The mitochondrial pathways of apoptosis
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Apoptosis is a process of programmed cell death that serves as a major mechanism for the precise regulation of cell numbers, and as a defense mechanism to remove unwanted and potentially dangerous cells. Studies in nematode, Drosophila and mammals have shown that, although regulation of the cell death machinery is somehow different from one species to another, it is controlled by homologous proteins and involves mitochondria. In mammals, activation of caspases (cysteine proteases that are the main executioners of apoptosis) is under the tight control of the Bcl-2 family proteins, named in reference to the first discovered mammalian cell death regulator. These proteins mainly act by regulating the release of caspases activators from mitochondria. Although for a long time the absence of mitochondrial changes was considered as a hallmark of apoptosis, mitochondria appear today as the central executioner of apoptosis. In this chapter, we present the current view on the mitochondrial pathway of apoptosis with a particular attention to new aspects of the regulation of the Bcl-2 proteins family control of mitochondrial membrane permeabilization: the mechanisms implicated in their mitochondrial targeting and activation during apoptosis, the function(s) of the oncosuppressive protein p53 at the mitochondria and the role of the processes of mitochondrial fusion and fission.
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The major players of the apoptotic pathway are largely conserved between mammals and Drosophila and C. elegans.
“The details of the apoptotic pathway differ between mammals and the model organisms Drosophila and C. elegans, however the major players are largely conserved (Figure 1).”
From Programmed cell death in aging (2015) · cites this paper as Estaquier et al., 2012
Cites
Apoptosis: A Basic Biological Phenomenon with Wideranging Implications in Tissue Kinetics
Kerr, J. F. R., Wyllie, A. H., & Currie, A. R. (1972) · British Journal of Cancer · doi:10.1038/bjc.1972.33 · Cited by 15,673 · see citing works
Induction of Apoptotic Program in Cell-Free Extracts: Requirement for dATP and Cytochrome c
Liu, X., Kim, C. N., Yang, J., Jemmerson, R., & Wang, X. (1996) · Cell · doi:10.1016/s0092-8674(00)80085-9 · Cited by 5,167 · see citing works
Prevention of Apoptosis by Bcl-2: Release of Cytochrome c from Mitochondria Blocked
Yang, J., Liu, X., Bhalla, K. N., Kim, C. N., Ibrado, A. M., Cai, J., Peng, T.-I., Jones, D. P., & Wang, X. (1997) · Science · doi:10.1126/science.275.5303.1129 · Cited by 4,913 · see citing works
The Release of Cytochrome c from Mitochondria: A Primary Site for Bcl-2 Regulation of Apoptosis
Kluck, R. M., Bossy‐Wetzel, E., Green, D. R., & Newmeyer, D. D. (1997) · Science · doi:10.1126/science.275.5303.1132 · Cited by 4,715 · see citing works
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
Cleavage of BID by Caspase 8 Mediates the Mitochondrial Damage in the Fas Pathway of Apoptosis
Li, H., Zhu, H., Xu, C.-J., & Yuan, J. (1998) · Cell · doi:10.1016/s0092-8674(00)81590-1 · Cited by 4,445 · see citing works
Tumor suppressor p53 is a direct transcriptional activator of the human bax gene
Toshiyuki, M., & Reed, J. C. (1995) · Cell · doi:10.1016/0092-8674(95)90412-3 · Cited by 4,063 · see citing works
Luo, X., Budihardjo, I., Zou, H., Slaughter, C., & Wang, X. (1998) · Cell · doi:10.1016/s0092-8674(00)81589-5 · Cited by 3,626 · 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
Du, C., Fang, M., Li, Y., Li, L., & Wang, X. (2000) · Cell · doi:10.1016/s0092-8674(00)00008-8 · Cited by 3,513 · see citing works
Chen, H., Detmer, S. A., Ewald, A. J., Griffin, E. E., Fraser, S. E., & Chan, D. C. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200211046 · Cited by 2,601 · see citing works
Verhagen, A. M., Ekert, P. G., Pakusch, M., Silke, J., Connolly, L. M., Reid, G. E., Moritz, R. L., Simpson, R. J., & Vaux, D. L. (2000) · Cell · doi:10.1016/s0092-8674(00)00009-x · Cited by 2,372 · see citing works
Vousden, K. H., & Lane, D. P. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2147 · Cited by 2,274 · see citing works
Noxa, a BH3-Only Member of the Bcl-2 Family and Candidate Mediator of p53-Induced Apoptosis
Oda, E., Ohki, R., Murasawa, H., Nemoto, J., Shibue, T., Yamashita, T., Tokino, T., Taniguchi, T., & Tanaka, †. N. (2000) · Science · doi:10.1126/science.288.5468.1053 · Cited by 2,112 · see citing works
Direct 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 · cited 4× · see citing works
“Parl is localized in the inner mitochondrial membrane, with the N-terminus exposed to the matrix and the C-terminus to the IMS (Jeyaraju et al., 2006).”
InfluentialThe Role of Mitochondria in Apoptosis
Wang, C., & Youle, R. J. (2009) · Annual Review of Genetics · doi:10.1146/annurev-genet-102108-134850 · Cited by 1,987 · see citing works
Dynamin-related Protein Drp1 Is Required for Mitochondrial Division in Mammalian Cells
Smirnova, E., Griparić, L., Shurland, D., & van der Bliek, A. M. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.8.2245 · Cited by 1,938 · see citing works
Mitochondria as the central control point of apoptosis
Desagher, S., & Martinou, J. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01803-1 · Cited by 1,915 · see citing works
Programmed Cell Death in Animal Development and Disease
Fuchs, Y., & Steller, H. (2011) · Cell · doi:10.1016/j.cell.2011.10.033 · Cited by 1,915 · see citing works
Genetic control of programmed cell death in the nematode C. elegans
Ellis, H. (1986) · Cell · doi:10.1016/0092-8674(86)90004-8 · Cited by 1,828 · see citing works
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
The Role of Dynamin-Related Protein 1, a Mediator of Mitochondrial Fission, in Apoptosis
Frank, S., Gaume, B., Bergmann-Leitner, E. S., Leitner, W. W., Robert, E. G., Catez, F., Smith, C. L., & Youle, R. J. (2001) · Developmental Cell · doi:10.1016/s1534-5807(01)00055-7 · Cited by 1,755 · see citing works
Developmental cell death: morphological diversity and multiple mechanisms
Clarke, P. H. (1990) · Anatomy and Embryology · doi:10.1007/bf00174615 · Cited by 1,695 · see citing works
OPA1 Controls Apoptotic Cristae Remodeling Independently from Mitochondrial Fusion
Frezza, C., Cipolat, S., Martins de Brito, O., Micaroni, M., Beznoussenko, G. V., Rudka, T., Bartoli, D., Polishuck, R. S., Danial, N. N., De Strooper, B., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.025 · Cited by 1,673 · see citing works
A novel form of Epstein-Barr virus latency in normal B cells in vivo
Miyashita, E. M., Yang, B., Lam, K. M. C., Crawford, D., & Thorley‐Lawson, D. A. (1995) · Cell · doi:10.1016/0092-8674(95)90513-8 · Cited by 1,591 · see citing works
Bid, Bax, and Lipids Cooperate to Form Supramolecular Openings in the Outer Mitochondrial Membrane
Kuwana, T., Mackey, M. R., Perkins, G. A., Ellisman, M. H., Latterich, M., Schneiter, R., Green, D. R., & Newmeyer, D. D. (2002) · Cell · doi:10.1016/s0092-8674(02)01036-x · Cited by 1,480 · see citing works
Delettre, C., Lenaers, G., Griffoin, J.-M., Gigarel, N., Lorenzo, C., Belenguer, P., Pelloquin, L., Grosgeorge, J., Turc-Carel, C., Perret, E., et al. (2000) · Nature Genetics · doi:10.1038/79936 · Cited by 1,446 · see citing works
Chipuk, J. E., Moldoveanu, T., Llambi, F., Parsons, M. J., & Green, D. R. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.01.025 · Cited by 1,432 · see citing works
Fridman, J. S., & Lowe, S. W. (2003) · Oncogene · doi:10.1038/sj.onc.1207116 · Cited by 1,401 · 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
Alexander, C., Votruba, M., Pesch, U. E. A., Thiselton, D. L., Mayer, S., Moore, A., Rodriguez, M., Kellner, U., Leo-Kottler, B., Auburger, G., et al. (2000) · Nature Genetics · doi:10.1038/79944 · Cited by 1,330 · see citing works
OPA1 requires mitofusin 1 to promote mitochondrial fusion
Cipolat, S., de Brito, O. M., Dal Zilio, B., & Scorrano, L. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407043101 · Cited by 1,300 · see citing works
Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission.
Taguchi, N., Ishihara, N., Jofuku, A., Oka, T., & Mihara, K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607279200 · Cited by 1,226 · see citing works
Curli biogenesis and function.
Barnhart, M. M., & Chapman, M. (2006) · Annual Review of Microbiology · doi:10.1146/annurev.micro.60.080805.142106 · Cited by 1,223 · see citing works
Bcl-2 initiates a new category of oncogenes: regulators of cell death.
Korsmeyer, S. (1992) · Blood · doi:10.1182/blood.v80.4.879.bloodjournal804879 · Cited by 1,210 · see citing works
Cassidy-Stone, A., Chipuk, J. E., Ingerman, E., Song, C., Yoo, C., Kuwana, T., Kurth, M. J., Shaw, J. T., Hinshaw, J. E., Green, D. R., et al. (2008) · Developmental Cell · doi:10.1016/j.devcel.2007.11.019 · Cited by 1,200 · see citing works
Olichon, A., Baricault, L., Gas, N., Guillou, E., Valette, A., Belenguer, P., & Lenaers, G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200677200 · Cited by 1,168 · see citing works
Hengartner, M. O., & Horvitz, H. R. (1994) · Cell · doi:10.1016/0092-8674(94)90506-1 · Cited by 1,167 · see citing works
Zamzami, N., Marchetti, P., Castedo, M., Zanin, C., Vayssière, J. L., Petit, P. X., & Kroemer, G. (1995) · The Journal of experimental medicine · doi:10.1084/jem.181.5.1661 · Cited by 1,166 · see citing works
Suzuki, Y., Imai, Y., Nakayama, H., Takahashi, K., Takio, K., & Takahashi, R. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00341-0 · Cited by 1,116 · see citing works
Cytoplasmic functions of the tumour suppressor p53
Green, D. R., & Kroemer, G. (2009) · Nature · doi:10.1038/nature07986 · Cited by 1,106 · see citing works
Mitochondrial reactive oxygen species in cell death signaling
Fleury, C., Mignotte, B., & Vayssière, J. (2002) · Biochimie · doi:10.1016/s0300-9084(02)01369-x · Cited by 1,069 · see citing works
Self-citationIshihara, N., Nomura, M., Jofuku, A., Kato, H., Suzuki, S. O., Masuda, K., Otera, H., Nakanishi, Y., Nonaka, I., Goto, Y.-I., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1907 · Cited by 1,066 · see citing works
Genetic Control of Programmed Cell Death in Drosophila
White, K., Grether, M. E., Abrams, J., Young, L. M., Farrell, K., & Steller, H. (1994) · Science · doi:10.1126/science.8171319 · Cited by 1,047 · see citing works
Roles of the mammalian mitochondrial fission and fusion mediators Fis1, Drp1, and Opa1 in apoptosis
Lee, Y.-J., Jeong, S.-Y., Karbowski, M., Smith, C. L., & Youle, R. J. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-04-0294 · Cited by 1,042 · see citing works
Cribbs, J. T., & Strack, S. (2007) · EMBO Reports · doi:10.1038/sj.embor.7401062 · Cited by 1,024 · see citing works
Mitochondrial fusion protects against neurodegeneration in the cerebellum
Chen, H., McCaffery, J. M., & Chan, D. C. (2007) · Cell · doi:10.1016/j.cell.2007.06.026 · Cited by 924 · see citing works
p53 ubiquitination: Mdm2 and beyond
Brooks, C. L., & Gu, W. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.020 · Cited by 924 · see citing works
Structural Basis of Mitochondrial Tethering by Mitofusin Complexes
Koshiba, T., Detmer, S. A., Kaiser, J. T., Chen, H., McCaffery, J. M., & Chan, D. C. (2004) · Science · doi:10.1126/science.1099793 · Cited by 910 · see citing works
Death Signal-induced Localization of p53 Protein to Mitochondria
Marchenko, N. D., Zaika, A. I., & Moll, U. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.21.16202 · Cited by 902 · see citing works
Regulation of mitochondrial morphology through proteolytic cleavage of OPA1
Ishihara, N., Fujita, Y., Oka, T., & Mihara, K. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601184 · Cited by 899 · see citing works
Bcl-2 initiates a new category of oncogenes: regulators of cell death
Korsmeyer, S. J. (1992) · Blood · doi:10.1182/blood.v80.4.879.879 · Cited by 887 · see citing works
The PINK1/Parkin pathway regulates mitochondrial morphology
Poole, A. C., Thomas, R. E., Andrews, L. A., McBride, H. M., Whitworth, A. J., & Pallanck, L. J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709336105 · Cited by 885 · see citing works
VDAC2 Inhibits BAK Activation and Mitochondrial Apoptosis
Cheng, E. H.-Y., Sheiko, T. V., Fisher, J. K., Craigen, W. J., & Korsmeyer, S. J. (2003) · Science · doi:10.1126/science.1083995 · Cited by 852 · see citing works
Karbowski, M., Lee, Y.-J., Gaume, B., Jeong, S.-Y., Frank, S., Nechushtan, A., Santel, A., Fuller, M., Smith, C. L., & Youle, R. J. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200209124 · Cited by 846 · see citing works
p53-Dependent apoptosis in the absence of transcriptional activation of p53-target genes
Caelles, C., Helmberg, A., & Karin, M. (1994) · Nature · doi:10.1038/370220a0 · Cited by 843 · see citing works
mtDNA mutations increase tumorigenicity in prostate cancer
Petros, J. A., Baumann, A. K., Ruiz‐Pesini, E., Amin, M. B., Sun, C. Q., Hall, J., Lim, S.-D., Issa, M. M., Flanders, W. D., Hosseini, S. H., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408894102 · Cited by 834 · see citing works
Yoon, Y., Krueger, E. W., Oswald, B. J., & McNiven, M. A. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.15.5409-5420.2003 · Cited by 820 · see citing works
Song, Z., Chen, H., Fiket, M., Alexander, C., & Chan, D. C. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200704110 · Cited by 818 · see citing works
The dynamin-related GTPase Dnm1 regulates mitochondrial fission in yeast
Bleazard, W., McCaffery, J. M., King, E. J., Bale, S., Mozdy, A. D., Tieu, Q., Nunnari, J. M., & Shaw, J. M. (1999) · Nature Cell Biology · doi:10.1038/13014 · Cited by 795 · see citing works
Transcriptional Repression of the Anti-apoptoticsurvivin Gene by Wild Type p53
Hoffman, W. H., Biade, S., Zilfou, J. T., Chen, J., & Murphy, M. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m106643200 · Cited by 794 · see citing works
Chang, C., & Blackstone, C. D. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.c700083200 · Cited by 792 · see citing works
Mitochondrial p53 activates Bak and causes disruption of a Bak–Mcl1 complex
Leu, J. I.-J., Dumont, P., Hafey, M. J., Murphy, M. E., & George, D. L. (2004) · Nature Cell Biology · doi:10.1038/ncb1123 · Cited by 771 · see citing works
SLP‐2 is required for stress‐induced mitochondrial hyperfusion
Tondera, D., Grandemange, S., Jourdain, A. A., Karbowski, M., Mattenberger, Y., Herzig, S., Cruz, S. D., Clerc, P., Lauria, I., Merkwirth, C., et al. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.89 · Cited by 767 · see citing works
Hegde, R. P., Srinivasula, S. M., Zhang, Z., Wassell, R. P., Mukattash, R., Cilenti, L., DuBois, G. C., Lazebnik, Y. A., Zervos, A. S., Fernandes‐Alnemri, T., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109721200 · Cited by 745 · see citing works
Mitochondrial Morphology and Dynamics in Yeast and Multicellular Eukaryotes
Okamoto, K., & Shaw, J. M. (2005) · Annual Review of Genetics · doi:10.1146/annurev.genet.38.072902.093019 · Cited by 737 · see citing works
Cipolat, S., Rudka, T., Hartmann, D., Costa, V., Serneels, L., Craessaerts, K., Metzger, K., Frezza, C., Annaert, W. G., D'adamio, L., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.021 · Cited by 735 · see citing works
A Human Dynamin-related Protein Controls the Distribution of Mitochondria
Смирнова, Е. А., Shurland, D., Ryazantsev, S. N., & van der Bliek, A. M. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.2.351 · Cited by 734 · see citing works
Mitofusin 1 and 2 play distinct roles in mitochondrial fusion reactions via GTPase activity
Ishihara, N., Eura, Y., & Mihara, K. (2004) · Journal of Cell Science · doi:10.1242/jcs.01565 · Cited by 731 · see citing works
BAD and glucokinase reside in a mitochondrial complex that integrates glycolysis and apoptosis
Danial, N. N., Gramm, C. F., Scorrano, L., Zhang, C.-Y., Krauss, S., Ranger, A. M., Robert Datta, S., Greenberg, M. E., Licklider, L. J., Lowell, B. B., et al. (2003) · Nature · doi:10.1038/nature01825 · Cited by 705 · see citing works
Life and death by death receptors
Guicciardi, M. E., & Gores, G. J. (2009) · The FASEB Journal · doi:10.1096/fj.08-111005 · Cited by 689 · see citing works
Deng, H., Dodson, M. W., Huang, H., & Guo, M. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803998105 · Cited by 683 · see citing works
Legros, F., Lombès, A., Frachon, P., & Rojo, M. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-06-0330 · Cited by 676 · see citing works
C. elegans Dynamin-Related Protein DRP-1 Controls Severing of the Mitochondrial Outer Membrane
Labrousse, A. M., Zappaterra, M. D., Rube, D. A., & van der Bliek, A. M. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80391-3 · Cited by 670 · see citing works
The dynamin-related GTPase Drp1 is required for embryonic and brain development in mice
Wakabayashi, J., Zhang, Z., Wakabayashi, N., Tamura, Y., Fukaya, M., Kensler, T. W., Iijima, M., & Sesaki, H. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200903065 · Cited by 667 · see citing works
Cell death in the nervous system
Bredesen, D. E., Rao, R. V., & Mehlen, P. (2006) · Nature · doi:10.1038/nature05293 · Cited by 638 · see citing works
Majewski, N., Nogueira, V., Bhaskar, P. T., Coy, P. E., Skeen, J. E., Gottlob, K., Chandel, N. S., Thompson, C. B., Robey, R. B., & Hay, N. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.11.014 · Cited by 633 · see citing works
Mitochondria: a historical review.
Ernster, L., & Schatz, G. W. (1981) · The Journal of Cell Biology · doi:10.1083/jcb.91.3.227s · Cited by 632 · see citing works
Role of Bax and Bak in mitochondrial morphogenesis
Karbowski, M., Norris, K. L., Cleland, M. M., Jeong, S.-Y., & Youle, R. J. (2006) · Nature · doi:10.1038/nature05111 · Cited by 625 · see citing works
Humanin peptide suppresses apoptosis by interfering with Bax activation
Guo, B., Zhai, D., Cabezas, E., Welsh, K., Nouraini, S., Satterthwait, A. C., & Reed, J. C. (2003) · Nature · doi:10.1038/nature01627 · Cited by 619 · see citing works
bcl-2 inhibits death of central neural cells induced by multiple agents.
Zhong, L. T., Sarafian, T. A., Kane, D. J., Charles, A. C., Mah, S. P., Edwards, R. H., & Bredesen, D. E. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.10.4533 · Cited by 619 · see citing works
Mitochondrial bioenergetics and structural network organization
Benard, G., Bellance, N., James, D., Parrone, P., Fernandez, H., Letellier, T., & Rossignol, R. (2007) · Journal of Cell Science · doi:10.1242/jcs.03381 · Cited by 618 · see citing works
Developmentally Regulated Mitochondrial Fusion Mediated by a Conserved, Novel, Predicted GTPase
Hales, K. G., & Fuller, M. T. (1997) · Cell · doi:10.1016/s0092-8674(00)80319-0 · Cited by 611 · see citing works
Stepwise Activation of BAX and BAK by tBID, BIM, and PUMA Initiates Mitochondrial Apoptosis
Kim, H., Tu, H.-C., Ren, D., Takeuchi, O., Jeffers, J. R., Zambetti, G. P., Hsieh, J. J.-D., & Cheng, E. H.-Y. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.030 · Cited by 600 · see citing works
PETIT, P. X., Lecoeur, H., Zorn, E., Dauguet, C., Mignotte, B., & Gougeon, M. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.130.1.157 · Cited by 592 · see citing works
Self-citationTwo distinct mechanisms alter p53 in breast cancer: mutation and nuclear exclusion.
Moll, U. M., RIOU, G. F., & Levine, A. J. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.15.7262 · Cited by 575 · see citing works
Regulation of OPA1 processing and mitochondrial fusion by m -AAA protease isoenzymes and OMA1
Ehses, S., Lauria, I., Mancuso, G., Bernacchia, A., Geimer, S., Tondera, D., Martinou, J., Westermann, B., Rugarli, E. I., & Langer, T. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200906084 · Cited by 570 · see citing works
Prohibitins act as a membrane‐bound chaperone for the stabilization of mitochondrial proteins
Nijtmans, L. G. J., de Jong, L., Artal‐Sanz, M., Coates, P. J., BERDEN, J. A., Back, J. W., Muijsers, A. O., van der Spek, H., & Grivell, L. A. (2000) · The EMBO Journal · doi:10.1093/emboj/19.11.2444 · Cited by 553 · see citing works
Induction of apoptosis in HeLa cells by trans-activation-deficient p53.Preprint
Haupt, Y., Rowan, S., Shaulian, E., Vousden, K. H., & Oren, M. (1995) · Genes & Development · doi:10.1101/gad.9.17.2170 · Cited by 547 · see citing works
PUMA Couples the Nuclear and Cytoplasmic Proapoptotic Function of p53
Chipuk, J. E., Bouchier‐Hayes, L., Kuwana, T., Newmeyer, D. D., & Green, D. R. (2005) · Science · doi:10.1126/science.1114297 · Cited by 547 · see citing works
The Serine Protease Omi/HtrA2 Regulates Apoptosis by Binding XIAP through a Reaper-like Motif
Martins, L. M., Iaccarino, I., Tenev, T., Gschmeissner, S., Totty, N. F., Lemoine, N. R., Savopoulos, J. W., Gray, C. W., Creasy, C. L., Dingwall, C., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109784200 · Cited by 544 · see citing works
The Death Domain Superfamily in Intracellular Signaling of Apoptosis and Inflammation
Park, H. H., Lo, Y.-C., Lin, S., Wang, L., Yang, J. K., & Wu, H. (2007) · Annual Review of Immunology · doi:10.1146/annurev.immunol.25.022106.141656 · Cited by 523 · see citing works
Merkwirth, C., Dargazanli, S., Tatsuta, T., Geimer, S., Löwer, B., Wunderlich, F. T., von Kleist-Retzow, J., Waisman, A., Westermann, B., & Langer, T. (2008) · Genes & Development · doi:10.1101/gad.460708 · Cited by 519 · see citing works
Apoptosis-the molecular basis of cell death
Bowen, I. D. (1992) · Endeavour · doi:10.1016/0160-9327(92)90055-t · Cited by 519 · see citing works
Inducible proteolytic inactivation of OPA1 mediated by the OMA1 protease in mammalian cells
Head, B., Griparic, L., Amiri, M., Gandre-Babbe, S., & van der Bliek, A. M. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200906083 · Cited by 515 · see citing works
Acetylation of p53 inhibits its ubiquitination by Mdm2
Li, M., Luo, J., Brooks, C. L., & Gu, W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200578200 · Cited by 503 · see citing works
The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1 dependent mitochondrial division
Karbowski, M., Neutzner, A., & Youle, R. J. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200611064 · Cited by 474 · see citing works
Griparić, L., van der Wel, N. N., Orozco, I. J., Peters, P. J., & van der Bliek, A. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400920200 · Cited by 468 · see citing works
Regulation of the mitochondrial dynamin-like protein Opa1 by proteolytic cleavage
Griparić, L., Kanazawa, T., & van der Bliek, A. M. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200704112 · Cited by 467 · see citing works
Apoptosome: a platform for the activation of initiator caspases
Bao, Q., & Shi, Y. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402028 · Cited by 467 · see citing works
Induction of apoptosis by Drosophila reaper, hid and grim through inhibition of IAP function
Goyal, L., McCall, K., Agapite, J., Hartwieg, E. A., & Steller, H. (2000) · The EMBO Journal · doi:10.1093/emboj/19.4.589 · Cited by 465 · see citing works
Polyubiquitination of p53 by a Ubiquitin Ligase Activity of p300
Grossman, S. R., Deato, M. D. E., Brignone, C., Chan, H. M., Kung, A. L., Tagami, H., Nakatani, Y., & Livingston, D. M. (2003) · Science · doi:10.1126/science.1080386 · Cited by 454 · see citing works
Clusterin inhibits apoptosis by interacting with activated Bax
Zhang, H., Kim, J. K., Edwards, C. A., Xu, Z., Taichman, R., & Wang, C.-Y. (2005) · Nature Cell Biology · doi:10.1038/ncb1291 · Cited by 453 · see citing works
Genetic Basis of Mitochondrial Function and Morphology in Saccharomyces cerevisiae
Dimmer, K. S., Fritz, S., Fuchs, F., Messerschmitt, M., Weinbach, N., Neupert, W., & Westermann, B. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-12-0588 · Cited by 443 · see citing works
Aladjem, M. I., Spike, B. T., Rodewald, L. W., Hope, T. J., Klemm, M., Jaenisch, R., & Wahl, G. M. (1998) · Current Biology · doi:10.1016/s0960-9822(98)70061-2 · Cited by 442 · see citing works
Olichon, A., Emorine, L. J., Descoins, E., Pelloquin, L., Brichese, L., Gas, N., Guillou, E., Delettre, C., Valette, A., Hamel, C., et al. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02985-x · Cited by 430 · see citing works
Mitochondrial fission in apoptosis, neurodegeneration and aging
Bossy‐Wetzel, E., Barsoum, M. J., Godzik, A., Schwarzenbacher, R., & Lipton, S. A. (2003) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2003.10.015 · Cited by 428 · see citing works
Moll, U. M., LaQuaglia, M. P., Bénard, J., & RIOU, G. F. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.10.4407 · Cited by 426 · see citing works
CaM kinase Iα–induced phosphorylation of Drp1 regulates mitochondrial morphology
Han, X.-J., Lü, Y.-F., Li, S.-A., Kaitsuka, T., Sato, Y., Tomizawa, K., Nairn, A. C., Takei, K., Matsui, H., & Matsushita, M. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200802164 · Cited by 423 · see citing works
Wolozin, B. L., Iwasaki, K., Vito, P., Ganjei, J. K., Lacaná, E., Sunderland, T., Zhao, B., Kusiak, J. W., Wasco, W., & D'adamio, L. (1996) · Science · doi:10.1126/science.274.5293.1710 · Cited by 422 · see citing works
MARCH‐V is a novel mitofusin 2‐ and Drp1‐binding protein able to change mitochondrial morphology
Nakamura, N., Kimura, Y. N., Tokuda, M., Honda, S., & Hirose, S. (2006) · EMBO Reports · doi:10.1038/sj.embor.7400790 · Cited by 419 · see citing works
The SPFH domain-containing proteins: more than lipid raft markers
Browman, D., Hoegg, M. B., & Robbins, S. M. (2007) · Trends in Cell Biology · doi:10.1016/j.tcb.2007.06.005 · Cited by 403 · see citing works
Mutation spectrum and splicing variants in the OPA1 gene
Delettre, C., Griffoin, J., Kaplan, J., Dollfus, H., Lorenz, B., Faivre, L. O., Lenaers, G., Belenguer, P., & Hamel, C. (2001) · Human Genetics · doi:10.1007/s00439-001-0633-y · Cited by 398 · see citing works
Kluck, R. M., Martin, S. J., Hoffman, B. M., Zhou, J. S., Green, D. R., & Newmeyer, D. D. (1997) · The EMBO Journal · doi:10.1093/emboj/16.15.4639 · Cited by 383 · see citing works
Herlan, M., Vogel, F., Bornhövd, C., Neupert, W., & Reichert, A. S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211311200 · Cited by 378 · 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
Hid, Rpr and Grim negatively regulate DIAP1 levels through distinct mechanisms
Yoo, S. J., Huh, J. R., Muro, I., Yu, H., Wang, L., Wang, S. L., Feldman, R. M. R., Clem, R. J., Müller, H. ‐. J., & Hay, B. A. (2002) · Nature Cell Biology · doi:10.1038/ncb793 · Cited by 373 · see citing works
Sumo1 Conjugates Mitochondrial Substrates and Participates in Mitochondrial Fission
Harder, Z., Zunino, R., & McBride, H. M. (2004) · Current Biology · doi:10.1016/j.cub.2004.02.004 · Cited by 367 · see citing works
Erster, S. H., Mihara, M., Kim, R. H., Petrenko, O., & Moll, U. M. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.15.6728-6741.2004 · Cited by 367 · see citing works
The MDM2 RING-finger domain is required to promote p53 nuclear export
Geyer, R. K., Yu, Z. K., & Maki, C. G. (2000) · Nature Cell Biology · doi:10.1038/35023507 · Cited by 361 · see citing works
Prohibitins Regulate Membrane Protein Degradation by the m -AAA Protease in Mitochondria
Steglich, G., Neupert, W., & Langer, T. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.5.3435 · Cited by 357 · see citing works
Loo, G., van Gurp, M., Depuydt, B., Srinivasula, S. M., Rodríguez, I., Alnemri, E. S., Gevaert, K., Vandekerckhove, J. S., Declercq, W., & Vandenabeele, P. (2002) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400970 · Cited by 357 · see citing works
Nikolaev, A. Y., Li, M., Puskas, N., Qin, J., & Gu, W. J. (2003) · Cell · doi:10.1016/s0092-8674(02)01255-2 · Cited by 355 · see citing works
MAPL is a new mitochondrial SUMO E3 ligase that regulates mitochondrial fission
Braschi, E., Zunino, R., & McBride, H. M. (2009) · EMBO Reports · doi:10.1038/embor.2009.86 · Cited by 350 · see citing works
Fzo1, a Protein Involved in Mitochondrial Fusion, Inhibits Apoptosis
Sugioka, R., Shimizu, S., & Tsujimoto, Y. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408910200 · Cited by 341 · see citing works
Zanna, C., Ghelli, A. M., Porcelli, A. M., Karbowski, M., Youle, R. J., Schimpf, S., Wissinger, B., Pinti, M., Cossarizza, A., Vidoni, S., et al. (2007) · Brain · doi:10.1093/brain/awm335 · Cited by 334 · see citing works
Estaquier, J., & Arnoult, D. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402107 · Cited by 330 · see citing works
Self-citationCaspases – controlling intracellular signals by protease zymogen activation
Stennicke, H. R., & Salvesen, G. S. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(99)00281-2 · Cited by 329 · see citing works
Zhu, W., Cowie, A., Wasfy, G. W., Penn, L. Z., Leber, B. F., & Andrews, D. W. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00788.x · Cited by 327 · see citing works
Small-molecule inhibitor of p53 binding to mitochondria protects mice from gamma radiation
Strom, E., Sathe, S. S., Komarov, P. G., Chernova, O. B., Pavlovska, I., Shyshynova, I., Bosykh, D. A., Burdelya, L. G., Macklis, R. M., Skaliter, R., et al. (2006) · Nature Chemical Biology · doi:10.1038/nchembio809 · Cited by 327 · see citing works
Vayssière, J., PETIT, P. X., Risler, Y., & Mignotte, B. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.24.11752 · Cited by 311 · see citing works
Self-citationPitts, K. R., Yoon, Y., Krueger, E. W., & McNiven, M. A. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.12.4403 · Cited by 311 · see citing works
Dual role of proapoptotic BAD in insulin secretion and beta cell survival
Danial, N. N., Walensky, L. D., Zhang, C.-Y., Choi, C. S., Fisher, J. K., Molina, A. J. A., Datta, S. R., Pitter, K. L., Bird, G. H., Wikstrom, J. D., et al. (2008) · Nature Medicine · doi:10.1038/nm1717 · Cited by 307 · see citing works
Bensaad, K., & Vousden, K. H. (2007) · Trends in Cell Biology · doi:10.1016/j.tcb.2007.04.004 · Cited by 305 · see citing works
Developmental apoptosis in C. elegans: a complex CEDnario
Lettre, G., & Hengartner, M. O. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1836 · Cited by 298 · see citing works
Flotillins and the PHB Domain Protein Family: Rafts, Worms and Anaesthetics
Morrow, I. C., & Parton, R. G. (2005) · Traffic · doi:10.1111/j.1600-0854.2005.00318.x · Cited by 296 · see citing works
The DIAP1 RING finger mediates ubiquitination of Dronc and is indispensable for regulating apoptosis
Wilson, R., Goyal, L., Ditzel, M., Zachariou, A., Baker, D. A., Agapite, J., Steller, H., & Meier, P. (2002) · Nature Cell Biology · doi:10.1038/ncb799 · Cited by 296 · see citing works
Yamaguchi, R., Lartigue, L., Perkins, G. A., Scott, R. T., Dixit, A., Kushnareva, Y., Kuwana, T., Ellisman, M. H., & Newmeyer, D. D. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.07.010 · Cited by 290 · see citing works
Novel role of p53 in maintaining mitochondrial genetic stability through interaction with DNA Pol γ
Achanta, G., Sasaki, R., Li, F., Carew, J. S., Lu, W., Pelicano, H., Keating, M. J., & Huang, P. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600819 · Cited by 285 · see citing works
Shidara, Y., Yamagata, K., Kanamori, T., Nakano, K., Kwong, J. Q., Manfredi, G., Oda, H., & Ohta, S. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-2012 · Cited by 284 · see citing works
Nineteenth century research on naturally occurring cell death and related phenomena
Clarke, P. H., & Clarke, S. (1996) · Anatomy and Embryology · doi:10.1007/bf00214700 · Cited by 268 · see citing works
Arnoult, D., Grodet, A., Lee, Y.-J., Estaquier, J., & Blackstone, C. D. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505970200 · Cited by 265 · see citing works
Self-citationBax- or Bak-Induced Mitochondrial Fission Can Be Uncoupled from Cytochrome c Release
Sheridan, C., Delivani, P., Cullen, S. P., & Martin, S. J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.08.002 · Cited by 264 · see citing works
Cardiolipin acts as a mitochondrial signalling platform to launch apoptosis
Schug, Z. T., & Gottlieb, E. (2009) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2009.05.004 · Cited by 259 · see citing works
Mai, S., Klinkenberg, M., Auburger, G., Bereiter-Hahn, J., & Jendrach, M. (2010) · Journal of Cell Science · doi:10.1242/jcs.059246 · Cited by 256 · see citing works
Cartron, P., Gallenne, T., Bougras-Cartron, G., Gautier, F., Manero, F., Vusio, P., Méflah, K., Vallette, F. M., & Juin, P. P. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.10.028 · Cited by 255 · see citing works
Self-citationBAD: undertaker by night, candyman by day
Danial, N. N. (2008) · Oncogene · doi:10.1038/onc.2009.44 · Cited by 252 · see citing works
Molecular Machinery of Mitochondrial Fusion and Fission
Westermann, B. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800011200 · Cited by 251 · see citing works
Tomita, Y. A., Marchenko, N. D., Erster, S. H., Nemajerová, A., Dehner, A., Klein, C., Pan, H., Kessler, H., Pančoška, P., & Moll, U. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m507611200 · Cited by 248 · see citing works
Proteomic analysis of the mouse liver mitochondrial inner membrane
Da Cruz, S., Xenarios, I., Langridge, J., Vilbois, F., Parone, P. A., & Martinou, J.-C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304940200 · Cited by 247 · see citing works
Origin and ,evolution of organelle genomes
Gray, M. W. (1993) · Current Opinion in Genetics & Development · doi:10.1016/0959-437x(93)90009-e · Cited by 246 · see citing works
Regulation of Apoptosis and Differentiation by p53 in Human Embryonic Stem Cells
Qin, H., Yu, T., Qing, T., Liu, Y., Zhao, Y., Cai, J., Li, J., Song, Z., Qu, X., Zhou, P., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m610464200 · Cited by 244 · see citing works
ASC is a Bax adaptor and regulates the p53–Bax mitochondrial apoptosis pathway
Ohtsuka, T., Ryu, H., Minamishima, Y. A., Macip, S., Sagara, J., Nakayama, K. I., Aaronson, S. A., & Lee, S. W. (2004) · Nature Cell Biology · doi:10.1038/ncb1087 · Cited by 243 · see citing works
Arnoult, D., Rismanchi, N., Grodet, A., Roberts, R. G., Seeburg, D. P., Estaquier, J., Sheng, M., & Blackstone, C. D. (2005) · Current Biology · doi:10.1016/j.cub.2005.10.041 · Cited by 234 · see citing works
Self-citationInhibiting the Mitochondrial Fission Machinery Does Not Prevent Bax/Bak-Dependent Apoptosis
Parone, P. A., James, D. I., Cruz, S. D., Mattenberger, Y., Donzé, O., Barja, F., & Martinou, J. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.02282-05 · Cited by 231 · see citing works
BH3-only proteins and their roles in programmed cell death
Giam, M., Huang, D. C. S., & Bouillet, P. (2008) · Oncogene · doi:10.1038/onc.2009.50 · Cited by 230 · see citing works
Nuclear and mitochondrial apoptotic pathways of p53
Moll, U. M., & Zaika, A. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02284-0 · Cited by 226 · see citing works
Koonin, E. V., Makarova, K. S., Rogozin, I. B., Davidovic, L., Letellier, M.-C., & Pellegrini, L. (2003) · Genome biology · doi:10.1186/gb-2003-4-3-r19 · Cited by 226 · see citing works
The prohibitin family of mitochondrial proteins regulate replicative lifespan
Coates, P. J., Jamieson, D. J., Smart, K. A., Prescott, A. R., & Hall, P. A. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00261-2 · Cited by 212 · see citing works
Cui, M., Tang, X., Christian, W. V., Yoon, Y., & Tieu, K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.066662 · Cited by 205 · see citing works
Ugo1p Links the Fzo1p and Mgm1p GTPases for Mitochondrial Fusion
Sesaki, H., & Jensen, R. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401363200 · Cited by 198 · see citing works
Esser, K., Tursun, B., Ingenhoven, M., Michaelis, G., & Pratje, E. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)01000-8 · Cited by 196 · see citing works
Berger, K. H., & Yaffe, M. P. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.7.4043 · Cited by 196 · see citing works
Role for CED-9 and Egl-1 as Regulators of Mitochondrial Fission and Fusion Dynamics
Delivani, P., Adrain, C., Taylor, R. C., Duriez, P. J., & Martin, S. J. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.034 · Cited by 193 · see citing works
Apoptosis is triggered when prosurvival Bcl-2 proteins cannot restrain Bax
Fletcher, J. I., Meusburger, S., Hawkins, C. J., Riglar, D. T., Lee, E. F., Fairlie, W. D., Huang, D. C. S., & Adams, J. M. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808691105 · Cited by 193 · see citing works
Emerging Role for Members of the Bcl-2 Family in Mitochondrial Morphogenesis
Autret, A., & Martin, S. J. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.10.011 · Cited by 190 · see citing works
Metalloprotease‐mediated OPA1 processing is modulated by the mitochondrial membrane potential
Guillery, O., Malka, F., Landes, T., Guillou, E., Blackstone, C. D., Lombès, A., Belenguer, P., Arnoult, D., & Rojo, M. (2008) · Biology of the Cell · doi:10.1042/bc20070110 · Cited by 189 · see citing works
Borner, C., Martinou, I., Mattmann, C., Irmler, M., Schaerer, E., Martinou, J., & Tschopp, J. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.126.4.1059 · Cited by 189 · see citing works
Bid, a BH3-only multi-functional molecule, is at the cross road of life and death
Yin, X.-M. (2006) · Gene · doi:10.1016/j.gene.2005.10.038 · Cited by 187 · see citing works
Prohibitin, an antiproliferative protein, is localized to mitochondria
Ikonen, E., Fiedler, K., Parton, R. G., & Simons, K. (1995) · FEBS Letters · doi:10.1016/0014-5793(94)01444-6 · Cited by 187 · see citing works
The role of BH3-only protein Bim extends beyond inhibiting Bcl-2–like prosurvival proteins
Mérino, D., Giam, M., Hughes, P., Siggs, O. M., Heger, K., O’Reilly, L. A., Adams, J. M., Strasser, A., Lee, E. F., Fairlie, W. D., et al. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200905153 · Cited by 186 · see citing works
Mitofusin 2 Protects Cerebellar Granule Neurons against Injury-induced Cell Death
Jahani‐Asl, A., Cheung, E. C., Neuspiel, M., MacLaurin, J. G., Fortin, A., Park, D. S., McBride, H. M., & Slack, R. S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703812200 · Cited by 185 · see citing works
Xu, D., Li, Y., Arcaro, M. J., Lackey, M., & Bergmann, A. (2005) · Development · doi:10.1242/dev.01790 · Cited by 182 · see citing works
Colussi, P. A., Quinn, L. M., Huang, D. C. S., et al. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.148.4.703 · Cited by 179 · see citing works
Yoshida, Y., Izumi, H., Torigoe, T., Ishiguchi, H., Itoh, H., Kang, D., & Kohno, K. (2003) · PubMed · Cited by 177 · see citing works
Duvezin‐Caubet, S., Koppen, M., Wagener, J., Zick, M., Israel, L., Bernacchia, A., Jagasia, R., Rugarli, E. I., Imhof, A., Neupert, W., et al. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-02-0164 · Cited by 175 · see citing works
Daish, T. J., Mills, K., & Kumar, S. (2004) · Developmental Cell · doi:10.1016/j.devcel.2004.09.018 · Cited by 171 · see citing works
Muro, I., Hay, B. A., & Clem, R. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203464200 · Cited by 170 · see citing works
Lai, Z., Ferry, K. V., Diamond, M. A., Wee, K. E., Kim, Y. B., Ma, J., Yang, T., Benfield, P. A., Copeland, R. A., & Auger, K. R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011517200 · Cited by 168 · see citing works
Nguyen, M.-H., Branton, P. E., Walton, P. A., Oltvai, Z. N., Korsmeyer, S. J., & Shore, G. C. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)89417-6 · Cited by 167 · see citing works
Mitochondrial Disruption in Drosophila Apoptosis
Abdelwahid, E., Yokokura, T., Krieser, R. J., Balasundaram, S., Fowle, W. H., & White, K. (2007) · Developmental Cell · doi:10.1016/j.devcel.2007.04.004 · Cited by 165 · see citing works
The C. elegans Opa1 Homologue EAT-3 Is Essential for Resistance to Free Radicals
Kanazawa, T., Zappaterra, M., Hasegawa, A., Wright, A. P., Newman-Smith, E. D., BUTTLE, K. F., McDonald, K. L., Mannella, C. A., & van der Bliek, A. M. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.1000022 · Cited by 164 · see citing works
Mammalian initiator apoptotic caspases
Ho, P., & Hawkins, C. J. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04966.x · Cited by 163 · see citing works
Effects of OPA1 mutations on mitochondrial morphology and apoptosis: Relevance to ADOA pathogenesis
Olichon, A., Landes, T., Pelloquin, L., Emorine, L. J., Mils, V., Guichet, A., Delettre, C., Hamel, C., Amati‐Bonneau, P., Bonneau, D., et al. (2006) · Journal of Cellular Physiology · doi:10.1002/jcp.20950 · Cited by 163 · see citing works
Mechanism of intramembrane proteolysis investigated with purified rhomboid proteases
Lemberg, M. K., Menéndez, J., Misik, A., Garcia, M., Koth, C. M., & Freeman, M. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600537 · Cited by 160 · 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
Drob-1, a Drosophila member of the Bcl-2/CED-9 family that promotes cell death
Igaki, T., Kanuka, H., Inohara, N., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.2.662 · Cited by 157 · see citing works
Jiang, P., Du, W., Heese, K., et al. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01025-06 · Cited by 157 · see citing works
Bellot, G., Cartron, P., Er, E., Oliver, L., Juin, P. P., Armstrong, L. C., BORNSTEIN, P. K., Mihara, K., Manon, S., & Vallette, F. M. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402055 · Cited by 156 · see citing works
Self-citationp53 gene mutations, p53 protein accumulation and compartmentalization in colorectal adenocarcinoma.
Bòsari, S., Viale, G., Roncalli, M. G., Graziani, D. M. G., Borsani, G., Lee, A. K. C., & Coggi, G. (1995) · Europe PMC (PubMed Central) · Cited by 155 · see citing works
Käser, M., Kambacheld, M., Kisters–Woike, B., & Langer, T. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305584200 · Cited by 155 · see citing works
Molecular mechanism of Reaper-Grim-Hid-mediated suppression of DIAP1-dependent Dronc ubiquitination
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Shen, Y. H., & Shenk, T. E. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.19.8940 · Cited by 148 · see citing works
Chen, Z. X., & Pervaiz, S. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.132 · Cited by 144 · see citing works
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Gaumer, S., Guénal, I., Brun, S., et al. (2000) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400714 · Cited by 140 · see citing works
Tang, X., Zhu, Y., Han, L., Kim, A. L., Kopelovich, L., Bickers, D. R., & Athar, M. (2007) · Journal of Clinical Investigation · doi:10.1172/jci32481 · Cited by 135 · see citing works
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Deng, X., Gao, F., Flagg, T. O., Anderson, J., & May, W. S. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01647-05 · Cited by 135 · see citing works
Tan, J. Y., Zhuang, L., Leong, H. S., Iyer, N. G., Liu, E. T., & Yu, Q. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-1226 · Cited by 130 · see citing works
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Wasilewski, M., & Scorrano, L. (2009) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2009.03.007 · Cited by 129 · see citing works
Mitochondrial outer-membrane permeabilization and remodelling in apoptosis
Jourdain, A. A., & Martinou, J. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.05.001 · Cited by 127 · see citing works
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Gaziev, A. I., Abdullaev, S., & Podlutsky, A. (2014) · Biogerontology · doi:10.1007/s10522-014-9515-2 · Cited by 77 · see citing works
Wang, L., Tian, Z., Yang, Q., Li, H., Guan, H., Shi, B., Hou, P., & Ji, M. (2015) · Oncotarget · doi:10.18632/oncotarget.4542 · Cited by 69 · see citing works
Zhao, P., Li, X., Yang, Q., Lu, Y., Wang, G., Yang, H., Dong, J., & Zhang, H. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.1038802 · Cited by 43 · see citing works
Regulation of mitochondrial function by forkhead transcription factors
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Wei, C., Li, H., Wang, Y., Peng, X., Shao, H., Li, H., Bai, S., & Xu, C. (2016) · Experimental Biology and Medicine · doi:10.1177/1535370216643417 · Cited by 32 · see citing works
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- Authors
- Estaquier, J., Vallette, F., Vayssiere, J.-L., & Mignotte, B.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- École Pratique des Hautes Études (FR)
- Corresponding author
- Mignotte, Bernard
- Venue
- Advances in experimental medicine and biology
- Publisher
- Springer Netherlands
- Published
- 2011-12-22
- Volume
- 942
- Pages
- 157-183
- ISSN
- 0065-2598 (ISSN-L)
- OpenAlex
- W116732461
- Cited by
- 637
- References
- 264
- Citations by year
- 2026: 15 · 2025: 42 · 2024: 41 · 2023: 75 · 2022: 75 · 2021: 57 · 2020: 52 · 2019: 37 · 2018: 42 · 2017: 23 · 2016: 36 · 2015: 49 · 2014: 35 · 2013: 42 · 2012: 15
- FWCI
- 38.19
- Type
- book chapter
- Language
- en
- Open access
- green
- uvsq.hal.science
- Licence
- Locations
- Advances in experimental medicine and biology (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion, other-oa)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- mitochondrial apoptosis, Bcl-2 family proteins, caspase activation, mitochondrial membrane permeabilization, p53, mitochondrial fusion, mitochondrial fission, programmed cell death
- MeSH terms
- Animals, Enzyme Activation, Mitochondria, Apoptosis, Caspases
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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