Organelle-specific initiation of cell death
Abstract
In a majority of pathophysiological settings, cell death is not accidental - it is controlled by a complex molecular apparatus. Such a system operates like a computer: it receives several inputs that inform on the current state of the cell and the extracellular microenvironment, integrates them and generates an output. Thus, depending on a network of signals generated at specific subcellular sites, cells can respond to stress by attemptinwg to recover homeostasis or by activating molecular cascades that lead to cell death by apoptosis or necrosis. Here, we discuss the mechanisms whereby cellular compartments - including the nucleus, mitochondria, plasma membrane, endoplasmic reticulum, Golgi apparatus, lysosomes, cytoskeleton and cytosol - sense homeostatic perturbations and translate them into a cell-death-initiating signal.
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Pro-apoptotic BH3-only proteins are activated transcriptionally or post-translationally as specific organelles or cellular compartments experience perturbations of homeostasis, operating as cellular transducers of stress signaling.
“These pro-apoptotic members of the BCL2 protein family (which contain a single BH3 domain) are activated transcriptionally or post-translationally as specific organelles or cellular compartments experience perturbations of homeostasis, de facto operating as cellular transducers of stress signaling [60–63].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [63]
Cites
1 retracted
Proapoptotic BAX and BAK Modulate the Unfolded Protein Response by a Direct Interaction with IRE1α
Hetz, C. A., Bernasconi, P., Fisher, J. K., Lee, A., Bassik, M. C., Antonsson, B. E., Brandt, G. S., Iwakoshi, N. N., Schinzel, A. C., Glimcher, L. H., et al. (2006) · Science · doi:10.1126/science.1123480 · Cited by 666 · 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
Mitochondrial membrane permeabilization in cell death
Kroemer, G., Galluzzi, L., & Brenner, C. (2007) · Physiological Reviews · doi:10.1152/physrev.00013.2006 · Cited by 3,598 · see citing works
Self-citationSTING is an endoplasmic reticulum adaptor that facilitates innate immune signalling
Ishikawa, H., & Barber, G. N. (2008) · Nature · doi:10.1038/nature07317 · Cited by 3,576 · see citing works
Classification of cell death: recommendations of the Nomenclature Committee on Cell Death 2009
Kroemer, G., Galluzzi, L., Vandenabeele, P., Abrams, J., Alnemri, E. S., Baehrecke, E. H., Blagosklonny, M. V., El-Deiry, W. S., Golstein, P., Green, D. R., et al. (2009) · Cell Death & Differentiation · doi:10.1038/cdd.2008.150 · Cited by 3,399 · see citing works
Self-citationCaspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β
Nakagawa, T., Zhu, H., Morishima, N., Li, E., Xu, J., Yankner, B. A., & Yuan, J. (2000) · Nature · doi:10.1038/47513 · Cited by 3,262 · see citing works
STING regulates intracellular DNA-mediated, type I interferon-dependent innate immunity
Ishikawa, H., Ma, Z., & Barber, G. N. (2009) · Nature · doi:10.1038/nature08476 · Cited by 2,759 · 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
Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress
Tabas, I. A., & Ron, D. (2011) · Nature Cell Biology · doi:10.1038/ncb0311-184 · Cited by 2,603 · see citing works
Mitochondria and cell death: outer membrane permeabilization and beyond
Tait, S. W. G., & Green, D. R. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2952 · Cited by 2,593 · 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-citationDirect Activation of Bax by p53 Mediates Mitochondrial Membrane Permeabilization and Apoptosis
Chipuk, J. E., Kuwana, T., Bouchier-Hayes, L., Droin, N. M., Newmeyer, D. D., Schuler, M., & Green, D. R. (2004) · Science · doi:10.1126/science.1092734 · Cited by 2,066 · see citing works
p53 Has a Direct Apoptogenic Role at the Mitochondria
Mihara, M., Erster, S. H., Zaika, A. I., Petrenko, O., Chittenden, T. D., Pančoška, P., & Moll, U. M. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00050-9 · Cited by 1,771 · see citing works
Regulated necrosis: the expanding network of non-apoptotic cell death pathways
Berghe, T. V., Linkermann, A., Jouan-Lanhouet, S., Walczak, H., & Vandenabeele, P. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3737 · Cited by 1,735 · see citing works
ER-stress-induced transcriptional regulation increases protein synthesis leading to cell death
Han, J., Back, S. H., Hur, J., Lin, Y.-H., Gildersleeve, R., Shan, J., Yuan, C. L., Krokowski, D., Wang, S., Hatzoglou, M., et al. (2013) · Nature Cell Biology · doi:10.1038/ncb2738 · Cited by 1,691 · see citing works
Suppression of ceramide-mediated programmed cell death by sphingosine-1-phosphate
Cuvillier, O., Pirianov, G., Kleuser, B., Vanek, P. G., Coso, O. A., Gutkind, J. S., & Spiegel, S. (1996) · Nature · doi:10.1038/381800a0 · Cited by 1,532 · see citing works
Organelle-specific initiation of cell death pathways
Ferri, K. F., & Kroemer, G. (2001) · Nature Cell Biology · doi:10.1038/ncb1101-e255 · Cited by 1,455 · see citing works
Self-citationER Stress Triggers Apoptosis by Activating BH3-Only Protein Bim
Puthalakath, H., O’Reilly, L. A., Gunn, P. A., Lee, L., Kelly, P. N., Huntington, N. D., Hughes, P., Michalak, E. M., McKimm‐Breschkin, J. L., Motoyama, N., et al. (2007) · Cell · doi:10.1016/j.cell.2007.04.027 · Cited by 1,428 · see citing works
A Selective Inhibitor of eIF2α Dephosphorylation Protects Cells from ER Stress
Boyce, M., Bryant, K. F., Jousse, C., Long, K., Harding, H. P., Scheuner, D. L., Kaufman, R. J., Ma, D., Coen, D. M., Ron, D., et al. (2005) · Science · doi:10.1126/science.1101902 · Cited by 1,403 · see citing works
Feedback Inhibition of the Unfolded Protein Response by GADD34-Mediated Dephosphorylation of eIF2α
Novoa, I., Zeng, H., Harding, H. P., & Ron, D. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.5.1011 · Cited by 1,392 · see citing works
BAX and BAK Regulation of Endoplasmic Reticulum Ca 2+ : A Control Point for Apoptosis
Scorrano, L., Oakes, S. A., Opferman, J. T., Cheng, E. H. Y., Sorcinelli, M. D., Pozzan, T., & Korsmeyer, S. J. (2003) · Science · doi:10.1126/science.1081208 · Cited by 1,387 · see citing works
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 · see citing works
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 1,352 · see citing works
Nishitoh, H., Matsuzawa, A., Tobiume, K., Saegusa, K., Takeda, K., Inoue, K., Hori, S., Kakizuka, A., & Ichijo, H. (2002) · Genes & Development · doi:10.1101/gad.992302 · Cited by 1,331 · 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
PARP inhibition: PARP1 and beyond
Rouleau, M., Patel, A., Hendzel, M. J., Kaufmann, S. H., & Poirier, G. G. (2010) · Nature Reviews Cancer · doi:10.1038/nrc2812 · Cited by 1,298 · see citing works
Mechanism of Toxicity in Rotenone Models of Parkinson's Disease
Sherer, T., Betarbet, R. S., Testa, C. M., Seo, B. B., Richardson, J. R., Kim, J. H., Miller, G. W., Yagi, T., Matsuno‐Yagi, A., & Greenamyre, J. T. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-34-10756.2003 · Cited by 1,073 · see citing works
JNK phosphorylation of Bim-related members of the Bcl2 family induces Bax-dependent apoptosis
Lei, K., & Davis, R. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0438011100 · Cited by 1,068 · see citing works
Puthalakath, H., Huang, D. C. S., O'REILLY, L. A., King, S. M., & Strasser, A. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80456-6 · Cited by 1,053 · see citing works
A role for ATR in the DNA damage-induced phosphorylation of p53
Tibbetts, R. S., Brumbaugh, K. M., Williams, J. M., Sarkaria, J. N., Cliby, W. A., Shieh, S.-Y., Taya, Y., Prives, C., & Abraham, R. T. (1999) · Genes & Development · doi:10.1101/gad.13.2.152 · Cited by 1,046 · see citing works
A physical and functional map of the human TNF-α/NF-κB signal transduction pathway
Bouwmeester, T., Bauch, A., Ruffner, H., Angrand, P., Bergamini, G., Croughton, K., Cruciat, C., Eberhard, D., Gagneur, J., Ghidelli, S., et al. (2004) · Nature Cell Biology · doi:10.1038/ncb1086 · Cited by 1,030 · see citing works
Mitochondrial Import Efficiency of ATFS-1 Regulates Mitochondrial UPR Activation
Nargund, A. M., Pellegrino, M., Fiorese, C. J., Baker, B. M., & Haynes, C. M. (2012) · Science · doi:10.1126/science.1223560 · Cited by 1,027 · see citing works
Many cuts to ruin: a comprehensive update of caspase substrates
Fischer, U., Jänicke, R. U., & Schulze‐Osthoff, K. (2003) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401160 · Cited by 1,025 · see citing works
Endoplasmic reticulum-mitochondria contacts: Function of the junction
Rowland, A. A., & Voeltz, G. K. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3440 · Cited by 1,018 · see citing works
Bid-deficient mice are resistant to Fas-induced hepatocellular apoptosis
Yin, X.-M., Wang, K., Gross, A., Zhao, Y., Zinkel, S., Klocke, B., Roth, K. A., & Korsmeyer, S. J. (1999) · Nature · doi:10.1038/23730 · Cited by 1,004 · 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
PARP-1 cleavage fragments: signatures of cell-death proteases in neurodegeneration
Chaitanya, G. V., Alexander, J. S., & Babu, P. P. (2010) · Cell Communication and Signaling · doi:10.1186/1478-811x-8-31 · Cited by 929 · see citing works
Mitotic catastrophe: a mechanism for avoiding genomic instability
Vitale, I., Galluzzi, L., Castedo, M., & Kroemer, G. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3115 · Cited by 834 · see citing works
Self-citationYamaguchi, H., & Wang, H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406933200 · Cited by 825 · see citing works
Cell Surface Trafficking of Fas: A Rapid Mechanism of p53-Mediated Apoptosis
Bennett, M. R., Macdonald, K., Chan, S., Luzio, J. P., Simari, R. D., & Weissberg, P. L. (1998) · Science · doi:10.1126/science.282.5387.290 · Cited by 755 · see citing works
Rudel, T., & Bokoch, G. (1997) · Science · doi:10.1126/science.276.5318.1571 · Cited by 748 · 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
Mitochondria: master regulators of danger signalling
Galluzzi, L., Kepp, O., & Kroemer, G. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3479 · Cited by 733 · see citing works
Self-citationRequirement for Caspase-2 in Stress-Induced Apoptosis Before Mitochondrial Permeabilization
Lassus, P., Opitz-Araya, X., & Lazebnik, Y. A. (2002) · Science · doi:10.1126/science.1074721 · Cited by 719 · see citing works
G protein-coupled receptors: novel targets for drug discovery in cancer
Lappano, R., & Maggiolini, M. (2010) · Nature Reviews Drug Discovery · doi:10.1038/nrd3320 · Cited by 717 · 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
Tinel, A., & Tschopp, J. (2004) · Science · doi:10.1126/science.1095432 · Cited by 665 · see citing works
Puthalakath, H., Villunger, A., O'Reilly, L. A., Beaumont, J. G., Coultas, L., Cheney, R. E., Huang, D. C. S., & Strasser, A. (2001) · Science · doi:10.1126/science.1062257 · Cited by 656 · see citing works
IRE1α Cleaves Select microRNAs During ER Stress to Derepress Translation of Proapoptotic Caspase-2
Upton, J.-P., Wang, L., Han, D., Wang, E. S., Huskey, N. E., Lim, L., Truitt, M., McManus, M. T., Ruggero, D., Goga, A., et al. (2012) · Science · doi:10.1126/science.1226191 · Cited by 640 · see citing works
Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival
Schwickart, M., Huang, X., Lill, J. R., Liu, J., Ferrando, R., French, D. M., Maecker, H., O’Rourke, K., Bazan, F., Eastham-Anderson, J., et al. (2010) · Nature · doi:10.1038/nature08646 · Cited by 628 · see citing works
The effects of deregulated DNA damage signalling on cancer chemotherapy response and resistance
Bouwman, P., & Jonkers, J. (2012) · Nature Reviews Cancer · doi:10.1038/nrc3342 · Cited by 615 · see citing works
Jin, Z., Li, Y., Pitti, R. M., Lawrence, D. A., Pham, V. C., Lill, J. R., & Ashkenazi, A. (2009) · Cell · doi:10.1016/j.cell.2009.03.015 · Cited by 588 · see citing works
Cell death assays for drug discovery
Kepp, O., Galluzzi, L., Lipinski, M. M., Yuan, J., & Kroemer, G. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3373 · Cited by 556 · see citing works
Self-citationTyrosine dephosphorylation of H2AX modulates apoptosis and survival decisions
Cook, P. J., Ju, B. G., Telese, F., Wang, X., Glass, C. K., & Rosenfeld, M. G. (2009) · Nature · doi:10.1038/nature07849 · Cited by 534 · see citing works
Organization of the ER–Golgi interface for membrane traffic control
Brandizzí, F., & Barlowe, C. K. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3588 · Cited by 523 · see citing works
Hsp70 stabilizes lysosomes and reverts Niemann–Pick disease-associated lysosomal pathology
Kirkegaard, T., Roth, A. G., Petersen, N. H. T., Mahalka, A. K., Olsen, O. D., Moilanen, I., Zylicz, A., Knudsen, J., Sandhoff, K., Arenz, C., et al. (2010) · Nature · doi:10.1038/nature08710 · Cited by 519 · see citing works
The mitochondrial UPR – protecting organelle protein homeostasis
Haynes, C. M., & Ron, D. (2010) · Journal of Cell Science · doi:10.1242/jcs.075119 · Cited by 490 · see citing works
Lysosomal Membrane Permeabilization Induces Cell Death in a Mitochondrion-dependent Fashion
Boya, P., Andreau, K., Poncet, D., Zamzami, N., Perfettini, J.-L., Metivier, D., Ojcius, D. M., Jäättelä, M., & Kroemer, G. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20021952 · Cited by 483 · see citing works
Self-citationXIAP discriminates between type I and type II FAS-induced apoptosis
Jost, P. J., Grabow, S., Gray, D., McKenzie, M. D., Nachbur, U., Huang, D. C. S., Bouillet, P., Thomas, H. E., Borner, C., Silke, J., et al. (2009) · Nature · doi:10.1038/nature08229 · Cited by 482 · see citing works
Petrasek, J., Iracheta‐Vellve, A., Csák, T., Satishchandran, A., Kodys, K., Kurt‐Jones, E. A., Fitzgerald, K. A., & Szabó, G. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1308331110 · Cited by 452 · see citing works
Besch, R., Poeck, H., Hohenauer, T., Senft, D., Häcker, G. A., Berking, C., Hornung, V., Endres, S., Ruzicka, T., Rothenfußer, S., et al. (2009) · Journal of Clinical Investigation · doi:10.1172/jci37155 · Cited by 429 · see citing works
Elgendy, M., Sheridan, C., Brumatti, G., & Martin, S. J. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.02.009 · Cited by 426 · see citing works
Requirement for GD3 Ganglioside in CD95- and Ceramide-Induced Apoptosis
Maria, R. D., Lenti, L., Malisan, F., D’Agostino, F., Tomassini, B., Zeuner, A., Rippo, M. R., & Testi, R. (1997) · Science · doi:10.1126/science.277.5332.1652 · Cited by 421 · see citing works
PML Regulates Apoptosis at Endoplasmic Reticulum by Modulating Calcium Release
Giorgi, C., Ito, K., Lin, H., Santangelo, C., Wieckowski, M. R., Lebiedzińska, M., Bononi, A., Bonora, M., Duszyński, J., Bernardi, R., et al. (2010) · Science · doi:10.1126/science.1189157 · Cited by 420 · see citing works
Mitochondrial membrane permeabilization in neuronal injury
Galluzzi, L., Blomgren, K., & Kroemer, G. (2009) · Nature Reviews Neuroscience · doi:10.1038/nrn2665 · Cited by 418 · see citing works
Self-citationDroga-Mazovec, G., Bojič, L., Petelin, A., Ivanova, S., Romih, R., Repnik, U., Salvesen, G. S., Stoka, V., Turk, V., & Turk, B. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802513200 · Cited by 399 · see citing works
Wen, Y.-D., Sheng, R., Zhang, L.-S., Han, R., Zhang, X., Zhang, X., Han, F., Fukunaga, K., & Qin, Z.-H. (2008) · Autophagy · doi:10.4161/auto.6412 · Cited by 390 · see citing works
Chen, L., Park, S.-M., Tumanov, A. V., Hau, A., Sawada, K., Feig, C., Turner, J. R., Fu, Y., Romero, I. L., Lengyel, E. R., et al. (2010) · Nature · doi:10.1038/nature09075 · Cited by 377 · see citing works
p53 is associated with cellular microtubules and is transported to the nucleus by dynein
Giannakakou, P., Sackett, D. L., Ward, Y., Webster, K. R., Blagosklonny, M. V., & Fojo, T. (2000) · Nature Cell Biology · doi:10.1038/35036335 · Cited by 374 · see citing works
Young, M. M., Takahashi, Y., Khan, O. A., Park, S., Hori, T., Yun, J. K., Sharma, A. K., Amin, S., Hu, C., Zhang, J., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.309104 · Cited by 372 · see citing works
Schenck, A., Goto‐Silva, L., Collinet, C., Rhinn, M., Giner, A., Habermann, B. H., Brand, M., & Zerial, M. (2008) · Cell · doi:10.1016/j.cell.2008.02.044 · Cited by 333 · see citing works
Cathepsin D links TNF-induced acid sphingomyelinase to Bid-mediated caspase-9 and -3 activation
Heinrich, M., Neumeyer, J., Jakob, M., Hallas, C., Tchikov, V., Winoto‐Morbach, S., Wickel, M., Schneider‐Brachert, W., Trauzold, A., Hethke, A., et al. (2004) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401382 · Cited by 333 · see citing works
BAX Inhibitor-1 Is a Negative Regulator of the ER Stress Sensor IRE1α
Lisbona, F., Rojas‐Rivera, D., Thielen, P., Zamorano, S., Todd, D. J., Martinon, F., Glavic, Á., Kress, C. L., Lin, J. H., Walter, P., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.02.017 · Cited by 318 · see citing works
The deubiquitinase USP9X suppresses pancreatic ductal adenocarcinoma
Initiative, A. P. C. G., Pérez-Mancera, P. A., Rust, A. G., van der Weyden, L., Kristiansen, G., Li, A., Sarver, A. L., Silverstein, K. A. T., Grützmann, R., Aust, D., et al. (2012) · Nature · doi:10.1038/nature11114 · Cited by 316 · see citing works
Mitochondrial translocation of cofilin is an early step in apoptosis induction
Chua, B. T., Volbracht, C., Tan, K. O., Li, R., Yu, V. C. K., & Li, P. (2003) · Nature Cell Biology · doi:10.1038/ncb1070 · Cited by 315 · 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
Regulation of TNFR1 and CD95 signalling by receptor compartmentalization
Schütze, S., Tchikov, V., & Schneider‐Brachert, W. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2430 · Cited by 298 · see citing works
Chk1 Suppresses a Caspase-2 Apoptotic Response to DNA Damage that Bypasses p53, Bcl-2, and Caspase-3
Sidi, S., Sanda, T., Kennedy, R. D., Hagen, A. T., Jette, C. A., Hoffmans, R., Pascual, J., Imamura, S., Kishi, S., Amatruda, J. F., et al. (2008) · Cell · doi:10.1016/j.cell.2008.03.037 · Cited by 295 · see citing works
The Tumor Suppressor Par-4 Activates an Extrinsic Pathway for Apoptosis
Burikhanov, R., Zhao, Y., Goswami, A., Qiu, S. G., Schwarze, S. R., & Rangnekar, V. M. (2009) · Cell · doi:10.1016/j.cell.2009.05.022 · Cited by 255 · see citing works
Mediation of Neuronal Apoptosis by Kv2.1-Encoded Potassium Channels
Pal, S. K., Hartnett, K. A., Nerbonne, J. M., Levitan, E. S., & Aizenman, E. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-12-04798.2003 · Cited by 249 · see citing works
Fehrenbacher, N., Bastholm, L., Kirkegaard‐Sørensen, T., Rafn, B., Bøttzauw, T., Nielsen, C. W., Weber, E., Shirasawa, S., Kallunki, T., & Jäättelä, M. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-0463 · Cited by 242 · see citing works
Oxidant-induced apoptosis is mediated by oxidation of the actin-regulatory protein cofilin
Klamt, F., Zdanov, S., Levine, R. L., Pariser, A. C., Zhang, Y., Zhang, B., Yu, L., Veenstra, T. D., & Shacter, E. B. (2009) · Nature Cell Biology · doi:10.1038/ncb1968 · Cited by 241 · see citing works
Crosstalk between ER stress and immunogenic cell death
Kepp, O., Menger, L., Vacchelli, E., Locher, C., Adjemian, S., Yamazaki, T., Martins, I., Sukkurwala, A. Q., Michaud, M., Senovilla, L., et al. (2013) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2013.05.001 · Cited by 233 · see citing works
Self-citationLane, J. D., Lucocq, J. M., Pryde, J. G., Barr, F. A., Woodman, P. G., Allan, V., & Lowe, M. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200110007 · Cited by 223 · see citing works
Groth‐Pedersen, L., Ostenfeld, M. S., Høyer-Hansen, M. H., Nylandsted, J., & Jäättelä, M. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-3520 · Cited by 215 · see citing works
Bröker, L. E., Huisman, C., Span, S. W., Rodríguez, J. A., Kruyt, F. A. E., & Giaccone, G. (2004) · Cancer Research · doi:10.1158/0008-5472.can-03-3060 · Cited by 206 · see citing works
MAVS-Mediated Apoptosis and Its Inhibition by Viral Proteins
Lei, Y. L., Moore, C. B., Liesman, R. M., O’Connor, B. P., Bergstralh, D. T., Chen, Z. J., Pickles, R. J., & Ting, J. P. ‐. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005466 · Cited by 204 · see citing works
Tu, S. S., McStay, G. P., Boucher, L.-M., Mak, T. W., Beere, H. M., & Green, D. R. (2005) · Nature Cell Biology · doi:10.1038/ncb1340 · Cited by 196 · see citing works
Deconstructing p53 transcriptional networks in tumor suppression
Bieging, K. T., & Attardi, L. D. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2011.10.006 · Cited by 194 · 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
Tinel, A., Janssens, S., Lippens, S., Cuenin, S., Logette, E., Jaccard, B., Quadroni, M., & Tschopp, J. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601473 · Cited by 166 · see citing works
Luke, C. J., Pak, S. C., Askew, Y. S., Naviglia, T. L., Askew, D. J., Nobar, S. M., Vetica, A. C., Long, O. S., Watkins, S. C., Stolz, D. B., et al. (2007) · Cell · doi:10.1016/j.cell.2007.07.013 · Cited by 166 · see citing works
Into, T., Kiura, K., Yasuda, M., Kataoka, H., Inoue, N., Hasebe, A., Takeda, K., Akira, S., & Shibata, K. (2004) · Cellular Microbiology · doi:10.1046/j.1462-5822.2003.00356.x · Cited by 158 · see citing works
Dumitru, R., Gama, V., Fagan, B. M., Bower, J. J., Swahari, V., Pevny, L., & Deshmukh, M. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.04.002 · Cited by 157 · see citing works
Caspase-2 activation in the absence of PIDDosome formation
Manzl, C., Krumschnabel, G., Bock, F. J., Sohm, B., Labi, V., Baumgartner, F., Logette, E., Tschopp, J., & Villunger, A. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200811105 · Cited by 157 · see citing works
The Patched dependence receptor triggers apoptosis through a DRAL–caspase-9 complex
Mille, F., Thibert, C., Fombonne, J., Rama, N., Guix, C., Hayashi, H., Corset, V., Reed, J. C., & Mehlen, P. (2009) · Nature Cell Biology · doi:10.1038/ncb1880 · Cited by 154 · see citing works
Hwang, J. J., Lee, S.-J., Kim, T.-Y., Cho, J.-H., & Koh, J. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.0199-08.2008 · Cited by 153 · see citing works
Schmelzle, T., Mailleux, A., Overholtzer, M., Carroll, J. S., Solimini, N. L., Lightcap, E. S., Veiby, O. P., & Brugge, J. S. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700115104 · Cited by 145 · see citing works
Guenebeaud, C., Goldschneider, D., Castets, M., Guix, C., Chazot, G., Delloye-Bourgeois, C., Eisenberg-Lerner, A., Shohat, G., Zhang, M., Laudet, V., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.11.021 · Cited by 137 · see citing works
Actin Stabilization by Jasplakinolide Enhances Apoptosis Induced by Cytokine Deprivation
Posey, S. C., & Bierer, B. E. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.7.4259 · Cited by 137 · see citing works
LI, R., Moudgil, T. L., Ross, H. J., & Hu, H. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401554 · Cited by 136 · see citing works
p53 regulates a non-apoptotic death induced by ROS
Montero, J., Dutta, C., van Bodegom, D., Weinstock, D. M., & Letai, A. G. (2013) · Cell Death and Differentiation · doi:10.1038/cdd.2013.52 · Cited by 134 · see citing works
Raval, G. N., Bharadwaj, S., Levine, E. A., Willingham, M. C., Geary, R. L., Kute, T., & Prasad, G. L. (2003) · Oncogene · doi:10.1038/sj.onc.1206719 · Cited by 134 · see citing works
Yamashima, T., Tonchev, A. B., Tsukada, T., Saido, T. C., Imajoh‐Ohmi, S., Momoi, T., & Kominami, E. (2003) · Hippocampus · doi:10.1002/hipo.10127 · Cited by 131 · see citing works
Attenuation of the Lysosomal Death Pathway by Lysosomal Cholesterol Accumulation
Appelqvist, H., Nilsson, C., Garner, B., Brown, A. J., Kågedal, K., & Öllinger, K. M. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2010.10.030 · Cited by 124 · see citing works
Morishima, N., Nakanishi, K., & Nakano, A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.233502 · Cited by 115 · see citing works
Apoptosome-Independent Activation of the Lysosomal Cell Death Pathway by Caspase-9
Gyrd‐Hansen, M., Farkas, T., Fehrenbacher, N., Bastholm, L., Høyer-Hansen, M. H., Elling, F., Wallach, D., Flavell, R. A., Kroemer, G., Nylandsted, J., et al. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00716-06 · Cited by 111 · see citing works
Self-citationMicrotubule-targeted agents: When mitochondria become essential to chemotherapy
Rovini, A. M. F., Savry, A., Braguer, D., & Carré, M. (2011) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2011.01.001 · Cited by 105 · see citing works
Apoptosis of uninfected cells induced by HIV envelope glycoproteins
Ahr, B., Robert-Hebmann, V., Devaux, C. A., & Biard‐Piechaczyk, M. (2004) · Retrovirology · doi:10.1186/1742-4690-1-12 · Cited by 105 · see citing works
Calpain-mediated Hsp70.1 cleavage in hippocampal CA1 neuronal death
Sahara, S., & Yamashima, T. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.02.087 · Cited by 104 · 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
A Complex between Atg7 and Caspase-9
Han, J., Hou, W., Goldstein, L. A., Stolz, D. B., Watkins, S. C., & Rabinowich, H. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.536854 · Cited by 101 · see citing works
TRPV1 receptors mediate particulate matter-induced apoptosis
Agopyan, N., Head, J., Yu, S., & Simon, S. A. (2004) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00299.2003 · Cited by 101 · see citing works
FOXO3 signalling links ATM to the p53 apoptotic pathway following DNA damage
Chung, Y. M., Park, S., Tsai, W.-B., Wang, S., Ikeda, M.-A., Berek, J. S., Chen, D. J., & Hu, M. C. ‐. (2012) · Nature Communications · doi:10.1038/ncomms2008 · Cited by 100 · see citing works
Vilas, G. L., Corvi, M. M., Plummer, G. J., Seime, A. M., Lambkin, G. R., & Berthiaume, L. G. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0600824103 · Cited by 97 · see citing works
Maadidi, S. E., Faletti, L. E., Berg, B., Wenzl, C., Wieland, K., Chen, Z. J., Maurer, U., & Borner, C. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1300842 · Cited by 95 · see citing works
Notomi, S., Hisatomi, T., Murakami, Y., Terasaki, H., Sonoda, S., Asato, R., Takeda, A., Ikeda, Y., Enaida, H., Sakamoto, T., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0053338 · Cited by 93 · see citing works
Kang, M., Chung, J., & Ryoo, H. D. (2012) · Nature Cell Biology · doi:10.1038/ncb2447 · Cited by 91 · see citing works
PIDD Death-Domain Phosphorylation by ATM Controls Prodeath versus Prosurvival PIDDosome Signaling
Ando, K., Kernan, J. L., Liu, P. H., Sanda, T., Logette, E., Tschopp, J., Look, A. T., Wang, J., Bouchier‐Hayes, L., & Sidi, S. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.06.024 · Cited by 91 · see citing works
Protection against oxidant‐mediated lysosomal rupture: a new anti‐apoptotic activity of Bcl‐2?
Zhao, M., Eaton, J. W., & Brunk, U. T. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)02195-5 · Cited by 89 · see citing works
Namba, T., Tian, F., Chu, K., Hwang, S., Yoon, K., Byun, S., Hiraki, M., Mandinova, A., & Lee, S. W. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.09.020 · Cited by 85 · see citing works
Moriceau, S., Kantari‐Mimoun, C., Mocek, J., Davezac, N., Gabillet, J., Guerrera, I. C., Brouillard, F., Tondelier, D., Sermet‐Gaudelus, I., Danel, C. J., et al. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0803312 · Cited by 78 · see citing works
VanBrocklin, M. W., Verhaegen, M. E., Soengas, M. S., & Holmen, S. L. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-3934 · Cited by 77 · see citing works
Hypoxia-Induced Modulation of Apoptosis and BCL-2 Family Proteins in Different Cancer Cell Types
Sermeus, A., Genin, M., Maincent, A., Fransolet, M., Notte, A., Leclère, L., Riquier, H., Arnould, T., & Michiels, C. (2012) · PLoS ONE · doi:10.1371/journal.pone.0047519 · Cited by 76 · see citing works
Arnandis, T., Vicens, I. F., García–Trevijano, E. R., Miralles, V. J., García, C., Torres, L., Vinã, J. R., & Zaragozá, R. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.46 · Cited by 76 · see citing works
Wabnitz, G. H., Goursot, C., Jahraus, B., Kirchgessner, H., Hellwig, A., Klemke, M., Konstandin, M. H., & Samstag, Y. (2010) · Cell Death and Disease · doi:10.1038/cddis.2010.36 · Cited by 75 · see citing works
Wille, A., Gerber, A., Heimburg, A., Reisenauer, A., Peters, C., Säftig, P., Reinheckel, T., Welte, T., & Bühling, F. (2004) · Biological Chemistry · doi:10.1515/bc.2004.082 · Cited by 75 · see citing works
Serine 58 of 14-3-3ζ Is a Molecular Switch Regulating ASK1 and Oxidant Stress-Induced Cell Death
Zhou, J., Shao, Z., Kerkelä, R., Ichijo, H., Muslin, A. J., Pombo, C. M., & Force, T. L. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01067-08 · Cited by 74 · see citing works
Dependence Receptors: From Basic Research to Drug Development
Mehlen, P., & Bredesen, D. E. (2011) · Science Signaling · doi:10.1126/scisignal.2001521 · Cited by 72 · see citing works
The Cathepsin B Death Pathway Contributes to TNF Plus IFN-γ-Mediated Human Endothelial Injury
Li, J. H., & Pober, J. S. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.3.1858 · Cited by 71 · see citing works
Sonic Hedgehog Promotes Tumor Cell Survival by Inhibiting CDON Pro-Apoptotic Activity
Delloye‐Bourgeois, C., Gibert, B., Rama, N., Delcros, J., Gadot, N., Scoazec, J., Krauss, R. S., Bernet, A., & Mehlen, P. (2013) · PLoS Biology · doi:10.1371/journal.pbio.1001623 · Cited by 66 · see citing works
Voisin, T., Firar, A. E., Rouyer‐Fessard, C., Gratio, V., & Laburthe, M. (2008) · The FASEB Journal · doi:10.1096/fj.07-098723 · Cited by 65 · see citing works
Weinmann, M., Jendrossek, V., Handrick, R., Güner, D., Goecke, B., & Belka, C. (2004) · Oncogene · doi:10.1038/sj.onc.1207481 · Cited by 62 · see citing works
Cathepsin D Primes Caspase-8 Activation by Multiple Intra-chain Proteolysis
Conus, S., Pop, C., Snipas, S. J., Salvesen, G. S., & Simon, H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.306399 · Cited by 57 · see citing works
ER stress does not cause upregulation and activation of caspase-2 to initiate apoptosis
Sandow, J. J., Dorstyn, L., O’Reilly, L. A., Tailler, M., Kumar, S., Strasser, A., & Ekert, P. G. (2013) · Cell Death and Differentiation · doi:10.1038/cdd.2013.168 · Cited by 56 · see citing works
Huang, W., Lin, Y.-S., Chen, C., Wang, C., Chiu, W. C., & Lin, C. (2009) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.108.148122 · Cited by 56 · see citing works
Nogueira, E., Fidalgo, M., Molnar, A., Kyriakis, J. M., Force, T. L., Zalvide, J. B., & Pombo, C. M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709724200 · Cited by 55 · see citing works
RIG1 suppresses Ras activation and induces cellular apoptosis at the Golgi apparatus
Tsai, F., Shyu, R., & Jiang, S. (2006) · Cellular Signalling · doi:10.1016/j.cellsig.2006.11.005 · Cited by 54 · see citing works
Caspase-mediated inhibition of sphingomyelin synthesis is involved in FasL-triggered cell death
Lafont, É., Milhas, D., Carpentier, S., Garcia, V., Jin, Z.-X., Umehara, H., Okazaki, T., Schulze‐Osthoff, K., Levade, T., Benoist, H., et al. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.130 · Cited by 53 · see citing works
Kirschnek, S., Ying, S., Fischer, S. F., Häcker, H., Villunger, A., Hochrein, H., & Häcker, G. A. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.2.671 · Cited by 52 · see citing works
Caspase cleavage of the Golgi stacking factor GRASP65 is required for Fas/CD95-mediated apoptosis
Cheng, J. P. X., Betin, V. M. S., Weir, H. J. M., Shelmani, G. M. A., Moss, D. K., & Lane, J. D. (2010) · Cell Death and Disease · doi:10.1038/cddis.2010.59 · Cited by 51 · see citing works
Dampening of death pathways by schnurri-2 is essential for T-cell development
Staton, T. L., Lazarevic, V., Jones, D. C., Lanser, A. J., Takagi, T., Ishii, S., & Glimcher, L. H. (2011) · Nature · doi:10.1038/nature09848 · Cited by 36 · see citing works
Pinto, V. I., Senini, V. W., Wang, Y., Kazembe, M. P., & McCulloch, C. A. (2013) · The FASEB Journal · doi:10.1096/fj.13-233759 · Cited by 32 · see citing works
Noack, J., Jordi, M., Zauner, L., Alessi, D., Burch, A., Tinguely, M., Hersberger, M., Bernasconi, M., & Nadal, D. (2012) · Cell Death and Disease · doi:10.1038/cddis.2012.60 · Cited by 29 · see citing works
The adaptor protein CRK is a pro-apoptotic transducer of endoplasmic reticulum stress
Austgen, K., Johnson, E. T., Park, T., Curran, T., & Oakes, S. A. (2011) · Nature Cell Biology · doi:10.1038/ncb2395 · Cited by 29 · see citing works
Ezrin is a negative regulator of death receptor-induced apoptosis
Kuo, W.-C., Yang, K.-T., Hsieh, S.-L., & Lai, M.-Z. (2009) · Oncogene · doi:10.1038/onc.2009.417 · Cited by 27 · see citing works
How, P. C., & Shields, D. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.175174 · Cited by 25 · see citing works
Short RNA Duplexes Elicit RIG-I–Mediated Apoptosis in a Cell Type– and Length-Dependent Manner
Ishibashi, O., Ali, M. M., Luo, S., Ohba, T., Katabuchi, H., Takeshita, T., & Takizawa, T. (2011) · Science Signaling · doi:10.1126/scisignal.2001614 · Cited by 19 · 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-citationAcetyl Coenzyme A: A Central Metabolite and Second Messenger
Pietrocola, F., Galluzzi, L., Pedro, J. M. B., Madeo, F., & Kroemer, G. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.014 · Cited by 1,349 · see citing works
Self-citationEssential 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-citationNecroptosis: Mechanisms and Relevance to Disease
Galluzzi, L., Kepp, O., Chan, F. K.-M., & Kroemer, G. (2016) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-052016-100247 · Cited by 721 · see citing works
Self-citationSalinomycin kills cancer stem cells by sequestering iron in lysosomes
Mai, T. T., Hamaï, A., Hienzsch, A., Cañeque, T., Müller, S., Wicinski, J., Cabaud, O., Leroy, C., David, A., Acevedo, V., et al. (2017) · Nature Chemistry · doi:10.1038/nchem.2778 · Cited by 612 · see citing works
Linking cellular stress responses to systemic homeostasis
Galluzzi, L., Yamazaki, T., & Kroemer, G. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0068-0 · Cited by 529 · see citing works
Self-citationClassification of current anticancer immunotherapies
Galluzzi, L., Vacchelli, E., Pedro, J. M. B., Buqué, A., Senovilla, L., Baracco, E. E., Bloy, N., Castoldi, F., Abastado, J., Agostinis, P., et al. (2014) · Oncotarget · doi:10.18632/oncotarget.2998 · Cited by 471 · see citing works
Self-citationPhotodynamic therapy in cancer treatment - an update review
Santos, A. F. D., de Almeida, D. R. Q., Terra, L. F., Maur�cio, B., & Labriola, L. (2019) · Journal of Cancer Metastasis and Treatment · doi:10.20517/2394-4722.2018.83 · Cited by 450 · see citing works
Cell death and immunity in cancer: From danger signals to mimicry of pathogen defense responses
Garg, A. D., & Agostinis, P. (2017) · Immunological Reviews · doi:10.1111/imr.12574 · Cited by 448 · see citing works
Molecular and Translational Classifications of DAMPs in Immunogenic Cell Death
Garg, A. D., Galluzzi, L., Apétoh, L., Baert, T., Birge, R. B., Pedro, J. M. B., Breckpot, K., Brough, D., Chaurio, R. A., Cirone, M., et al. (2015) · Frontiers in Immunology · doi:10.3389/fimmu.2015.00588 · Cited by 409 · see citing works
Self-citationOrganelle-specific regulation of ferroptosis
Chen, X., Kang, R., Kroemer, G., & Tang, D. (2021) · Cell Death and Differentiation · doi:10.1038/s41418-021-00859-z · Cited by 401 · see citing works
Self-citationCombinatorial Strategies for the Induction of Immunogenic Cell Death
Bezu, L., Gomes-da-Silva, L. C., Dewitte, H., Breckpot, K., Fucikova, J. P., Špíšek, R., Galluzzi, L., Kepp, O., & Kroemer, G. (2015) · Frontiers in Immunology · doi:10.3389/fimmu.2015.00187 · Cited by 389 · see citing works
Self-citationFeng, X.-R., Xu, W.-G., Li, Z., Song, W.-T., Ding, J.-X., & Chen, X.-S. (2019) · Advancement of science · doi:10.1002/advs.201900101 · Cited by 294 · see citing works
He, L., Li, Y., Tan, C., Ye, R., Chen, M., Cao, J., Ji, L., & Mao, Z. (2015) · Chemical Science · doi:10.1039/c5sc01955a · Cited by 359 · 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
Self-citationA Forward Vision for Chemodynamic Therapy: Issues and Opportunities
Zhao, P., Li, H., & Bu, W. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202210415 · Cited by 338 · see citing works
Nanoscale metal-organic frameworks for mitochondria-targeted radiotherapy-radiodynamic therapy
Ni, K., Lan, G., Veroneau, S. S., Duan, X., Song, Y., & Lin, W. (2018) · Nature Communications · doi:10.1038/s41467-018-06655-7 · Cited by 331 · see citing works
Trial watch: IDO inhibitors in cancer therapy
Vacchelli, E., Aranda, F., Eggermont, A. M. M., Sautès‐Fridman, C., Tartour, É., Kennedy, E. P., Platten, M., Zitvogel, L., Kroemer, G., & Galluzzi, L. (2014) · OncoImmunology · doi:10.4161/21624011.2014.957994 · Cited by 327 · see citing works
Self-citationBCL-2 family: integrating stress responses at the ER to control cell demise
Pihán, P., Carreras-Sureda, A., & Hetz, C. (2017) · Cell Death & Differentiation · doi:10.1038/cdd.2017.82 · Cited by 274 · see citing works
AMPK and PFKFB3 mediate glycolysis and survival in response to mitophagy during mitotic arrest
Domènech, E. B., Maestre, C., Esteban‐Martínez, L., Partida, D., Pascual, R., Fernández‐Miranda, G., Seco, E., Campos‐Olivas, R., Pérez‐Martínez, M., Megı́as, D., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3231 · Cited by 267 · see citing works
Persister cancer cells: Iron addiction and vulnerability to ferroptosis
Rodriguez, R., Schreiber, S. L., & Conrad, M. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.12.001 · Cited by 271 · see citing works
Autophagy in acute brain injury
Galluzzi, L., Bravo-San Pedro, J. M., Blomgren, K., & Kroemer, G. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2016.51 · Cited by 234 · see citing works
Self-citationTargeting ferroptosis in acute kidney injury
Ni, L., Cheng, Y., & Wu, X. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04628-9 · Cited by 225 · see citing works
Mitochondrial 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
Self-citationOrganelle-Specific Initiation of Autophagy
Sica, V., Galluzzi, L., Bravo-San Pedro, J. M., Izzo, V., Maiuri, M. C., & Kroemer, G. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.07.021 · Cited by 205 · see citing works
Self-citationMitochondrial ROS metabolism: 10 Years later
Andreyev, A. Y., Kushnareva, Y. E., Murphy, A. N., & Starkov, A. A. (2015) · Biochemistry (Moscow) · doi:10.1134/s0006297915050028 · Cited by 194 · see citing works
Association of tamoxifen resistance and lipid reprogramming in breast cancer
Hultsch, S., Kankainen, M., Paavolainen, L., Kovanen, R., Ikonen, E., Kangaspeska, S., Pietiäinen, V. M., & Kallioniemi, O. (2018) · BMC Cancer · doi:10.1186/s12885-018-4757-z · Cited by 195 · see citing works
Zhang, D., Zheng, Y., Tan, C., Sun, J., Zhang, W., Ji, L., & Mao, Z. (2017) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.6b13808 · Cited by 192 · see citing works
The effects of baicalein and baicalin on mitochondrial function and dynamics: A review
de Oliveira, M. R., Nabavi, S. F., Habtemariam, S., Orhan, İ., Daglia, M., & Nabavi, S. M. (2015) · Pharmacological Research · doi:10.1016/j.phrs.2015.08.021 · Cited by 181 · see citing works
Therapeutic targeting of autophagy in cardiovascular disease
Schiattarella, G. G., & Hill, J. A. (2015) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2015.11.019 · Cited by 180 · see citing works
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Self-citationdos Santos, A. F., Terra, L. F., Wailemann, R. A. M., Oliveira, T. C., Gomes, V. M., Mineiro, M. F., Meotti, F. C., Bruni‐Cardoso, A., Baptista, M. S., & Labriola, L. (2017) · BMC Cancer · doi:10.1186/s12885-017-3179-7 · Cited by 176 · see citing works
Sargeant, T. J., Lloyd-Lewis, B., Resemann, H. K., Ramos-Montoya, A., Skepper, J., & Watson, C. J. (2014) · Nature Cell Biology · doi:10.1038/ncb3043 · Cited by 168 · see citing works
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Thornton, C., Leaw, B., Mallard, C. E., Nair, S., Jinnai, M., & Hagberg, H. (2017) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2017.00248 · Cited by 163 · see citing works
Zhou, Z., Liu, J., Huang, J., Rees, T. W., Wang, Y., Wang, H., Li, X., Chao, H., & Stang, P. J. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1912549116 · Cited by 161 · see citing works
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Lim, C. K., Fernández-Gomez, F. J., Braidy, N., Estrada, C., Costa, C., Costa, S., Bessede, A., Fernandez-Villalba, E., Zinger, A., Herrero, M. T., et al. (2017) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.12.009 · Cited by 159 · see citing works
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Pozhitkov, A. E., Neme, R., Domazet‐Lošo, T., Leroux, B. G., Soni, S., Tautz, D., & Noble, P. A. (2017) · Open Biology · doi:10.1098/rsob.160267 · Cited by 142 · see citing works
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Fucikova, J., Truxova, I., Hensler, M., Becht, E., Kasikova, L., Moserova, I., Vosahlikova, S., Klouckova, J., Church, S. E., Cremer, I., et al. (2016) · Blood · doi:10.1182/blood-2016-08-731737 · Cited by 135 · see citing works
Self-citationGarg, A. D., Romano, E., Rufo, N., & Agostinis, P. (2016) · Cell Death and Differentiation · doi:10.1038/cdd.2016.5 · Cited by 131 · see citing works
Bertrand, R. L. (2017) · Medical Hypotheses · doi:10.1016/j.mehy.2017.02.017 · Cited by 129 · see citing works
Wang, X., Li, H., Peng, P., Gong, Z., Huang, J. X., & Peng, H. (2022) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2022.110148 · Cited by 125 · see citing works
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Xi, H., Wang, S., Wang, B., Hong, X., Liu, X., Li, M., Shen, R., & Dong, Q. (2022) · Oncology Reports · doi:10.3892/or.2022.8423 · Cited by 124 · see citing works
Chen, X., Li, Y., Li, S., Gao, M., Ren, L., & Tang, B. Z. (2018) · Advanced Functional Materials · doi:10.1002/adfm.201804362 · Cited by 123 · see citing works
He, B., Shi, Y., Liang, Y., Yang, A., Fan, Z., Yuan, L., Zou, X., Chang, X. Y., Zhang, H., Wang, X., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-04700-z · Cited by 122 · see citing works
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Gallorini, M., Petzel, C., Bolay, C., Hiller, K., Cataldi, A., Buchalla, W., Krifka, S., & Schweikl, H. (2015) · Biomaterials · doi:10.1016/j.biomaterials.2015.03.047 · Cited by 116 · see citing works
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Self-citationHaase, G., & Rabouille, C. (2015) · Frontiers in Neuroscience · doi:10.3389/fnins.2015.00448 · Cited by 74 · see citing works
Zhu, M., Li, H. Y., Bai, L. H., Wang, L., & Zou, X. (2020) · Poultry Science · doi:10.1016/j.psj.2019.12.073 · Cited by 70 · see citing works
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Zheng, Y., He, L., Zhang, D., Tan, C., Ji, L., & Mao, Z. (2017) · Dalton Transactions · doi:10.1039/c7dt02273e · Cited by 70 · see citing works
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Kavčič, N., Pegan, K., & Turk, B. (2017) · Biological Chemistry · doi:10.1515/hsz-2016-0252 · Cited by 66 · see citing works
Augustine, R., Dalvi, Y. B., Dan, P., George, N., Helle, D. U., Varghese, R., Thomas, S., Menu, P., & Sandhyarani, N. (2018) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.8b01102 · Cited by 66 · see citing works
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Treulen, F., Arias, M. E., Águila, L., Uribe, P., & Felmer, R. N. (2018) · Cryobiology · doi:10.1016/j.cryobiol.2018.06.001 · Cited by 66 · see citing works
Zhang, D., Zheng, Y., Zhang, H., He, L., Tan, C., Sun, J., Zhang, W., Peng, X., Zhan, Q., Ji, L., et al. (2017) · Nanoscale · doi:10.1039/c7nr05349e · Cited by 64 · see citing works
Liu, J., Tu, F., Wang, Y., Li, X., Xie, Z., Liu, H., Li, Q., & Pan, Z. (2016) · Scientific Reports · doi:10.1038/srep21197 · Cited by 65 · see citing works
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Parandhaman, D. K., & Narayanan, S. (2014) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2014.00031 · Cited by 60 · see citing works
Vacchelli, E., Semeraro, M., Enot, D. P., Chaba, K., Poirier-Colame, V., Dartigues, P., Perier, A., Villa, I., Rusakiewicz, S., Gronnier, C., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.4428 · Cited by 60 · see citing works
Self-citationSrivastava, M., Hegde, M. B., CHIRUVELLA, K. K., Koroth, J., Bhattacharya, S., Choudhary, B., & Raghavan, S. C. (2014) · Scientific Reports · doi:10.1038/srep06147 · Cited by 59 · see citing works
Gatti, L., Cassinelli, G., Zaffaroni, N., Lanzi, C., & Perego, P. (2015) · Drug Resistance Updates · doi:10.1016/j.drup.2015.04.001 · Cited by 58 · see citing works
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Schorr, S., & van der Laan, M. (2017) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2017.09.021 · Cited by 56 · see citing works
Zhou, H., Forveille, S., Sauvat, A., Sica, V., Izzo, V., Durand, S., Müller, K., Liu, P., Zitvogel, L., Rekdal, Ø., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.5613 · Cited by 57 · see citing works
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Taylor, R. C., & Hetz, C. A. (2020) · Aging Cell · doi:10.1111/acel.13265 · Cited by 54 · see citing works
Wrzesinski, K., & Fey, S. J. (2018) · Bioengineering · doi:10.3390/bioengineering5010022 · Cited by 54 · see citing works
Nury, T., Sghaier, R., Zarrouk, A., Ménétrier, F., Uzun, T., Leoni, V., Caccia, C., Meddeb, W., Namsi, A., Sassi, K., et al. (2018) · Biochimie · doi:10.1016/j.biochi.2018.07.009 · Cited by 54 · see citing works
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Woolbright, B. L., Ayres, M., & Taylor, J. A. (2018) · Urologic Oncology Seminars and Original Investigations · doi:10.1016/j.urolonc.2018.04.010 · Cited by 51 · see citing works
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Hoenke, S., Serbian, I., Deigner, H., & Csük, R. (2020) · Molecules · doi:10.3390/molecules25225443 · Cited by 51 · see citing works
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Buqué, A., Bloy, N., Aranda, F., Cremer, I., Eggermont, A. M. M., Fridman, W. H., Fucikova, J. P., Galon, J., Špíšek, R., Tartour, É., et al. (2016) · OncoImmunology · doi:10.1080/2162402x.2016.1149674 · Cited by 50 · see citing works
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Kang, M., & Shadel, G. S. (2016) · Tuberculosis & respiratory diseases · doi:10.4046/trd.2016.79.4.207 · Cited by 50 · see citing works
Bejoy, J., Yuan, X., Song, L., Hua, T., Jeske, R., Sart, S., Sang, Q. A., & Li, Y. (2019) · Stem Cells International · doi:10.1155/2019/2382534 · Cited by 52 · see citing works
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Tavecchio, M., Lisanti, S., Bennett, M. J., Languino, L. R., & Altieri, D. C. (2015) · Scientific Reports · doi:10.1038/srep15981 · Cited by 49 · see citing works
Li, Q., Zhou, T. J., Wu, F., Li, N., Wang, R., Zhao, Q. S., Ma, Y., Zhang, J., & Ma, B. (2018) · Drug Metabolism Reviews · doi:10.1080/03602532.2018.1512614 · Cited by 49 · see citing works
Sheng, J., Shen, L., Sun, L., Zhang, X., Cui, R., & Wang, L. (2019) · Cell Proliferation · doi:10.1111/cpr.12609 · Cited by 49 · see citing works
Yang, C.-N., Kok, S., Wang, H. ‐., Chang, J. Z., Lai, E. H., Shun, C., Yang, H., Chen, M. ‐., Hong, C., & Lin, S. ‐. (2018) · International Endodontic Journal · doi:10.1111/iej.13055 · Cited by 48 · see citing works
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Zhao, P., Li, H., & Bu, W. (2023) · Angewandte Chemie · doi:10.1002/ange.202210415 · Cited by 49 · see citing works
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Cancino, J., Jung, J. E., & Luini, A. (2013) · Histochemistry and Cell Biology · doi:10.1007/s00418-013-1130-9 · Cited by 47 · see citing works
Huang, C., Wang, S.-Y., Lin, L., Wang, P., Chen, T., Hsu, W., Lin, T., Liou, C., & Chuang, J. (2015) · Disease Models & Mechanisms · doi:10.1242/dmm.021667 · Cited by 45 · see citing works
Carnosic Acid as a Promising Agent in Protecting Mitochondria of Brain Cells
de Oliveira, M. R. (2018) · Molecular Neurobiology · doi:10.1007/s12035-017-0842-6 · Cited by 45 · see citing works
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Bento, A. C., Bippes, C. C., Kohler, C., Hemion, C., Frank, S., & Neutzner, A. (2018) · Scientific Reports · doi:10.1038/s41598-018-30963-z · Cited by 44 · see citing works
Du, Q. B., Yang, Y., Guo, L., Tian, M., Ge, X., Tian, Z., Zhao, L., Xu, Z., Li, J., & Liu, Z. (2018) · Dyes and Pigments · doi:10.1016/j.dyepig.2018.11.009 · Cited by 44 · see citing works
β-galactosidase responsive AIE fluorogene for identification and removal of senescent cancer cells
Gao, Z., Gao, H., Zheng, D., Xu, T., Chen, Y., Liang, C., Wang, L., Ding, D., & Yang, Z. (2020) · Science China Chemistry · doi:10.1007/s11426-019-9659-2 · Cited by 43 · see citing works
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Gregory, C. D., Ford, C. A., & Voss, J. J. L. P. (2016) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-39406-0_3 · Cited by 41 · see citing works
The oncolytic compound LTX-401 targets the Golgi apparatus
Zhou, H., Sauvat, A., Gomes-da-Silva, L. C., Durand, S., Forveille, S., Iribarren, K., Yamazaki, T., Souquère, S., Bezu, L., Müller, K., et al. (2016) · Cell Death and Differentiation · doi:10.1038/cdd.2016.86 · Cited by 41 · see citing works
Self-citationTian, X., Ma, S., Wang, Y., Hou, L., Shi, Y., Yao, M., Wang, X., Zhang, H., & Jiang, L. (2015) · DNA and Cell Biology · doi:10.1089/dna.2015.2885 · Cited by 40 · see citing works
- Authors
- Galluzzi, L., Bravo-San Pedro, J. M., & Kroemer, G.
- Affiliations
- Sorbonne Paris Cité (FR)
- Inserm (FR)
- Corresponding author
- Galluzzi, Lorenzo
- Kroemer, Guido
- Venue
- Nature Cell Biology
- Published
- 2014-08
- Volume
- 16
- Issue
- 8
- Pages
- 728-736
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- OpenAlex
- W2036020241
- Cited by
- 239
- References
- 151
- Citations by year
- 2026: 7 · 2025: 8 · 2024: 9 · 2023: 11 · 2022: 13 · 2021: 20 · 2020: 20 · 2019: 15 · 2018: 28 · 2017: 21 · 2016: 36 · 2015: 39 · 2014: 10 · 2013: 1
- FWCI
- 3.33
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Ligue Contre le Cancer
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- cell death, apoptosis, necrosis, mitochondrial signaling, endoplasmic reticulum stress, lysosomes, Golgi apparatus, cytoskeleton, plasma membrane, nuclear signaling, subcellular signaling
- MeSH terms
- Cell Membrane, Cell Nucleus, Cytoskeleton, Endoplasmic Reticulum, Golgi Apparatus, Humans, Lysosomes, Mitochondria, Models, Biological, Necrosis, Stress, Physiological, Organelles, Signal Transduction, Cell Death, Apoptosis
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