Regulated necrosis: the expanding network of non-apoptotic cell death pathways
Abstract
Cell death research was revitalized by the understanding that necrosis can occur in a highly regulated and genetically controlled manner. Although RIPK1 (receptor-interacting protein kinase 1)- and RIPK3-MLKL (mixed lineage kinase domain-like)-mediated necroptosis is the most understood form of regulated necrosis, other examples of this process are emerging, including cell death mechanisms known as parthanatos, oxytosis, ferroptosis, NETosis, pyronecrosis and pyroptosis. Elucidating how these pathways of regulated necrosis are interconnected at the molecular level should enable this process to be therapeutically targeted.
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MPT refers to abrupt loss of impermeability of IMM to small solutes, resulting in rapid Δψm dissipation, osmotic breakdown of both mitochondrial membranes, and RCD.
“The term MPT refers to an abrupt loss of the impermeability of the IMM to small solutes, resulting in rapid Δψm dissipation, osmotic breakdown of both mitochondrial membranes, and RCD [373, 374].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [374]
MPT-driven necrosis is a form of RCD initiated by specific perturbations of intracellular microenvironment such as severe oxidative stress and cytosolic Ca2+ overload, which generally manifests with necrotic morphotype.
“MPT-driven necrosis is a form of RCD initiated by specific perturbations of the intracellular microenvironment such as severe oxidative stress and cytosolic Ca2+ overload, which generally manifests with a necrotic morphotype [373, 374].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [374]
MPT-driven necrosis has been proposed to follow opening of PTPC, a supramolecular complex assembled at junctions between IMM and OMM.
“At the biochemical level, MPT-driven necrosis has been proposed to follow the opening of the so-called “permeability transition pore complex” (PTPC), a supramolecular complex assembled at the junctions between the IMM and OMM [103, 374].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [374]
Ferroptosis manifests with a necrotic morphotype with predominant mitochondrial alterations including shrinkage, electron-dense ultrastructure, reduced/disappeared cristae, and ruptured OMM.
“manifests with a necrotic morphotype (with a predominance of mitochondrial alterations encompassing shrinkage, an electron-dense ultrastructure, reduced/disappeared cristae, and ruptured OMM) [374]”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [374]
Enzymes such as caspases, thought to have key causal role in RCD execution, in majority of scenarios only accelerate rather than causally determine cellular demise.
“Moreover, the community has focused for a long time on specific enzymes that were thought to have a key causal role in RCD execution, but in a majority of scenarios only appear to accelerate (rather than causally determine) cellular demise (e.g., caspases) [17, 374].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [374]
Cell death in all forms including ACD is ultimately associated with a bioenergetic and redox crisis that may be its actual cause.
“Indeed, cell death in all its forms (including ACD) is ultimately associated with a bioenergetic and redox crisis that may constitute its actual cause [17, 374].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [374]
Cites
2 retracted
GRIM-19 Mediated Translocation of STAT3 to Mitochondria is Necessary for TNF Induced Necroptosis.
Shulga, N., & Pastorino, J. G. (2012) · Journal of Cell Science · doi:10.1242/jcs.103093 · Cited by 101 · see citing works
RetractedValencia, A., Sapp, E., Kimm, J. S., McClory, H., Reeves, P., Alexander, J. S., Ansong, K. A., Masso, N., Frosch, M. P., Kegel, K. B., et al. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds516 · Cited by 93 · see citing works
RetractedFerroptosis: An Iron-Dependent Form of Nonapoptotic Cell Death
Dixon, S. J., Lemberg, K. M., Lamprecht, M. R., Skouta, R., Zaitsev, E. M., Gleason, C. E., Patel, D. N., Bauer, A. J., Cantley, A. M., Yang, W. S., et al. (2012) · Cell · doi:10.1016/j.cell.2012.03.042 · Cited by 18,691 · see citing works
Neutrophil Extracellular Traps Kill Bacteria
Brinkmann, V., Reichard, U., Goosmann, C., Fauler, B., Uhlemann, Y., Weiss, D. S., Weinrauch, Y., & Zychlinsky, A. (2004) · Science · doi:10.1126/science.1092385 · Cited by 10,268 · see citing works
Regulation of Ferroptotic Cancer Cell Death by GPX4
Yang, W. S., SriRamaratnam, R., Welsch, M. E., Shimada, K., Skouta, R., Viswanathan, V. S., Cheah, J. H., Clemons, P. A., Shamji, A. F., Clish, C. B., et al. (2014) · Cell · doi:10.1016/j.cell.2013.12.010 · Cited by 7,713 · see citing works
Du, C., Fang, M., Li, Y., Li, L., & Wang, X. (2000) · Cell · doi:10.1016/s0092-8674(00)00008-8 · Cited by 3,513 · see citing works
Chemical inhibitor of nonapoptotic cell death with therapeutic potential for ischemic brain injury
Degterev, A., Huang, Z., Boyce, M., Li, Y., Jagtap, P., Mizushima, N., Cuny, G. D., Mitchison, T. J., Moskowitz, M. A., & Yuan, J. (2005) · Nature Chemical Biology · doi:10.1038/nchembio711 · Cited by 3,068 · see citing works
Mixed Lineage Kinase Domain-like Protein Mediates Necrosis Signaling Downstream of RIP3 Kinase
Sun, L., Wang, H., Wang, Z., He, S., Chen, S., Liao, D., Wang, L., Yan, J., Liu, W., Lei, X., et al. (2012) · Cell · doi:10.1016/j.cell.2011.11.031 · Cited by 2,698 · see citing works
Apoptosis: controlled demolition at the cellular level
Taylor, R. C., Cullen, S. P., & Martin, S. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2312 · Cited by 2,617 · 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
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
Galluzzi, L., Vitale, I., Abrams, J. M., Alnemri, E. S., Baehrecke, E. H., Blagosklonny, M. V., Dawson, T. M., Dawson, V. L., El-Deiry, W. S., Fulda, S., et al. (2012) · Cell Death & Differentiation · doi:10.1038/cdd.2011.96 · Cited by 2,421 · see citing works
Self-citationMolecular 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
Self-citationBaines, C. P., Kaiser, R. A., Purcell, N. H., Blair, N. S., Osinska, H., Hambleton, M. A., Brunskill, E. W., Sayen, M. R., Gottlieb, R. A., Dorn, G. W., et al. (2005) · Nature · doi:10.1038/nature03434 · Cited by 2,280 · 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
Holler, N., Zaru, R., Micheau, O., Thome, M., Attinger, A., Valitutti, S., Bodmer, J.-L., Schneider, P., Seed, B., & Tschopp, J. (2000) · Nature Immunology · doi:10.1038/82732 · Cited by 1,932 · 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
De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-κB signalling
Wertz, I. E., O’Rourke, K. M., Zhou, H., Eby, M. T., Aravind, L., Seshagiri, S., Wu, P., Wiesmann, C., Baker, R. T., Boone, D. L., et al. (2004) · Nature · doi:10.1038/nature02794 · Cited by 1,852 · see citing works
Genetic control of programmed cell death in the nematode C. elegans
Ellis, H. (1986) · Cell · doi:10.1016/0092-8674(86)90004-8 · Cited by 1,828 · see citing works
Nakagawa, T., Shimizu, S., Watanabe, T., Yamaguchi, O., Otsu, K., Yamagata, H., Inohara, H., Kubo, T., & Tsujimoto, Y. (2005) · Nature · doi:10.1038/nature03317 · Cited by 1,635 · see citing works
Seiler, A., Schneider, M., Förster, H., Roth, S., Wirth, E. K., Culmsee, C., Plesnila, N., Kremmer, E., Rådmark, O., Wurst, W., et al. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.07.005 · Cited by 1,470 · see citing works
Pro-inflammatory programmed cell death
Cookson, B. T., & Brennan, M. A. (2001) · Trends in Microbiology · doi:10.1016/s0966-842x(00)01936-3 · Cited by 1,422 · 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
Self-citationTNF-α Induces Two Distinct Caspase-8 Activation Pathways
Wang, L., Du, F., & Wang, X. (2008) · Cell · doi:10.1016/j.cell.2008.03.036 · Cited by 1,352 · see citing works
Effect of Cyclosporine on Reperfusion Injury in Acute Myocardial Infarction
Piot, C. A., Croisille, P., Staat, P., Thibault, H., Rioufol, G., Mewton, N., Belghiti, R. E., Cung, T. T., Bonnefoy‐Cudraz, E., Angoulvant, D., et al. (2008) · New England Journal of Medicine · doi:10.1056/nejmoa071142 · Cited by 1,339 · 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
Plasma membrane translocation of trimerized MLKL protein is required for TNF-induced necroptosis
Cai, Z., Jitkaew, S., Zhao, J., Chiang, H.-C., Choksi, S., Liu, J., Ward, Y., Wu, L.-G., & Liu, Z.-G. (2014) · Nature Cell Biology · doi:10.1038/ncb2883 · Cited by 1,322 · 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 · see citing works
Cytoplasmic LPS Activates Caspase-11: Implications in TLR4-Independent Endotoxic Shock
Hagar, J. A., Powell, D. A., Aachoui, Y., Ernst, R. K., & Miao, E. A. (2013) · Science · doi:10.1126/science.1240988 · Cited by 1,265 · see citing works
New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs
Gibson, B. A., & Kraus, W. L. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3376 · Cited by 1,226 · see citing works
Li, J., McQuade, T., Siemer, A. B., Napetschnig, J., Moriwaki, K., Hsiao, Y.-S., Damko, E., Moquin, D., Walz, T., McDermott, A., et al. (2012) · Cell · doi:10.1016/j.cell.2012.06.019 · Cited by 1,222 · see citing works
The Pseudokinase MLKL Mediates Necroptosis via a Molecular Switch Mechanism
Murphy, J. M., Czabotar, P. E., Hildebrand, J. M., Lucet, I. S., Zhang, J.-G., Alvarez-Diaz, S., Lewis, R., Lalaoui, N., Metcalf, D., Webb, A. I., et al. (2013) · Immunity · doi:10.1016/j.immuni.2013.06.018 · Cited by 1,220 · see citing works
IAP 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
Cell death by pyroptosis drives CD4 T-cell depletion in HIV-1 infection
Doitsh, G., Galloway, N. L. K., Geng, X., Yang, Z., Monroe, K. M., Zepeda, O., Hunt, P. W., Hatano, H., Sowinski, S., Muñoz-Arias, I., et al. (2013) · Nature · doi:10.1038/nature12940 · Cited by 1,181 · see citing works
Infection-induced NETosis is a dynamic process involving neutrophil multitasking in vivo
Yipp, B. G., Petri, B., Salina, D., Jenne, C. N., Scott, B. N. V., Zbytnuik, L. D., Pittman, K., Asaduzzaman, M., Wu, K., Meijndert, H. C., et al. (2012) · Nature Medicine · doi:10.1038/nm.2847 · Cited by 1,169 · see citing works
Fink, S. L., & Cookson, B. T. (2006) · Cellular Microbiology · doi:10.1111/j.1462-5822.2006.00751.x · Cited by 1,114 · see citing works
Bertrand, M. J. M., Milutinovic, S., Dickson, K. M., Ho, W. C., Boudreault, A., Durkin, J. P., Gillard, J. W., Jaquith, J. B., Morris, S. J., & Barker, P. A. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.05.014 · Cited by 1,102 · see citing works
The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore
Kokoszka, J. E., Waymire, K. G., Levy, S. E., Sligh, J. E., Cai, J., Jones, D. P., MacGregor, G. R., & Wallace, D. C. (2004) · Nature · doi:10.1038/nature02229 · Cited by 1,086 · 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
RIP3 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
NAD+ metabolism in health and disease
Belenky, P. A., Bogan, K. L., & Brenner, C. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.11.006 · Cited by 983 · see citing works
Toll-like Receptor 3-mediated Necrosis via TRIF, RIP3, and MLKL
Kaiser, W. J., Sridharan, H., Huang, C., Mandal, P., Upton, J. W., Gough, P. J., Sehon, C. A., Marquis, R. W., Bertin, J., & Mocarski, E. S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.462341 · Cited by 959 · see citing works
Lockshin, R. A., & Beaulaton, J. (1974) · Life Sciences · doi:10.1016/0024-3205(74)90321-x · Cited by 955 · see citing works
Schulze‐Osthoff, K., Bakker, A. C., Vanhaesebroeck, B., Beyaert, R., Jacob, W. A., & Fiers, W. C. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42768-8 · Cited by 935 · see citing works
Vercammen, D., Beyaert, R., Denecker, G., Goossens, V., Loo, G., Declercq, W., Grooten, J., Fiers, W., & Vandenabeele, P. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.187.9.1477 · Cited by 925 · see citing works
Self-citationDimers of mitochondrial ATP synthase form the permeability transition pore
Giorgio, V., von Stockum, S., Antoniel, M., Fabbro, A., Fogolari, F., Forte, M. A., Glick, G. D., Petronilli, V., Zoratti, M., Szabó, I., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1217823110 · Cited by 924 · see citing works
Tumor necrosis factor can induce both apoptic and necrotic forms of cell lysis.
Laster, S. M., Wood, J. G., & Gooding, L. R. (1988) · The Journal of Immunology · doi:10.4049/jimmunol.141.8.2629 · Cited by 909 · see citing works
Zhao, J., Jitkaew, S., Cai, Z., Choksi, S., Li, Q., Luo, J., & Liu, Z.-G. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1200012109 · Cited by 901 · see citing works
Poly(ADP-ribose) polymerase and the therapeutic effects of its inhibitors
Jagtap, P. G., & Szabó, C. (2005) · Nature Reviews Drug Discovery · doi:10.1038/nrd1718 · Cited by 896 · 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
PKR; a sentinel kinase for cellular stress
Williams, B. R. (1999) · Oncogene · doi:10.1038/sj.onc.1203127 · Cited by 820 · see citing works
Schinzel, A. C., Takeuchi, O., Huang, Z., Fisher, J. K., Zhou, Z., Rubens, J., Hetz, C., Danial, N. N., Moskowitz, M. A., & Korsmeyer, S. J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505294102 · 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
Neutrophil extracellular trap cell death requires both autophagy and superoxide generation
Remijsen, Q., Berghe, T. V., Wirawan, E., Asselbergh, B., Parthoens, E., De Rycke, R., Noppen, S., Delforge, M., Willems, J., & Vandenabeele, P. (2011) · Cell Research · doi:10.1038/cr.2010.150 · Cited by 818 · see citing works
Self-citationProperties of the Permeability Transition Pore in Mitochondria Devoid of Cyclophilin D
Basso, E., Fante, L., Fowlkes, J., Petronilli, V., Forte, M. A., & Bernardi, P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500089200 · Cited by 808 · see citing works
Chen, X., Li, W., Ren, J., Huang, D., He, W., Song, Y., Yang, C., Li, W., Zheng, X., Chen, P., et al. (2013) · Cell Research · doi:10.1038/cr.2013.171 · Cited by 778 · see citing works
p53 Opens the Mitochondrial Permeability Transition Pore to Trigger Necrosis
Vaseva, A. V., Marchenko, N. D., Ji, K., Tsirka, S. E., Holzmann, S., & Moll, U. M. (2012) · Cell · doi:10.1016/j.cell.2012.05.014 · Cited by 740 · see citing works
The morphology of various types of cell death in prenatal tissues
Schweichel, J. ‐., & Merker, H. ‐. (1973) · Teratology · doi:10.1002/tera.1420070306 · Cited by 738 · 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
Chronic Granulomatous Disease: The European Experience
van den Berg, J. M., van Koppen, E., Åhlin, A., Belohradsky, B. H., Bernatowska, E. A., Corbeel, L., Español, T., Fischer, A., Kurenko-Deptuch, M., Mouy, R., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005234 · Cited by 685 · see citing works
Salmonella induces macrophage death by caspase‐1‐dependent necrosis
Brennan, M. A., & Cookson, B. T. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.02103.x · Cited by 674 · see citing works
Lysosomal cell death at a glance
Aits, S., & Jäättelä, M. (2013) · Journal of Cell Science · doi:10.1242/jcs.091181 · Cited by 667 · see citing works
Necroptosis, necrosis and secondary necrosis converge on similar cellular disintegration features
Berghe, T. V., Vanlangenakker, N., Parthoens, E., Deckers, W., Devos, M., Festjens, N., Guerin, C. J., Brunk, U. T., Declercq, W., & Vandenabeele, P. (2010) · Cell Death & Differentiation · doi:10.1038/cdd.2009.184 · Cited by 639 · see citing works
Self-citationDying for a cause: NETosis, mechanisms behind an antimicrobial cell death modality
Remijsen, Q., Kuijpers, T. W., Wirawan, E., Lippens, S., Vandenabeele, P., & Berghe, T. V. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.1 · Cited by 612 · see citing works
Self-citationZarnegar, B. J., Wang, Y., Mahoney, D. J., Dempsey, P. W., Cheung, H. H., He, J., Shiba, T. L., Yang, X., Yeh, W., Mak, T. W., et al. (2008) · Nature Immunology · doi:10.1038/ni.1676 · Cited by 607 · see citing works
Liu, Y., Shoji-Kawata, S., Sumpter, R. M., Wei, Y., Ginet, V., Zhang, L., Posner, B., Tran, K. A., Green, D. R., Xavier, R. J., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1319661110 · Cited by 607 · see citing works
FADD prevents RIP3-mediated epithelial cell necrosis and chronic intestinal inflammation
Welz, P.-S., Wullaert, A., Vlantis, K., Kondylis, V., Fernández-Majada, V., Ermolaeva, M., Kirsch, P., Sterner-Kock, A., van Loo, G., & Pasparakis, M. (2011) · Nature · doi:10.1038/nature10273 · Cited by 594 · see citing works
RIP Kinase-Dependent Necrosis Drives Lethal Systemic Inflammatory Response Syndrome
Duprez, L., Takahashi, N., Hauwermeiren, F. V., Vandendriessche, B., Goossens, V., Berghe, T. V., Declercq, W., Libert, C., Cauwels, A., & Vandenabeele, P. (2011) · Immunity · doi:10.1016/j.immuni.2011.09.020 · Cited by 591 · see citing works
Self-citationDeath receptor signal transducers: nodes of coordination in immune signaling networks
Wilson, N., Dixit, V., & Ashkenazi, A. (2009) · Nature Immunology · doi:10.1038/ni.1714 · Cited by 569 · see citing works
Two independent pathways of regulated necrosis mediate ischemia–reperfusion injury
Linkermann, A., Bräsen, J. H., Darding, M., Jin, M. K., Sanz, A. B., Heller, J.-O., Zen, F. D., Weinlich, R., Ortíz, A., Walczak, H., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1305538110 · Cited by 568 · see citing works
Self-citationVirus 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
c-IAP1 and c-IAP2 Are Critical Mediators of Tumor Necrosis Factor α (TNFα)-induced NF-κB Activation
Varfolomeev, E. E., Goncharov, T., Fedorova, A. V., Dynek, J. N., Zobel, K., Deshayes, K., Fairbrother, W. J., & Vucic, D. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.c800128200 · Cited by 554 · 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
Newton, K., Sun, X., & Dixit, V. M. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.4.1464-1469.2004 · Cited by 544 · see citing works
Both cIAP1 and cIAP2 regulate TNFα-mediated NF-κB activation
Mahoney, D. J., Cheung, H. H., Mrad, R. L., Plenchette, S., Simard, C., Enwere, E., Arora, V., Mak, T. W., Lacasse, E. C., Waring, J., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711122105 · Cited by 540 · see citing works
Molecular Mechanisms of Glutamate Receptor-Mediated Excitotoxic Neuronal Cell Death
Sattler, R., & Tymianski, M. (2001) · Molecular Neurobiology · doi:10.1385/mn:24:1-3:107 · Cited by 537 · see citing works
Cleavage of the Plasma Membrane Na+/Ca2+ Exchanger in Excitotoxicity
Bano, D., Young, K. W., Guérin, C. J., Feuvre, R. A. L., Rothwell, N. J., Naldini, L., Rizzuto, R., Carafoli, E., & Nicotera, P. (2005) · Cell · doi:10.1016/j.cell.2004.11.049 · Cited by 532 · see citing works
Oxytosis: a novel form of programmed cell death
Shirlee Tan, B. S. P., David Schubert, B. S. P., & Pamela Maher, B. S. P. (2001) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026013394741 · Cited by 522 · see citing works
Zamboni, D. S., Kobayashi, K. S., Kohlsdorf, T., Ogura, Y., Long, E. M., Vance, R. E., Kuida, K., Mariathasan, S., Dixit, V. M., Flavell, R. A., et al. (2006) · Nature Immunology · doi:10.1038/ni1305 · Cited by 515 · see citing works
Łoś, M., Mozoluk, M., Ferrari, D., Stępczyńska, A., Stroh, C., Renz, A., Herceg, Z., Wang, Z., & Schulze‐Osthoff, K. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-05-0272 · Cited by 505 · see citing works
Inhibitor of Apoptosis Proteins Limit RIP3 Kinase-Dependent Interleukin-1 Activation
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., et al. (2012) · Immunity · doi:10.1016/j.immuni.2012.01.012 · Cited by 491 · see citing works
Takahashi, N., Duprez, L., Grootjans, S., Cauwels, A., Nerinckx, W., DuHadaway, J. B., Goossens, V, Roelandt, R., Van Hauwermeiren, F., Libert, C., et al. (2012) · Cell Death & Disease · doi:10.1038/cddis.2012.176 · Cited by 465 · see citing works
Self-citationLinkermann, A., Bräsen, J. H., Himmerkus, N., Liu, S., Huber, T. B., Kunzendorf, U., & Krautwald, S. (2012) · Kidney International · doi:10.1038/ki.2011.450 · Cited by 462 · see citing works
Self-citationRole of the c subunit of the F O ATP synthase in mitochondrial permeability transition
Bonora, M., Bononi, A., Marchi, E. D., Giorgi, C., Lebiedzińska, M., Marchi, S., Patergnani, S., Rimessi, A., Suski, J. M., Wojtala, A., et al. (2013) · Cell Cycle · doi:10.4161/cc.23599 · Cited by 454 · see citing works
Mlkl knockout mice demonstrate the indispensable role of Mlkl in necroptosis
Wu, J., Huang, Z., Ren, J., Zhang, Z., He, P., Li, Y., Ma, J., Chen, W., Zhang, Y., Zhou, X., et al. (2013) · Cell Research · doi:10.1038/cr.2013.91 · Cited by 452 · 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
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
Functional complementation between FADD and RIP1 in embryos and lymphocytes
Zhang, H., Zhou, X., McQuade, T. J., Li, J., Chan, F. K.-M., & Zhang, J. (2011) · Nature · doi:10.1038/nature09878 · Cited by 422 · 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
A cytomegalovirus-encoded inhibitor of apoptosis that suppresses caspase-8 activation
Skaletskaya, A., Bartle, L. M., Chittenden, T. D., McCormick, A. L., Mocarski, E. S., & Goldmacher, V. S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.141108798 · Cited by 418 · 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
Lockshin, R. A., & Williams, C. M. (1964) · Journal of Insect Physiology · doi:10.1016/0022-1910(64)90034-4 · Cited by 399 · see citing works
Sphingosine-induced apoptosis is dependent on lysosomal proteases
Kågedal, K., Ming, Z. H. A. O., Svensson, I., & Brunk, U. T. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3590335 · Cited by 379 · see citing works
Mitochondrial and Nuclear Cross Talk in Cell Death
Andrabi, S. A., Dawson, T. M., & Dawson, V. L. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1427.014 · Cited by 378 · see citing works
Clarke, S. J., McStay, G. P., & Halestrap, A. P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202191200 · Cited by 376 · see citing works
Therapeutic applications of PARP inhibitors: Anticancer therapy and beyond
Curtin, N. J., & Szabo, C. (2013) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2013.01.006 · Cited by 369 · see citing works
Shikonin circumvents cancer drug resistance by induction of a necroptotic death
Han, W., Li, L., Qiu, S., Lu, Q., Pan, Q., Gu, Y., Luo, J., & Hu, X. (2007) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-06-0511 · Cited by 364 · see citing works
TRAIL induces necroptosis involving RIPK1/RIPK3-dependent PARP-1 activation
Jouan-Lanhouet, S., Arshad, M. I., Piquet-Pellorce, C., Martin-Chouly, C., Le Moigne-Muller, G., Van Herreweghe, F., Takahashi, N., Sergent, O., Lagadic-Gossmann, D., Vandenabeele, P., et al. (2012) · Cell Death & Differentiation · doi:10.1038/cdd.2012.90 · Cited by 357 · see citing works
Self-citationInterferon-induced RIP1/RIP3-mediated necrosis requires PKR and is licensed by FADD and caspases
Thapa, R. J., Nogusa, S., Chen, P., Maki, J. L., Lerro, A., Andrake, M., Rall, G. F., Degterev, A., & Balachandran, S. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1301218110 · Cited by 355 · 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
Molecular Mechanisms and Pathophysiology of Necrotic Cell Death
Vanlangenakker, N., Berghe, T. V., Krysko, D. V., Festjens, N., & Vandenabeele, P. (2008) · Current Molecular Medicine · doi:10.2174/156652408784221306 · Cited by 347 · see citing works
Self-citationCaspase Substrates and Cellular Remodeling
Crawford, E. D., & Wells, J. A. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061809-121639 · Cited by 343 · see citing works
Survival Function of the FADD-CASPASE-8-cFLIPL Complex
Dillon, C. P., Oberst, A., Weinlich, R., Janke, L. J., Kang, T.-B., Ben-Moshe, T., Mak, T. W., Wallach, D., & Green, D. R. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.03.010 · Cited by 331 · see citing works
Moquin, D. M., McQuade, T., & Chan, F. K.-M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0076841 · Cited by 320 · see citing works
Trichonas, G., Murakami, Y., Thanos, A., Morizane, Y., Kayama, M., Debouck, C. M., Hisatomi, T., Miller, J. W., & Vavvas, D. G. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009179107 · Cited by 313 · see citing works
Stat3 controls lysosomal-mediated cell death in vivo
Kreuzaler, P. A., Staniszewska, A. D., Li, W., Omidvar, N., Kedjouar, B., Turkson, J., Poli, V., Flavell, R. A., Clarkson, R. W. E., & Watson, C. J. (2011) · Nature Cell Biology · doi:10.1038/ncb2171 · Cited by 312 · see citing works
Specific aspartyl and calpain proteases are required for neurodegeneration in C. elegans
Syntichaki, P., Xu, K., Driscoll, M., & Tavernarakis, N. (2002) · Nature · doi:10.1038/nature01108 · Cited by 305 · see citing works
Widespread Mitochondrial Depletion via Mitophagy Does Not Compromise Necroptosis
Tait, S. W. G., Oberst, A., Quarato, G., Milasta, S., Haller, M., Wang, R., Karvela, M., Ichim, G., Yatim, N., Albert, M. L., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.10.034 · Cited by 303 · see citing works
Self-citationBonnet, M. C., Preukschat, D., Welz, P.-S., van Loo, G., Ermolaeva, M. A., Bloch, W., Haase, I., & Pasparakis, M. (2011) · Immunity · doi:10.1016/j.immuni.2011.08.014 · Cited by 295 · see citing works
Willingham, S. B., Bergstralh, D. T., O'Connor, W., Morrison, A. C., Taxman, D. J., Duncan, J. A., Barnoy, S., Venkatesan, M. M., Flavell, R. A., Deshmukh, M., et al. (2007) · Cell Host & Microbe · doi:10.1016/j.chom.2007.07.009 · Cited by 291 · see citing works
Duncan, J. A., Gao, X., Huang, M. T.-H., O’Connor, B. P., Thomas, C. E., Willingham, S. B., Bergstralh, D. T., Jarvis, G. A., Sparling, P. F., & Ting, J. P. ‐. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0802696 · Cited by 278 · 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 275 · see citing works
Poly(ADP-ribose) signaling in cell death
Virág, L., Robaszkiewicz, A., Rodriguez-Vargas, J. M., & Oliver, F. J. (2013) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2013.01.007 · Cited by 273 · see citing works
Sphingosine-induced apoptosis is dependent on lysosomal proteases
Kågedal, K., Ming, Z. H. A. O., Svensson, I., et al. (2001) · Biochemical Journal · doi:10.1042/bj3590335 · Cited by 273 · see citing works
Physiologic Functions of Cyclophilin D and the Mitochondrial Permeability Transition Pore
Elrod, J. W., & Molkentin, J. D. (2013) · Circulation Journal · doi:10.1253/circj.cj-13-0321 · Cited by 266 · see citing works
You, Z., Savitz, S. I., Yang, J., Degterev, A., Yuan, J., Cuny, G. D., Moskowitz, M. A., & Whalen, M. J. (2008) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2008.44 · Cited by 266 · see citing works
A Role of RIP3-Mediated Macrophage Necrosis in Atherosclerosis Development
Lin, J., Li, H., Yang, M. H., Ren, J., Huang, Z., Han, F., Huang, J., Ma, J., Zhang, D., Zhang, Z., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2012.12.012 · Cited by 266 · see citing works
Chen, W., Zhou, Z., Li, L., Zhong, C., Zheng, X., Wu, X., Zhang, Y., Ma, H., Huang, D., Li, W., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.435545 · Cited by 265 · see citing works
Rosenbaum, D. M., Degterev, A., David, J., Rosenbaum, P. S., Roth, S., Grotta, J. C., Cuny, G. D., Yuan, J., & Savitz, S. I. (2009) · Journal of Neuroscience Research · doi:10.1002/jnr.22314 · Cited by 248 · see citing works
Shaping organisms with apoptosis
Suzanne, M., & Steller, H. (2013) · Cell Death and Differentiation · doi:10.1038/cdd.2013.11 · Cited by 243 · see citing works
Necrotic Death Pathway in FAS Receptor Signaling
Matsumura, H., Shimizu, Y., Ohsawa, Y., Kawahara, A., Uchiyama, Y., & Nagata, S. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.6.1247 · Cited by 240 · see citing works
Structure–activity relationship study of novel necroptosis inhibitors
Teng, X., Degterev, A., Jagtap, P. G., et al. (2005) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2005.07.077 · Cited by 237 · see citing works
Zhao, Y. O., Khaminets, A., Hunn, J. P., & Howard, J. C. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000288 · Cited by 230 · see citing works
Vanlangenakker, N., Bertrand, M. J. M., Bogaert, P., Vandenabeele, P., & Berghe, T. V. (2011) · Cell Death and Disease · doi:10.1038/cddis.2011.111 · Cited by 228 · see citing works
Self-citationJavadov, S. A. (2000) · Cardiovascular Research · doi:10.1016/s0008-6363(99)00365-x · Cited by 225 · see citing works
Riboflavin kinase couples TNF receptor 1 to NADPH oxidase
Yazdanpanah, B., Wiegmann, K., Tchikov, V., Krut, O., Pongratz, C., Schramm, M., Kleinridders, A., Wunderlich, T., Kashkar, H., Utermöhlen, O., et al. (2009) · Nature · doi:10.1038/nature08206 · Cited by 215 · see citing works
Activity and specificity of necrostatin-1, small-molecule inhibitor of RIP1 kinase
Degterev, A., Maki, J. L., & Yuan, J. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.133 · Cited by 214 · see citing works
Yang, Q.-H., & Du, C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401253200 · Cited by 213 · see citing works
Ca2+-dependent proteases in ischemic neuronal death
Yamashima, T. (2004) · Cell Calcium · doi:10.1016/j.ceca.2004.03.001 · Cited by 213 · see citing works
Basit, F., Cristofanon, S., & Fulda, S. (2013) · Cell Death & Differentiation · doi:10.1038/cdd.2013.45 · Cited by 211 · see citing works
Sokolovska, A., Becker, C., Ip, W., Rathinam, V. A. K., Brudner, M., Paquette, N., Tanne, A. J., Vanaja, S. K., Moore, K. J., Fitzgerald, K. A., et al. (2013) · Nature Immunology · doi:10.1038/ni.2595 · Cited by 205 · see citing works
Poly(ADP-ribose): PARadigms and PARadoxes
Bürkle, A., & Virág, L. (2013) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2012.12.010 · Cited by 197 · see citing works
NADPH Oxidases in Heart Failure: Poachers or Gamekeepers?
Zhang, M., Perino, A., Ghigo, A., Hirsch, E., & Shah, A. M. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4550 · Cited by 196 · see citing works
de la Cruz, V. P., Carrillo-Mora, P. U., & Santamarı́a, A. (2012) · International Journal of Tryptophan Research · doi:10.4137/ijtr.s8158 · Cited by 193 · see citing works
Structural Insights into RIP3-Mediated Necroptotic Signaling
Xie, T., Peng, W., Yan, C., Wu, J., Gong, X., & Shi, Y. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.08.044 · Cited by 192 · see citing works
Regulation of Poly(ADP-ribose) Polymerase-1 by DNA Structure-specific Binding
Lonskaya, I., Potaman, V. N., Shlyakhtenko, L. S., Oussatcheva, E. A., Lyubchenko, Y. L., & Soldatenkov, V. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413483200 · Cited by 186 · see citing works
Case, C. L., Shin, S., & Roy, C. R. (2009) · Infection and Immunity · doi:10.1128/iai.01382-08 · Cited by 176 · see citing works
Intralysosomal iron chelation protects against oxidative stress‐induced cellular damage
Kurz, T., Gustafsson, B., & Brunk, U. T. (2006) · The FEBS Journal · doi:10.1111/j.1742-4658.2006.05321.x · Cited by 175 · see citing works
Lim, S. Y., Davidson, S. M., Mocanu, M. M., Yellon, D. M., & Smith, C. (2007) · Cardiovascular Drugs and Therapy · doi:10.1007/s10557-007-6067-6 · Cited by 175 · see citing works
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 · see citing works
ETosis: A Novel Cell Death Pathway
Wartha, F., & Henriques-Normark, B. (2008) · Science Signaling · doi:10.1126/stke.121pe25 · Cited by 173 · see citing works
Mattson, M. P., Zhu, H., Yu, J., & Kindy, M. S. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-04-01358.2000 · Cited by 172 · see citing works
NADPH oxidases as a source of oxidative stress and molecular target in ischemia/reperfusion injury
Kleikers, P. W. M., Wingler, K., Hermans, J. J. R., Diebold, I., Altenhöfer, S., Radermacher, K. A., Janssen, B. J., Görlach, A., & Schmidt, H. H. H. W. (2012) · Journal of Molecular Medicine · doi:10.1007/s00109-012-0963-3 · Cited by 172 · see citing works
Holzinger, D., Gieldon, L., Mysore, V., Nippe, N., Taxman, D. J., Duncan, J. A., Broglie, P. M., Marketon, K., Austermann, J., Vogl, T., et al. (2012) · Journal of Leukocyte Biology · doi:10.1189/jlb.0112014 · Cited by 170 · see citing works
Small heat-shock proteins protect from heat-stroke-associated neurodegeneration
Kourtis, N., Nikoletopoulou, V., & Tavernarakis, N. (2012) · Nature · doi:10.1038/nature11417 · Cited by 169 · see citing works
Sosna, J., Voigt, S., Mathieu, S., Lange, A., Thon, L., Davarnia, P., Herdegen, T., Linkermann, A., Rittger, A., Chan, F. K.-M., et al. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1381-6 · Cited by 162 · see citing works
Self-citationRIP1-driven autoinflammation targets IL-1α independently of inflammasomes and RIP3
Lukens, J. R., Vogel, P., Johnson, G. R., Kelliher, M. A., Iwakura, Y., Lamkanfi, M., & Kanneganti, T. (2013) · Nature · doi:10.1038/nature12174 · Cited by 157 · see citing works
Mitochondrial Permeability Transition and Cell Death: The Role of Cyclophilin D
Javadov, S. A., & Kuznetsov, A. V. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00076 · Cited by 157 · see citing works
Kalai, M., Loo, G., Berghe, T. V., Meeus, A., Burm, W., Saelens, X., & Vandenabeele, P. (2002) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401051 · Cited by 151 · see citing works
Self-citationGalluzzi, L., Berghe, T. V., Vanlangenakker, N., Büttner, S., Eisenberg, T., Vandenabeele, P., Madeo, F., & Kroemer, G. (2011) · International review of cytology · doi:10.1016/b978-0-12-386039-2.00001-8 · Cited by 150 · see citing works
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 149 · see citing works
Mack, C., Sickmann, A., Lembo, D., & Brune, W. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800168105 · Cited by 141 · see citing works
Antigen-mediated T cell expansion regulated by parallel pathways of death
Ch’en, I. L., Beisner, D. R., Degterev, A., Lynch, C., Yuan, J., Hoffmann, A., & Hedrick, S. Μ. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808043105 · Cited by 141 · see citing works
Shikonin Kills Glioma Cells through Necroptosis Mediated by RIP-1
Huang, C., Luo, Y., Zhao, J., Yang, F., Zhao, H., Fan, W., & Ge, P. (2013) · PLoS ONE · doi:10.1371/journal.pone.0066326 · Cited by 140 · see citing works
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
Positive and negative phosphorylation regulates RIP1- and RIP3-induced programmed necrosis
McQuade, T. J., Cho, Y., & Chan, F. K.-M. (2013) · Biochemical Journal · doi:10.1042/bj20130860 · Cited by 129 · see citing works
Colbert, L. E., Fisher, S. B., Hardy, C. W., Hall, W. A., Saka, B., Shelton, J. W., Petrova, A. V., Warren, M. D., Pantazides, B. G., Gandhi, K., et al. (2013) · Cancer · doi:10.1002/cncr.28144 · Cited by 126 · see citing works
Structure–activity relationship analysis of a novel necroptosis inhibitor, Necrostatin-5
Wang, K., Li, J., Degterev, A., et al. (2006) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2006.11.056 · Cited by 121 · see citing works
Cancer cell injury by cytotoxins from cobra venom is mediated through lysosomal damage
Feofanov, A. V., Sharonov, G. V., Astapova, M. V., Rodionov, D. I., Utkin, Y. N., & Arseniev, A. S. (2005) · Biochemical Journal · doi:10.1042/bj20041892 · Cited by 119 · see citing works
Cyclophilin D gene ablation protects mice from ischemic renal injury
Devalaraja-Narashimha, K. B., Diener, A. M., & Padanilam, B. J. (2009) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00239.2009 · Cited by 118 · see citing works
Wilson, C. A., & Browning, J. L. (2002) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401107 · Cited by 112 · see citing works
Regulation of Cell Survival and Death by Pyridine Nucleotides
Oka, S., Hsu, C., & Sadoshima, J. (2012) · Circulation Research · doi:10.1161/circresaha.111.247932 · Cited by 109 · see citing works
Dantrolene is neuroprotective in Huntington's disease transgenic mouse model
Chen, X., Wu, J., Lvovskaya, S., Herndon, E., Supnet, C. B., & Борисович, Б. И. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-81 · Cited by 107 · see citing works
Zou, J., Kawai, T., Tsuchida, T., Kozaki, T., Tanaka, H., Shin, K.-S., Kumar, H., & Akira, S. (2013) · Immunity · doi:10.1016/j.immuni.2012.12.007 · Cited by 103 · see citing works
Lysosomal biogenesis and function is critical for necrotic cell death in Caenorhabditis elegans
Artal‐Sanz, M., Samara, C., Syntichaki, P., & Tavernarakis, N. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200511103 · Cited by 100 · see citing works
Grooten, J., Goossens, V., Vanhaesebroeck, B., & Fiers, W. C. (1993) · Cytokine · doi:10.1016/s1043-4666(05)80003-1 · Cited by 99 · see citing works
Henke, N., Albrecht, P., Bouchachia, I., Ryazantseva, M., Knoll, K., Lewerenz, J., Kaznacheyeva, E. V., Maher, P. A., & Methner, A. (2013) · Cell Death and Disease · doi:10.1038/cddis.2012.216 · Cited by 97 · see citing works
Structure–activity relationship study of a novel necroptosis inhibitor, necrostatin-7
Zheng, W., Degterev, A., Hsu, E., et al. (2008) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2008.08.058 · Cited by 90 · see citing works
Autoschizis: a novel cell death
Jamison, J. M., Gilloteaux, J., Taper, H. S., Calderon, P. B., & Summers, J. L. (2002) · Biochemical Pharmacology · doi:10.1016/s0006-2952(02)00904-8 · Cited by 87 · see citing works
Derré, I., & Isberg, R. R. (2004) · Infection and Immunity · doi:10.1128/iai.72.11.6221-6229.2004 · Cited by 77 · see citing works
The role of PARP activation in glutamate-induced necroptosis in HT-22 cells
Xu, X., Chua, C. C., Zhang, M., Geng, D., Liu, C., Hamdy, R. C., & Chua, B. H. L. (2010) · Brain Research · doi:10.1016/j.brainres.2010.04.080 · Cited by 76 · see citing works
New components of the necroptotic pathway
Zhou, Z., Han, V. K. M., & Han, J. (2012) · Protein & Cell · doi:10.1007/s13238-012-2083-9 · Cited by 75 · see citing works
Averette, K. M., Pratt, M. R., Yang, Y., Bassilian, S., Whitelegge, J. P., Loo, J. A., Muir, T. W., & Bradley, K. A. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007913 · Cited by 66 · see citing works
Song, S., Gao, J., Wang, R. C., Li, R., Tian, Y., Wei, J.-Q., & Cui, J. (2012) · Molecular Medicine Reports · doi:10.3892/mmr.2012.1147 · Cited by 63 · see citing works
Yoshida, M., Yamashima, T., Zhao, L., et al. (2002) · Acta Neuropathologica · doi:10.1007/s00401-002-0554-4 · Cited by 55 · see citing works
Gabelloni, M. L., Sabbione, F., Jancic, C. C., Bass, J. I. F., Keitelman, I. A., Iula, L., Oleastro, M., Geffner, J. R., & Trevani, A. S. (2013) · European Journal of Immunology · doi:10.1002/eji.201243089 · Cited by 54 · see citing works
Gilloteaux, J., Jamison, J. M., Neal, D. R., Loukas, M., Doberzstyn, T., & Summers, J. L. (2010) · Ultrastructural Pathology · doi:10.3109/01913121003662304 · Cited by 53 · see citing works
Lysosomes as the target of yessotoxin in invertebrate and vertebrate cell lines
Malagoli, D., Marchesini, E., & Ottaviani, E. (2006) · Toxicology Letters · doi:10.1016/j.toxlet.2006.08.013 · Cited by 49 · see citing works
Kristián, T., Balan, I. S., Schuh, R. A., & Onken, M. (2011) · Journal of Neuroscience Research · doi:10.1002/jnr.22626 · Cited by 47 · see citing works
Yu, G., Zucchi, R., Ronca-Testoni, S., et al. (2000) · Basic Research in Cardiology · doi:10.1007/s003950050175 · Cited by 42 · see citing works
Morgan, M. J., Kim, Y., & Liu, Z.-G. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0803428 · Cited by 37 · see citing works
Dantrolene mitigates caerulein-induced pancreatitis in vivo in mice
Orabi, A. I., Shah, A. U., Ahmad, M. U., et al. (2010) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00498.2009 · Cited by 35 · see citing works
Karch, J. M., & Molkentin, J. D. (2012) · Circulation Research · doi:10.1161/circresaha.112.280990 · Cited by 33 · see citing works
Inhibition of poly(ADP-ribose) polymerase activity is insufficient to induce tetraploidy
Rosenthal, D. S. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.3.841 · Cited by 30 · see citing works
A novel necroptosis inhibitor—necrostatin-21 and its SAR study
Wu, Z., Li, Y., Cai, Y. C., Yuan, J., & Yuan, C. (2013) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2013.06.073 · Cited by 29 · see citing works
Multitasking p53 promotes necrosis
Baumann, K. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3401 · Cited by 26 · see citing works
Dantrolene is neuroprotective in vitro, but does not affect survival in SOD1G93A mice
Staats, K. A., Rillaer, M. V., Scheveneels, W., et al. (2012) · Neuroscience · doi:10.1016/j.neuroscience.2012.06.050 · Cited by 20 · 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
Self-citationInactivation of the ferroptosis regulator Gpx4 triggers acute renal failure in mice
Friedmann Angeli, J. P., Schneider, M., Proneth, B., Tyurina, Y. Y., Tyurin, V. A., Hammond, V. J., Herbach, N., Aichler, M., Walch, A., Eggenhofer, E., et al. (2014) · Nature Cell Biology · doi:10.1038/ncb3064 · Cited by 3,732 · see citing works
Mittler, R. (2017) · Trends in Plant Science · doi:10.1016/j.tplants.2016.08.002 · Cited by 3,499 · see citing works
NF-κB, inflammation, immunity and cancer: coming of age
Taniguchi, K., & Karin, M. (2018) · Nature Reviews Immunology · doi:10.1038/nri.2017.142 · Cited by 2,679 · see citing works
Glutaminolysis and transferrin regulate ferroptosis
Gao, M., Monian, P., Quadri, N., Ramasamy, R., & Jiang, X. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.06.011 · Cited by 2,069 · see citing works
Ferroptosis is an autophagic cell death process
Gao, M., Monian, P., Pan, Q., Zhang, W., Xiang, J., & Jiang, X. (2016) · Cell Research · doi:10.1038/cr.2016.95 · Cited by 1,899 · 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
Synchronized renal tubular cell death involves ferroptosis
Linkermann, A., Skouta, R., Himmerkus, N., Mulay, S. R., Dewitz, C., De Zen, F., Prokai, A., Zuchtriegel, G., Krombach, F., Welz, P.-S., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1415518111 · Cited by 1,126 · see citing works
Self-citationIdentification of ACSL4 as a biomarker and contributor of ferroptosis
Yuan, H., Li, X., Zhang, X., Kang, R., & Tang, D. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.08.124 · Cited by 1,071 · see citing works
P53 in survival, death and metabolic health: a lifeguard with a licence to kill.
Kruiswijk, F., Labuschagne, C. F., & Vousden, K. H. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm4007 · Cited by 1,080 · see citing works
Human Haploid Cell Genetics Reveals Roles for Lipid Metabolism Genes in Nonapoptotic Cell Death
Dixon, S. J., Winter, G. E., Musavi, L. S., Lee, E. D., Snijder, B., Rebsamen, M., Superti-Furga, G., & Stockwell, B. R. (2015) · ACS Chemical Biology · doi:10.1021/acschembio.5b00245 · Cited by 1,043 · 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
Self-citationGlobal survey of cell death mechanisms reveals metabolic regulation of ferroptosis
Shimada, K., Skouta, R., Kaplan, A., Yang, W. S., Hayano, M., Dixon, S. J., Brown, L. M., Valenzuela, C. A., Wolpaw, A. J., & Stockwell, B. R. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2079 · Cited by 1,017 · see citing works
Resolution of inflammation: a new therapeutic frontier
Fullerton, J. N., & Gilroy, D. W. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.39 · Cited by 937 · see citing works
Chen, X., He, W.-T., Hu, L., Li, J., Fang, Y., Wang, X., Xu, X., Wang, Z., Huang, K., & Han, J. (2016) · Cell Research · doi:10.1038/cr.2016.100 · Cited by 831 · see citing works
Apoptotic Caspases Prevent the Induction of Type I Interferons by Mitochondrial DNA
Rongvaux, A., Jackson, R., Harman, C. C. D., Li, T., West, A. P., de Zoete, M. R., Wu, Y., Yordy, B., Lakhani, S. A., Kuan, C.-Y., et al. (2014) · Cell · doi:10.1016/j.cell.2014.11.037 · Cited by 847 · see citing works
Consensus guidelines for the detection of immunogenic cell death
Kepp, O., Senovilla, L., Vitale, I., Vacchelli, E., Adjemian, S., Agostinis, P., Apetoh, L., Aranda, F., Barnaba, V., Bloy, N., et al. (2014) · OncoImmunology · doi:10.4161/21624011.2014.955691 · Cited by 832 · see citing works
Self-citationHSPB1 as a novel regulator of ferroptotic cancer cell death
Sun, X., Ou, Z., Xie, M., Kang, R., Fan, Y., Niu, X., Wang, H., Cao, L., & Tang, D. (2015) · Oncogene · doi:10.1038/onc.2015.32 · Cited by 666 · see citing works
Regulated necrosis: disease relevance and therapeutic opportunities
Conrad, M., Angeli, J. P. F., Vandenabeele, P., & Stockwell, B. R. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2015.6 · Cited by 630 · see citing works
Self-citationInitiation and execution mechanisms of necroptosis: an overview
Grootjans, S., Vanden Berghe, T., & Vandenabeele, P. (2017) · Cell Death & Differentiation · doi:10.1038/cdd.2017.65 · Cited by 566 · see citing works
Self-citationRIPK1 maintains epithelial homeostasis by inhibiting apoptosis and necroptosis
Dannappel, M., Vlantis, K., Kumari, S., Polykratis, A., Kim, C., Wachsmuth, L., Eftychi, C., Lin, J., Corona, T., Hermance, N., et al. (2014) · Nature · doi:10.1038/nature13608 · Cited by 534 · see citing works
Regulated 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
Self-citationImmune mechanisms linked to depression via oxidative stress and neuroprogression
Bakunina, N., Pariante, C. M., & Zunszain, P. A. (2015) · Immunology · doi:10.1111/imm.12443 · Cited by 444 · see citing works
Phototherapy in cancer treatment: strategies and challenges
Cai, Y., Chai, T., Nguyen, W., Liu, J., Xiao, E., Ran, X., Ran, Y., Du, D., Chen, W., & Chen, X. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02140-y · Cited by 453 · see citing works
Immunological impact of cell death signaling driven by radiation on the tumor microenvironment
Rodriguez-Ruiz, M. E., Vitale, I., Harrington, K. J., Melero, I., & Galluzzi, L. (2020) · Nature Immunology · doi:10.1038/s41590-019-0561-4 · Cited by 385 · see citing works
Louandre, C., Marcq, I., Bouhlal, H., Lachaier, E., Godin, C., Saidak, Z., François, C., Chatelain, D., Debuysscher, V., Barbare, J.-C., et al. (2015) · Cancer Letters · doi:10.1016/j.canlet.2014.11.014 · Cited by 374 · see citing works
Sweeney, T. E., Wong, H. R., & Khatri, P. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aaf7165 · Cited by 334 · 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
An essential role for functional lysosomes in ferroptosis of cancer cells
Torii, S., Shintoku, R., Kubota, C., Yaegashi, M., Torii, R., Sasaki, M., Suzuki, T., Mori, M., Yoshimoto, Y., Takeuchi, T., et al. (2016) · Biochemical Journal · doi:10.1042/bj20150658 · Cited by 349 · see citing works
Unraveling the Potential Role of Glutathione in Multiple Forms of Cell Death in Cancer Therapy
Lv, H., Zhen, C., Liu, J., Yang, P., Hu, L., & Shang, P. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/3150145 · Cited by 320 · see citing works
Dixon, S. J. (2017) · Immunological Reviews · doi:10.1111/imr.12533 · Cited by 314 · see citing works
Beckwith, K. S., Beckwith, M. S., Ullmann, S., Sætra, R. S., Kim, H., Marstad, A., Åsberg, S. E., Strand, T. A., Haug, M., Niederweis, M., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16143-6 · Cited by 282 · see citing works
Organelle-specific initiation of cell death
Galluzzi, L., Bravo-San Pedro, J. M., & Kroemer, G. (2014) · Nature Cell Biology · doi:10.1038/ncb3005 · Cited by 239 · see citing works
Iannielli, A., Bido, S., Folladori, L., Segnali, A., Cancellieri, C., Maresca, A., Massimino, L., Rubio, A., Morabito, G., Caporali, L., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.01.089 · Cited by 239 · see citing works
Roca, F. J., Whitworth, L. J., Redmond, S., Jones, A. A., & Ramakrishnan, L. (2019) · Cell · doi:10.1016/j.cell.2019.08.004 · Cited by 233 · see citing works
AIM2 inflammasome surveillance of DNA damage shapes neurodevelopment
Lammert, C. R., Frost, E. L., Bellinger, C. E., Bolte, A. C., McKee, C. A., Hurt, M. E., Paysour, M. J., Ennerfelt, H. E., & Lukens, J. R. (2020) · Nature · doi:10.1038/s41586-020-2174-3 · Cited by 223 · see citing works
Lytic cell death in metabolic liver disease
Gautheron, J., Gores, G. J., & Rodrigues, C. M. P. (2020) · Journal of Hepatology · doi:10.1016/j.jhep.2020.04.001 · Cited by 225 · see citing works
“However, recent findings highlight multiple forms of regulated necrotic modalities, including necroptosis, pyroptosis and ferroptosis, that share key morphologic features with passive necrosis yet have welldefined and regulated causal mechanisms [2, 3].”
BackgroundMitochondrial Permeability Transition: New Findings and Persisting Uncertainties
Izzo, V., Bravo-San Pedro, J. M., Sica, V., Kroemer, G., & Galluzzi, L. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.04.006 · Cited by 205 · see citing works
Current Challenges and Opportunities of Photodynamic Therapy against Cancer
Huis in ‘t Veld, R. V., Heuts, J., Ma, S., Cruz, L. J., Ossendorp, F. A., & Jager, M. J. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15020330 · Cited by 159 · see citing works
A20 and cell death-driven inflammation
Priem, D., van Loo, G., & Bertrand, M. J. M. (2020) · Trends in Immunology · doi:10.1016/j.it.2020.03.001 · Cited by 139 · see citing works
Kondylis, V., Polykratis, A., Ehlken, H., Ochoa-Callejero, L., Straub, B. K., Krishna-Subramanian, S., Van, T.-M., Curth, H.-M., Heise, N., Weih, F., et al. (2015) · Cancer Cell · doi:10.1016/j.ccell.2015.10.001 · Cited by 131 · see citing works
Pathophysiological role of different tubular epithelial cell death modes in acute kidney injury
Sancho-Martínez, S. M., López-Novoa, J. M., & López-Hernández, F. J. (2015) · Clinical Kidney Journal · doi:10.1093/ckj/sfv069 · Cited by 130 · see citing works
Self-defense of macrophages against oxidative injury: Fighting for their own survival
Virág, L., Jaén, R. I., Regdon, Z., Boscá, L., & Prieto, P. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101261 · Cited by 121 · see citing works
Walkowski, B., Kleibert, M., Majka, M., & Wojciechowska, M. (2022) · Cells · doi:10.3390/cells11091553 · Cited by 117 · see citing works
HS-1371, a novel kinase inhibitor of RIP3-mediated necroptosis
Park, H.-H., Park, S.-Y., Mah, S., Park, J.-H., Hong, S.-S., Hong, S., & Kim, Y.-S. (2018) · Experimental & Molecular Medicine · doi:10.1038/s12276-018-0152-8 · Cited by 110 · see citing works
Activation of cell-surface proteases promotes necroptosis, inflammation and cell migration
Cai, Z., Zhang, A., Choksi, S., Li, W., Li, T., Zhang, X.-M., & Liu, Z.-G. (2016) · Cell Research · doi:10.1038/cr.2016.87 · Cited by 103 · see citing works
Linear ubiquitination at a glance
Spit, M., Rieser, E., & Walczak, H. (2019) · Journal of Cell Science · doi:10.1242/jcs.208512 · Cited by 94 · see citing works
Self-citationHulina, A., Grdić Rajković, M., Jakšić Despot, D., Jelić, D., Dojder, A., Čepelak, I., & Rumora, L. (2018) · Cell Stress and Chaperones · doi:10.1007/s12192-017-0847-0 · Cited by 92 · see citing works
Metabolism and iron signaling in ferroptotic cell death
Gao, M., Monian, P., & Jiang, X. (2015) · Oncotarget · doi:10.18632/oncotarget.5671 · Cited by 71 · see citing works
The Tumor Suppressor Hace1 Is a Critical Regulator of TNFR1-Mediated Cell Fate
Tortola, L., Nitsch, R., Bertrand, M. J. M., Kogler, M., Redouane, Y., Kozieradzki, I., Uribesalgo, I., Fennell, L. M., Daugaard, M., Klug, H., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.04.032 · Cited by 64 · see citing works
Self-citationInterferons Transcriptionally Up-Regulate MLKL Expression in Cancer Cells
Knuth, A.-K., Rösler, S., Schenk, B., Kowald, L., van Wijk, S. J. L., & Fulda, S. (2019) · Neoplasia · doi:10.1016/j.neo.2018.11.002 · Cited by 63 · see citing works
Regdon, Z., Robaszkiewicz, A., Kovács, K., Rygielska, Ż., Hegedűs, C., Bodoor, K., Szabó, É., & Virág, L. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.11.034 · Cited by 59 · see citing works
Ito, F., Yanatori, I., Maeda, Y., Nimura, K., Ito, S., Hirayama, T., Nagasawa, H., Kohyama, N., Okazaki, Y., Akatsuka, S., et al. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101616 · Cited by 45 · see citing works
“Recent studies imply that cell death regulated by certain signal pathways in the initial phase may result in multiple forms of necrosis, ending in the rupture of plasma membrane [53].”
BackgroundRIP1 kinase activity-dependent roles in embryonic development of Fadd-deficient mice
Liu, Y., Fan, C., Zhang, Y., Yu, X., Wu, X., Zhang, X., Zhao, Q., Zhang, H., Xie, Q., Li, M., et al. (2017) · Cell Death & Differentiation · doi:10.1038/cdd.2017.78 · Cited by 42 · see citing works
Linkermann, A., Konstantinidis, K., & Kitsis, R. N. (2016) · Cell Death & Differentiation · doi:10.1038/cdd.2015.151 · Cited by 36 · see citing works
Self-citationZhang, D., Wang, T., Zhou, Y., & Zhang, X. (2023) · Medicine · doi:10.1097/md.0000000000033468 · Cited by 28 · see citing works
RIP3 antagonizes a TSC2-mediated pro-survival pathway in glioblastoma cell death
Fettweis, G., Di Valentin, E., L'homme, L., Lassence, C., Dequiedt, F., Fillet, M., Coupienne, I., & Piette, J. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.10.014 · Cited by 26 · see citing works
Bencze, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms24010362 · Cited by 20 · see citing works
Boda, F., Banfai, K., Garai, K., Kovacs, B., Almasi, A., Scheffer, D., Sinkler, R. L., Csonka, R., Czompoly, T., & Kvell, K. (2020) · Journal of Venomous Animals and Toxins including Tropical Diseases · doi:10.1590/1678-9199-jvatitd-2020-0057 · Cited by 2 · see citing works
- Authors
- Berghe, T. V., Linkermann, A., Jouan-Lanhouet, S., Walczak, H., & Vandenabeele, P.
- Affiliations
- Vlaams Instituut voor Biotechnologie (BE)
- Christian-Albrechts-Universität zu Kiel (DE)
- University College London (GB)
- Corresponding author
- Vandenabeele, Peter
- ORCID
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2014-01-23
- Volume
- 15
- Issue
- 2
- Pages
- 135-147
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W2081053802
- Cited by
- 1,735
- References
- 188
- Citations by year
- 2026: 71 · 2025: 115 · 2024: 100 · 2023: 143 · 2022: 136 · 2021: 163 · 2020: 136 · 2019: 157 · 2018: 160 · 2017: 140 · 2016: 175 · 2015: 151 · 2014: 86 · 2013: 1
- FWCI
- 17.32
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Ghent University Academic Bibliography (Ghent University) (submittedVersion)
- Funders
- Wellcome Trust (096831)
- Cancer Research UK
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Ferroptosis and cancer prognosis
- Social Sciences › Anthropology › Death, Funerary Practices, and Mourning
- Keywords
- regulated necrosis, non-apoptotic cell death, necroptosis, RIPK1, RIPK3, MLKL, parthanatos, oxytosis, ferroptosis, NETosis, pyroptosis, cell death pathways, therapeutic targeting
- MeSH terms
- Humans, Necrosis, Protein Kinases, Signal Transduction, Cell Death, Apoptosis, Receptor-Interacting Protein Serine-Threonine Kinases, Molecular Targeted Therapy
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