The DOI matches its Crossref record; 126 of the 130 references it cites were found in a registry or an index.
Die another way – non-apoptotic mechanisms of cell death
Open accessAbstract
Regulated, programmed cell death is crucial for all multicellular organisms. Cell death is essential in many processes, including tissue sculpting during embryogenesis, development of the immune system and destruction of damaged cells. The best-studied form of programmed cell death is apoptosis, a process that requires activation of caspase proteases. Recently it has been appreciated that various non-apoptotic forms of cell death also exist, such as necroptosis and pyroptosis. These non-apoptotic cell death modalities can be either triggered independently of apoptosis or are engaged should apoptosis fail to execute. In this Commentary, we discuss several regulated non-apoptotic forms of cell death including necroptosis, autophagic cell death, pyroptosis and caspase-independent cell death. We outline what we know about their mechanism, potential roles in vivo and define outstanding questions. Finally, we review data arguing that the means by which a cell dies actually matters, focusing our discussion on inflammatory aspects of cell death.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“In contrast to the highly pro-inflammatory necrotic types of cell death, such as necroptosis and pyroptosis, apoptosis and autophagy do not tend to trigger an inflammatory response166.”
From Inflammation and its resolution in atherosclerosis: mediators and therapeutic opportunities (2019) · cites this paper as [166]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
Narendra, D., Tanaka, A., Suen, D.-F., & Youle, R. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200809125 · Cited by 4,026
Proapoptotic BAX and BAK: A Requisite Gateway to Mitochondrial Dysfunction and Death
Wei, M. C., Zong, W.-X., Cheng, E. H.-Y., Lindsten, T., Panoutsakopoulou, V., Ross, A. J., Roth, K. A., MacGregor, G. R., Thompson, C. B., & Korsmeyer, S. J. (2001) · Science · doi:10.1126/science.1059108 · Cited by 3,988
Bcl-2 Antiapoptotic Proteins Inhibit Beclin 1-Dependent Autophagy
Pattingre, S., Tassa, A., Qu, X., Garuti, R., Liang, X. H., Mizushima, N., Packer, M., Schneider, M. D., & Levine, B. (2005) · Cell · doi:10.1016/j.cell.2005.07.002 · Cited by 3,536
Pyroptosis: host cell death and inflammation
Bergsbaken, T., Fink, S. L., & Cookson, B. T. (2009) · Nature Reviews Microbiology · doi:10.1038/nrmicro2070 · Cited by 3,288
Calreticulin exposure dictates the immunogenicity of cancer cell death
Obeid, M., Tesniere, A., Ghiringhelli, F., Fimia, G. M., Apetoh, L., Perfettini, J.-L., Castedo, M., Mignot, G., Panaretakis, T., Casares, N., et al. (2007) · Nature Medicine · doi:10.1038/nm1523 · Cited by 3,216
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
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 2,708
Caspase Functions in Cell Death and DiseasePreprint
McIlwain, D. R., Berger, T., & Mak, T. W. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008656 · Cited by 2,702
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
Autophagy in Human Health and Disease
Choi, A. M. K., Ryter, S. W., & Levine, B. (2013) · New England Journal of Medicine · doi:10.1056/nejmra1205406 · Cited by 2,583
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
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
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
Self-citationReceptor 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
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 1,987
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
How dying cells alert the immune system to danger
Kono, H., & Rock, K. L. (2008) · Nature Reviews Immunology · doi:10.1038/nri2215 · Cited by 1,737
Autophagic cell death: the story of a misnomer
Kroemer, G., & Levine, B. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2529 · Cited by 1,453
TNF-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 1,398
DRAM, a p53-Induced Modulator of Autophagy, Is Critical for Apoptosis
Crighton, D., Wilkinson, S., O'Prey, J., Syed, N., Smith, P., Harrison, P. R., Gasco, M., Garrone, O., Crook, T., & Ryan, K. M. (2006) · Cell · doi:10.1016/j.cell.2006.05.034 · Cited by 1,380
Autophagy-Dependent Anticancer Immune Responses Induced by Chemotherapeutic Agents in Mice
Michaud, M., Martins, I., Sukkurwala, A. Q., Adjemian, S., Ma, Y., Pellegatti, P., Shen, S., Kepp, O., Scoazec, M., Mignot, G., et al. (2011) · Science · doi:10.1126/science.1208347 · Cited by 1,377
Role of Bcl-2 family proteins in a non-apoptotic programmed cell death dependent on autophagy genes
Shimizu, S., Kanaseki, T., Mizushima, N., Mizuta, T., Arakawa-Kobayashi, S., Thompson, C. B., & Tsujimoto, Y. (2004) · Nature Cell Biology · doi:10.1038/ncb1192 · Cited by 1,358
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
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
Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors
Thome, M., Schneider, P., Hofmann, K., Fickenscher, H., Meinl, E., Neipel, F., Mattmann, C., Burns, K., Bodmer, J.-L., Schröter, M., et al. (1997) · Nature · doi:10.1038/386517a0 · Cited by 1,316
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 3×
“In vivo support of this model comes from the finding that embryonic lethality caused by caspase-8 or FADD loss in vivo can be completely rescued by RIPK3 ablation (Dillon et al., 2012; Kaiser et al., 2011; Oberst et al., 2011).”
BackgroundSelf-citationRegulation of an ATG7 - beclin 1 Program of Autophagic Cell Death by Caspase-8
Yu, L., Alva, A. S., Su, H. C., Dutt, P., Freundt, E. C., Welsh, S. J., Baehrecke, E. H., & Lenardo, M. J. (2004) · Science · doi:10.1126/science.1096645 · Cited by 1,249
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
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
Immunogenic and tolerogenic cell death
Green, D. R., Ferguson, T., Zitvogel, L., & Kroemer, G. (2009) · Nature Reviews Immunology · doi:10.1038/nri2545 · Cited by 1,176
Self-citationCalpain-mediated cleavage of Atg5 switches autophagy to apoptosis
Yousefi, S., Perozzo, R., Schmid, I., Ziemiecki, A., Schaffner, T., Scapozza, L., Brunner, T., & Simon, H.-U. (2006) · Nature Cell Biology · doi:10.1038/ncb1482 · Cited by 1,158
Functional and physical interaction between Bcl‐XL and a BH3‐like domain in Beclin‐1
Maiuri, M. C., Toumelin-Braizat, G. L., Criollo, A., Rain, J., Gautier, F., Juin, P. P., Tasdemir, E., Pierron, G., Troulinaki, K., Tavernarakis, N., et al. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601689 · Cited by 1,154
Apaf1 Is Required for Mitochondrial Pathways of Apoptosis and Brain Development
Yoshida, H., Kong, Y., Yoshida, R., Elia, A., Hakem, A., Hakem, R., Penninger, J. M., & Mak, T. W. (1998) · Cell · doi:10.1016/s0092-8674(00)81733-x · Cited by 1,138
Protection against Fatal Sindbis Virus Encephalitis by Beclin, a Novel Bcl-2-Interacting Protein
Liang, X. H., Kleeman, L. K., Jiang, H., Gordon, G. W., Goldman, J. E., Berry, G., Herman, B. A., & Levine, B. (1998) · Journal of Virology · doi:10.1128/jvi.72.11.8586-8596.1998 · Cited by 1,128
Fink, S. L., & Cookson, B. T. (2006) · Cellular Microbiology · doi:10.1111/j.1462-5822.2006.00751.x · Cited by 1,114
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
Ray, C. A., Black, R. A., Kronheim, S. R., Greenstreet, T. A., Sleath, P. R., Salvesen, G. S., & Pickup, D. J. (1992) · Cell · doi:10.1016/0092-8674(92)90223-y · Cited by 977
Wang, Z., Jiang, H., Chen, S., Du, F., & Wang, X. (2012) · Cell · doi:10.1016/j.cell.2011.11.030 · Cited by 949
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 941
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 925
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
Apaf1 (CED-4 Homolog) Regulates Programmed Cell Death in Mammalian Development
Cecconi, F., Álvarez-Bolado, G., Meyer, B. I., Roth, K. A., & Gruß, P. (1998) · Cell · doi:10.1016/s0092-8674(00)81732-8 · Cited by 894
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 878
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 837
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 803
The Salmonella invasin SipB induces macrophage apoptosis by binding to caspase-1
Hersh, D., Monack, D. M., Smith, M. R., Ghori, N., Falkow, S., & Zychlinsky, A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.2396 · Cited by 788
Upton, J. W., Kaiser, W. J., & Mocarski, E. S. (2012) · Cell Host & Microbe · doi:10.1016/j.chom.2012.01.016 · Cited by 758
He, S., Liang, Y., Shao, F., & Wang, X. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1116302108 · Cited by 751
Activity of Protein Kinase RIPK3 Determines Whether Cells Die by Necroptosis or Apoptosis
Newton, K., Dugger, D. L., Wickliffe, K. E., Kapoor, N., de Almagro, M. C., Vucic, D., Komuves, L., Ferrando, R. E., French, D. M., Webster, J., et al. (2014) · Science · doi:10.1126/science.1249361 · Cited by 687
Autophagic programmed cell death by selective catalase degradation
Yu, L., Wan, F., Dutta, S., Welsh, S., Liu, Z., Freundt, E. C., Baehrecke, E. H., & Lenardo, M. J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0511288103 · Cited by 680
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
Cellular Mechanisms Controlling Caspase Activation and FunctionPreprint
Parrish, A. B., Freel, C. D., & Kornbluth, S. A. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008672 · Cited by 659
Regulation of RIP1 kinase signalling at the crossroads of inflammation and cell death
Ofengeim, D., & Yuan, J. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3683 · Cited by 635
Kazama, H., Ricci, J.-E., Herndon, J. M., Hoppe, G., Green, D. R., & Ferguson, T. A. (2008) · Immunity · doi:10.1016/j.immuni.2008.05.013 · Cited by 627
Self-citationAutophagy in Human Health and Disease
Doria, A., Gatto, M., & Punzi, L. (2013) · New England Journal of Medicine · doi:10.1056/nejmc1303158 · Cited by 620
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 · cited 1×
“Accordingly, a cell-permeating Beclin-1-derived peptide has recently been found to induce cell death – termed autosis – in an autophagy-dependent but apoptosis- and necroptosis-independent manner (Liu et al., 2013).”
BackgroundSelf-citationFADD 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 · cited 2×
“RIPK3-dependent inflammation and necrosis in the intestine and skin (Bonnet et al., 2011; Panayotova-Dimitrova et al., 2013; Weinlich et al., 2013; Welz et al., 2011).”
BackgroundVirus 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
Beginnings of a Good Apoptotic Meal: The Find-Me and Eat-Me Signaling Pathways
Ravichandran, K. S. (2011) · Immunity · doi:10.1016/j.immuni.2011.09.004 · Cited by 559
Essential Roles of Atg5 and FADD in Autophagic Cell Death
Pyo, J.-O., Jang, M.-H., Kwon, Y., Lee, H.-J., Jun, J.-I., Woo, H., Cho, D.-H., Choi, B., Lee, H., Kim, J.-H., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413934200 · Cited by 553
Colell, A., Ricci, J.-E., Tait, S., Milasta, S., Maurer, U., Bouchier-Hayes, L., Fitzgerald, P., Guio-Carrion, A., Waterhouse, N. J., Li, C. W., et al. (2007) · Cell · doi:10.1016/j.cell.2007.03.045 · Cited by 516
Self-citationApoptosis blocks Beclin 1-dependent autophagosome synthesis: an effect rescued by Bcl-xL
Luo, S., & Rubinsztein, D. C. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.121 · Cited by 495
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
Self-citationInhibitor 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
Dissecting p53 tumor suppressor functions in vivo
Schmitt, C. A., Fridman, J. S., Yang, M., Baranov, E., Hoffman, R. M., & Lowe, S. W. (2002) · Cancer Cell · doi:10.1016/s1535-6108(02)00047-8 · Cited by 481
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 462
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 459
Arnoult, D., Gaume, B. R., Karbowski, M., Sharpe, J. C., Cecconi, F., & Youle, R. J. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg423 · Cited by 455
Elgendy, M., Sheridan, C., Brumatti, G., & Martin, S. J. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.02.009 · Cited by 426
Regulation and Function of Autophagy during Cell Survival and Cell DeathPreprint
Das, G., Shravage, B. V., & Baehrecke, E. H. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008813 · Cited by 422
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
Fink, S. L., Bergsbaken, T., & Cookson, B. T. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707370105 · Cited by 412
Vaughn, A. E., & Deshmukh, M. (2008) · Nature Cell Biology · doi:10.1038/ncb1807 · Cited by 408
Steroid regulated programmed cell death during Drosophila metamorphosis
Jiang, C., Baehrecke, E. H., & Thummel, C. S. (1997) · Development · doi:10.1242/dev.124.22.4673 · Cited by 392
Autophagy, Not Apoptosis, Is Essential for Midgut Cell Death in Drosophila
Denton, D., Shravage, B., Simin, R., Mills, K., Berry, D. L., Baehrecke, E. H., & Kumar, S. (2009) · Current Biology · doi:10.1016/j.cub.2009.08.042 · Cited by 385
Loss of Omi mitochondrial protease activity causes the neuromuscular disorder of mnd2 mutant mice
Jones, J. M., Datta, P., Srinivasula, S. M., Ji, W., Gupta, S., Zhang, Z., Davies, E., Hajnóczky, G., Saunders, T. L., Keuren, M. L. V., et al. (2003) · Nature · doi:10.1038/nature02052 · Cited by 383
Caspase-independent cell death: leaving the set without the final cut
Tait, S. W. G., & Green, D. R. (2008) · Oncogene · doi:10.1038/onc.2008.311 · Cited by 366
Self-citationRIP3: a molecular switch for necrosis and inflammationPreprint
Moriwaki, K., & Chan, F. K.-M. (2013) · Genes & Development · doi:10.1101/gad.223321.113 · Cited by 364
Vaccinia virus immune evasion: mechanisms, virulence and immunogenicity
Smith, G. L., Benfield, C. T. O., de Motes, C. M., Mazzon, M., Ember, S. W., Ferguson, B. J., & Sumner, R. P. (2013) · Journal of General Virology · doi:10.1099/vir.0.055921-0 · Cited by 364
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 · cited 1×
“In vivo support of this model comes from the finding that embryonic lethality caused by caspase-8 or FADD loss in vivo can be completely rescued by RIPK3 ablation (Dillon et al., 2012; Kaiser et al., 2011; Oberst et al., 2011).”
BackgroundSelf-citationInterdigital cell death can occur through a necrotic and caspase-independent pathway
Chautan, M., Chazal, G., Cecconi, F., Gruß, P., & Golstein, P. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80425-4 · Cited by 325
Martinou, I., Desagher, S., Eskes, R., Antonsson, B. E., André, É., Fakan, S., & Martinou, J. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.144.5.883 · Cited by 316
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
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
Apoptotic cell clearance by bronchial epithelial cells critically influences airway inflammation
Juncadella, I. J., Kadl, A., Sharma, A. K., Shim, Y. M., Hochreiter, A. E., Borish, L., & Ravichandran, K. S. (2012) · Nature · doi:10.1038/nature11714 · Cited by 290
ATG12 Conjugation to ATG3 Regulates Mitochondrial Homeostasis and Cell Death
Radoshevich, L., Murrow, L., Chen, N., Fernandez, E., Roy, S., Fung, C., & Debnath, J. (2010) · Cell · doi:10.1016/j.cell.2010.07.018 · Cited by 290
Evidence of a Novel Event during Neuronal Death
Deshmukh, M., & Johnson, E. M. (1998) · Neuron · doi:10.1016/s0896-6273(00)80587-5 · Cited by 281
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 272
NEMO and RIP1 Control Cell Fate in Response to Extensive DNA Damage via TNF-α Feedforward Signaling
Biton, S., & Ashkenazi, A. (2011) · Cell · doi:10.1016/j.cell.2011.02.023 · Cited by 262
Betin, V. M. S., & Lane, J. D. (2009) · Journal of Cell Science · doi:10.1242/jcs.046250 · Cited by 261
Muñoz‐Pinedo, C., Guío-Carrión, A., Goldstein, J. C., FITZGERALD, P. J., Newmeyer, D. D., & Green, D. R. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603007103 · Cited by 253
Self-citationBergsbaken, T., & Cookson, B. T. (2007) · PLoS Pathogens · doi:10.1371/journal.ppat.0030161 · Cited by 251
Cellular IAPs inhibit a cryptic CD95-induced cell death by limiting RIP1 kinase recruitment
Geserick, P., Hupe, M., Moulin, M., Wong, W. W.-L., Feoktistova, M., Kellert, B., Gollnick, H. P. M., Silke, J., & Leverkus, M. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200904158 · Cited by 244
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 242
Control of Autophagic Cell Death by Caspase-10 in Multiple Myeloma
Lamy, L., Ngo, V. N., Emre, N. C. T., Shaffer, A. L., Yang, Y., Tian, E., Nair, V., Kruhlak, M. J., Zingone, A., Landgren, O., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.02.017 · Cited by 229
Means to an end: apoptosis and other cell death mechanisms
(2011) · Choice Reviews Online · doi:10.5860/choice.48-5678 · Cited by 224
Otto, G. P., Wu, M. Y., Kazgan, N., Anderson, O. R., & Kessin, R. H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212467200 · Cited by 221
Basit, F., Cristofanon, S., & Fulda, S. (2013) · Cell Death & Differentiation · doi:10.1038/cdd.2013.45 · Cited by 211
Bim Inhibits Autophagy by Recruiting Beclin 1 to Microtubules
Luo, S., Garcı́a-Arencibia, M., Zhao, R., Puri, C., Toh, P. P. C., Sadiq, O., & Rubinsztein, D. C. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.05.040 · Cited by 209
A Perspective on Mammalian Caspases as Positive and Negative Regulators of Inflammation
Martin, S. J., Henry, C. M., & Cullen, S. P. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.04.026 · Cited by 206
Resistance to Caspase-Independent Cell Death Requires Persistence of Intact Mitochondria
Tait, S. W. G., Parsons, M. J., Llambi, F., Bouchier‐Hayes, L., Connell, S., Muñoz‐Pinedo, C., & Green, D. R. (2010) · Developmental Cell · doi:10.1016/j.devcel.2010.03.014 · Cited by 204
Self-citationAdult Apaf-1-Deficient Mice Exhibit Male Infertility
Honarpour, N., Du, C., Richardson, J. A., Hammer, R. E., Wang, X., & Herz, J. (2000) · Developmental Biology · doi:10.1006/dbio.1999.9585 · Cited by 203
Necroptosis in Immunity and Ischemia-Reperfusion Injury
Linkermann, A., Hackl, M. J., Kunzendorf, U., Walczak, H., Krautwald, S., & Jevnikar, A. M. (2013) · American Journal of Transplantation · doi:10.1111/ajt.12448 · Cited by 193
Inflammasomes: far beyond inflammation
Henao‐Mejia, J., Elinav, E., Strowig, T., & Flavell, R. A. (2012) · Nature Immunology · doi:10.1038/ni.2257 · Cited by 188
Bcl-2 complexed with Beclin-1 maintains full anti-apoptotic function
Ciechomska, I. A., Goemans, G. C., Skepper, J. N., & Tolkovsky, A. M. (2009) · Oncogene · doi:10.1038/onc.2009.60 · Cited by 186
RIPK-Dependent Necrosis and Its Regulation by Caspases: A Mystery in Five Acts
Green, D. R., Oberst, A., Dillon, C. P., Weinlich, R., & Salvesen, G. S. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.09.003 · Cited by 175
Self-citationAutophagy in Protein and Organelle TurnoverPreprint
Mizushima, N. (2011) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2011.76.011023 · Cited by 170
It cuts both ways: reconciling the dual roles of caspase 8 in cell death and survival
Oberst, A., & Green, D. R. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3214 · Cited by 160
Self-citationAutophagy Suppresses RIP Kinase-Dependent Necrosis Enabling Survival to mTOR Inhibition
Bray, K., Mathew, R., Lau, A., Kamphorst, J. J., Fan, J., Chen, J., Chen, H.-Y., Ghavami, A., Stein, M. N., DiPaola, R. S., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041831 · Cited by 159
Protective Roles for Caspase-8 and cFLIP in Adult Homeostasis
Weinlich, R., Oberst, A., Dillon, C. P., Janke, L. J., Milasta, S., Lukens, J. R., Rodriguez, D. A., Gurung, P., Savage, C., Kanneganti, T. D., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.08.045 · Cited by 157
Self-citationTNF can activate RIPK3 and cause programmed necrosis in the absence of RIPK1
Moujalled, D., Cook, W. D., Okamoto, T., Murphy, J. M., Lawlor, K. E., Vince, J. E., & Vaux, D. L. (2013) · Cell Death and Disease · doi:10.1038/cddis.2012.201 · Cited by 155
Galluzzi, 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 152
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 140
Rébé, C., Cathelin, S., Launay, S., Filomenko, R., Prévotat, L., L'ollivier, C., Gyan, E., Micheau, O., Grant, S., Dubart-Kupperschmitt, A., et al. (2007) · Blood · doi:10.1182/blood-2006-03-011585 · Cited by 138
Lartigue, L., Kushnareva, Y., Seong, Y., Lin, H. H., Faustin, B., & Newmeyer, D. D. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-07-0649 · Cited by 138
Butylated hydroxyanisole is more than a reactive oxygen species scavenger
Festjens, N., Kalai, M., Smet, J., Meeus, A., Coster, R. V., Saelens, X., & Vandenabeele, P. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401746 · Cited by 105
Nonomura, K., Yamaguchi, Y., Hamachi, M., Koike, M., Uchiyama, Y., Nakazato, K., Mochizuki, A., Sakaue-Sawano, A., Miyawaki, A., Yoshida, H., et al. (2013) · Developmental Cell · doi:10.1016/j.devcel.2013.11.015 · Cited by 103
Switch from Caspase-dependent to Caspase-independent Death during Heart Development
Bahí, N., Zhang, J., Llovera, M., Ballester, M., Comella, J. X., & Sanchís, D. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601025200 · Cited by 103
Autophagy Gene Disruption Reveals a Non-vacuolar Cell Death Pathway in Dictyostelium
Kosta, A., Roisin-Bouffay, C., Luciani, M., Otto, G. P., Kessin, R. H., & Golstein, P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408924200 · Cited by 92
Apoptotic and Nonapoptotic Caspase Functions in Animal DevelopmentPreprint
Miura, M. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008664 · Cited by 81
cFLIP Regulates Skin Homeostasis and Protects against TNF-Induced Keratinocyte Apoptosis
Panayotova‐Dimitrova, D., Feoktistova, M., Ploesser, M., Kellert, B., Hupe, M., Horn, S., Makarov, R., Jensen, F., Porubský, Š., Schmieder, A., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.09.035 · Cited by 78
Autophagy functions in programmed cell death
Berry, D. L., & Baehrecke, E. H. (2008) · Autophagy · doi:10.4161/auto.5575 · Cited by 67
Chromatin modification of Apaf-1 restricts the apoptotic pathway in mature neurons
Wright, K. M., Smith, M. I., Farrag, L., & Deshmukh, M. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200708086 · Cited by 56
Ferraro, E., Pulicati, A., Cencioni, M. T., Cozzolino, M., Navoni, F., Martino, S. D., Nardacci, R., Carrı̀, M. T., & Cecconi, F. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-09-0858 · Cited by 55
Autophagy activity contributes to programmed cell death in Caenorhabditis elegans
Wang, H., Lu, Q., Cheng, S., Wang, X., & Zhang, H. (2013) · Autophagy · doi:10.4161/auto.26152 · Cited by 39
Goemans, C. G., Boya, P., Skirrow, C. J., & Tolkovsky, A. M. (2008) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402290 · Cited by 26
Flagged first, then by citations
4 of the 130 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Targeting apoptosis in cancer therapy
Carneiro, B. A., & El‐Deiry, W. S. (2020) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-020-0341-y · Cited by 2,676
Inflammation and its resolution in atherosclerosis: mediators and therapeutic opportunities
Bäck, M., Yurdagul, A., Tabas, I., Öörni, K., & Kovanen, P. T. (2019) · Nature Reviews Cardiology · doi:10.1038/s41569-019-0169-2 · Cited by 1,341
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
“Taken together with the notion that the absence of either Ripk3, Casp8 or Fadd fails to rescue Ripk1 / mice from neonatal lethality,(180,185) these results pointed to the existence of a switch mechanism that regulates cell fate upon TNFR1 ligation.(204,205) Intriguingly, such switch may not operate in all cell types,…”
BackgroundSelf-citationApoptotic 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
“2008; Callus and Vaux, 2007; Tait et al., 2014).”
BackgroundInfluentialMitochondrial apoptosis: killing cancer using the enemy within
Lopez, J., & Tait, S. W. G. (2015) · British Journal of Cancer · doi:10.1038/bjc.2015.85 · Cited by 817
“Importantly, MOMP often leads to cell death irrespective of caspase activity (Tait et al, 2014).”
BackgroundSelf-citation
Metadata
- Authors
- Tait, S. W. G., Ichim, G., & Green, D. R.
- Affiliations
- Cancer Research UK Scotland Institute (GB)
- St. Jude Children's Research Hospital (US)
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2014-05-15
- Volume
- 127
- Issue
- 10
- Pages
- 2135-2144
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- PMC
- PMC4021468
- OpenAlex
- W2021358525
- Cited by
- 366
- References
- 130
- Citations by year
- 2026: 11 · 2025: 16 · 2024: 21 · 2023: 14 · 2022: 26 · 2021: 34 · 2020: 41 · 2019: 48 · 2018: 40 · 2017: 43 · 2016: 35 · 2015: 30 · 2014: 5
- FWCI
- 3.55
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Cell Science (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (submittedVersion)
- HighWire Press Open Archive (submittedVersion)
- Funders
- Biotechnology and Biological Sciences Research Council (BB/K008374/1)
- National Institute of General Medical Sciences (R01GM096208)
- National Institute of Allergy and Infectious Diseases (R01AI044828)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- non-apoptotic cell death, programmed cell death, necroptosis, pyroptosis, autophagic cell death, caspase-independent cell death, apoptosis, inflammation, immune system development
- MeSH terms
- Animals, Autophagy, Humans, Cell Death, Apoptosis
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review