Cited by 2,593Cell death mechanisms and regulationMitochondrial Function and PathologyAutophagy in Disease and Therapy

The DOI matches its Crossref record; 152 of the 152 references it cites were found in a registry or an index.

Mitochondria and cell death: outer membrane permeabilization and beyond

Tait, Stephen W. G., Green, Douglas R.·2010·Nature Reviews Molecular Cell Biology

Open this paper in CoChat — free account

Abstract

Mitochondrial outer membrane permeabilization (MOMP) is often required for activation of the caspase proteases that cause apoptotic cell death. Various intermembrane space (IMS) proteins, such as cytochrome c, promote caspase activation following their mitochondrial release. As a consequence, mitochondrial outer membrane integrity is highly controlled, primarily through interactions between pro- and anti-apoptotic members of the B cell lymphoma 2 (BCL-2) protein family. Following MOMP by pro-apoptotic BCL-2-associated X protein (BAX) or BCL-2 antagonist or killer (BAK), additional regulatory mechanisms govern the mitochondrial release of IMS proteins and caspase activity. MOMP typically leads to cell death irrespective of caspase activity by causing a progressive decline in mitochondrial function, although cells can survive this under certain circumstances, which may have pathophysiological consequences.

Integrity signals

Registry

Crossref · 10.1038/nrm2952

Cites

152 of 152 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

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
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
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 4,806
Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
Narendra, D., Tanaka, A., Suen, D.-F., & Youle, R. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200809125 · Cited by 4,026
Proapoptotic BAX and BAK: A Requisite Gateway to Mitochondrial Dysfunction and Death
Wei, M. C., Zong, W.-X., Cheng, E. H.-Y., Lindsten, T., Panoutsakopoulou, V., Ross, A. J., Roth, K. A., MacGregor, G. R., Thompson, C. B., & Korsmeyer, S. J. (2001) · Science · doi:10.1126/science.1059108 · Cited by 3,988
Core Signaling Pathways in Human Pancreatic Cancers Revealed by Global Genomic Analyses
Jones, S., Zhang, X., Parsons, D. W., Lin, J. C.-H., Leary, R. J., Angenendt, P., Mankoo, P., Carter, H., Kamiyama, H., Jimeno, A., et al. (2008) · Science · doi:10.1126/science.1164368 · Cited by 3,969
Smac, a Mitochondrial Protein that Promotes Cytochrome c–Dependent Caspase Activation by Eliminating IAP Inhibition
Du, C., Fang, M., Li, Y., Li, L., & Wang, X. (2000) · Cell · doi:10.1016/s0092-8674(00)00008-8 · Cited by 3,513
Fission and selective fusion govern mitochondrial segregation and elimination by autophagy
Twig, G., Elorza, A., Molina, A. J. A., Mohamed, H., Wikstrom, J. D., Walzer, G., Stiles, L., Haigh, S. E., Katz, S., Las, G., et al. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601963 · Cited by 3,082
Apoptosis: controlled demolition at the cellular level
Taylor, R. C., Cullen, S. P., & Martin, S. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2312 · Cited by 2,708
Identification of DIABLO, a Mammalian Protein that Promotes Apoptosis by Binding to and Antagonizing IAP Proteins
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
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
Endonuclease G is an apoptotic DNase when released from mitochondria
Li, L. Y., Luo, X., & Wang, X. (2001) · Nature · doi:10.1038/35083620 · Cited by 1,787
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
Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics
Letai, A., Bassik, M. C., Walensky, L. D., Sorcinelli, M. D., Weiler, S., & Korsmeyer, S. J. (2002) · Cancer Cell · doi:10.1016/s1535-6108(02)00127-7 · Cited by 1,677
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
Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death
Nakagawa, T., Shimizu, S., Watanabe, T., Yamaguchi, O., Otsu, K., Yamagata, H., Inohara, H., Kubo, T., & Tsujimoto, Y. (2005) · Nature · doi:10.1038/nature03317 · Cited by 1,635
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 1,513
Self-citation
Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome
Beere, H. M., Wolf, B. B., Cain, K., Mosser, D. D., Mahboubi, A., Kuwana, T., Tailor, P., Morimoto, R. I., Cohen, G. M., & Green, D. R. (2000) · Nature Cell Biology · doi:10.1038/35019501 · Cited by 1,513
Self-citation
The BCL-2 Family Reunion
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 1,476
Self-citation
X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death
Muchmore, S. W., Sattler, M., Liang, H., Meadows, R. P., Harlan, J. E., Yoon, H. S., Nettesheim, D. G., Chang, B. S., Thompson, C. B., Wong, S., et al. (1996) · Nature · doi:10.1038/381335a0 · Cited by 1,467
Differential Requirement for Caspase 9 in Apoptotic Pathways In Vivo
Hakem, R., Hakem, A., Duncan, G. S., Henderson, J. T., Woo, M., Soengas, M. S., Elia, A., de la Pompa, J. L., Kägi, D., Khoo, W., et al. (1998) · Cell · doi:10.1016/s0092-8674(00)81477-4 · Cited by 1,296
tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome cPreprint
Wei, M. C., Lindsten, T., Mootha, V. K., Weiler, S., Gross, A., Ashiya, M., Thompson, C. B., & Korsmeyer, S. J. (2000) · Genes & Development · doi:10.1101/gad.14.16.2060 · Cited by 1,292
Proapoptotic Bak is sequestered by Mcl-1 and Bcl-x L , but not Bcl-2, until displaced by BH3-only proteinsPreprint
Willis, S. N., Chen, L., Dewson, G., Wei, A. H., Naik, E., Fletcher, J. I., Adams, J. M., & Huang, D. C. S. (2005) · Genes & Development · doi:10.1101/gad.1304105 · Cited by 1,236
IAP Antagonists Induce Autoubiquitination of c-IAPs, NF-κB Activation, and TNFα-Dependent Apoptosis
Varfolomeev, E., Blankenship, J. W., Wayson, S. M., Fedorova, A. V., Kayagaki, N., Garg, P., Zobel, K., Dynek, J. N., Elliott, L. O., Wallweber, H. J. A., et al. (2007) · Cell · doi:10.1016/j.cell.2007.10.030 · Cited by 1,218
Bid Induces the Oligomerization and Insertion of Bax into the Outer Mitochondrial Membrane
Eskes, R., Desagher, S., Antonsson, B. E., & Martinou, J. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.3.929-935.2000 · Cited by 1,212
Chemical Inhibition of the Mitochondrial Division Dynamin Reveals Its Role in Bax/Bak-Dependent Mitochondrial Outer Membrane Permeabilization
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
Self-citation
A Serine Protease, HtrA2, Is Released from the Mitochondria and Interacts with XIAP, Inducing Cell Death
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 1,140
Apaf1 Is Required for Mitochondrial Pathways of Apoptosis and Brain Development
Yoshida, H., Kong, Y., Yoshida, R., Elia, A., Hakem, A., Hakem, R., Penninger, J. M., & Mak, T. W. (1998) · Cell · doi:10.1016/s0092-8674(00)81733-x · Cited by 1,138
Cytosol-to-membrane redistribution of Bax and Bcl-X L during apoptosis
Hsu, Y., Wolter, K. G., & Youle, R. J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.8.3668 · Cited by 1,134
Conversion of Bcl-2 to a Bax-like Death Effector by Caspases
Cheng, E. H. Y., Kirsch, D. G., Clem, R. J., Ravi, R. K., Kastan, M. B., Bedi, A., Ueno, K., & Hardwick, J. M. (1997) · Science · doi:10.1126/science.278.5345.1966 · Cited by 1,106
Structure of Bax
Suzuki, M., Youle, R. J., & Tjandra, N. (2000) · Cell · doi:10.1016/s0092-8674(00)00167-7 · Cited by 1,104
IAP Antagonists Target cIAP1 to Induce TNFα-Dependent Apoptosis
Vince, J. E., Wong, W. W.-L., Khan, N. R., Feltham, R., Chau, D., Ahmed, A. U., Benetatos, C. A., Chunduru, S. K., Condon, S. M., McKinlay, M. A., et al. (2007) · Cell · doi:10.1016/j.cell.2007.10.037 · Cited by 1,076
The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant
Goldstein, J. C., Waterhouse, N. J., Juin, P. P., Evan, G. I., & Green, D. R. (2000) · Nature Cell Biology · doi:10.1038/35004029 · Cited by 1,073
Self-citation
A Distinct Pathway Remodels Mitochondrial Cristae and Mobilizes Cytochrome c during Apoptosis
Scorrano, L., Ashiya, M., Buttle, K., Weiler, S., Oakes, S. A., Mannella, C. A., & Korsmeyer, S. J. (2002) · Developmental Cell · doi:10.1016/s1534-5807(01)00116-2 · Cited by 1,072
Mitochondrial fission factor Drp1 is essential for embryonic development and synapse formation in mice
Ishihara, 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
Inhibition of Bax Channel-Forming Activity by Bcl-2
Antonsson, B. E., Conti, F., Ciavatta, A., Montessuit, S., Lewis, S., Martinou, I., Bernasconi, L., Bernard, A., Mermod, J., Mazzei, G. J., et al. (1997) · Science · doi:10.1126/science.277.5324.370 · Cited by 1,028
Bid-deficient mice are resistant to Fas-induced hepatocellular apoptosis
Yin, X.-M., Wang, K., Gross, A., Zhao, Y., Zinkel, S., Klocke, B., Roth, K. A., & Korsmeyer, S. J. (1999) · Nature · doi:10.1038/23730 · Cited by 1,004
A Unified Model for Apical Caspase Activation
Boatright, K. M., Renatus, M., Scott, F. L., Sperandio, S., Shin, H., Pedersen, I. M., Ricci, J., Edris, W. A., Sutherlin, D. P., Green, D. R., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00051-0 · Cited by 986
Self-citation
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
Cytochrome c release from mitochondria proceeds by a two-step process
Ott, M., Robertson, J. D., Gogvadze, V. G., Zhivotovsky, B., & Orrenius, S. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.241655498 · Cited by 955
Apaf1 (CED-4 Homolog) Regulates Programmed Cell Death in Mammalian Development
Cecconi, F., Álvarez-Bolado, G., Meyer, B. I., Roth, K. A., & Gruß, P. (1998) · Cell · doi:10.1016/s0092-8674(00)81732-8 · Cited by 894
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
Negative regulation of the Apaf-1 apoptosome by Hsp70
Saleh, A., Srinivasula, S. M., Balkir, L., Robbins, P. D., & Alnemri, E. S. (2000) · Nature Cell Biology · doi:10.1038/35019510 · Cited by 823
Cyclophilin D is a component of mitochondrial permeability transition and mediates neuronal cell death after focal cerebral ischemia
Schinzel, A. C., Takeuchi, O., Huang, Z., Fisher, J. K., Zhou, Z., Rubens, J., Hetz, C., Danial, N. N., Moskowitz, M. A., & Korsmeyer, S. J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505294102 · Cited by 820
Human inhibitor of apoptosis proteins: why XIAP is the black sheep of the family
Eckelman, B. P., Salvesen, G. S., & Scott, F. L. (2006) · The EMBO Reports · doi:10.1038/sj.embor.7400795 · Cited by 813
Mitochondrial Rhomboid PARL Regulates Cytochrome c Release during Apoptosis via OPA1-Dependent Cristae Remodeling
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 756
BAX activation is initiated at a novel interaction site
Gavathiotis, E., Suzuki, M., Davis, M. L., Pitter, K., Bird, G. H., Katz, S. G., Tu, H.-C., Kim, H., Cheng, E. H.-Y., Tjandra, N., et al. (2008) · Nature · doi:10.1038/nature07396 · Cited by 700
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
Apaf-1 and Caspase-9 in p53-Dependent Apoptosis and Tumor Inhibition
Soengas, M. S., Alarcon, R. M., Yoshida, H., J., A., Giaccia, Hakem, R., Mak, T. W., & Lowe, S. W. (1999) · Science · doi:10.1126/science.284.5411.156 · Cited by 664
Induction of Immunological Tolerance by Apoptotic Cells Requires Caspase-Dependent Oxidation of High-Mobility Group Box-1 Protein
Kazama, H., Ricci, J.-E., Herndon, J. M., Hoppe, G., Green, D. R., & Ferguson, T. A. (2008) · Immunity · doi:10.1016/j.immuni.2008.05.013 · Cited by 627
Self-citation
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
Disruption of Mitochondrial Function during Apoptosis Is Mediated by Caspase Cleavage of the p75 Subunit of Complex I of the Electron Transport Chain
Ricci, J., Muñoz‐Pinedo, C., FITZGERALD, P. J., Bailly‐Maitre, B., Perkins, G. A., Yadava, N., Scheffler, I. E., Ellisman, M. H., & Green, D. R. (2004) · Cell · doi:10.1016/j.cell.2004.05.008 · Cited by 608
Self-citation
Autocrine TNFα Signaling Renders Human Cancer Cells Susceptible to Smac-Mimetic-Induced Apoptosis
Petersen, S. L., Wang, L., Yalcin-Chin, A., Li, L., Peyton, M., Minna, J. D., Harran, P. G., & Wang, X. (2007) · Cancer Cell · doi:10.1016/j.ccr.2007.08.029 · Cited by 579
Membrane Binding by tBid Initiates an Ordered Series of Events Culminating in Membrane Permeabilization by Bax
Lovell, J. F., Billen, L. P., Bindner, S., Shamas‐Din, A., Fradin, C., Leber, B. F., & Andrews, D. W. (2008) · Cell · doi:10.1016/j.cell.2008.11.010 · Cited by 564
Negative regulation of cytochrome c‐mediated oligomerization of Apaf‐1 and activation of procaspase‐9 by heat shock protein 90
Pandey, P., Saleh, A., Nakazawa, A., Kumar, S., Srinivasula, S. M., Kumar, V., Weichselbaum, R. R., Nalin, C. M., Alnemri, E. S., Kufe, D. W., et al. (2000) · The EMBO Journal · doi:10.1093/emboj/19.16.4310 · Cited by 556
Caspase-3 Activation via Mitochondria Is Required for Long-Term Depression and AMPA Receptor Internalization
Li, Z., Jo, J., Jia, J., Lo, S., Whitcomb, D. J., Jiao, S., Cho, K., & Sheng, M. (2010) · Cell · doi:10.1016/j.cell.2010.03.053 · Cited by 533
GAPDH and Autophagy Preserve Survival after Apoptotic Cytochrome c Release in the Absence of Caspase Activation
Colell, A., Ricci, J.-E., Tait, S., Milasta, S., Maurer, U., Bouchier-Hayes, L., Fitzgerald, P., Guio-Carrion, A., Waterhouse, N. J., Li, C. W., et al. (2007) · Cell · doi:10.1016/j.cell.2007.03.045 · Cited by 516
Self-citation
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
Caspase-mediated loss of mitochondrial function and generation of reactive oxygen species during apoptosis
Ricci, J.-E., Gottlieb, R. A., & Green, D. R. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200208089 · Cited by 504
Self-citation
Essential role for caspase 8 in T-cell homeostasis and T-cell-mediated immunityPreprint
Salmena, L., Lemmers, B., Hakem, A., Matysiak‐Zablocki, E., Murakami, K., Au, P. Y. B., Berry, D. M., Tamblyn, L., Shehabeldin, A., Migon, E., et al. (2003) · Genes & Development · doi:10.1101/gad.1063703 · Cited by 486
XIAP discriminates between type I and type II FAS-induced apoptosis
Jost, P. J., Grabow, S., Gray, D., McKenzie, M. D., Nachbur, U., Huang, D. C. S., Bouillet, P., Thomas, H. E., Borner, C., Silke, J., et al. (2009) · Nature · doi:10.1038/nature08229 · Cited by 482
Dissecting p53 tumor suppressor functions in vivo
Schmitt, C. A., Fridman, J. S., Yang, M., Baranov, E., Hoffman, R. M., & Lowe, S. W. (2002) · Cancer Cell · doi:10.1016/s1535-6108(02)00047-8 · Cited by 481
Bax and Bak Coalesce into Novel Mitochondria-Associated Clusters during Apoptosis
Nechushtan, A., Smith, C. L., Lamensdorf, I., Yoon, S., & Youle, R. J. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.6.1265 · Cited by 480
Inhibition of caspase-9 through phosphorylation at Thr 125 by ERK MAPK
Allan, L. A., MORRICE, N. A., Brady, S. C., Magee, G. J., Pathak, S., & Clarke, P. R. (2003) · Nature Cell Biology · doi:10.1038/ncb1005 · Cited by 474
Cytochrome C Maintains Mitochondrial Transmembrane Potential and Atp Generation after Outer Mitochondrial Membrane Permeabilization during the Apoptotic Process
Waterhouse, N. J., Goldstein, J. C., von Ahsen, O., Schüler, M., Newmeyer, D. D., & Green, D. R. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.2.319 · Cited by 460
Self-citation
Mitochondrial release of AIF and EndoG requires caspase activation downstream of Bax/Bak‐mediated permeabilization
Arnoult, D., Gaume, B. R., Karbowski, M., Sharpe, J. C., Cecconi, F., & Youle, R. J. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg423 · Cited by 455
BAX-dependent transport of cytochrome c reconstituted in pure liposomes
Saito, M. L., Korsmeyer, S. J., & Schlesinger, P. H. (2000) · Nature Cell Biology · doi:10.1038/35019596 · Cited by 451
Calpain I Induces Cleavage and Release of Apoptosis-inducing Factor from Isolated Mitochondria
Polster, B. M., Basáñez, G., Etxebarria, A., Hardwick, J. M., & Nicholls, D. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m413269200 · Cited by 438
Structural Basis of Pore Formation by the Bacterial Toxin Pneumolysin
Tilley, S. J., Orlova, E. V., Gilbert, R. J. C., Andrew, P. W., & Saibil, H. R. (2005) · Cell · doi:10.1016/j.cell.2005.02.033 · Cited by 421
Glucose metabolism inhibits apoptosis in neurons and cancer cells by redox inactivation of cytochrome c
Vaughn, A. E., & Deshmukh, M. (2008) · Nature Cell Biology · doi:10.1038/ncb1807 · Cited by 408
Cytochrome c activation of CPP32‐like proteolysis plays a critical role in a Xenopus cell‐free apoptosis system
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
Self-citation
Distinctive Roles of PHAP Proteins and Prothymosin-α in a Death Regulatory Pathway
Jiang, X., Kim, H.-E., Shu, H., Zhao, Y., Zhang, H., Kofron, J. L., Donnelly, J. B., Burns, D., Ng, S., Rosenberg, S. H., et al. (2003) · Science · doi:10.1126/science.1076807 · Cited by 378
Caspase-independent cell death: leaving the set without the final cut
Tait, S. W. G., & Green, D. R. (2008) · Oncogene · doi:10.1038/onc.2008.311 · Cited by 366
Self-citation
To Trigger Apoptosis, Bak Exposes Its BH3 Domain and Homodimerizes via BH3:Groove Interactions
Dewson, G., Kratina, T., Sim, H. W., Puthalakath, H., Adams, J. M., Colman, P. M., & Kluck, R. M. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.04.005 · Cited by 348
Formation of apoptosome is initiated by cytochrome c -induced dATP hydrolysis and subsequent nucleotide exchange on Apaf-1
Kim, H.-E., Du, F., Fang, M., & Wang, X. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507900102 · Cited by 344
Endoplasmic reticulum BIK initiates DRP1‐regulated remodelling of mitochondrial cristae during apoptosis
Germain, M., Mathai, J. P., McBride, H. M., & Shore, G. C. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600592 · Cited by 337
Inhibiting Drp1-mediated mitochondrial fission selectively prevents the release of cytochrome c during apoptosis
Estaquier, J., & Arnoult, D. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402107 · Cited by 330
DRP-1-mediated mitochondrial fragmentation during EGL-1-induced cell death in C. elegans
Jagasia, R., Grote, P., Westermann, B., & Conradt, B. (2005) · Nature · doi:10.1038/nature03316 · Cited by 319
The Release of Cytochrome c from Mitochondria during Apoptosis of NGF-deprived Sympathetic Neurons Is a Reversible Event
Martinou, I., Desagher, S., Eskes, R., Antonsson, B. E., André, É., Fakan, S., & Martinou, J. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.144.5.883 · Cited by 316
Deficiency in Bak and Bax perturbs thymic selection and lymphoid homeostasis
Rathmell, J. C., Lindsten, T., Zong, W., Cinalli, R. M., & Thompson, C. B. (2002) · Nature Immunology · doi:10.1038/ni834 · Cited by 302
The Apoptosome Activates Caspase-9 by Dimerization
Pop, C., Timmer, J. C., Sperandio, S., & Salvesen, G. S. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.03.009 · Cited by 294
Opa1-Mediated Cristae Opening Is Bax/Bak and BH3 Dependent, Required for Apoptosis, and Independent of Bak Oligomerization
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
Bax, but not Bcl-x L , decreases the lifetime of planar phospholipid bilayer membranes at subnanomolar concentrations
Basáñez, G., Nechushtan, A., Drozhinin, O., Chanturiya, A., Choe, E., Tutt, S., Wood, K. A., Hsu, Y.-T., Zimmerberg, J. J., & Youle, R. J. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.10.5492 · Cited by 285
Evidence of a Novel Event during Neuronal Death
Deshmukh, M., & Johnson, E. M. (1998) · Neuron · doi:10.1016/s0896-6273(00)80587-5 · Cited by 281
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 281
Correlated three-dimensional light and electron microscopy reveals transformation of mitochondria during apoptosis
Sun, M., Williams, J. M., Muñoz‐Pinedo, C., Perkins, G. A., Brown, J. M., Ellisman, M. H., Green, D. R., & Frey, T. (2007) · Nature Cell Biology · doi:10.1038/ncb1630 · Cited by 279
Self-citation
Bax- 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 276
Cleavage of BID during cytotoxic drug and UV radiation-induced apoptosis occurs downstream of the point of Bcl-2 action and is catalysed by caspase-3: a potential feedback loop for amplification of apoptosis-associated mitochondrial cytochrome c release
Slee, E. A., Keogh, S. A., & Martin, S. J. (2000) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400689 · Cited by 276
Release of OPA1 during Apoptosis Participates in the Rapid and Complete Release of Cytochrome c and Subsequent Mitochondrial Fragmentation
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
Different mitochondrial intermembrane space proteins are released during apoptosis in a manner that is coordinately initiated but can vary in duration
Muñoz‐Pinedo, C., Guío-Carrión, A., Goldstein, J. C., FITZGERALD, P. J., Newmeyer, D. D., & Green, D. R. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603007103 · Cited by 253
Self-citation
The Apoptosome: Physiological, Developmental, and Pathological Modes of Regulation
Schafer, Z. T., & Kornbluth, S. A. (2006) · Developmental Cell · doi:10.1016/j.devcel.2006.04.008 · Cited by 247
The X-Ray Structure of a BAK Homodimer Reveals an Inhibitory Zinc Binding Site
Moldoveanu, T., Liu, Q., Tocilj, A., Watson, M., Shore, G. C., & Gehring, K. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.10.014 · Cited by 239
Phosphorylation of Caspase-9 by CDK1/Cyclin B1 Protects Mitotic Cells against Apoptosis
Allan, L. A., & Clarke, P. R. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.03.019 · Cited by 237
Bax-type Apoptotic Proteins Porate Pure Lipid Bilayers through a Mechanism Sensitive to Intrinsic Monolayer Curvature
Basáñez, G., Sharpe, J. C., Galanis, J., Brandt, T. B., Hardwick, J. M., & Zimmerberg, J. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206069200 · Cited by 234
Living with death: the evolution of the mitochondrial pathway of apoptosis in animals
Oberst, A., Bender, C., & Green, D. R. (2008) · Cell Death and Differentiation · doi:10.1038/cdd.2008.65 · Cited by 233
Self-citation
Inhibiting 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
Mitochondria are selectively eliminated from eukaryotic cells after blockade of caspases during apoptosis
Xue, L., Fletcher, G. C., & Tolkovsky, A. M. (2001) · Current Biology · doi:10.1016/s0960-9822(01)00100-2 · Cited by 230
Apoptosis and autophagy: Regulation of caspase‐9 by phosphorylation
Allan, L. A., & Clarke, P. R. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07330.x · Cited by 226
Bak Activation for Apoptosis Involves Oligomerization of Dimers via Their α6 Helices
Dewson, G., Kratina, T., Czabotar, P. E., Day, C. L., Adams, J. M., & Kluck, R. M. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.11.008 · Cited by 220
tRNA Binds to Cytochrome c and Inhibits Caspase Activation
Mei, Y., Yong, J., Liu, H., Shi, Y., Meinkoth, J. L., Dreyfuss, G., & Yang, X. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.01.023 · Cited by 215
Inducible Dimerization and Inducible Cleavage Reveal a Requirement for Both Processes in Caspase-8 Activation
Oberst, A., Pop, C., Tremblay, A. G., Blais, V., Denault, J.-B., Salvesen, G. S., & Green, D. R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.095083 · Cited by 214
Self-citation
Resistance to Caspase-Independent Cell Death Requires Persistence of Intact Mitochondria
Tait, S. W. G., Parsons, M. J., Llambi, F., Bouchier‐Hayes, L., Connell, S., Muñoz‐Pinedo, C., & Green, D. R. (2010) · Developmental Cell · doi:10.1016/j.devcel.2010.03.014 · Cited by 204
Self-citation
The BH3‐only Bnip3 binds to the dynamin Opa1 to promote mitochondrial fragmentation and apoptosis by distinct mechanisms
Landes, T., Emorine, L. J., Courilleau, D., Rojo, M., Belenguer, P., & Pelloquin, L. (2010) · EMBO Reports · doi:10.1038/embor.2010.50 · Cited by 200
Cytochrome c as an electron shuttle between the outer and inner mitochondrial membranes.
Bernardi, P., & AZZONE, G. F. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68946-5 · Cited by 199
Physiological Concentrations of K+ Inhibit Cytochrome c-dependent Formation of the Apoptosome
Cain, K., Langlais, C., Sun, X.-M., Brown, D. G., & Cohen, G. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m107419200 · Cited by 197
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
Reconstitution of the Death-Inducing Signaling Complex Reveals a Substrate Switch that Determines CD95-Mediated Death or Survival
Hughes, M. A., Harper, N. W., Butterworth, M., Cain, K., Cohen, G. M., & MacFarlane, M. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.06.012 · Cited by 185
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
Mitochondrial Release of Pro-apoptotic Proteins
Uren, R. T., Dewson, G., Bonzon, C., Lithgow, T. J., Newmeyer, D. D., & Kluck, R. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m411106200 · Cited by 170
A non-apoptotic role for caspase-9 in muscle differentiation
Murray, T. V., McMahon, J. M., Howley, B. A., Stanley, A., Ritter, T., Mohr, A., Zwacka, R. M., & Fearnhead, H. O. (2008) · Journal of Cell Science · doi:10.1242/jcs.024547 · Cited by 167
A reversible component of mitochondrial respiratory dysfunction in apoptosis can be rescued by exogenous cytochrome c
Mootha, V. K., Wei, M. C., Buttle, K. F., Scorrano, L., Panoutsakopoulou, V., Mannella, C. A., & Korsmeyer, S. J. (2001) · The EMBO Journal · doi:10.1093/emboj/20.4.661 · Cited by 167
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
Apoptotic Protease Activating Factor 1 (Apaf-1)–Independent Cell Death Suppression by Bcl-2
Haraguchi, M., Torii, S., Matsuzawa, S., Xie, Z., Kitada, S., Krajewski, S., Yoshida, H., Mak, T. W., & Reed, J. C. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.191.10.1709 · Cited by 158
VDAC2 is required for truncated BID‐induced mitochondrial apoptosis by recruiting BAK to the mitochondria
Roy, S. S., Ehrlich, A. M., Craigen, W. J., & Hajnóczky, G. (2009) · EMBO Reports · doi:10.1038/embor.2009.219 · Cited by 150
Critical function of endogenous XIAP in regulating caspase activation during sympathetic neuronal apoptosis
Potts, P. R., Singh, S., Knezek, M., Thompson, C. B., & Deshmukh, M. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200307130 · Cited by 149
Real-time single cell analysis of Smac/DIABLO release during apoptosis
Rehm, M., Düßmann, H., & Prehn, J. H. M. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200303123 · Cited by 146
Dynamics of outer mitochondrial membrane permeabilization during apoptosis
Rehm, M., Huber, H. J., Hellwig, C. T., Anguissola, S., Düßmann, H., & Prehn, J. H. M. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2008.187 · Cited by 141
The Apaf‐1•procaspase‐9 apoptosome complex functions as a proteolytic‐based molecular timer
Malladi, S., Challa-Malladi, M., Fearnhead, H. O., & Bratton, S. B. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.152 · Cited by 140
Caspase-independent Mitochondrial Cell Death Results from Loss of Respiration, Not Cytotoxic Protein Release
Lartigue, L., Kushnareva, Y., Seong, Y., Lin, H. H., Faustin, B., & Newmeyer, D. D. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-07-0649 · Cited by 138
A three-helix homo-oligomerization domain containing BH3 and BH1 is responsible for the apoptotic activity of BaxPreprint
George, N. M., Evans, J. J. D., & Luo, X. (2007) · Genes & Development · doi:10.1101/gad.1553607 · Cited by 130
Intracellular Nucleotides Act as Critical Prosurvival Factors by Binding to Cytochrome C and Inhibiting Apoptosome
Chandra, D., Bratton, S. B., Person, M. D., Tian, Y., Martín, Á. G., Ayres, M., Fearnhead, H. O., Gandhi, V. V., & Tang, D. G. (2006) · Cell · doi:10.1016/j.cell.2006.05.026 · Cited by 127
Mitochondrial Outer Membrane Proteins Assist Bid in Bax-mediated Lipidic Pore Formation
Schafer, B., Quispe, J. D., Choudhary, V., Chipuk, J. E., Ajero, T. G., Du, H., Schneiter, R., & Kuwana, T. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-10-1056 · Cited by 124
Nitrosylation of Cytochrome c during Apoptosis
Schonhoff, C. M., Gaston, B. M., & Mannick, J. B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212459200 · Cited by 121
Importance of the redox state of cytochrome c during caspase activation in cytosolic extracts
Hampton, M. B., Zhivotovsky, B., SLATER, F. G. A., BURGESS, H. D., & Orrenius, S. (1998) · Biochemical Journal · doi:10.1042/bj3290095 · Cited by 119
Reduced Apaf-1 levels in cardiomyocytes engage strict regulation of apoptosis by endogenous XIAP
Potts, M. B., Vaughn, A. E., McDonough, H., Patterson, C., & Deshmukh, M. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200504082 · Cited by 116
Assembly of the Mitochondrial Apoptosis-induced Channel, MAC
Martinez‐Caballero, S., Dejean, L. M., Kinnally, M., Oh, K. J., Mannella, C. A., & Kinnally, K. W. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m806610200 · Cited by 115
Roles of mitophagy and the mitochondrial permeability transition in remodeling of cultured rat hepatocytes
Rodríguez‐Enríquez, S., Kai, Y., Maldonado, E. N., Currin, R. T., & Lemasters, J. J. (2009) · Autophagy · doi:10.4161/auto.5.8.9825 · Cited by 115
Generation and Characterization of Endonuclease G Null Mice
Irvine, R. A., Adachi, N., Shibata, D. K., Cassell, G. D., Yu, K., Karanjawala, Z. E., Hsieh, C.-L., & Lieber, M. R. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.1.294-302.2005 · Cited by 111
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 110
PHAPI, CAS, and Hsp70 Promote Apoptosome Formation by Preventing Apaf-1 Aggregation and Enhancing Nucleotide Exchange on Apaf-1
Kim, H.-E., Jiang, X., Du, F., & Wang, X. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.03.014 · Cited by 104
Disruption of the M80-Fe ligation stimulates the translocation of cytochrome c to the cytoplasm and nucleus in nonapoptotic cells
Godoy, L. C., Muñoz‐Pinedo, C., Castro, L., Cardaci, S., Schonhoff, C. M., King, M., Tórtora, V., Marı́n, M., Miao, Q., Jiang, J. F., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809279106 · Cited by 101
Self-citation
Single-cell quantification of Bax activation and mathematical modelling suggest pore formation on minimal mitochondrial Bax accumulation
Düßmann, H., Rehm, M., Concannon, C. G., Anguissola, S., Würstle, M. L., Kacmar, S., Völler, P., Huber, H. J., & Prehn, J. H. M. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.123 · Cited by 101
Mitochondrial Regulation of Caspase Activation by Cytochrome Oxidase and Tetramethylphenylenediamine via Cytosolic Cytochrome c Redox State
Borutaitė, V., & Brown, G. C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700322200 · Cited by 98
Apoptosis induced by microinjection of cytochrome c is caspase-dependent and is inhibited by Bcl-2
Brustugun, O. T., Fladmark, K. E., Døskeland, S. O., Orrenius, S., & Zhivotovsky, B. (1998) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400399 · Cited by 98
Decreased apoptosome activity with neuronal differentiation sets the threshold for strict IAP regulation of apoptosis
Wright, K. M., Linhoff, M. W., Potts, P. R., & Deshmukh, M. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200406073 · Cited by 95
Calcium Blocks Formation of Apoptosome by Preventing Nucleotide Exchange in Apaf-1
Bao, Q., Lu, W., Rabinowitz, J. D., & Shi, Y. (2007) · Molecular Cell · doi:10.1016/j.molcel.2006.12.013 · Cited by 90
Dynamics and structure of the Bax-Bak complex responsible for releasing mitochondrial proteins during apoptosis
Zhou, L., & Chang, D. C. (2008) · Journal of Cell Science · doi:10.1242/jcs.024703 · Cited by 83
Lack of Apaf-1 expression confers resistance to cytochrome c-driven apoptosis in cardiomyocytes
Sanchís, D., Mayorga, M. E., Ballester, M., & Comella, J. X. (2003) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401267 · Cited by 73
Analysis of redox regulation of cytochrome c-induced apoptosis in a cell-free system
Pan, Z., Voehringer, D. W., & Meyn, R. E. (1999) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400544 · Cited by 69
A cytochrome c mutant with high electron transfer and antioxidant activities but devoid of apoptogenic effect
Abdullaev, Z., Bodrova, M. E., Chernyak, B. V., Dolgikh, D. A., Kluck, R. M., PEREVERZEV, M. O., Arseniev, A. S., Efremov, R. G., Kirpichnikov, M. P., MOKHOVA, E. N., et al. (2002) · Biochemical Journal · doi:10.1042/0264-6021:3620749 · Cited by 58
Apoptosome-deficient Cells Lose Cytochromecthrough Proteasomal Degradation but Survive by Autophagy-dependent Glycolysis
Ferraro, E., Pulicati, A., Cencioni, M. T., Cozzolino, M., Navoni, F., Martino, S. D., Nardacci, R., Carrı̀, M. T., & Cecconi, F. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-09-0858 · Cited by 55
MAC inhibitors suppress mitochondrial apoptosis
Peixoto, P. M. V., Ryu, S.-Y., Bombrun, A., Antonsson, B. E., & Kinnally, K. W. (2009) · Biochemical Journal · doi:10.1042/bj20090664 · Cited by 51
pp32/PHAPI determines the apoptosis response of non-small-cell lung cancer
Hoffarth, S., Zitzer, A. O., Wiewrodt, R. G., Hähnel, P. S., Beyer, V., Kreft, A., Biesterfeld, S., & Schüler, M. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402256 · Cited by 46
An intracellular wave of cytochrome c propagates and precedes Bax redistribution during apoptosis
Lartigue, L., Medina, C. F., Schembri, L., Chabert, P., Zanese, M., Tomasello, M. F., Dalibart, R., Thoraval, D. H., Crouzet, M., Ichas, F., et al. (2008) · Journal of Cell Science · doi:10.1242/jcs.029587 · Cited by 45
Spatial and Temporal Dynamics of Mitochondrial Membrane Permeability Waves during Apoptosis
Bhola, P. D., Mattheyses, A. L., & Simon, S. M. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2009.07.056 · Cited by 45
Bax, along with Lipid Conspirators, Allows Cytochrome c to Escape Mitochondria
Hardwick, J. M., & Polster, B. M. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00751-7 · Cited by 43
Laser micro-irradiation of mitochondria: is there an amplified mitochondrial death signal in neural cells?
Khodjakov, A. L., Rieder, C. L., Mannella, C. A., & Kinnally, K. W. (2003) · Mitochondrion · doi:10.1016/j.mito.2003.10.002 · Cited by 39
Genome-wide silencing in Drosophila captures conserved apoptotic effectors
Chew, S. K., Chen, P., Link, N., Galindo, K. A., Pogue, K., & Abrams, J. (2009) · Nature · doi:10.1038/nature08087 · Cited by 39
A cytochrome c mutant with high electron transfer and antioxidant activities but devoid of apoptogenic effect
ABDULLAEV, Z. K., BODROVA, M. E., Chernyak, B. V., et al. (2002) · Biochemical Journal · doi:10.1042/bj3620749 · Cited by 38
Modulation of Caspase-Independent Cell Death Leads to Resensitization of Imatinib Mesylate–Resistant Cells
Lavallard, V., Pradelli, L. A., Paul, A., Bénéteau, M., Jacquel, A., Auberger, P., & Ricci, J. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-2731 · Cited by 30
Intra-mitochondrial degradation of Tim23 curtails the survival of cells rescued from apoptosis by caspase inhibitors
Goemans, C. G., Boya, P., Skirrow, C. J., & Tolkovsky, A. M. (2008) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402290 · Cited by 26
Evaluating cytochrome c diffusion in the intermembrane spaces of mitochondria during cytochrome c release
Gillick, K., & Crompton, M. (2008) · Journal of Cell Science · doi:10.1242/jcs.021303 · Cited by 18

Flagged first, then by citations

Sorted by citations

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
Self-citation
The unfolded protein response: controlling cell fate decisions under ER stress and beyond
Hetz, C. A. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3270 · Cited by 4,223
Activation of apoptosis signalling pathways by reactive oxygen species
Redza-Dutordoir, M., & Averill-Bates, D. A. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.09.012 · Cited by 3,731
Control of apoptosis by the BCL-2 protein family: implications for physiology and therapy
Czabotar, P. E., Lessene, G., Strasser, A., & Adams, J. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3722 · Cited by 3,219
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
Self-citation

See all 2,593

Authors: Tait, S. W. G., & Green, D. R.
Affiliations: St. Jude Children's Research Hospital (US)
Corresponding author: Green, Douglas R.
ORCID: Tait, Stephen W. G.
Green, Douglas R.
Venue: Nature Reviews Molecular Cell Biology
Publisher: Springer Science and Business Media LLC
Published: 2010-08-04
Volume: 11
Issue: 9
Pages: 621-632
ISSN: 1471-0072 (ISSN-L)
1471-0080
DOI: 10.1038/nrm2952
OpenAlex: W2066571367
Cited by: 2,593
References: 151
Citations by year: 2026: 142 · 2025: 110 · 2024: 104 · 2023: 131 · 2022: 143 · 2021: 182 · 2020: 188 · 2019: 160 · 2018: 214 · 2017: 195 · 2016: 200 · 2015: 194 · 2014: 203 · 2013: 175 · 2012: 134
FWCI: 11.64
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature Reviews Molecular Cell Biology (publishedVersion)
PubMed (publishedVersion)
ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (submittedVersion)
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
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Keywords: mitochondrial outer membrane permeabilization, apoptosis, caspase activation, Bcl-2 family proteins, Bax, Bak, cytochrome c release, mitochondrial function, cell death
MeSH terms: Animals, Humans, Mitochondria, Cell Death, Caspases, bcl-2-Associated X Protein, Mitochondrial Membranes

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Mitochondria and cell death: outer membrane permeabilization and beyond

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks