Non‐apoptotic functions of apoptosis‐regulatory proteins

The BCL-2 protein family: opposing activities that mediate cell death

Youle, R. J., & Strasser, A. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2308 · Cited by 4,704 · 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-eating and self-killing: crosstalk between autophagy and apoptosis

Maiuri, M. C., Zalckvar, E., Kimchi, A., & Kroemer, G. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2239 · Cited by 3,560 · 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

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

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

Molecular definitions of cell death subroutines: recommendations of the Nomenclature Committee on Cell Death 2012

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

Molecular mechanisms of necroptosis: an ordered cellular explosion

Vandenabeele, P., Galluzzi, L., Vanden Berghe, T., & Kroemer, G. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2970 · Cited by 2,382 · see citing works

Integrating cell-signalling pathways with NF-κB and IKK function

Perkins, N. D. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2083 · Cited by 2,350 · see citing works

Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death

Baines, 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

Altered Cytokine Export and Apoptosis in Mice Deficient in Interleukin-1β Converting Enzyme

Kuida, K., Lippke, J. A., Ku, G., Harding, M. W., Livingston, D. J., Su, M. S. S., & Flavell, R. A. (1995) · Science · doi:10.1126/science.7535475 · Cited by 1,606 · see citing works

Mice deficient in IL-1β-converting enzyme are defective in production of mature IL-1β and resistant to endotoxic shock

Li, P., Allen, H., Banerjee, S., Franklin, S., Herzog, L., Johnston, C. G., McDowell, J., Paskind, M. P., Rodman, L., Salfeld, J. G., et al. (1995) · Cell · doi:10.1016/0092-8674(95)90490-5 · Cited by 1,408 · see citing works

Mechanisms of cytochrome c release from mitochondria

Garrido, C., Galluzzi, L., Brunet, M., Puig, P., Mirjolet, C., & Kroemer, G. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401950 · Cited by 1,394 · see citing works

Inflammation meets cancer, with NF-κB as the matchmaker

Ben‐Neriah, Y., & Karin, M. (2011) · Nature Immunology · doi:10.1038/ni.2060 · Cited by 1,379 · see citing works

Essential role of the mitochondrial apoptosis-inducing factor in programmed cell death

Joza, N. A., Susín, S. A., Daugas, É., Stanford, W. L., Cho, S. K., Li, C. Y. J., Sasaki, T., Elia, A., Cheng, H.-Y. M., Ravagnan, L., et al. (2001) · Nature · doi:10.1038/35069004 · Cited by 1,365 · see citing works

Targeted disruption of the mouse Caspase 8 gene ablates cell death induction by the TNF receptors, Fas/Apo1, and DR3 and is lethal prenatally.

Varfolomeev, E., Schuchmann, M., Luria, V., Chiannilkulchai, N., Beckmann, J., Mett, I., Rebrikov, D., Brodianski, V. M., Kemper, O., Kollet, O., et al. (1998) · Immunity · doi:10.1016/s1074-7613(00)80609-3 · Cited by 1,332 · see citing works

Mitochondrial dynamics and apoptosis

Suen, D.-F., Norris, K. L., & Youle, R. J. (2008) · Genes & Development · doi:10.1101/gad.1658508 · Cited by 1,270 · see citing works

Mitochondria and the Autophagy–Inflammation–Cell Death Axis in Organismal Aging

Green, D. R., Galluzzi, L., & Kroemer, G. (2011) · Science · doi:10.1126/science.1201940 · Cited by 1,245 · see citing works

cIAP1 and cIAP2 Facilitate Cancer Cell Survival by Functioning as E3 Ligases that Promote RIP1 Ubiquitination

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 Death Domain Kinase RIP Mediates the TNF-Induced NF-κB Signal

Kelliher, M. A., Grimm, S., Ishida, Y., Kuo, F., Stanger, B. Z., & Leder, P. (1998) · Immunity · doi:10.1016/s1074-7613(00)80535-x · 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

Isozymes of mammalian hexokinase: structure, subcellular localization and metabolic function

Wilson, J. E. (2003) · Journal of Experimental Biology · doi:10.1242/jeb.00241 · Cited by 1,085 · 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

Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death

Baines, C. P., Kaiser, R. A., Sheiko, T., Craigen, W. J., & Molkentin, J. D. (2007) · Nature Cell Biology · doi:10.1038/ncb1575 · Cited by 971 · see citing works

The Fas Signaling Pathway: More Than a Paradigm

Wajant, H. (2002) · Science · doi:10.1126/science.1071553 · Cited by 957 · see citing works

Inflammatory Caspases

Martinon, F., & Tschopp, J. (2004) · Cell · doi:10.1016/j.cell.2004.05.004 · Cited by 940 · see citing works

Inhibition of Caspases Increases the Sensitivity of L929 Cells to Necrosis Mediated by Tumor Necrosis Factor

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

Caspase 3–mediated stimulation of tumor cell repopulation during cancer radiotherapy

Huang, Q., Li, F., Liu, X., Li, W., Shi, W., Liu, F.-F., O'Sullivan, B., He, Z., Peng, Y., Tan, A.-C., et al. (2011) · Nature Medicine · doi:10.1038/nm.2385 · Cited by 886 · see citing works

FADD: Essential for Embryo Development and Signaling from Some, But Not All, Inducers of Apoptosis

Yeh, W., de la Pompa, J. L., McCurrach, M. E., Shu, H., Elia, A., Shahinian, A., Ng, M. S. W., Wakeham, A. C., Khoo, W., Mitchell, K., et al. (1998) · Science · doi:10.1126/science.279.5358.1954 · Cited by 886 · see citing works

Active Caspase-1 Is a Regulator of Unconventional Protein Secretion

Keller, M., Rüegg, A., Werner, S., & Beer, H. (2008) · Cell · doi:10.1016/j.cell.2007.12.040 · Cited by 851 · see citing works

Murine Caspase-11, an ICE-Interacting Protease, Is Essential for the Activation of ICE

Wang, S., Miura, M., Jung, Y., Zhu, H., Li, E., & Yuan, J. (1998) · Cell · doi:10.1016/s0092-8674(00)80943-5 · Cited by 699 · see citing works

Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts

G�thel, S. F., & Marahiel, M. A. (1999) · Cellular and Molecular Life Sciences · doi:10.1007/s000180050299 · Cited by 649 · see citing works

AIF deficiency compromises oxidative phosphorylation

Vahsen, N., Candé, C., Brière, J.-J., Bénit, P., Joza, N. A., Larochette, N., Mastroberardino, P. G., Péquignot, M. O., Casares, N., Lazar, V., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600461 · Cited by 622 · see citing works

Mitochondrial creatine kinase in human health and disease

Schlattner, U., Tokarska-Schlattner, M., & Wallimann, T. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2005.09.004 · Cited by 617 · 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

Caspase-3 triggers early synaptic dysfunction in a mouse model of Alzheimer's disease

D'Amelio, M., Cavallucci, V., Middei, S., Marchetti, C., Pacioni, S., Ferri, A., Diamantini, A., De Zio, D., Carrara, P., Battistini, L., et al. (2011) · Nature Neuroscience · doi:10.1038/nn.2709 · Cited by 572 · see citing works

Caspase-2 Induces Apoptosis by Releasing Proapoptotic Proteins from Mitochondria

Guo, Y., Srinivasula, S. M., Druilhe, A., Fernandes‐Alnemri, T., & Alnemri, E. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108029200 · Cited by 521 · see citing works

Cytochrome c Deficiency Causes Embryonic Lethality and Attenuates Stress-Induced Apoptosis

Li, K., Li, Y., Shelton, J. M., Richardson, J. A., Spencer, E., Chen, Z. J., Wang, X., & Williams, R. S. (2000) · Cell · doi:10.1016/s0092-8674(00)80849-1 · Cited by 509 · see citing works

The mitochondrial protease HtrA2 is regulated by Parkinson's disease-associated kinase PINK1

Plun‐Favreau, H., Klupsch, K., Moisoi, N., Gandhi, S., Kjaer, S., Frith, D., Harvey, K., Deas, E., Harvey, R. J., McDonald, N. Q., et al. (2007) · Nature Cell Biology · doi:10.1038/ncb1644 · Cited by 476 · 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

Differential modulation of endotoxin responsiveness by human caspase-12 polymorphisms

Saleh, M., Vaillancourt, J. P., Graham, R. K., Huyck, M., Srinivasula, S. M., Alnemri, E. S., Steinberg, M. H., Nolan, V., Baldwin, C. T., Hotchkiss, R. S., et al. (2004) · Nature · doi:10.1038/nature02451 · Cited by 423 · see citing works

Viral Control of Mitochondrial Apoptosis

Galluzzi, L., Brenner, C., Morselli, E., Touat-Hamici, Z., & Kroemer, G. (2008) · PLoS Pathogens · doi:10.1371/journal.ppat.1000018 · Cited by 423 · 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

Targeted deletion of AIF decreases mitochondrial oxidative phosphorylation and protects from obesity and diabetes

Pospisilik, J. A., Knauf, C., Joza, N., Benit, P., Orthofer, M., Cani, P. D., Ebersberger, I., Nakashima, T., Sarao, R., Neely, G., et al. (2007) · Cell · doi:10.1016/j.cell.2007.08.047 · Cited by 404 · see citing works

Caspase Activation Is Required for Terminal Erythroid Differentiation

Zermati, Y., Garrido, C., Amsellem, S., Fishelson, S., Bouscary, D., Valensi, F., Varet, B. R., Solary, É., & Hermine, O. (2001) · The Journal of Experimental Medicine · doi:10.1084/jem.193.2.247 · Cited by 402 · see citing works

The cell death inhibitor Bcl‐2 and its homologues influence control of cell cycle entry.

O’Reilly, L. A., Huang, D. C. S., & Strasser, A. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb01090.x · Cited by 380 · see citing works

Bcl-2 Protein Family Members: Versatile Regulators of Calcium Signaling in Cell Survival and Apoptosis

Rong, Y., & Distelhorst, C. (2007) · Annual Review of Physiology · doi:10.1146/annurev.physiol.70.021507.105852 · Cited by 357 · see citing works

Platelet formation is the consequence of caspase activation within megakaryocytes

de Botton, S. (2002) · Blood · doi:10.1182/blood-2002-03-0686 · Cited by 352 · see citing works

The anti‐apoptosis function of Bcl‐2 can be genetically separated from its inhibitory effect on cell cycle entry

Huang, D. C. S., O’Reilly, L. A., Strasser, A., & Cory, S. (1997) · The EMBO Journal · doi:10.1093/emboj/16.15.4628 · Cited by 333 · see citing works

Endonuclease G Regulates Budding Yeast Life and Death

Büttner, S., Eisenberg, T., Carmona-Gutierrez, D., Ruli, D., Knauer, H., Ruckenstuhl, C., Sigrist, C., Wissing, S., Kollroser, M., Fröhlich, K.-U., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2006.12.021 · Cited by 331 · see citing works

Bcl-2 and Bcl-XL Regulate Proinflammatory Caspase-1 Activation by Interaction with NALP1

Bruey, J., Bruey-Sédano, N., Luciano, F., Zhai, D., Balpai, R., Xu, C., Kress, C. L., Bailly‐Maitre, B., Li, X., Osterman, A. L., et al. (2007) · Cell · doi:10.1016/j.cell.2007.01.045 · Cited by 319 · see citing works

Specific involvement of caspases in the differentiation of monocytes into macrophages

Sordet, O., Rébé, C., Plenchette, S., Zermati, Y., Hermine, O., Vainchenker, W., Garrido, C., Solary, É., & Dubrez, L. (2002) · Blood · doi:10.1182/blood-2002-06-1778 · Cited by 313 · see citing works

TRADD Protein Is an Essential Component of the RIG-like Helicase Antiviral Pathway

Michallet, M., Meylan, E., Ermolaeva, M., Vázquez, J., Rebsamen, M., Curran, J. A., Poeck, H., Bscheider, M., Hartmann, G., König, M. F., et al. (2008) · Immunity · doi:10.1016/j.immuni.2008.03.013 · Cited by 304 · see citing works

Hsp70 regulates erythropoiesis by preventing caspase-3-mediated cleavage of GATA-1

Ribeil, J., Zermati, Y., Vandekerckhove, J., Cathelin, S., Kersual, J., Dussiot, M., Coulon, S., Moura, I. C., Zeuner, A., Kirkegaard‐Sørensen, T., et al. (2006) · Nature · doi:10.1038/nature05378 · Cited by 297 · see citing works

The Adaptor Protein FADD Protects Epidermal Keratinocytes from Necroptosis In Vivo and Prevents Skin Inflammation

Bonnet, 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

JNK Suppresses Apoptosis via Phosphorylation of the Proapoptotic Bcl-2 Family Protein BAD

Yu, C., Minemoto, Y., Zhang, J., Liu, J., Tang, F., Bui, T. N., Xiang, J., & Lin, A. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00028-0 · Cited by 292 · see citing works

Energy Transduction: Proton Transfer Through the Respiratory Complexes

Hosler, J. P., Ferguson-Miller, S. M., & Mills, D. A. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.062003.101730 · Cited by 291 · see citing works

XIAP mediates NOD signaling via interaction with RIP2

Krieg, A. H., Correa, R. G., Garrison, J. B., Negrate, G. L., Welsh, K., Huang, Z., Knoefel, W. T., & Reed, J. C. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907131106 · Cited by 287 · see citing works

Bcl-xL regulates metabolic efficiency of neurons through interaction with the mitochondrial F1FO ATP synthase

Alavian, K. N., Li, H., Collis, L. P., Bonanni, L., Zeng, L., Sacchetti, S., Lazrove, E., Nabili, P., Flaherty, B., Graham, M. M., et al. (2011) · Nature Cell Biology · doi:10.1038/ncb2330 · Cited by 283 · see citing works

Specific Ablation of the Apoptotic Functions of Cytochrome c Reveals a Differential Requirement for Cytochrome c and Apaf-1 in Apoptosis

Hao, Z., Duncan, G. S., Chang, C., Elia, A., Fang, M., Wakeham, A. C., Okada, H., Calzascia, T., Jang, Y., You-Ten, A. J., et al. (2005) · Cell · doi:10.1016/j.cell.2005.03.016 · Cited by 278 · see citing works

Phosphorylation of BCL‐2 regulates ER Ca2+ homeostasis and apoptosis

Bassik, M. C., Scorrano, L., Oakes, S. A., Pozzan, T., & Korsmeyer, S. J. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600104 · Cited by 278 · see citing works

Function of TRADD in tumor necrosis factor receptor 1 signaling and in TRIF-dependent inflammatory responses

Ermolaeva, M., Michallet, M., Papadopoulou, N., Utermöhlen, O., Kranidioti, K., Kollias, G. A., Tschopp, J., & Pasparakis, M. (2008) · Nature Immunology · doi:10.1038/ni.1638 · Cited by 277 · see citing works

No death without life: vital functions of apoptotic effectors

Galluzzi, L., Joza, N. A., Tasdemir, E., Maiuri, M. C., Hengartner, M. O., Abrams, J., Tavernarakis, N., Penninger, J. M., Madeo, F., & Kroemer, G. (2008) · Cell Death and Differentiation · doi:10.1038/cdd.2008.28 · Cited by 256 · see citing works

A Role for FADD in T Cell Activation and Development

Walsh, C. M., Wen, B. G., Chinnaiyan, A. M., O’Rourke, K. M., Dixit, V. M., & Hedrick, S. Μ. (1998) · Immunity · doi:10.1016/s1074-7613(00)80549-x · Cited by 239 · see citing works

Proapoptotic BID Is an ATM Effector in the DNA-Damage Response

Kamer, I., Sarig, R., Zaltsman, Y., Niv, H., Oberkovitz, G., Regev, L., Haimovich, G., Lerenthal, Y., Marcellus, R. C., & Gross, A. (2005) · Cell · doi:10.1016/j.cell.2005.06.014 · Cited by 226 · see citing works

Severe X-Linked Mitochondrial Encephalomyopathy Associated with a Mutation in Apoptosis-Inducing Factor

Ghezzi, D., Sevrioukova, I. F., Invernizzi, F., Lamperti, C., Mora, M., D’Adamo, P., Novara, F., Zuffardi, O., Uziel, G., & Zeviani, M. (2010) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2010.03.002 · Cited by 224 · see citing works

The permeability transition pore complex in cancer cell death

Brenner, C., & Grimm, S. (2006) · Oncogene · doi:10.1038/sj.onc.1209609 · Cited by 220 · see citing works

Regulation of mitochondrial metabolism by ER Ca 2+ release: an intimate connection

Rutter, G. A., & Rizzuto, R. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01585-1 · Cited by 208 · see citing works

The BH3-Only Protein Bid Is Dispensable for DNA Damage- and Replicative Stress-Induced Apoptosis or Cell-Cycle Arrest

Kaufmann, T., Tai, L., Ekert, P. G., Huang, D. C. S., Norris, F., Lindemann, R. K., Johnstone, R. W., Dixit, V. M., & Strasser, A. (2007) · Cell · doi:10.1016/j.cell.2007.03.017 · Cited by 206 · see citing works

Bcl‐xL/Bcl‐2 coordinately regulates apoptosis, cell cycle arrest and cell cycle entry

Janumyan, Y., Sansam, C. G., Chattopadhyay, A., Cheng, N., Soucie, E. L., Penn, L. Z., Andrews, D. W., Knudson, C. M., & Yang, E. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg533 · Cited by 193 · see citing works

Dissociating the dual roles of apoptosis‐inducing factor in maintaining mitochondrial structure and apoptosis

Cheung, E. C., Joza, N. A., Steenaart, N. A. E., McClellan, K. A., Neuspiel, M., McNamara, S., MacLaurin, J. G., Rippstein, P. U., Park, D. S., Shore, G. C., et al. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601276 · Cited by 191 · see citing works

STRUCTURE AND MODE OF ACTION OF A VOLTAGE DEPENDENT ANION‐SELECTIVE CHANNEL (VDAC) LOCATED IN THE OUTER MITOCHONDRIAL MEMBRANE DEPENDENT ANION‐SELECTIVE CHANNEL (VDAC)*

Colombini, M. (1980) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1980.tb47198.x · Cited by 188 · see citing works

A link between cell cycle and cell death: Bax and Bcl‐2 modulate Cdk2 activation during thymocyte apoptosis

Gil‐Gómez, G., Berns, A. J. M., & Brady, H. J. M. (1998) · The EMBO Journal · doi:10.1093/emboj/17.24.7209 · Cited by 183 · see citing works

Syncytial fusion of human trophoblast depends on caspase 8

Black, S., Kadyrov, M., Kaufmann, P., Ugele, B., Emans, N., & Huppertz, B. (2003) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401307 · Cited by 178 · see citing works

Caspase-3 regulates cell cycle in B cells: a consequence of substrate specificity

Woo, M., Hakem, R., Furlonger, C. L., Hakem, A., Duncan, G. S., Sasaki, T., Bouchard, D., Lu, L., Wu, G. E., Paige, C. J., et al. (2003) · Nature Immunology · doi:10.1038/ni976 · Cited by 176 · see citing works

Generation and Characterization of Smac/DIABLO-Deficient Mice

Okada, H., Suh, W., Jin, J., Woo, M., Du, C., Elia, A., Duncan, G. S., Wakeham, A. C., Itié, A., Lowe, S. W., et al. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.10.3509-3517.2002 · Cited by 172 · see citing works

Buffy, a Drosophila Bcl‐2 protein, has anti‐apoptotic and cell cycle inhibitory functions

Quinn, L. M., Coombe, M., Mills, K., Daish, T., Colussi, P., Kumar, S., & Richardson, H. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg355 · Cited by 157 · see citing works

Bcl-2 Retards Cell Cycle Entry through p27Kip1, pRB Relative p130, and Altered E2F Regulation

Vairo, G., Soos, T. J., Upton, T. M., Zalvide, J. B., DeCaprio, J. A., Ewen, M. E., Koff, A., & Adams, J. M. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.13.4745-4753.2000 · Cited by 144 · see citing works

Non-apoptotic role of BID in inflammation and innate immunity

Yeretssian, G., Correa, R. G., Doiron, K., Fitzgerald, P., Dillon, C. P., Green, D. R., Reed, J. C., & Saleh, M. (2011) · Nature · doi:10.1038/nature09982 · Cited by 122 · see citing works

The N-terminal End of Bax Contains a Mitochondrial-targeting Signal

Cartron, P., Priault, M., Oliver, L., Méflah, K., Manon, S., & Vallette, F. M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m208955200 · Cited by 122 · see citing works

An essential role for the Leishmania major metacaspase in cell cycle progression

Ambit, A., Fasel, N. J., Coombs, G. H., & Mottram, J. C. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402232 · Cited by 120 · see citing works

Structural Diversity of Mitochondria

Mannella, C. A. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1427.020 · Cited by 120 · see citing works

Nonapoptotic Role for Apaf-1 in the DNA Damage Checkpoint

Zermati, Y., Mouhamad, S., Stergiou, L., Besse, B., Galluzzi, L., Boehrer, S., Pauleau, A., Rosselli, F., D’Amelio, M., Amendola, R., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.09.030 · Cited by 107 · see citing works

Loss of Aif function causes cell death in the mouse embryo, but the temporal progression of patterning is normal

Brown, D., Yu, B., Joza, N. A., Bénit, P., Meneses, J. J., Firpo, M. T., Rustin, P., Penninger, J. M., & Martin, G. R. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603950103 · Cited by 101 · see citing works

Endonuclease G is required for early embryogenesis and normal apoptosis in mice

Zhang, J., Dong, M., Li, L. Y., Fan, Y., Pathre, P., Dong, J., Lou, D., Wells, J. M., Olivares–Villagómez, D., Kaer, L. V., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2636393100 · Cited by 100 · see citing works

XIAP Regulates Cytosol-Specific Innate Immunity to Listeria Infection

Bauler, L. D., Duckett, C. S., & O’Riordan, M. X. (2008) · PLoS Pathogens · doi:10.1371/journal.ppat.1000142 · Cited by 98 · see citing works

EndoG is dispensable in embryogenesis and apoptosis

David, K. K., Sasaki, M., Yu, S.-W., Dawson, T. M., & Dawson, V. L. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401787 · Cited by 96 · see citing works

Early prenatal ventriculomegaly due to an AIFM1 mutation identified by linkage analysis and whole exome sequencing

Berger, I., Ben‐Neriah, Z., Dor-Wollman, T., Shaag, A., Saada, A., Zenvirt, S., Raas‐Rothschild, A., Nadjari, M., Kaestner, K. H., & Elpeleg, O. N. (2011) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2011.09.020 · Cited by 88 · see citing works

Mechanism of Bcl-2 and Bcl-X L inhibition of NLRP1 inflammasome: Loop domain-dependent suppression of ATP binding and oligomerization

Faustin, B., Chen, Y., Zhai, D., Negrate, G. L., Lartigue, L., Satterthwait, A. C., & Reed, J. C. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809414106 · Cited by 86 · see citing works

New role of the BCL2 family of proteins in the regulation of mitochondrial dynamics

Rolland, S. G. M., & Conradt, B. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2010.07.014 · Cited by 82 · see citing works

Bcl-2 protein localizes to the chromosomes of mitotic nuclei and is correlated with the cell cycle in cultured epithelial cell lines

Lu, Q., Hanby, A. M., Hajibagheri, M. A. N., Gschmeissner, S. E., Lu, P., Taylor‐Papadimitriou, J., Krajewski, S., Reed, J. C., & Wright, N. A. (1994) · Journal of Cell Science · doi:10.1242/jcs.107.2.363 · Cited by 78 · see citing works

A Dominant Negative Fas-associated Death Domain Protein Mutant Inhibits Proliferation and Leads to Impaired Calcium Mobilization in Both T-cells and Fibroblasts

Hueber, A., Zörnig, M., Bernard, A., Chautan, M., & Evan, G. I. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.14.10453 · Cited by 74 · see citing works

Conditional Fas-Associated Death Domain Protein (FADD):GFP Knockout Mice Reveal FADD Is Dispensable in Thymic Development but Essential in Peripheral T Cell Homeostasis

Zhang, Y., Rosenberg, S., Wang, H., Imtiyaz, H. Z., Hou, Y.-J., & Zhang, J. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.5.3033 · Cited by 67 · see citing works

Endonuclease G: A role for the enzyme in recombination and cellular proliferation

Huang, K.-J., Ku, C., & Lehman, I. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603445103 · Cited by 65 · see citing works

Role of Smac in human leukaemic cell apoptosis and proliferation

Jia, L., Patwari, Y., Kelsey, S. M., Srinivasula, S. M., Agrawal, S. G., Alnemri, E. S., & Newland, A. C. (2003) · Oncogene · doi:10.1038/sj.onc.1206322 · Cited by 65 · see citing works

Caspase‐8 and caspase‐10 activate NF‐κB through RIP, NIK and IKKα kinases

Shikama, Y., Yamada, M., & Miyashita, T. (2003) · European Journal of Immunology · doi:10.1002/eji.200324013 · Cited by 62 · see citing works

Fas-Associated Death Domain-Containing Protein-Mediated Antiviral Innate Immune Signaling Involves the Regulation of Irf7

Balachandran, S., Venkataraman, T., Fisher, P. B., & Barber, G. N. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.4.2429 · Cited by 60 · see citing works

TRADD interacts with STAT1-α and influences interferon-γ signaling

Wesemann, D. R., Qin, H., Kokorina, N. A., & Benveniste, E. N. (2004) · Nature Immunology · doi:10.1038/ni1025 · Cited by 51 · see citing works

The molecular archaeology of a mitochondrial death effector: AIF in Drosophila

Joza, N. A., Galindo, K. A., Pospisilik, J. A., Bénit, P., Rangachari, M., Kanitz, E. E., Nakashima, Y., Neely, G. G., Rustin, P., Abrams, J., et al. (2008) · Cell Death and Differentiation · doi:10.1038/cdd.2008.24 · Cited by 50 · see citing works

Bcl-2-Induced Changes in E2F Regulatory Complexes Reveal the Potential for Integrated Cell Cycle and Cell Death Functions

Lind, E. F., Wayne, J., Wang, Q.-Z., Staeva, T. P., Stolzer, A. L., & Petrie, H. T. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.162.9.5374 · Cited by 46 · see citing works

Expression and Functional Roles of Caspase-5 in Inflammatory Responses of Human Retinal Pigment Epithelial Cells

Bian, Z.-M., Elner, S. G., Khanna, H., Murga‐Zamalloa, C., Patil, S. B., & Elner, V. M. (2011) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.11-7570 · Cited by 44 · see citing works

Caspase 6 Regulates B Cell Activation and Differentiation into Plasma Cells

Watanabe, C., Shu, G. L., Zheng, T. S., Flavell, R. A., & Clark, E. A. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.181.10.6810 · Cited by 42 · see citing works

Peripheral benzodiazepine receptor: structure and function in health and disease.

Papadopoulos, V. D. (2003) · PubMed · Cited by 39 · see citing works

Serine protease Omi/HtrA2 targets WARTS kinase to control cell proliferation

Kuninaka, S., Iida, S.-I., Hara, T., Nomura, M., Naoe, H., Morisaki, T., Nitta, M., Arima, Y., Mimori, T., Yonehara, S., et al. (2006) · Oncogene · doi:10.1038/sj.onc.1210042 · Cited by 37 · see citing works

Caspase-2 is required for DNA damage-induced expression of the CDK inhibitor p21WAF1/CIP1

Sohn, D., Budach, W., & Jänicke, R. U. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.34 · Cited by 37 · see citing works

Proapoptotic Bid mediates the Atr-directed DNA damage response to replicative stress

Liu, Y., Bertram, C. C., Shi, Q., & Zinkel, S. S. (2010) · Cell Death and Differentiation · doi:10.1038/cdd.2010.151 · Cited by 35 · see citing works

RIP1-mediated regulation of lymphocyte survival and death responses

Zhang, J., Zhang, H., Li, J., Rosenberg, S., Zhang, E. C., Zhou, X., Qin, F., & Farabaugh, M. E. (2011) · Immunologic Research · doi:10.1007/s12026-011-8249-3 · Cited by 35 · see citing works

The Adenine Nucleotide Translocator: A New Potential Chemotherapeutic Target

Belzacq, A.-S., & Brenner, C. (2003) · Current Drug Targets · doi:10.2174/1389450033490867 · Cited by 31 · see citing works

A Fas-Associated Death Domain Protein/Caspase-8-Signaling Axis Promotes S-Phase Entry and Maintains S6 Kinase Activity in T Cells Responding to IL-2

Arechiga, A. F., Bell, B. D., Leverrier, S., Weist, B. M., Porter, M. B., Wu, Z., Kanno, Y., Ramos, S. J., Ong, S. T., Siegel, R. M., et al. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.8.5291 · Cited by 31 · see citing works

The time course of unconditioned morphine-induced psychomotor sensitization mirrors the phosphorylation of FADD and MEK/ERK in rat striatum: Role of PEA-15 as a FADD-ERK binding partner in striatal plasticity

Ramos‐Miguel, A., Esteban, S., & Garcı́a-Sevilla, J. A. (2009) · European Neuropsychopharmacology · doi:10.1016/j.euroneuro.2009.08.005 · Cited by 29 · see citing works

Apaf-1 Deficiency Causes Chromosomal Instability

Mouhamad, S., Galluzzi, L., Zermati, Y., Castedo, M., & Kroemer, G. (2007) · Cell Cycle · doi:10.4161/cc.6.24.5046 · Cited by 29 · see citing works

Endonuclease G plays a role in immunoglobulin class switch DNA recombination by introducing double-strand breaks in switch regions

Zan, H., Zhang, J., Al-Qahtani, A., Pone, E. J., White, C. A., Lee, D., Yel, L., Mai, T., & Casali, P. (2010) · Molecular Immunology · doi:10.1016/j.molimm.2010.10.023 · Cited by 26 · see citing works

Non-apoptotic Fas-induced regulation of cytokines in undifferentiated and decidualized human endometrial stromal cells depends on caspase-activity

Fluhr, H., Wenig, H., Spratte, J., Heidrich, S., Ehrhardt, J., & Zygmunt, M. (2010) · Molecular Human Reproduction · doi:10.1093/molehr/gaq082 · Cited by 17 · see citing works

Apoptosis-inducing factor is a target gene of C/EBPα and participates in adipocyte differentiation

Shen, S.-M., Yu, Y., Wu, Z., Zheng, Y., Chen, G., & Wang, L. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.05.061 · Cited by 13 · see citing works

Overexpression of Raidd cDNA inhibits differentiation of mouse preadipocytes

Felmer, R. N., Horvat, S., Clinton, M., & Clark, A. J. (2003) · Cell Proliferation · doi:10.1046/j.1365-2184.2003.00253.x · Cited by 9 · see citing works

Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018.

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

Sugar for the brain: the role of glucose in physiological and pathological brain function

Mergenthaler, P., Lindauer, U., Dienel, G. A., & Meisel, A. (2013) · Trends in Neurosciences · doi:10.1016/j.tins.2013.07.001 · Cited by 1,612 · see citing works

Emerging regulation and functions of autophagy

Boya, P., Reggiori, F., & Codogno, P. (2013) · Nature Cell Biology · doi:10.1038/ncb2788 · Cited by 1,216 · see citing works

Mitochondrial control of inflammation

Marchi, S., Guilbaud, E., Tait, S. W. G., Yamazaki, T., & Galluzzi, L. (2023) · Nature Reviews Immunology · doi:10.1038/s41577-022-00760-x · Cited by 1,027 · see citing works

Decoding cell death signals in liver inflammation

Brenner, C., Galluzzi, L., Kepp, O., & Kroemer, G. (2013) · Journal of Hepatology · doi:10.1016/j.jhep.2013.03.033 · Cited by 1,022 · 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

Metabolic targets for cancer therapy

Galluzzi, L., Kepp, O., Heiden, M. G. V., & Kroemer, G. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4145 · Cited by 705 · see citing works

Mitochondrial dysfunction and sarcopenia of aging: from signaling pathways to clinical trials

Marzetti, E., Calvani, R., Cesari, M., Buford, T. W., Lorenzi, M., Behnke, B. J., & Leeuwenburgh, C. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.06.024 · Cited by 627 · see citing works

Mitochondrial Control of Cellular Life, Stress, and Death

Galluzzi, L., Kepp, O., Trojel‐Hansen, C., & Kroemer, G. (2012) · Circulation Research · doi:10.1161/circresaha.112.268946 · Cited by 545 · see citing works

Oxidative stress and pulmonary fibrosis

Cheresh, P., Kim, S.-J., Tulasiram, S., & Kamp, D. W. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2012.11.021 · Cited by 527 · see citing works

Role 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

Molecular mechanisms of cell death: central implication of ATP synthase in mitochondrial permeability transition

Bonora, M., Wieckowski, M. R., Chinopoulos, C., Kepp, O., Kroemer, G., Galluzzi, L., & Pinton, P. (2015) · Oncogene · doi:10.1038/onc.2014.96 · Cited by 330 · see citing works

NOD-Like Receptors: Master Regulators of Inflammation and Cancer

Saxena, M., & Yeretssian, G. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00327 · Cited by 272 · see citing works

Regulation of autophagy by stress-responsive transcription factors

Pietrocola, F., Izzo, V., Niso‐Santano, M., Vacchelli, E., Galluzzi, L., Maiuri, M. C., & Kroemer, G. (2013) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2013.05.008 · Cited by 270 · 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

Caspase involvement in autophagy

Tsapras, P., & Nezis, I. P. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.43 · Cited by 191 · see citing works

Caspase-dependent non-apoptotic processes in development

Nakajima, Y.-I., & Kuranaga, E. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.36 · Cited by 184 · see citing works

Beclin 1 interactome controls the crosstalk between apoptosis, autophagy and inflammasome activation: Impact on the aging process

Salminen, A., Kaarniranta, K., & Kauppinen, A. (2013) · Ageing Research Reviews · doi:10.1016/j.arr.2012.11.004 · Cited by 173 · see citing works

Structural biology of the Bcl-2 family and its mimicry by viral proteins

Kvansakul, M., & Hinds, M. G. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.436 · Cited by 140 · see citing works

Bcl-2 family proteins: master regulators of cell survival

Hatok, J., & Račay, P. (2016) · BioMolecular Concepts · doi:10.1515/bmc-2016-0015 · Cited by 136 · see citing works

The potential role of necroptosis in inflammaging and aging

Royce, G. H., Brown‐Borg, H. M., & Deepa, S. S. (2019) · GeroScience · doi:10.1007/s11357-019-00131-w · Cited by 135 · see citing works

Dual Function of Mitochondrial Nm23-H4 Protein in Phosphotransfer and Intermembrane Lipid Transfer

Schlattner, U., Tokarska-Schlattner, M., Ramírez‐Ríos, S., Tyurina, Y. Y., Amoscato, A. A., Mohammadyani, D., Huang, Z., Jiang, J., Yanamala, N. V. K., Seffouh, A., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.408633 · Cited by 131 · see citing works

Cellular Senescence and Regulated Cell Death of Tubular Epithelial Cells in Diabetic Kidney Disease

Shen, S., Ji, C., & Wei, K. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.924299 · Cited by 108 · see citing works

Mitochondrial regulation of cell death: a phylogenetically conserved control

Galluzzi, L., Kepp, O., & Kroemer, G. (2016) · Microbial Cell · doi:10.15698/mic2016.03.483 · Cited by 106 · see citing works

Noncanonical Cell Fate Regulation by Bcl-2 Proteins

Chong, S. J. F., Marchi, S., Petroni, G., Kroemer, G., Galluzzi, L., & Pervaiz, S. (2020) · Trends in Cell Biology · doi:10.1016/j.tcb.2020.03.004 · Cited by 103 · see citing works

The Achilles’ heel of cancer: targeting tumors via lysosome-induced immunogenic cell death

Taritsa, I. C., Neote, K. S., & Eric, F. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04912-8 · Cited by 95 · see citing works

Functions of BCL-X L at the Interface between Cell Death and Metabolism

Michels, J., Kepp, O., Senovilla, L., Lissa, D., Castedo, M., Kroemer, G., & Galluzzi, L. (2013) · International Journal of Cell Biology · doi:10.1155/2013/705294 · Cited by 92 · see citing works

MicroRNA-34a Modulates Neural Stem Cell Differentiation by Regulating Expression of Synaptic and Autophagic Proteins

Morgado, A. L., Xavier, J. M., Dionísio, P. A., Ribeiro, M. F., Dias, R. B., Sebastião, A. M., Solá, S., & Rodrigues, C. M. P. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8794-6 · Cited by 86 · see citing works

Mitochondrial involvement in myocyte death and heart failure

Goldenthal, M. J. (2016) · Heart Failure Reviews · doi:10.1007/s10741-016-9531-1 · Cited by 71 · see citing works

Ca2+ signaling and cell death

Dhaouadi, N., Vitto, V. A. M., Pinton, P., Galluzzi, L., & Marchi, S. (2023) · Cell Calcium · doi:10.1016/j.ceca.2023.102759 · Cited by 71 · see citing works

Lipid peroxidation and apoptotic response in rat brain areas induced by long‐term administration of nandrolone: the mutual crosstalk between ROS and NF ‐ kB

Turillazzi, E., Neri, M., Cerretani, D., Cantatore, S., Frati, P., Moltoni, L., Busardò, F. P., Pomara, C., Riezzo, I., & Fineschi, V. (2016) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.12748 · Cited by 70 · see citing works

Apoptotic proteins with non-apoptotic activity: expression and function in cancer

Shoshan‐Barmatz, V., Arif, T., & Shteinfer‐Kuzmine, A. (2023) · APOPTOSIS · doi:10.1007/s10495-023-01835-3 · Cited by 70 · see citing works

The Drosophila effector caspase Dcp-1 regulates mitochondrial dynamics and autophagic flux via SesB

DeVorkin, L., Go, N. E., Hou, Y. C., Moradian, A., Morin, G. B., & Gorski, S. M. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201303144 · Cited by 66 · see citing works

BCL-xL inhibition potentiates cancer therapies by redirecting the outcome of p53 activation from senescence to apoptosis

Bharti, V., Watkins, R., Kumar, A., Shattuck-Brandt, R. L., Mossing, A., Mittra, A., Shen, C., Tsung, A., Davies, A. E., Hanel, W. G., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111826 · Cited by 57 · see citing works

Mitochondrial VDAC1 Silencing Leads to Metabolic Rewiring and the Reprogramming of Tumour Cells into Advanced Differentiated States

Arif, T., Paul, A., Krelin, Y., Shteinfer‐Kuzmine, A., & Shoshan‐Barmatz, V. (2018) · Cancers · doi:10.3390/cancers10120499 · Cited by 55 · see citing works

Necrosis, and then stress induced necrosis-like cell death, but not apoptosis, should be the preferred cell death mode for chemotherapy: clearance of a few misconceptions

Zhang, J., Lou, X., Jin, L., Zhou, R., Liu, S., Xu, N., & Liao, D. J. (2014) · Oncoscience · doi:10.18632/oncoscience.61 · Cited by 53 · see citing works

Natural Polyphenols and Apoptosis Induction in Cancer Therapy

Estrela, L. R. M. (2013) · Journal of Carcinogenesis & Mutagenesis · doi:10.4172/2157-2518.s6-004 · Cited by 50 · see citing works

Targeting Malignant Mitochondria With Therapeutic Peptides

Constance, J. E., & Lim, C. S. (2012) · Therapeutic Delivery · doi:10.4155/tde.12.75 · Cited by 47 · see citing works

Analysis of Expression, Cellular Localization, and Function of Three Inhibitors of Apoptosis (IAPs) from Litopenaeus vannamei during WSSV Infection and in Regulation of Antimicrobial Peptide Genes (AMPs)

Wang, P., Wan, D.-H., Gu, Z.-H., Qiu, W., Chen, Y.-G., Weng, S., Yu, X., & He, J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0072592 · Cited by 47 · see citing works

Mitochondrial Translocation of p53 Modulates Neuronal Fate by Preventing Differentiation-Induced Mitochondrial Stress

Xavier, J. M., Morgado, A. L., Solá, S., & Rodrigues, C. M. P. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5417 · Cited by 45 · see citing works

Acetylcholinesterase promotes apoptosis in insect neurons

Knorr, D. Y., Georges, N. S., Pauls, S., & Heinrich, R. (2020) · APOPTOSIS · doi:10.1007/s10495-020-01630-4 · Cited by 45 · see citing works

IGF-1 modulates gene expression of proteins involved in inflammation, cytoskeleton, and liver architecture

Díaz, V. J. L., Castilla‐Cortázar, I., Martín‐Estal, I., García‐Magariño, M., Aguirre, G. A., Puche, J., de la Garza, R. G., Morales, L., & Muñoz, Ú. (2017) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-016-0545-x · Cited by 44 · see citing works

Apoptotic regulators promote cytokinetic midbody degradation in C. elegans

Chai, Y., Tian, D., Yang, Y., Feng, G., Cheng, Z., Li, W., & Ou, G. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201209050 · Cited by 41 · see citing works

Hippocampal cell fate regulation by chronic cocaine during periods of adolescent vulnerability: Consequences of cocaine exposure during adolescence on behavioral despair in adulthood

García‐Cabrerizo, R., Keller, B., & García-Fuster, M. J. (2015) · Neuroscience · doi:10.1016/j.neuroscience.2015.07.040 · Cited by 41 · see citing works

Caspase-3 and RasGAP: a stress-sensing survival/demise switch

Khalil, H., Bertrand, M. J. M., Vandenabeele, P., & Widmann, C. (2013) · Trends in Cell Biology · doi:10.1016/j.tcb.2013.08.002 · Cited by 40 · see citing works

Can the interplay between autophagy and apoptosis be targeted as a novel therapy for Parkinson's disease?

Bekker, M., Abrahams, S., Loos, B., & Bardien, S. (2020) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2020.12.013 · Cited by 40 · see citing works

Caspase-3–dependent cleavage of Bcl-xL in the stroma exosomes is required for their uptake by hematological malignant cells

Vardaki, I., Sanchez, C., Fonseca, P., Olsson, M., Chioureas, D., Rassidakis, G. Z., Ullén, A., Zhivotovsky, B., Björkholm, M., & Panaretakis, T. (2016) · Blood · doi:10.1182/blood-2016-05-715961 · Cited by 39 · see citing works

Cyclin B/CDK1 and Cyclin A/CDK2 phosphorylate DENR to promote mitotic protein translation and faithful cell division

von Hohenberg, K. C., Müller, S., Schleich, S., Meister, M. F., Bohlen, J., Hofmann, T. G., & Teleman, A. A. (2022) · Nature Communications · doi:10.1038/s41467-022-28265-0 · Cited by 37 · see citing works

Lithocholic bile acid accumulated in yeast mitochondria orchestrates a development of an anti-aging cellular pattern by causing age-related changes in cellular proteome

Beach, A., Richard, V. R., Bourque, S. D., Boukh‐Viner, T., Kyryakov, P., Gomez-Perez, A., Arlia‐Ciommo, A., Feldman, R., Leonov, A., Piano, A., et al. (2015) · Cell Cycle · doi:10.1080/15384101.2015.1026493 · Cited by 38 · see citing works

FADD adaptor and PEA-15/ERK1/2 partners in major depression and schizophrenia postmortem brains: Basal contents and effects of psychotropic treatments

García-Fuster, M. J., Dı́ez-Alarcia, R., Ferrer‐Alcón, M., Harpe, R. L., Meana, J. J., & García-Sevilla, J. A. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.07.027 · Cited by 34 · see citing works

Inhibition of neuronal necroptosis mediated by RIP1/RIP3/MLKL provides neuroprotective effects on kaolin‐induced hydrocephalus in mice

Liu, C., Chen, Y., Cui, W., Cao, Y. L., Zhao, L., Wang, H., Liu, X., Fan, S., Huang, K., Tong, A., et al. (2021) · Cell Proliferation · doi:10.1111/cpr.13108 · Cited by 35 · see citing works

Reducing VDAC1 expression induces a non-apoptotic role for pro-apoptotic proteins in cancer cell differentiation

Arif, T., Krelin, Y., & Shoshan‐Barmatz, V. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.04.005 · Cited by 35 · see citing works

Mechanisms by Which Different Functional States of Mitochondria Define Yeast Longevity

Beach, A., Leonov, A., Arlia‐Ciommo, A., Svistkova, V., Lutchman, V., & Titorenko, V. I. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms16035528 · Cited by 32 · see citing works

Caspase‐7 participates in differentiation of cells forming dental hard tissues

Matalová, E., Lesot, H., Švandová, E., Berghe, T. V., Sharpe, P. T., Healy, C., Vandenabeele, P., & Tucker, A. S. (2013) · Development Growth & Differentiation · doi:10.1111/dgd.12066 · Cited by 31 · see citing works

Mitochondria and nucleus cross‐talk: Signaling in metabolism, apoptosis, and differentiation, and function in cancer

Shteinfer‐Kuzmine, A., Verma, A., Arif, T., Aizenberg, O., Paul, A., & Shoshan‐Barmatz, V. (2020) · IUBMB Life · doi:10.1002/iub.2407 · Cited by 31 · see citing works

The pro-apoptotic BAX protein influences cell growth and differentiation from the nucleus in healthy interphasic cells

Brayer, S., Joannes, A., Jaillet, M., Gregianin, E., Mahmoudi, S., Marchal-Sommé, J., Fabre, A., Mordant, P., Cazes, A., Crestani, B., et al. (2017) · Cell Cycle · doi:10.1080/15384101.2017.1371882 · Cited by 30 · see citing works

Possible Contribution of Proteins of Bcl-2 Family in Neuronal Death Following Transient Global Brain Ischemia

Pilchová, I., Klacanova, K., Chomová, M., Tatarková, Z., Dobrota, D., & Račay, P. (2014) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-014-0104-3 · Cited by 27 · see citing works

Driving Apoptosis-relevant Proteins Toward Neural Differentiation

Solá, S., Aranha, M. M., & Rodrigues, C. M. P. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8289-2 · Cited by 25 · see citing works

Cell death proteins: An evolutionary role in cellular adaptation before the advent of apoptosis

Dick, S. A., & Megeney, L. A. (2013) · BioEssays · doi:10.1002/bies.201300052 · Cited by 25 · see citing works

Augmented generation of protein fragments during wakefulness as the molecular cause of sleep: a hypothesis

Varshavsky, A. J. (2012) · Protein Science · doi:10.1002/pro.2148 · Cited by 24 · see citing works

Chronic MDMA induces neurochemical changes in the hippocampus of adolescent and young adult rats: Down-regulation of apoptotic markers

García‐Cabrerizo, R., & García-Fuster, M. J. (2015) · NeuroToxicology · doi:10.1016/j.neuro.2015.06.001 · Cited by 24 · see citing works

Insufficient Apaf-1 expression in early stages of neural differentiation of human embryonic stem cells might protect them from apoptosis

Karimzadeh, S., Hosseinkhani, S., Fathi, A., Ataei, F., & Baharvand, H. (2018) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2018.01.005 · Cited by 22 · see citing works

Oxidative Stress and Pulmonary Fibrosis

Manni, M. L., & Oury, T. D. (2014) · Springer eBooks · doi:10.1007/978-3-642-30018-9_122 · Cited by 22 · see citing works

Novel insights into the mitochondrial permeability transition

Bonora, M., Pedro, J. M. B., Kroemer, G., Galluzzi, L., & Pinton, P. (2014) · Cell Cycle · doi:10.4161/15384101.2014.949082 · Cited by 22 · see citing works

Rewiring of Cancer Cell Metabolism by Mitochondrial VDAC1 Depletion Results in Time-Dependent Tumor Reprogramming: Glioblastoma as a Proof of Concept

Arif, T., Stern, O., Pittala, S., Caspi, V. C., & Shoshan‐Barmatz, V. (2019) · Cells · doi:10.3390/cells8111330 · Cited by 22 · see citing works

Acetylation of NDPK-D Regulates Its Subcellular Localization and Cell Survival

Fujita, Y., Fujiwara, K., Zenitani, S., & Yamashita, T. (2015) · PLoS ONE · doi:10.1371/journal.pone.0139616 · Cited by 21 · see citing works

Drugging cancer metabolism: Expectations vs. reality

Montrose, D. C., & Galluzzi, L. (2019) · International review of cytology · doi:10.1016/bs.ircmb.2019.07.007 · Cited by 21 · see citing works

Cell death classification: A new insight based on molecular mechanisms

Dehghan, S., Kheshtchin, N., Hassannezhad, S., & Soleimani, M. (2023) · Experimental Cell Research · doi:10.1016/j.yexcr.2023.113860 · Cited by 18 · see citing works

Apoptosis in Living Animals Is Assisted by Scavenger Cells and Thus May Not Mainly Go through the Cytochrome C-Caspase Pathway

Liu, B., Xu, N., Man, Y., Shen, H., Avital, I., Stojadinovic, A., & Liao, D. J. (2013) · Journal of Cancer · doi:10.7150/jca.7577 · Cited by 16 · see citing works

The neuroplastic index p-FADD/FADD and phosphoprotein PEA-15, interacting at GABAA receptor, are upregulated in brain cortex during midazolam-induced hypnosis in mice

Álvaro-Bartolomé, M., & Garcı́a-Sevilla, J. A. (2015) · European Neuropsychopharmacology · doi:10.1016/j.euroneuro.2015.07.019 · Cited by 15 · see citing works

When Death Was Young: An Ancestral Apoptotic Network in Bacteria

Carmona‐Gutiérrez, D., Kroemer, G., & Madeo, F. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.05.032 · Cited by 15 · see citing works

Differential regulation of the apoptotic machinery during megakaryocyte differentiation and platelet production by inhibitor of apoptosis protein Livin

Elrahman, I. A., Deutsch, V., Pick, M., Kay, S., Neuman, T., Perlman, R., & Ben‐Yehuda, D. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.454 · Cited by 13 · see citing works

Caspases and osteogenic markers—in vitro screening of inhibition impact

Adamová, E., Janečková, E., Klepárnı́k, K., & Matalová, E. (2015) · In Vitro Cellular & Developmental Biology - Animal · doi:10.1007/s11626-015-9964-1 · Cited by 12 · see citing works

Osteogenic Potential of Caspases Related to Endochondral Ossification

Janečková, E., Bíliková, P., & Matalová, E. (2017) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155417739283 · Cited by 11 · see citing works

Output Regulation and Function Optimization of Mitochondria in Eukaryotes

Zeng, M., He, Y. T., Du, H., Yang, J., & Wan, H. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.598112 · Cited by 10 · see citing works

Shen-Yuan-Dan Capsule Attenuates Verapamil-Induced Zebrafish Heart Failure and Exerts Antiapoptotic and Anti-Inflammatory Effects via Reactive Oxygen Species–Induced NF-κB Pathway

Li, X., Liu, H., Li, Y., Qin, X., Li, M., Shang, J., Xing, W., Gong, Y., Liu, W., & Zhou, M. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.626515 · Cited by 10 · see citing works

Development and characterization of pH-sensitive zerumbone-encapsulated liposomes for lung fibrosis via inhalation route

Elsayed, N., How, C. W., & Foo, J. B. (2024) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2024.114599 · Cited by 9 · see citing works

Domesticated and optimized mitochondria: Mitochondrial modifications based on energetic status and cellular stress

Zeng, M., He, Y. T., Zhou, H., Du, H., Shao, C., Yang, J., & Wan, H. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.118766 · Cited by 9 · see citing works

Reversion of Pneumolysin-Induced Executioner Caspase Activation Redirects Cells to Survival

Nerlich, A. G., Teruel, I. V. W.-R., Mieth, M., Hönzke, K., Rückert, J. C., Mitchell, T. J., Suttorp, N., Hippenstiel, S., & Hocke, A. C. (2020) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiaa639 · Cited by 8 · see citing works

Increased expression of the proapoptotic presenilin associated protein is involved in neuronal tangle formation in human brain

Yang, C. G., Sun, Z.-P., Jiang, J., Cai, X.-L., Wang, Y., Wang, H., Che, C., Tu, E., Pan, A., Zhang, Y., et al. (2024) · Scientific Reports · doi:10.1038/s41598-024-77026-0 · Cited by 7 · see citing works

Caspase-9 has a nonapoptotic function in Xenopus embryonic primitive blood formation

Tran, H. T., Fransen, M., Dimitrakopoulou, D., Imschoot, G. V., Willemarck, N., & Vleminckx, K. (2017) · Journal of Cell Science · doi:10.1242/jcs.186411 · Cited by 7 · see citing works

Autophagy Promotes Survival of CHP-212 Neuroblastoma Cells Treated With Casiopeínas®

Vázquez-Aguirre, A., Gutiérrez, A. G., Moreno‐Esparza, R., Lemus, E. H., Ruíz-Azuara, L., & Mejía, C. (2019) · Anticancer Research · doi:10.21873/anticanres.13517 · Cited by 7 · see citing works

Metabolism and Cancer: Old and New Players

Cerella, C., Michiels, C., Dashwood, R. H., Surh, Y., & Diederich, M. F. (2013) · International Journal of Cell Biology · doi:10.1155/2013/293201 · Cited by 6 · see citing works

Role of polymorphisms in BCL-2 and BAX genes in modulating the risk of developing non-Hodgkin lymphoma

Wang, W., Tao, Y.-P., Han, X., Li, X., Zi, Y., Yang, C., & Li, J. (2013) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.3109/10428194.2013.842992 · Cited by 6 · see citing works

Detection of Apoptotic Versus Autophagic Cell Death by Flow Cytometry

Sica, V., Maiuri, M. C., Kroemer, G., & Galluzzi, L. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-3581-9_1 · Cited by 6 · see citing works

Modulation of Apoptosis in Colon Cancer Cells by Bioactive Compounds

Bostan, M., Mihaila, M. A., Hotnog, C. M., Bleoţu, C., Anton, G., Roman, V., & Braşoveanu, L. I. (2016) · InTech eBooks · doi:10.5772/63382 · Cited by 6 · see citing works

Non-Apoptotic Caspase Activity Preferentially Targets a Novel Consensus Sequence Associated With Cytoskeletal Proteins in the Developing Auditory Brainstem

Weghorst, F., Mirzakhanyan, Y., Hernandez, K. L., Gershon, P. D., & Cramer, K. S. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.844844 · Cited by 5 · see citing works

Preface

Galluzzi, L., & Kroemer, G. (2014) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-416618-9.10000-7 · Cited by 5 · see citing works

Programmed cell death of keratinocytes: an active driver in psoriasis

Yuwen, T., Tian, J., Chen, Y., Zhou, Z., Lian, N., & Chen, X. (2026) · APOPTOSIS · doi:10.1007/s10495-025-02207-9 · Cited by 4 · see citing works

Effects of sulfated and non-sulfated β-glucan extracted from Agaricus brasiliensis in breast adenocarcinoma cells – MCF-7

Baranoski, A., de Oliveira, M. T., Semprebon, S. C., Niwa, A. M., Ribeiro, L. R., & Mantovani, M. S. (2015) · Toxicology Mechanisms and Methods · doi:10.3109/15376516.2015.1043762 · Cited by 4 · see citing works

Preface

Galluzzi, L., & Kroemer, G. (2014) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-801329-8.10000-5 · Cited by 4 · see citing works

Expression and significance of quantum dots in RAW 264.7 macrophages

Li, C., Zhang, P., Hao, Y., He, D., Shen, Y., & Lu, R. (2018) · Oncology Letters · doi:10.3892/ol.2018.9362 · Cited by 3 · see citing works

Cellular and Molecular Mechanisms of Tumor Promotion

Bode, A. M., & Zhang, T. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-95488-4.00059-0 · Cited by 3 · see citing works

Ars moriendi: Proteases as sculptors of cellular suicide

Heib, M., Weiß, J., Saggau, C., Hoyer, J., Chico, J. F., Voigt, S., & Adam, D. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2021.119191 · Cited by 2 · see citing works

Epigenetics of mitochondrial and inflammation in cardiac fibrosis

He, H., Lin, L.-C., Liu, Z., Liu, P., Mao, S., Cao, W., Zhao, J., & Tao, H. (2025) · Cellular Signalling · doi:10.1016/j.cellsig.2025.112133 · Cited by 1 · see citing works

Mitochondrial Dysfunction in Stem Cell Aging

Meiliana, A., Dewi, N. M., & Wijaya, A. (2015) · The Indonesian Biomedical Journal · doi:10.18585/inabj.v7i1.18

InnovativeIn VitroModels for the Study of Lung Diseases

Picchio, V., Cammisotto, V., Pagano, F., Carnevale, R., & Chimenti, I. (2021) · IntechOpen eBooks · doi:10.5772/intechopen.95300 · Cited by 1 · see citing works

Mitochondria in Cell Death Regulation

Vitale, I., Manic, G., Kroemer, G., & Galluzzi, L. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-394447-4.30046-3 · Cited by 1 · see citing works

Investigating the role of apoptosis regulator EndoG on exogenous DNA uptake, stability, replication and recombination

Misic, V. (2013) · Brock University Digital Repository (Brock University) · Cited by 1 · see citing works

Papel da expressão celular e extracelular do Par-4 na formação tumoral e sensibilidade a droga

Filho, L. A. D. O. (2017) · doi:10.11606/t.5.2017.tde-07082017-082945

Apoptotic proteins with non-apoptotic activity: expression and function in cancer

Shoshan‐Barmatz, V., Arif, T., & Shteinfer‐Kuzmine, A. (2023) · APOPTOSIS · doi:10.1007/s10495-023-01835-3 · Cited by 70 · see citing works

Double agents of cell death: novel emerging functions of apoptotic regulators

Lamb, H. M. (2020) · FEBS Journal · doi:10.1111/febs.15308 · Cited by 22 · see citing works

Expansion and evolution of cell death programmes

Degterev, A., & Yuan, J. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2393 · Cited by 548 · see citing works

Non-apoptotic functions of BCL-2 family proteins

Gross, A., & Katz, S. G. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.22 · Cited by 195 · see citing works

Non‐lethal message from the Holy Land: The first international conference on nonapoptotic roles of apoptotic proteins

Arama, E., Baena-López, L. A., & Fearnhead, H. O. (2020) · FEBS Journal · doi:10.1111/febs.15547 · Cited by 12 · see citing works