Proapoptotic BAX and BAK: A Requisite Gateway to Mitochondrial Dysfunction and Death

Cytochrome c and dATP-Dependent Formation of Apaf-1/Caspase-9 Complex Initiates an Apoptotic Protease Cascade

Li, P., Nijhawan, D., Budihardjo, I., Srinivasula, S. M., Ahmad, M., Alnemri, E. S., & Wang, X. (1997) · Cell · doi:10.1016/s0092-8674(00)80434-1 · Cited by 7,289 · see citing works

The Bcl-2 Protein Family: Arbiters of Cell Survival

Adams, J. M., & Cory, S. (1998) · Science · doi:10.1126/science.281.5381.1322 · Cited by 5,303 · see citing works

Control of inositol 1,4,5-trisphosphate-induced Ca2+ release by cytosolic Ca2+

Bootman, M. D., Missiaen, L., Parys, J. B., SMEDT, H. D., & Casteels, R. (1995) · Biochemical Journal · doi:10.1042/bj3060445 · Cited by 5,120 · 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

Mutation of the mouse klotho gene leads to a syndrome resembling ageing

Kuro-o, M., Matsumura, Y., Aizawa, H., Kawaguchi, H., Suga, T., Utsugi, T., Ohyama, Y., Kurabayashi, M., Kaname, T., Kume, E., et al. (1997) · Nature · doi:10.1038/36285 · Cited by 3,837 · see citing works

Bid, a Bcl2 Interacting Protein, Mediates Cytochrome c Release from Mitochondria in Response to Activation of Cell Surface Death Receptors

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

BCL-2 family members and the mitochondria in apoptosisPreprint

Gross, A., McDonnell, J. M., & Korsmeyer, S. J. (1999) · Genes & Development · doi:10.1101/gad.13.15.1899 · Cited by 3,623 · see citing works

Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β

Nakagawa, T., Zhu, H., Morishima, N., Li, E., Xu, J., Yankner, B. A., & Yuan, J. (2000) · Nature · doi:10.1038/47513 · Cited by 3,262 · see citing works

Mitochondrial control of cell death

Kroemer, G., & Reed, J. C. (2000) · Nature Medicine · doi:10.1038/74994 · Cited by 3,103 · see citing works

Two CD95 (APO‐1/Fas) signaling pathways

Scaffidi, C., Fulda, S., Srinivasan, A., Friesen, C., Li, F., Tomaselli, K. J., Debatin, K., Krammer, P. H., & Peter, M. E. (1998) · The EMBO Journal · doi:10.1093/emboj/17.6.1675 · Cited by 3,000 · see citing works

Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controlsPreprint

Kaufman, R. J. (1999) · Genes & Development · doi:10.1101/gad.13.10.1211 · Cited by 2,247 · see citing works

Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC

Shimizu, S., Narita, M., Tsujimoto, Y., & Tsujimoto, Y. (1999) · Nature · doi:10.1038/20959 · Cited by 2,178 · see citing works

Reduced Apoptosis and Cytochrome c–Mediated Caspase Activation in Mice Lacking Caspase 9

Kuida, K., Haydar, T. F., Kuan, C.-Y., Gu, Y., Taya, C., Karasuyama, H., Su, M. S.-S., Rakic, P., & Flavell, R. A. (1998) · Cell · doi:10.1016/s0092-8674(00)81476-2 · Cited by 1,643 · see citing works

The Combined Functions of Proapoptotic Bcl-2 Family Members Bak and Bax Are Essential for Normal Development of Multiple Tissues

Lindsten, T., Ross, A. J., King, A., Zong, W.-X., Rathmell, J. C., Shiels, H. A., Ulrich, E., Waymire, K. G., Mahar, P., Frauwirth, K., et al. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00136-2 · Cited by 1,489 · see citing works

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 1,284 · see citing works

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 1,265 · see citing works

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 1,190 · see citing works

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 · see citing works

Caspase Cleaved BID Targets Mitochondria and Is Required for Cytochrome c Release, while BCL-XL Prevents This Release but Not Tumor Necrosis Factor-R1/Fas Death

Gross, A., Yin, X.-M., Wang, K., Wei, M. C., Jockel, J., Milliman, C., Erdjument-Bromage, H., Tempst, P., & Korsmeyer, S. J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.2.1156 · Cited by 1,045 · see citing works

BH3-Only Proteins—Essential Initiators of Apoptotic Cell Death

Huang, D. C. S., & Strasser, A. (2000) · Cell · doi:10.1016/s0092-8674(00)00187-2 · Cited by 1,044 · see citing works

Apoptotic Pathways

Green, D. R. (2000) · Cell · doi:10.1016/s0092-8674(00)00003-9 · Cited by 1,011 · see citing works

Bid-deficient mice are resistant to Fas-induced hepatocellular apoptosis

Yin, X.-M., Wang, K., Gross, A., Zhao, Y., Zinkel, S., Klocke, B., Roth, K. A., & Korsmeyer, S. J. (1999) · Nature · doi:10.1038/23730 · Cited by 1,004 · see citing works

A stable human-derived packaging cell line for production of high titer retrovirus/vesicular stomatitis virus G pseudotypes.

Ory, D., Neugeboren, B. I., & Mulligan, R. C. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.21.11400 · Cited by 926 · see citing works

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 · see citing works

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

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

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 453 · see citing works

Bok is a pro-apoptotic Bcl-2 protein with restricted expression in reproductive tissues and heterodimerizes with selective anti-apoptotic Bcl-2 family members

Hsu, S. Y., Kaipia, A. J., McGee, E. A., Lomeli, M. R., & Hsueh, A. J. W. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.23.12401 · Cited by 369 · see citing works

The Pro-Apoptotic Proteins, Bid and Bax, Cause a Limited Permeabilization of the Mitochondrial Outer Membrane That Is Enhanced by Cytosol

Kluck, R., Esposti, M., Perkins, G., Renken, C., Kuwana, T., Bossy‐Wetzel, E., Goldberg, M., Allen, T. D., Barber, M., Green, D., et al. (1999) · Journal of Cell Biology · doi:10.1083/jcb.147.4.809 · Cited by 342 · see citing works

p28 Bap31, a Bcl-2/Bcl-XL- and Procaspase-8–associated Protein in the Endoplasmic Reticulum

Ng, F. W. H., Nguyen, M., Kwan, T., Branton, P. E., Nicholson, D. W., Cromlish, J. A., & Shore, G. C. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.139.2.327 · Cited by 330 · see citing works

Bcl‐2 mutants with restricted subcellular location reveal spatially distinct pathways for apoptosis in different cell types.

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

Apoptotic crosstalk between the endoplasmic reticulum and mitochondria controlled by Bcl-2

Häcki, J., Egger, L., Monney, L., Conus, S., Rossé, T., Fellay, I., & Borner, C. (2000) · Oncogene · doi:10.1038/sj.onc.1203592 · Cited by 300 · see citing works

Maintenance of Calcium Homeostasis in the Endoplasmic Reticulum by Bcl-2

He, H., Lam, M. C., McCormick, T. S., & Distelhorst, C. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.138.6.1219 · Cited by 296 · see citing works

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 166 · see citing works

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

Galluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death & Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680 · see citing works

Cell Death

Danial, N. N., & Korsmeyer, S. J. (2004) · Cell · doi:10.1016/s0092-8674(04)00046-7 · Cited by 4,651 · see citing works

The Bcl2 family: regulators of the cellular life-or-death switch

Cory, S., & Adams, J. M. (2002) · Nature Reviews Cancer · doi:10.1038/nrc883 · Cited by 4,032 · 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

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 · see citing works

Mechanisms, regulation and functions of the unfolded protein response

Hetz, C., Zhang, K., & Kaufman, R. J. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0250-z · Cited by 2,666 · see citing works

Mitochondria and cell death: outer membrane permeabilization and beyond

Tait, S. W. G., & Green, D. R. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2952 · Cited by 2,593 · see citing works

Mediators of endoplasmic reticulum stress-induced apoptosis

Szegezdi, E., Logue, S. E., Gorman, A. M., & Samali, A. (2006) · The EMBO Reports · doi:10.1038/sj.embor.7400779 · Cited by 2,345 · see citing works

Glutaminolysis and transferrin regulate ferroptosis

Gao, M., Monian, P., Quadri, N., Ramasamy, R., & Jiang, X. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.06.011 · Cited by 2,069 · 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 · see citing works

The 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

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 · 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

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 · see citing works

Growth factor regulation of autophagy and cell survival in the absence of apoptosis

Lum, J. J., Bauer, D. E., Kong, M., Harris, M. H., Li, C., Lindsten, T., & Thompson, C. B. (2005) · Cell · doi:10.1016/j.cell.2004.11.046 · Cited by 1,487 · see citing works

Autophagic cell death: the story of a misnomer

Kroemer, G., & Levine, B. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2529 · Cited by 1,453 · see citing works

Role of Bcl-2 family proteins in a non-apoptotic programmed cell death dependent on autophagy genes

Shimizu, S., Kanaseki, T., Mizushima, N., Mizuta, T., Arakawa-Kobayashi, S., Thompson, C. B., & Tsujimoto, Y. (2004) · Nature Cell Biology · doi:10.1038/ncb1192 · Cited by 1,358 · see citing works

Activation of Apoptosis in Vivo by a Hydrocarbon-Stapled BH3 Helix

Walensky, L. D., Kung, A. L., Escher, I., Malia, T. J., Barbuto, S., Wright, R. D., Wagner, G., Verdine, G. L., & Korsmeyer, S. J. (2004) · Science · doi:10.1126/science.1099191 · Cited by 1,349 · 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

Mitochondrial cristae shape determines respiratory chain supercomplexes assembly and respiratory efficiency

Cogliati, S., Frezza, C., Soriano, M. E., Varanita, T., Quintana-Cabrera, R., Corrado, M., Cipolat, S., Costa, V., Casarin, A., Gomes, L. C., et al. (2013) · Cell · doi:10.1016/j.cell.2013.08.032 · Cited by 1,265 · see citing works

The Role for Endoplasmic Reticulum Stress in Diabetes Mellitus

Eizirik, D. L., Cardozo, A. K., & Cnop, M. (2008) · Endocrine Reviews · doi:10.1210/er.2007-0015 · Cited by 1,173 · see citing works

BH3 Domains of BH3-Only Proteins Differentially Regulate Bax-Mediated Mitochondrial Membrane Permeabilization Both Directly and Indirectly

Kuwana, T., Bouchier-Hayes, L., Chipuk, J. E., Bonzon, C., Sullivan, B. A., Green, D. R., & Newmeyer, D. D. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.02.003 · Cited by 1,185 · see citing works

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 · see citing works

Decoding cell death signals in liver inflammation

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

Essential versus accessory aspects of cell death: recommendations of the NCCD 2015

Galluzzi, L., Bravo-San Pedro, J. M., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Alnemri, E. S., Altucci, L., Andrews, D., Annicchiarico-Petruzzelli, M., et al. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2014.137 · Cited by 1,002 · see citing works

Apoptotic Caspases Suppress mtDNA-Induced STING-Mediated Type I IFN Production

White, M. J., McArthur, K., Metcalf, D., Lane, R. M., Cambier, J. C., Herold, M. J., van Delft, M. F., Bedoui, S., Lessene, G., Ritchie, M. E., et al. (2014) · Cell · doi:10.1016/j.cell.2014.11.036 · Cited by 983 · see citing works

Glycogen synthase kinase-3 regulates mitochondrial outer membrane permeabilization and apoptosis by destabilization of MCL-1

Maurer, U., Charvet, C., Wagman, A. S., Dejardin, E., & Green, D. R. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.02.009 · Cited by 881 · see citing works

Hierarchical regulation of mitochondrion-dependent apoptosis by BCL-2 subfamilies

Kim, H., Rafiuddin-Shah, M., Tu, H.-C., Jeffers, J. R., Zambetti, G. P., Hsieh, J. J.-D., & Cheng, E. H.-Y. (2006) · Nature Cell Biology · doi:10.1038/ncb1499 · Cited by 874 · 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

Apoptotic Caspases Prevent the Induction of Type I Interferons by Mitochondrial DNA

Rongvaux, A., Jackson, R., Harman, C. C. D., Li, T., West, A. P., de Zoete, M. R., Wu, Y., Yordy, B., Lakhani, S. A., Kuan, C.-Y., et al. (2014) · Cell · doi:10.1016/j.cell.2014.11.037 · Cited by 847 · see citing works

Spatial and temporal association of Bax with mitochondrial fission sites, Drp1, and Mfn2 during apoptosis

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

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 · see citing works

Thirty years of BCL-2: translating cell death discoveries into novel cancer therapies

Delbridge, A. R. D., Grabow, S., Strasser, A., & Vaux, D. L. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2015.17 · Cited by 752 · see citing works

Mechanisms of Action of Bcl-2 Family Proteins

Shamas-Din, A., Kale, J., Leber, B., & Andrews, D. W. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008714 · Cited by 705 · see citing works

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 · see citing works

A novel orally active proteasome inhibitor induces apoptosis in multiple myeloma cells with mechanisms distinct from Bortezomib

Chauhan, D., Catley, L., Li, G., Podar, K., Hideshima, T., Velankar, M., Mitsiades, C., Mitsiades, N., Yasui, H., Letai, A., et al. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.10.013 · Cited by 694 · see citing works

Betulin Is a Potent Anti-Tumor Agent that Is Enhanced by Cholesterol

Mullauer, F. B., Kessler, J. H., & Medema, J. P. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005361 · Cited by 688 · see citing works

Bcl-xL Retrotranslocates Bax from the Mitochondria into the Cytosol

Edlich, F., Banerjee, S., Suzuki, M., Cleland, M. M., Arnoult, D., Wang, C., Neutzner, A., Tjandra, N., & Youle, R. J. (2011) · Cell · doi:10.1016/j.cell.2011.02.034 · Cited by 630 · see citing works

Mitochondrial outer membrane permeabilization during apoptosis: the innocent bystander scenario

Chipuk, J. E., Bouchier-Hayes, L., & Green, D. R. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401963 · Cited by 631 · 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

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

Bax Crystal Structures Reveal How BH3 Domains Activate Bax and Nucleate Its Oligomerization to Induce Apoptosis

Czabotar, P. E., Westphal, D., Dewson, G., Ma, S., Hockings, C., Fairlie, W. D., Lee, E. F., Yao, S., Robin, A. Y., Smith, B. J., et al. (2013) · Cell · doi:10.1016/j.cell.2012.12.031 · Cited by 573 · see citing works

Akt-Directed Glucose Metabolism Can Prevent Bax Conformation Change and Promote Growth Factor-Independent Survival

Rathmell, J. C., Fox, C. J., Plas, D. R., Hammerman, P. S., Cinalli, R. M., & Thompson, C. B. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.20.7315-7328.2003 · Cited by 572 · see citing works

Mitochondrial inner membrane permeabilisation enables mtDNA release during apoptosis

Riley, J. S., Quarato, G., Cloix, C., Lopez, J., O'Prey, J., Pearson, M., Chapman, J., Sesaki, H., Carlin, L. M., Passos, J. F., et al. (2018) · The EMBO Journal · doi:10.15252/embj.201899238 · Cited by 551 · see citing works

Mitochondrial Regulation of Cell Death

Tait, S. W. G., & Green, D. R. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008706 · Cited by 530 · see citing works

Lysosomal Membrane Permeabilization Induces Cell Death in a Mitochondrion-dependent Fashion

Boya, P., Andreau, K., Poncet, D., Zamzami, N., Perfettini, J.-L., Metivier, D., Ojcius, D. M., Jäättelä, M., & Kroemer, G. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20021952 · Cited by 483 · see citing works

Mitochondria and cell signalling

Tait, S. W. G., & Green, D. R. (2012) · Journal of Cell Science · doi:10.1242/jcs.099234 · Cited by 453 · see citing works

The Opa1-Dependent Mitochondrial Cristae Remodeling Pathway Controls Atrophic, Apoptotic, and Ischemic Tissue Damage

Varanita, T., Soriano, M. E., Romanello, V., Zaglia, T., Quintana-Cabrera, R., Semenzato, M., Menabò, R., Costa, V., Civiletto, G., Pesce, P., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.007 · Cited by 460 · see citing works

JNK- and p38 kinase-mediated phosphorylation of Bax leads to its activation and mitochondrial translocation and to apoptosis of human hepatoma HepG2 cells

Kim, B.-J., Ryu, S.-W., & Song, B.-J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m510644200 · Cited by 470 · 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

Sphingolipid Metabolism Cooperates with BAK and BAX to Promote the Mitochondrial Pathway of Apoptosis

Chipuk, J. E., McStay, G. P., Bharti, A., Kuwana, T., Clarke, C. J., Siskind, L. J., Obeid, L. M., & Green, D. R. (2012) · Cell · doi:10.1016/j.cell.2012.01.038 · Cited by 436 · see citing works

Quantitation of mitochondrial dynamics by photolabeling of individual organelles shows that mitochondrial fusion is blocked during the Bax activation phase of apoptosis

Karbowski, M., Arnoult, D., Chen, H., Chan, D. C., Smith, C. L., & Youle, R. J. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200309082 · Cited by 433 · see citing works

BID regulation by p53 contributes to chemosensitivity

Sax, J. K., Fei, P., Murphy, M. E., Bernhard, E., Korsmeyer, S. J., & El-Deiry, W. S. (2002) · Nature Cell Biology · doi:10.1038/ncb866 · Cited by 420 · see citing works

The CD95 Type I/Type II model

Barnhart, B. C., Alappat, E. C., & Peter, M. E. (2003) · Seminars in Immunology · doi:10.1016/s1044-5323(03)00031-9 · Cited by 419 · see citing works

Cysteine Cathepsins Trigger Caspase-dependent Cell Death through Cleavage of Bid and Antiapoptotic Bcl-2 Homologues

Droga-Mazovec, G., Bojič, L., Petelin, A., Ivanova, S., Romih, R., Repnik, U., Salvesen, G. S., Stoka, V., Turk, V., & Turk, B. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802513200 · Cited by 399 · see citing works

Mitochondria: diversity in the regulation of the NLRP3 inflammasome

Gurung, P., Lukens, J. R., & Kanneganti, T.-D. (2015) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2014.11.008 · Cited by 393 · see citing works

ATF4 Regulates MYC-Mediated Neuroblastoma Cell Death upon Glutamine Deprivation

Qing, G., Li, B., Vu, A., Skuli, N., Walton, Z. E., Liu, X., Mayes, P. A., Wise, D. R., Thompson, C. B., Maris, J. M., et al. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.09.021 · Cited by 375 · see citing works

Mitochondrial membrane permeabilization is a critical step of lysosome-initiated apoptosis induced by hydroxychloroquine

Boya, P., Gonzalez-Polo, R.-A., Poncet, D., Andreau, K., Vieira, H. L., Roumier, T., Perfettini, J.-L., & Kroemer, G. (2003) · Oncogene · doi:10.1038/sj.onc.1206622 · Cited by 385 · see citing works

A Stapled BID BH3 Helix Directly Binds and Activates BAX

Walensky, L. D., Pitter, K., Morash, J., Oh, K. J., Barbuto, S., Fisher, J., Smith, E., Verdine, G. L., & Korsmeyer, S. J. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.08.020 · Cited by 383 · see citing works

Drug-Induced Death Signaling Strategy Rapidly Predicts Cancer Response to Chemotherapy

Montero, J., Sarosiek, K. A., DeAngelo, J. D., Maertens, O., Ryan, J., Ercan, D., Piao, H., Horowitz, N. S., Berkowitz, R. S., Matulonis, U., et al. (2015) · Cell · doi:10.1016/j.cell.2015.01.042 · Cited by 378 · see citing works

p73 Induces apoptosis via PUMA transactivation and Bax mitochondrial translocation

Melino, G., Bernassola, F., Ranalli, M., Yee, K., Zong, W. X., Corazzari, M., Knight, R. A., Green, D. R., Thompson, C., & Vousden, K. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m307469200 · Cited by 368 · see citing works

Die another way – non-apoptotic mechanisms of cell death

Tait, S. W. G., Ichim, G., & Green, D. R. (2014) · Journal of Cell Science · doi:10.1242/jcs.093575 · Cited by 366 · see citing works

Control of mitochondrial permeability by Bcl-2 family members

Sharpe, J. C., Arnoult, D., & Youle, R. J. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2003.10.016 · Cited by 367 · see citing works

Bak regulates mitochondrial morphology and pathology during apoptosis by interacting with mitofusins

Brooks, C., Wei, Q., Feng, L., Dong, G., Tao, Y., Mei, L., Xie, Z.-J., & Dong, Z. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0703976104 · Cited by 351 · see citing works

Mitochondria—Judges and Executioners of Cell Death Sentences

Bhola, P. D., & Letai, A. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.02.019 · Cited by 326 · see citing works

Inactivation of prosurvival Bcl-2 proteins activates Bax/Bak through the outer mitochondrial membrane

O'Neill, K. L., Huang, K., Zhang, J., Chen, Y., & Luo, X. (2016) · Genes & Development · doi:10.1101/gad.276725.115 · Cited by 323 · see citing works

BH3-Triggered Structural Reorganization Drives the Activation of Proapoptotic BAX

Gavathiotis, E., Reyna, D. E., Davis, M. L., Bird, G. H., & Walensky, L. D. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.019 · Cited by 310 · see citing works

Bax assembly into rings and arcs in apoptotic mitochondria is linked to membrane pores

Salvador‐Gallego, R., Mund, M., Cosentino, K., Schneider, J., Unsay, J., Schraermeyer, U., Engelhardt, J., Ries, J., & García‐Sáez, A. J. (2016) · The EMBO Journal · doi:10.15252/embj.201593384 · Cited by 296 · see citing works

Bax regulates primary necrosis through mitochondrial dynamics

Whelan, R. S., Konstantinidis, K., Wei, A.-C., Chen, Y., Reyna, D. E., Jha, S., Yang, Y., Calvert, J. W., Lindsten, T., Thompson, C. B., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1201608109 · Cited by 290 · see citing works

Bax and Bak function as the outer membrane component of the mitochondrial permeability pore in regulating necrotic cell death in mice

Karch, J., Kwong, J. Q., Burr, A. R., Sargent, M. A., Elrod, J. W., Peixoto, P. M., Martinez-Caballero, S., Osinska, H., Cheng, E. H.-Y., Robbins, J., et al. (2013) · eLife · doi:10.7554/elife.00772 · Cited by 290 · see citing works

BCL-2 family: integrating stress responses at the ER to control cell demise

Pihán, P., Carreras-Sureda, A., & Hetz, C. (2017) · Cell Death & Differentiation · doi:10.1038/cdd.2017.82 · Cited by 274 · see citing works

Cellular ATP demand creates metabolically distinct subpopulations of mitochondria

Ryu, K. W., Fung, T. S., Baker, D. C., Saoi, M., Park, J., Febres-Aldana, C. A., Aly, R. G., Cui, R., Sharma, A., Fu, Y., et al. (2024) · Nature · doi:10.1038/s41586-024-08146-w · Cited by 284 · see citing works

Bnip3 impairs mitochondrial bioenergetics and stimulates mitochondrial turnover

Rikka, S., Quinsay, M. N., Thomas, R. L., Kubli, D. A., Zhang, X., Murphy, A. N., & Gustafsson, Å. B. (2011) · Cell Death & Differentiation · doi:10.1038/cdd.2010.146 · Cited by 277 · see citing works

BOK Is a Non-canonical BCL-2 Family Effector of Apoptosis Regulated by ER-Associated Degradation

Llambi, F., Wang, Y.-M., Victor, B., Yang, M., Schneider, D. M., Gingras, S., Parsons, M. J., Zheng, J. H., Brown, S. A., Pelletier, S., et al. (2016) · Cell · doi:10.1016/j.cell.2016.02.026 · Cited by 261 · see citing works

A Mechanism of Virulence: Virulent <i>Mycobacterium tuberculosis</i> Strain H37Rv, but Not Attenuated H37Ra, Causes Significant Mitochondrial Inner Membrane Disruption in Macrophages Leading to Necrosis

Chen, M., Gan, H., & Remold, H. G. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.6.3707 · Cited by 255 · see citing works

An interconnected hierarchical model of cell death regulation by the BCL-2 family

Chen, H.-C., Kanai, M., Inoue-Yamauchi, A., Tu, H.-C., Huang, Y., Ren, D., Kim, H., Takeda, S., Reyna, D. E., Chan, P. M., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3236 · Cited by 249 · see citing works

Bax Exists in a Dynamic Equilibrium between the Cytosol and Mitochondria to Control Apoptotic Priming

Schellenberg, B., Wang, P., Keeble, J. A., Rodriguez-Enriquez, R., Walker, S., Owens, T. W., Foster, F., Tanianis-Hughes, J., Brennan, K., Streuli, C. H., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2012.12.022 · Cited by 237 · see citing works

Extracellular Regulated Kinase Phosphorylates Mitofusin 1 to Control Mitochondrial Morphology and Apoptosis

Pyakurel, A., Savoia, C., Hess, D., & Scorrano, L. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.02.021 · Cited by 244 · see citing works

Conserved principles of mammalian transcriptional regulation revealed by RNA half-life

Friedel, C. C., Dölken, L., Ruzsics, Z., Koszinowski, U. H., & Zimmer, R. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp542 · Cited by 230 · see citing works

A Role for Proapoptotic BID in the DNA-Damage Response

Zinkel, S. S., Hurov, K. E., Ong, C., Abtahi, F. M., Gross, A., & Korsmeyer, S. J. (2005) · Cell · doi:10.1016/j.cell.2005.06.022 · Cited by 239 · see citing works

Gliotoxin Is a Virulence Factor of <i>Aspergillus fumigatus</i> : <i>gliP</i> Deletion Attenuates Virulence in Mice Immunosuppressed with Hydrocortisone

Sugui, J. A., Pardo, J., Chang, Y. C., Zarember, K. A., Nardone, G., Galvez, E. M., Müllbacher, A., Gallin, J. I., Simon, M. M., & Kwon-Chung, K. J. (2007) · Eukaryotic Cell · doi:10.1128/ec.00141-07 · Cited by 242 · see citing works

Structural Model of Active Bax at the Membrane

Bleicken, S., Jeschke, G., Stegmueller, C., Salvador-Gallego, R., García-Sáez, A. J., & Bordignon, E. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.09.022 · Cited by 227 · see citing works

MTCH2/MIMP is a major facilitator of tBID recruitment to mitochondria

Zaltsman, Y., Shachnai, L., Yivgi-Ohana, N., Schwarz, M., Maryanovich, M., Houtkooper, R. H., Vaz, F. M., De Leonardis, F., Fiermonte, G., Palmieri, F., et al. (2010) · Nature Cell Biology · doi:10.1038/ncb2057 · Cited by 218 · see citing works

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

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

Activation of mitochondrial protease OMA1 by Bax and Bak promotes cytochrome c release during apoptosis

Jiang, X., Jiang, H., Shen, Z., & Wang, X. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1417253111 · Cited by 220 · see citing works

Mitochondrial Shape Governs BAX-Induced Membrane Permeabilization and Apoptosis

Renault, T. T., Floros, K. V., Elkholi, R., Corrigan, K.-A., Kushnareva, Y., Wieder, S. Y., Lindtner, C., Serasinghe, M. N., Asciolla, J. J., Buettner, C., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2014.10.028 · Cited by 217 · see citing works

Mcl-1, Bcl-XL and Stat3 expression are associated with progression of melanoma whereas Bcl-2, AP-2 and MITF levels decrease during progression of melanoma

Zhuang, L., Lee, C. S., Scolyer, R. A., McCarthy, S. W., Zhang, X. D., Thompson, J. F., & Hersey, P. (2007) · Modern Pathology · doi:10.1038/modpathol.3800750 · Cited by 202 · see citing works

VDAC2 enables BAX to mediate apoptosis and limit tumor development

Chin, H. S., Li, M. X., Tan, I. K. L., Ninnis, R. L., Reljic, B., Scicluna, K., Dagley, L. F., Sandow, J. J., Kelly, G. L., Samson, A. L., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-07309-4 · Cited by 196 · see citing works

Autophagy within the antigen donor cell facilitates efficient antigen cross-priming of virus-specific CD8+ T cells

Uhl, M., Kepp, O., Jusforgues-Saklani, H., Vicencio, J.-M., Kroemer, G., & Albert, M. L. (2009) · Cell Death &amp; Differentiation · doi:10.1038/cdd.2009.8 · Cited by 196 · see citing works

Bax dimerizes via a symmetric BH3:groove interface during apoptosis

Dewson, G., Ma, S., Frederick, P., Hockings, C., Tan, I., Kratina, T., & Kluck, R. M. (2012) · Cell Death &amp; Differentiation · doi:10.1038/cdd.2011.138 · Cited by 189 · see citing works

Differential retrotranslocation of mitochondrial Bax and Bak

Todt, F., Cakir, Z., Reichenbach, F., Emschermann, F., Lauterwasser, J., Kaiser, A., Ichim, G., Tait, S. W., Frank, S., Langer, H. F., et al. (2015) · The EMBO Journal · doi:10.15252/embj.201488806 · Cited by 172 · see citing works

Bax channel inhibitors prevent mitochondrion-mediated apoptosis and protect neurons in a model of global brain ischemia

Hetz, C., Vitte, P.-A., Bombrun, A., Rostovtseva, T. K., Montessuit, S., Hiver, A., Schwarz, M. K., Church, D. J., Korsmeyer, S. J., Martinou, J.-C., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505843200 · Cited by 176 · see citing works

BAX unleashed: the biochemical transformation of an inactive cytosolic monomer into a toxic mitochondrial pore

Walensky, L. D., & Gavathiotis, E. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.08.009 · Cited by 173 · see citing works

Bak Core and Latch Domains Separate during Activation, and Freed Core Domains Form Symmetric Homodimers

Brouwer, J. M., Westphal, D., Dewson, G., Robin, A. Y., Uren, R. T., Bartolo, R., Thompson, G. V., Colman, P. M., Kluck, R. M., & Czabotar, P. E. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.07.016 · Cited by 161 · see citing works

Autophagy promotes necrosis in apoptosis-deficient cells in response to ER stress

Ullman, E., Fan, Y., Stawowczyk, M., Chen, H.-M., Yue, Z., & Zong, W.-X. (2008) · Cell Death &amp; Differentiation · doi:10.1038/sj.cdd.4402234 · Cited by 161 · see citing works

Transient binding of an activator BH3 domain to the Bak BH3-binding groove initiates Bak oligomerization

Dai, H., Smith, A., Meng, X. W., Schneider, P. A., Pang, Y.-P., & Kaufmann, S. H. (2011) · Journal of Cell Biology · doi:10.1083/jcb.201102027 · Cited by 159 · see citing works

TERT promotes cellular and organismal survival independently of telomerase activity

Lee, J., Sung, Y. H., Cheong, C., Choi, Y. S., Jeon, H. K., Sun, W., Hahn, W. C., Ishikawa, F., & Lee, H.-W. (2008) · Oncogene · doi:10.1038/sj.onc.1211037 · Cited by 145 · see citing works

Bax targets mitochondria by distinct mechanisms before or during apoptotic cell death: a requirement for VDAC2 or Bak for efficient Bax apoptotic function

Ma, S. B., Nguyen, T. N., Tan, I., Ninnis, R., Iyer, S., Stroud, D. A., Menard, M., Kluck, R. M., Ryan, M. T., & Dewson, G. (2014) · Cell Death &amp; Differentiation · doi:10.1038/cdd.2014.119 · Cited by 138 · see citing works

Intracellular localization of the BCL-2 family member BOK and functional implications

Echeverry, N., Bachmann, D., Ke, F., Strasser, A., Simon, H. U., & Kaufmann, T. (2013) · Cell Death &amp; Differentiation · doi:10.1038/cdd.2013.10 · Cited by 137 · see citing works

Cleavage by Caspase 8 and Mitochondrial Membrane Association Activate the BH3-only Protein Bid during TRAIL-induced Apoptosis

Huang, K., Zhang, J., O’Neill, K. L., Gurumurthy, C. B., Quadros, R. M., Tu, Y., & Luo, X. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.711051 · Cited by 136 · see citing works

VDAC regulation by the Bcl-2 family of proteins

Tsujimoto, Y., & Shimizu, S. (2000) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400780 · Cited by 338 · see citing works

Apoptosis induced by direct triggering of mitochondrial apoptosis proceeds in the near-absence of some apoptotic markers

Ying, S., & Häcker, G. A. (2007) · APOPTOSIS · doi:10.1007/s10495-007-0117-1 · Cited by 19 · see citing works

The Role of Mitochondria in Apoptosis

Tang, Z. (2006) · Progress in Veterinary Medicine · Cited by 1 · see citing works

Mitochondria-dependent apoptosis and cellular pH regulation

Matsuyama, S., & Reed, J. C. (2000) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400779 · Cited by 341 · see citing works

Mitochondria and apoptosis regulation

Yu-shan, Z. (2008) · Shengming kexue