691 · see citing works
Suppression of Interleukin-33 Bioactivity through Proteolysis by Apoptotic Caspases
Lüthi, A. U., Cullen, S. P., McNeela, E. A., Duriez, P. J., Afonina, I. S., Sheridan, C., Brumatti, G., Taylor, R. C., Kersse, K., Vandenabeele, P., et al. (2009) · Immunity · doi:10.1016/j.immuni.2009.05.007 · Cited by 677 · see citing works
Bauernfeind, F., Bartok, E., Rieger, A., Franchi, L., Núñez, G., & Hornung, V. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1100613 · Cited by 617 · see citing works
Jin, Z., Li, Y., Pitti, R. M., Lawrence, D. A., Pham, V. C., Lill, J. R., & Ashkenazi, A. (2009) · Cell · doi:10.1016/j.cell.2009.03.015 · Cited by 588 · see citing works
Virus Inhibition of RIP3-Dependent Necrosis
Upton, J. W., Kaiser, W. J., & Mocarski, E. S. (2010) · Cell Host & Microbe · doi:10.1016/j.chom.2010.03.006 · Cited by 559 · see citing works
Caspase 8 inhibits programmed necrosis by processing CYLD
O’Donnell, M. A., Perez-Jimenez, E., Oberst, A., Ng, A., Massoumi, R., Xavier, R., Green, D. R., & Ting, A. T. (2011) · Nature Cell Biology · doi:10.1038/ncb2362 · Cited by 494 · see citing works
Cleavage of RIP3 inactivates its caspase-independent apoptosis pathway by removal of kinase domain
Feng, S., Yang, Y., Mei, Y., Ma, L., Zhu, D.-E., Höti, N., Castanares, M. A., & Wu, M. (2007) · Cellular Signalling · doi:10.1016/j.cellsig.2007.05.016 · Cited by 445 · see citing works
Molecular Mechanism of NLRP3 Inflammasome Activation
Jin, C., & Flavell, R. A. (2010) · Journal of Clinical Immunology · doi:10.1007/s10875-010-9440-3 · Cited by 440 · see citing works
Caspase-8 Serves Both Apoptotic and Nonapoptotic Roles1
Kang, T., Ben-Moshe, T., Varfolomeev, E., Pewzner‐Jung, Y., Yogev, N., Jurewicz, A., Waisman, A., Brenner, O., Haffner, R., Gustafsson, E., et al. (2004) · Journal of Immunology · doi:10.4049/jimmunol.173.5.2976 · Cited by 425 · see citing works
P2X7 Receptor Differentially Couples to Distinct Release Pathways for IL-1β in Mouse Macrophage
Pelegrı́n, P., Barroso-Gutierrez, C., & Surprenant, A. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.11.7147 · Cited by 413 · see citing works
The Human Anti-apoptotic Proteins cIAP1 and cIAP2 Bind but Do Not Inhibit Caspases
Eckelman, B. P., & Salvesen, G. S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m510863200 · Cited by 391 · see citing works
Tseng, P., Matsuzawa, A., Zhang, W., Mino, T., Vignali, D. A. A., & Karin, M. (2009) · Nature Immunology · doi:10.1038/ni.1819 · Cited by 388 · see citing works
The NLRP3 inflammasome in health and disease: the good, the bad and the ugly
Menu, P., & Vince, J. E. (2011) · Clinical & Experimental Immunology · doi:10.1111/j.1365-2249.2011.04440.x · Cited by 387 · see citing works
Self-citationCaspase 1-independent IL-1β release and inflammation induced by the apoptosis inducer Fas ligand
Miwa, K., Asano, M., Horai, R., Iwakura, Y., Nagata, S., & Suda, T. (1998) · Nature Medicine · doi:10.1038/3276 · Cited by 373 · see citing works
Vanlangenakker, N., Vanden Berghe, T., Bogaert, P., Laukens, B., Zobel, K., Deshayes, K., Vucic, D., Fulda, S., Vandenabeele, P., & Bertrand, M. J. M. (2011) · Cell Death & Differentiation · doi:10.1038/cdd.2010.138 · Cited by 339 · see citing works
Bertrand, M. J. M., Doiron, K., Labbè, K., Korneluk, R. G., Barker, P. A., & Saleh, M. (2009) · Immunity · doi:10.1016/j.immuni.2009.04.011 · Cited by 338 · see citing works
Stimulation of Toll-like receptor 3 and 4 induces interleukin-1β maturation by caspase-8
Maelfait, J., Vercammen, E., Janssens, S., Schotte, P., Haegman, M., Magez, S., & Beyaert, R. (2008) · The Journal of Experimental Medicine · doi:10.1084/jem.20071632 · Cited by 327 · see citing works
Mechanisms of interleukin-1β release
Eder, C. (2009) · Immunobiology · doi:10.1016/j.imbio.2008.11.007 · Cited by 307 · see citing works
Critical functions of priming and lysosomal damage for NLRP3 activation
Hornung, V., & Latz, E. (2010) · European Journal of Immunology · doi:10.1002/eji.200940185 · Cited by 297 · see citing works
van de Veerdonk, F. L., Smeekens, S. P., Joosten, L. A. B., Kullberg, B. J., Dinarello, C. A., van der Meer, J. W. M., & Netea, M. G. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914795107 · Cited by 248 · see citing works
Vince, J. E., Pantaki-Eimany, D., Feltham, R., Mace, P. D., Cordier, S. M., Schmukle, A. C., Davidson, A. J., Callus, B. A., Wong, W. W.-L., Gentle, I. E., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.072256 · Cited by 241 · see citing works
Self-citationRIP3, a Novel Apoptosis-inducing Kinase
Sun, X., Lee, J., Navas, T. A., Baldwin, D. T., Stewart, T. A., & Dixit, V. M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.24.16871 · Cited by 240 · see citing works
Vince, J. E., Chau, D., Callus, B. A., Wong, W. W.-L., Hawkins, C. J., Schneider, P., McKinlay, M. A., Benetatos, C. A., Condon, S. M., Chunduru, S. K., et al. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200801010 · Cited by 236 · see citing works
Self-citationGrech, A. P., Amesbury, M., Chan, T. D., Gardam, S., Basten, A., & Brink, R. A. (2004) · Immunity · doi:10.1016/j.immuni.2004.09.011 · Cited by 216 · see citing works
Smac Mimetics Activate the E3 Ligase Activity of cIAP1 Protein by Promoting RING Domain Dimerization
Feltham, R., Bettjeman, B., Budhidarmo, R., Mace, P. D., Shirley, S., Condon, S. M., Chunduru, S. K., McKinlay, M. A., Vaux, D. L., Silke, J., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.222919 · Cited by 168 · see citing works
Self-citationWeber, A., Kirejczyk, Z., Besch, R., Potthoff, S., Leverkus, M., & Häcker, G. A. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.190 · Cited by 142 · see citing works
Self-citationIdentification of RIP3, a RIP-like kinase that activates apoptosis and NFκB
Yu, P., Huang, B. C. B., Shen, M., Quast, J., Chan, E., Xu, X. M., Nolan, G. P., Payan, D. G., & Luo, Y. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80239-5 · Cited by 140 · see citing works
Mao, A., Li, S., Zhong, B., Li, Y., Yan, J., Li, Q., Teng, C., & Shu, H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.071043 · Cited by 134 · see citing works
Cutting Edge: Necrosis Activates the NLRP3 Inflammasome
Li, H., Ambade, A., & Re, F. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0901080 · Cited by 127 · see citing works
Molecular determinants of Smac mimetic induced degradation of cIAP1 and cIAP2
Darding, M., Feltham, R., Tenev, T., Bianchi, K., Benetatos, C. A., Silke, J., & Meier, P. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.10 · Cited by 108 · see citing works
Self-citationGardam, S., Turner, V. M., Anderton, H., Limaye, S., Basten, A., Köentgen, F., Vaux, D. L., Silke, J., & Brink, R. A. (2011) · Blood · doi:10.1182/blood-2010-10-312793 · Cited by 104 · see citing works
Self-citationGenetic and Molecular Basis of Inflammasome-mediated Disease
Hoffman, H. M., & Brydges, S. D. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.r110.135491 · Cited by 78 · see citing works
Antagonists of IAP proteins as cancer therapeutics
Dynek, J. N., & Vucic, D. (2010) · Cancer Letters · doi:10.1016/j.canlet.2010.06.013 · Cited by 52 · see citing works
‘Necrosome’-induced inflammation: must cells die for it?
Wallach, D., Kovalenko, A., & Kang, T. (2011) · Trends in Immunology · doi:10.1016/j.it.2011.07.004 · Cited by 48 · see citing works
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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 · see citing works
Activation and regulation of the inflammasomes
Latz, E., Xiao, T. S., & Stutz, A. (2013) · Nature Reviews Immunology · doi:10.1038/nri3452 · Cited by 2,884 · see citing works
Necroptosis and its role in inflammation
Pasparakis, M., & Vandenabeele, P. (2015) · Nature · doi:10.1038/nature14191 · Cited by 2,148 · see citing works
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 2,198 · see citing works
Regulated necrosis: the expanding network of non-apoptotic cell death pathways
Berghe, T. V., Linkermann, A., Jouan-Lanhouet, S., Walczak, H., & Vandenabeele, P. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3737 · Cited by 1,735 · see citing works
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 · see citing works
Necroptosis: The Release of Damage-Associated Molecular Patterns and Its Physiological Relevance
Kaczmarek, A., Vandenabeele, P., & Krysko, D. V. (2013) · Immunity · doi:10.1016/j.immuni.2013.02.003 · Cited by 1,411 · see citing works
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 · see citing works
Caspases in Cell Death, Inflammation, and Disease
Opdenbosch, N. V., & Lamkanfi, M. (2019) · Immunity · doi:10.1016/j.immuni.2019.05.020 · Cited by 1,230 · see citing works
Regulation of inflammasome activation
Man, S. M., & Kanneganti, T. (2015) · Immunological Reviews · doi:10.1111/imr.12296 · Cited by 1,071 · see citing works
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 · see citing works
Self-citationProgrammed 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
Necroptosis in development, inflammation and disease
Weinlich, R., Oberst, A., Beere, H. M., & Green, D. R. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.149 · Cited by 1,016 · see citing works
Essential versus accessory aspects of cell death: recommendations of the NCCD 2015
Galluzzi, L., Bravo-San Pedro, J. M., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Alnemri, E. S., Altucci, L., Andrews, D., Annicchiarico-Petruzzelli, M., et al. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2014.137 · Cited by 1,002 · see citing works
Triggering and resolution of inflammation in NASH
Schuster, S., Cabrera, D., Arrese, M., & Feldstein, A. E. (2018) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/s41575-018-0009-6 · Cited by 943 · see citing works
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 780 · see citing works
Pattern Recognition Receptors and the Host Cell Death Molecular Machinery
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 759 · see citing works
Malireddi, R. K. S., Kesavardhana, S., & Kanneganti, T. (2019) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2019.00406 · Cited by 750 · see citing works
Necroptosis: a regulated inflammatory mode of cell death
Dhuriya, Y. K., & Sharma, D. (2018) · Journal of Neuroinflammation · doi:10.1186/s12974-018-1235-0 · Cited by 725 · see citing works
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 701 · see citing works
RIPK3 promotes cell death and NLRP3 inflammasome activation in the absence of MLKL
Lawlor, K. E., Khan, N. R., Mildenhall, A., Gerlic, M., Croker, B. A., D’Cruz, A. A., Hall, C. M., Spall, S. K., Anderton, H., Masters, S. L., et al. (2015) · Nature Communications · doi:10.1038/ncomms7282 · Cited by 643 · see citing works
Self-citationWalsh, J. G., Muruve, D. A., & Power, C. (2014) · Nature Reviews Neuroscience · doi:10.1038/nrn3638 · Cited by 637 · see citing works
RIP3 Induces Apoptosis Independent of Pronecrotic Kinase Activity
Mandal, P., Berger, S. B., Pillay, S., Moriwaki, K., Huang, C., Guo, H., Lich, J. D., Finger, J. N., Kasparcova, V., Votta, B. J., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.10.021 · Cited by 619 · see citing works
Inflammation in gout: mechanisms and therapeutic targets
So, A. K.-L., & Martinon, F. (2017) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2017.155 · Cited by 619 · see citing works
RIPK1 Regulates RIPK3-MLKL-Driven Systemic Inflammation and Emergency Hematopoiesis
Rickard, J. A., O’Donnell, J. A., Evans, J. M., Lalaoui, N., Poh, A. R., Rogers, T., Vince, J. E., Lawlor, K. E., Ninnis, R. L., Anderton, H., et al. (2014) · Cell · doi:10.1016/j.cell.2014.04.019 · Cited by 589 · see citing works
Self-citationSamir, P., Malireddi, R. K. S., & Kanneganti, T.-D. (2020) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.00238 · Cited by 557 · see citing works
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 547 · see citing works
Caspase-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 534 · see citing works
K + Efflux-Independent NLRP3 Inflammasome Activation by Small Molecules Targeting Mitochondria
Groß, C. J., Mishra, R., Schneider, K. S., Médard, G., Wettmarshausen, J., Dittlein, D., Shi, H., Gorka, O., Koenig, P.-A., Fromm, S., et al. (2016) · Immunity · doi:10.1016/j.immuni.2016.08.010 · Cited by 530 · see citing works
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 529 · see citing works
The diverse role of RIP kinases in necroptosis and inflammation
Silke, J., Rickard, J. A., & Gerlic, M. (2015) · Nature Immunology · doi:10.1038/ni.3206 · Cited by 522 · see citing works
Self-citationRegulated cell death and inflammation: an auto-amplification loop causes organ failure
Linkermann, A., Stockwell, B. R., Krautwald, S., & Anders, H.-J. (2014) · Nature Reviews Immunology · doi:10.1038/nri3743 · Cited by 522 · 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
Self-citationActive MLKL triggers the NLRP3 inflammasome in a cell-intrinsic manner
Conos, S. A., Chen, K. W., De Nardo, D., Hara, H., Whitehead, L., Núñez, G., Masters, S. L., Murphy, J. M., Schroder, K., Vaux, D. L., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1613305114 · Cited by 485 · see citing works
Self-citationTRAF molecules in cell signaling and in human diseases
Xie, P. (2013) · Journal of Molecular Signaling · doi:10.1186/1750-2187-8-7 · Cited by 467 · see citing works
Newly described pattern recognition receptors team up against intracellular pathogens
Brož, P., & Monack, D. M. (2013) · Nature reviews. Immunology · doi:10.1038/nri3479 · Cited by 459 · see citing works
Vaccination with Necroptotic Cancer Cells Induces Efficient Anti-tumor Immunity
Aaes, T. L., Kaczmarek, A., Delvaeye, T., Craene, B. D., Koker, S. D., Heyndrickx, L., Delrue, I., Taminau, J., Wiernicki, B., Groote, P. D., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.03.037 · Cited by 448 · see citing works
Robinson, N., McComb, S., Mulligan, R., Dudani, R., Krishnan, L., & Sad, S. (2012) · Nature Immunology · doi:10.1038/ni.2397 · Cited by 438 · 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
Caspase-8 Blocks Kinase RIPK3-Mediated Activation of the NLRP3 Inflammasome
Kang, T.-B., Yang, S.-H., Toth, B., Kovalenko, A., & Wallach, D. (2013) · Immunity · doi:10.1016/j.immuni.2012.09.015 · Cited by 419 · see citing works
Necroptosis in health and diseases
Zhou, W., & Yuan, J. (2014) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2014.07.013 · Cited by 414 · see citing works
Mechanisms of NOD-like Receptor-Associated Inflammasome Activation
Wen, H., Miao, E. A., & Ting, J. P. ‐. (2013) · Immunity · doi:10.1016/j.immuni.2013.08.037 · Cited by 415 · 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 416 · see citing works
Newton, K., & Manning, G. (2016) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014830 · Cited by 401 · see citing works
Extrinsic and intrinsic apoptosis activate pannexin‐1 to drive NLRP3 inflammasome assembly
Chen, K. W., Demarco, B., Heilig, R., Shkarina, K., Boettcher, A., Farady, C. J., Pelczar, P., & Brož, P. (2019) · The EMBO Journal · doi:10.15252/embj.2019101638 · Cited by 389 · see citing works
Programmed necrotic cell death of macrophages: Focus on pyroptosis, necroptosis, and parthanatos
Robinson, N., Ganesan, R., Hegedűs, C., Kovács, K. É., Kufer, T. A., & Virág, L. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101239 · Cited by 370 · see citing works
RIPK1 and RIPK3: critical regulators of inflammation and cell death
Newton, K. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.01.001 · Cited by 367 · see citing works
Die another way – non-apoptotic mechanisms of cell death
Tait, S. W. G., Ichim, G., & Green, D. R. (2014) · Journal of Cell Science · doi:10.1242/jcs.093575 · Cited by 366 · see citing works
Microglia: Agents of the CNS Pro-Inflammatory Response
Rodríguez-Gómez, J. A., Kavanagh, E., Engskog-Vlachos, P., Engskog, M. K. R., Herrera, A. J., Espinosa-Oliva, A. M., Joseph, B., Hajji, N., Venero, J. L., & Burguillos, M. A. (2020) · Cells · doi:10.3390/cells9071717 · Cited by 365 · see citing works
RIP3: a molecular switch for necrosis and inflammationPreprint
Moriwaki, K., & Chan, F. K.-M. (2013) · Genes & Development · doi:10.1101/gad.223321.113 · Cited by 353 · see citing works
Caspases Connect Cell-Death Signaling to Organismal Homeostasis
Galluzzi, L., López-Soto, A., Kumar, S., & Kroemer, G. (2016) · Immunity · doi:10.1016/j.immuni.2016.01.020 · Cited by 350 · see citing works
Programmed Necrosis in the Cross Talk of Cell Death and Inflammation
Chan, F. K.-M., Luz, N. F., & Moriwaki, K. (2014) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032414-112248 · Cited by 350 · see citing works
Platelets mediate increased endothelium permeability in dengue through NLRP3-inflammasome activation
Hottz, E. D., Lopes, J. F., Freitas, C., Valls-de-Souza, R., Oliveira, M. F., Bozza, M. T., Da Poian, A. T., Weyrich, A. S., Zimmerman, G. A., Bozza, F. A., et al. (2013) · Blood · doi:10.1182/blood-2013-05-504449 · Cited by 348 · see citing works
Pathogenesis of acute stroke and the role of inflammasomes
Fann, D. Y., Lee, S.-Y., Manzanero, S., Chunduri, P., Sobey, C. G., & Arumugam, T. V. (2013) · Ageing Research Reviews · doi:10.1016/j.arr.2013.09.004 · Cited by 334 · see citing works
Necroptosis in the Pathophysiology of Disease
Khoury, M. K., Gupta, K., Franco, S. R., & Liu, B. (2019) · American Journal Of Pathology · doi:10.1016/j.ajpath.2019.10.012 · Cited by 326 · see citing works
Cell death pathways: intricate connections and disease implications
Kist, M., & Vucic, D. (2021) · The EMBO Journal · doi:10.15252/embj.2020106700 · Cited by 328 · see citing works
RNA viruses promote activation of the NLRP3 inflammasome through a RIP1-RIP3-DRP1 signaling pathway
Wang, X., Jiang, W., Yan, Y., Gong, T., Han, J., Tian, Z., & Zhou, R. (2014) · Nature Immunology · doi:10.1038/ni.3015 · Cited by 323 · see citing works
RIPK1 ensures intestinal homeostasis by protecting the epithelium against apoptosis
Takahashi, N., Vereecke, L., Bertrand, M. J. M., Duprez, L., Berger, S. B., Divert, T., Gonçalves, A., Sze, M., Gilbert, B., Kourula, S., et al. (2014) · Nature · doi:10.1038/nature13706 · Cited by 318 · see citing works
Dondelinger, Y., Aguileta, M. A., Goossens, V, Dubuisson, C., Grootjans, S., Dejardin, E., Vandenabeele, P., & Bertrand, M. J. M. (2013) · Cell Death & Differentiation · doi:10.1038/cdd.2013.94 · Cited by 312 · see citing works
The role of inflammasomes in kidney disease
Komada, T., & Muruve, D. A. (2019) · Nature Reviews Nephrology · doi:10.1038/s41581-019-0158-z · Cited by 311 · see citing works
Distinct roles of RIP1–RIP3 hetero- and RIP3–RIP3 homo-interaction in mediating necroptosis
Wu, X.-N., Yang, Z.-H., Wang, X.-K., Zhang, Y., Wan, H., Song, Y., Chen, X., Shao, J., & Han, J. (2014) · Cell Death & Differentiation · doi:10.1038/cdd.2014.77 · Cited by 299 · see citing works
Caspase-8 and RIP kinases regulate bacteria-induced innate immune responses and cell death
Weng, D., Marty-Roix, R., Ganesan, S., Proulx, M. K., Vladimer, G. I., Kaiser, W. J., Mocarski, E. S., Pouliot, K., Chan, F. K.-M., Kelliher, M. A., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1403477111 · Cited by 292 · see citing works
Bossaller, L., Chiang, P.-I., Schmidt‐Lauber, C., Ganesan, S., Kaiser, W. J., Rathinam, V. A. K., Mocarski, E. S., Subramanian, D., Green, D. R., Silverman, N. S., et al. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1202121 · Cited by 287 · see citing works
Cheng, X., Zhang, L., Zhang, K., Zhang, G., Hu, Y., Sun, X., Zhao, C., Li, H., Li, Y. M., & Zhao, J. (2018) · Annals of the Rheumatic Diseases · doi:10.1136/annrheumdis-2017-212056 · Cited by 280 · see citing works
Philip, N. H., Dillon, C. P., Snyder, A. G., Fitzgerald, P., Wynosky-Dolfi, M. A., Zwack, E. E., Hu, B., Fitzgerald, L. M., Mauldin, E. A., Copenhaver, A. M., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1403252111 · Cited by 280 · see citing works
Duong, B. H., Onizawa, M., Osés-Prieto, J. A., Advincula, R., Burlingame, A. L., Malynn, B. A., & Ma, A. I. (2015) · Immunity · doi:10.1016/j.immuni.2014.12.031 · Cited by 269 · see citing works
NOD-Like Receptors: Master Regulators of Inflammation and Cancer
Saxena, M., & Yeretssian, G. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00327 · Cited by 272 · see citing works
Toxin-Induced Necroptosis Is a Major Mechanism of Staphylococcus aureus Lung Damage
Kitur, K., Parker, D., Nieto, P. A., Ahn, D. S., Cohen, T. S., Chung, S., Wachtel, S., Bueno, S. M., & Prince, A. S. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1004820 · Cited by 268 · see citing works
Caspase-1: is IL-1 just the tip of the ICEberg?
Dénes, Á., López‐Castejón, G., & Brough, D. (2012) · Cell Death and Disease · doi:10.1038/cddis.2012.86 · Cited by 264 · see citing works
The Pathogen Candida albicans Hijacks Pyroptosis for Escape from Macrophages
Uwamahoro, N., Verma-Gaur, J., Shen, H.-H., Qu, Y., Lewis, R., Lu, J., Bambery, K., Masters, S. L., Vince, J. E., Naderer, T., et al. (2014) · mBio · doi:10.1128/mbio.00003-14 · Cited by 264 · see citing works
Self-citationTNFR1-dependent cell death drives inflammation in Sharpin-deficient mice
Rickard, J. A., Anderton, H., Etemadi, N., Nachbur, U., Darding, M., Peltzer, N., Lalaoui, N., Lawlor, K. E., Vanyai, H. K., Hall, C. M., et al. (2014) · eLife · doi:10.7554/elife.03464 · Cited by 261 · see citing works
Self-citationMolecular mechanisms of regulated necrosis
Galluzzi, L., Kepp, O., Krautwald, S., Kroemer, G., & Linkermann, A. (2014) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2014.02.006 · Cited by 258 · see citing works
Caspase-8 scaffolding function and MLKL regulate NLRP3 inflammasome activation downstream of TLR3
Kang, S., Fernandes‐Alnemri, T., Rogers, C., Mayes, L., Wang, Y., Dillon, C. P., Roback, L., Kaiser, W. J., Oberst, A., Sagara, J., et al. (2015) · Nature Communications · doi:10.1038/ncomms8515 · Cited by 255 · see citing works
XIAP Restricts TNF- and RIP3-Dependent Cell Death and Inflammasome Activation
Yabal, M., Müller, N., Adler, H., Knies, N., Groß, C. J., Damgaard, R. B., Kanegane, H., Ringelhan, M., Kaufmann, T., Heikenwälder, M., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.05.008 · Cited by 255 · see citing works
The Necroptosis Adaptor RIPK3 Promotes Injury-Induced Cytokine Expression and Tissue Repair
Moriwaki, K., Balaji, S., McQuade, T. J., Malhotra, N., Kang, J., & Chan, F. K.-M. (2014) · Immunity · doi:10.1016/j.immuni.2014.09.016 · Cited by 251 · see citing works
Caspase-8: The double-edged sword
Mandal, R., Compte, J., Kostova, I., Becker, S., & Strebhardt, K. (2020) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2020.188357 · Cited by 252 · see citing works
Photoreceptor cell death and rescue in retinal detachment and degenerations
Murakami, Y., Notomi, S., Hisatomi, T., Nakazawa, T., Ishibashi, T., Miller, J. W., & Vavvas, D. G. (2013) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2013.08.001 · Cited by 248 · see citing works
Determination of apoptotic and necrotic cell death in vitro and in vivo
Berghe, T. V., Grootjans, S., Goossens, V., Dondelinger, Y., Krysko, D. V., Takahashi, N., & Vandenabeele, P. (2013) · Methods · doi:10.1016/j.ymeth.2013.02.011 · Cited by 250 · see citing works
RIP kinases as modulators of inflammation and immunity
He, S., & Wang, X. (2018) · Nature Immunology · doi:10.1038/s41590-018-0188-x · Cited by 246 · see citing works
RIP kinases: key decision makers in cell death and innate immunity
Humphries, F., Yang, S., Wang, B., & Moynagh, P. N. (2014) · Cell Death and Differentiation · doi:10.1038/cdd.2014.126 · Cited by 243 · see citing works
Alvarez-Diaz, S., Dillon, C. P., Lalaoui, N., Tanzer, M. C., Rodriguez, D. A., Lin, A., Lebois, M., Hakem, R., Josefsson, E. C., O’Reilly, L. A., et al. (2016) · Immunity · doi:10.1016/j.immuni.2016.07.016 · Cited by 242 · see citing works
Self-citationDeath Receptor-Ligand Systems in Cancer, Cell Death, and InflammationPreprint
Walczak, H. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008698 · Cited by 243 · see citing works
Allam, R., Lawlor, K. E., Yu, E. C.-W., Mildenhall, A., Moujalled, D. M., Lewis, R. S., Ke, F., Mason, K. D., White, M. J., Stacey, K. J., et al. (2014) · EMBO Reports · doi:10.15252/embr.201438463 · Cited by 238 · see citing works
Self-citationDemarco, B., Grayczyk, J. P., Bjånes, E., Roy, D. L., Tonnus, W., Assenmacher, C., Radaelli, E., Fettrelet, T., Mack, V., Linkermann, A., et al. (2020) · Science Advances · doi:10.1126/sciadv.abc3465 · Cited by 237 · see citing works
Vince, J. E., Nardo, D. D., Gao, W., Vince, A. J., Hall, C. M., McArthur, K., Simpson, D. S., Vijayaraj, S. L., Lindqvist, L., Bouillet, P., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.10.103 · Cited by 234 · see citing works
Self-citationCaspase-8 as an Effector and Regulator of NLRP3 Inflammasome Signaling
Antonopoulos, C. H., Russo, H. M., Sanadi, C. E. E., Martin, B. N., Li, X., Kaiser, W. J., Mocarski, E. S., & Dubyak, G. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.652321 · Cited by 225 · see citing works
MLKL Activation Triggers NLRP3-Mediated Processing and Release of IL-1β Independently of Gasdermin-D
Gutierrez, K. D., Davis, M. A., Daniels, B. P., Olsen, T. M., Ralli-Jain, P., Tait, S. W. G., Gale, M., & Oberst, A. (2017) · The Journal of Immunology · doi:10.4049/jimmunol.1601757 · Cited by 229 · see citing works
Ubiquitin in the immune system
Zinngrebe, J., Montinaro, A., Peltzer, N., & Walczak, H. (2014) · The EMBO Reports · doi:10.1002/embr.201338025 · Cited by 227 · see citing works
Deo, P., Chow, S. H., Han, M., Speir, M., Huang, C., Schittenhelm, R. B., Dhital, S., Emery, J., Li, J., Kile, B. T., et al. (2020) · Nature Microbiology · doi:10.1038/s41564-020-0773-2 · Cited by 224 · see citing works
Self-citationAfonso, M. B., Rodrigues, P., Carvalho, T., Caridade, M., Borralho, P., Cortez-Pinto, H., Castro, R., & Rodrigues, C. (2015) · Clinical science · doi:10.1042/cs20140732 · Cited by 207 · see citing works
Molecular crosstalk between apoptosis, necroptosis, and survival signaling
Berghe, T. V., Kaiser, W. J., Bertrand, M. J. M., & Vandenabeele, P. (2015) · Molecular & Cellular Oncology · doi:10.4161/23723556.2014.975093 · Cited by 203 · see citing works
Multiple roles of caspase-8 in cell death, inflammation, and innate immunity
Ørning, P., & Lien, E. (2020) · Journal of Leukocyte Biology · doi:10.1002/jlb.3mr0420-305r · Cited by 199 · see citing works
Inflammasome, Inflammation, and Tissue Homeostasis
Rathinam, V. A. K., & Chan, F. K.-M. (2018) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2018.01.004 · Cited by 192 · see citing works
Complex Pathologic Roles of RIPK1 and RIPK3: Moving Beyond Necroptosis
Wegner, K. W., Saleh, D., & Degterev, A. (2017) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2016.12.005 · Cited by 190 · see citing works
de Almagro, M. C., & Vucic, D. (2012) · PubMed · Cited by 189 · see citing works
Molecular mechanisms of inflammasome signaling
Mathur, A., Hayward, J. A., & Man, S. M. (2017) · Journal of Leukocyte Biology · doi:10.1189/jlb.3mr0617-250r · Cited by 189 · see citing works
The E3 ubiquitin ligase Pellino2 mediates priming of the NLRP3 inflammasome
Humphries, F., Bergin, R., Jackson, R. P., Delagic, N., Wang, B., Yang, S., Dubois, A. V., Ingram, R. J., & Moynagh, P. N. (2018) · Nature Communications · doi:10.1038/s41467-018-03669-z · Cited by 187 · see citing works
Roles of RIPK3 in necroptosis, cell signaling, and disease
Morgan, M. J., & Kim, Y. (2022) · Experimental & Molecular Medicine · doi:10.1038/s12276-022-00868-z · Cited by 189 · see citing works
CHIP controls necroptosis through ubiquitylation- and lysosome-dependent degradation of RIPK3
Seo, J., Lee, E.-W., Sung, H., Seong, D., Dondelinger, Y., Shin, J., Jeong, M., Lee, H.-K., Kim, J.-H., Han, S. Y., et al. (2016) · Nature Cell Biology · doi:10.1038/ncb3314 · Cited by 182 · see citing works
Novel Roles for Caspase-8 in IL-1β and Inflammasome Regulation
Gurung, P., & Kanneganti, T. (2014) · American Journal Of Pathology · doi:10.1016/j.ajpath.2014.08.025 · Cited by 178 · see citing works
- 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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