Mechanisms of Action of Bcl-2 Family Proteins

Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programed cell death

Oltval, Z. N., Milliman, C. L., & Korsmeyer, S. J. (1993) · Cell · doi:10.1016/0092-8674(93)90509-o · Cited by 6,003 · 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

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 · 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

PUMA, a Novel Proapoptotic Gene, Is Induced by p53

Nakano, K., & Vousden, K. H. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00214-3 · Cited by 2,315 · 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

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

Differential Targeting of Prosurvival Bcl-2 Proteins by Their BH3-Only Ligands Allows Complementary Apoptotic Function

Chen, L., Willis, S. N., Wei, A., Smith, B. J., Fletcher, J. I., Hinds, M. G., Colman, P. M., Day, C. L., Adams, J. M., & Huang, D. C. S. (2005) · Molecular Cell · doi:10.1016/j.molcel.2004.12.030 · Cited by 1,816 · see citing works

Movement of Bax from the Cytosol to Mitochondria during Apoptosis

Wolter, K. G., Hsu, Y., Smith, C. L., Nechushtan, A., Xi, X., & Youle, R. J. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.139.5.1281 · Cited by 1,809 · 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

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

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

Structure of Bcl-x _L -Bak Peptide Complex: Recognition Between Regulators of Apoptosis

Sattler, M., Liang, H., Nettesheim, D., Meadows, R. P., Harlan, J. E., Eberstadt, M., Yoon, H. S., Shuker, S. B., Chang, B. S., Minn, A. J., et al. (1997) · Science · doi:10.1126/science.275.5302.983 · Cited by 1,476 · see citing works

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 · see citing works

Mitochondria primed by death signals determine cellular addiction to antiapoptotic BCL-2 family members

Certo, M. V., Moore, V. D. G., Nishino, M., Wei, G., Korsmeyer, S. J., Armstrong, S. A., & Letai, A. G. (2006) · Cancer Cell · doi:10.1016/j.ccr.2006.03.027 · Cited by 1,290 · see citing works

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 · 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

Bim: a novel member of the Bcl‐2 family that promotes apoptosis

O’Connor, L., Strasser, A., O’Reilly, L. A., Hausmann, G., Adams, J. M., Cory, S., & Huang, D. C. S. (1998) · The EMBO Journal · doi:10.1093/emboj/17.2.384 · Cited by 1,163 · see citing works

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 · see citing works

Barrel-Stave Model or Toroidal Model? A Case Study on Melittin Pores

Yang, L., Harroun, T. A., Weiss, T. M., Ding, L., & Huang, H. W. (2001) · Biophysical Journal · doi:10.1016/s0006-3495(01)75802-x · Cited by 1,114 · see citing works

Structure of Bax

Suzuki, M., Youle, R. J., & Tjandra, N. (2000) · Cell · doi:10.1016/s0092-8674(00)00167-7 · Cited by 1,104 · see citing works

BID: a novel BH3 domain-only death agonist.Preprint

Wang, K., Yin, X., Chao, D. T., Milliman, C. L., & Korsmeyer, S. J. (1996) · Genes & Development · doi:10.1101/gad.10.22.2859 · Cited by 941 · 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

Mule/ARF-BP1, a BH3-Only E3 Ubiquitin Ligase, Catalyzes the Polyubiquitination of Mcl-1 and Regulates Apoptosis

Zhong, Q., Gao, W., Du, F., & Wang, X. (2005) · Cell · doi:10.1016/j.cell.2005.06.009 · Cited by 844 · see citing works

Induction of apoptosis by the Bcl-2 homologue Bak

Chittenden, T., Harrington, E. A., O’Connor, R., Remington, C., Lutz, R. J., Evan, G. I., & Guild, B. C. (1995) · Nature · doi:10.1038/374733a0 · Cited by 732 · see citing works

Conformation of the Bax C‐terminus regulates subcellular location and cell death

Nechushtan, A., Smith, C. L., Hsu, Y., & Youle, R. J. (1999) · The EMBO Journal · doi:10.1093/emboj/18.9.2330 · Cited by 732 · 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

Multiple Functions of BCL-2 Family ProteinsPreprint

Hardwick, J. M., & Soane, L. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008722 · Cited by 670 · see citing works

Bmf: A Proapoptotic BH3-Only Protein Regulated by Interaction with the Myosin V Actin Motor Complex, Activated by Anoikis

Puthalakath, H., Villunger, A., O'Reilly, L. A., Beaumont, J. G., Coultas, L., Cheney, R. E., Huang, D. C. S., & Strasser, A. (2001) · Science · doi:10.1126/science.1062257 · Cited by 656 · see citing works

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

Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival

Schwickart, M., Huang, X., Lill, J. R., Liu, J., Ferrando, R., French, D. M., Maecker, H., O’Rourke, K., Bazan, F., Eastham-Anderson, J., et al. (2010) · Nature · doi:10.1038/nature08646 · Cited by 628 · see citing works

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

Bcl-2-family proteins and the role of mitochondria in apoptosis

Kuwana, T., & Newmeyer, D. D. (2003) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2003.10.004 · 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

A Unified Model of Mammalian BCL-2 Protein Family Interactions at the Mitochondria

Llambi, F., Moldoveanu, T., Tait, S. W. G., Bouchier-Hayes, L., Temirov, J., McCormick, L. L., Dillon, C. P., & Green, D. R. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.10.001 · Cited by 596 · see citing works

Nonionic Detergents Induce Dimerization among Members of the Bcl-2 Family

Hsu, Y., & Youle, R. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.21.13829 · Cited by 591 · see citing works

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 565 · see citing works

Role of the mitochondrial membrane permeability transition in cell death

Tsujimoto, Y., & Shimizu, S. (2006) · APOPTOSIS · doi:10.1007/s10495-006-0525-7 · Cited by 559 · see citing works

Modulation of apoptosis by the widely distributed Bcl-2 homologue Bak

Kiefer, M. C., Brauer, M. J., Powers, V. C., Wu, J. J., Umansky, S. R., Tomei, L., & Barr, P. J. (1995) · Nature · doi:10.1038/374736a0 · Cited by 505 · see citing works

Cloning of a bcl-2 homologue by interaction with adenovirus E1B 19K

Farrow, S. N., White, J. H. M., Martinou, I., Raven, T., Pun, K., Grinham, C. J., Martinou, J., & Brown, R. (1995) · Nature · doi:10.1038/374731a0 · Cited by 494 · see citing works

Solution Structure of BID, an Intracellular Amplifier of Apoptotic Signaling

Chou, J. J., Li, H., Salvesen, G. S., Yuan, J., & Wagner, G. (1999) · Cell · doi:10.1016/s0092-8674(00)80572-3 · Cited by 488 · see citing works

Cell Damage-induced Conformational Changes of the Pro-Apoptotic Protein Bak In Vivo Precede the Onset of Apoptosis

Griffiths, G. J., Dubrez, L., Morgan, C. P., Jones, N. A., Whitehouse, J., Corfe, B. M., Dive, C., & Hickman, J. A. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.144.5.903 · Cited by 479 · see citing works

Cardiolipin provides specificity for targeting of tBid to mitochondria

Lutter, M. L., Fang, M., Luo, X., Nishijima, M., Xie, X., & Wang, X. (2000) · Nature Cell Biology · doi:10.1038/35036395 · Cited by 472 · see citing works

Structural insights into the degradation of Mcl-1 induced by BH3 domains

Czabotar, P. E., Lee, E. F., van Delft, M. F., Day, C. L., Smith, B. J., Huang, D. C. S., Fairlie, W. D., Hinds, M. G., & Colman, P. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701297104 · Cited by 449 · see citing works

Membrane Remodeling Induced by the Dynamin-Related Protein Drp1 Stimulates Bax Oligomerization

Montessuit, S., Somasekharan, S. P., Terrones, O., Lucken‐Ardjomande, S., Herzig, S., Schwarzenbacher, R., Manstein, D. J., Bossy‐Wetzel, E., Basáñez, G., Meda, P., et al. (2010) · Cell · doi:10.1016/j.cell.2010.08.017 · Cited by 422 · see citing works

The MCL-1 BH3 helix is an exclusive MCL-1 inhibitor and apoptosis sensitizer

Stewart, M. L., Fire, E., Keating, A. E., & Walensky, L. D. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.391 · Cited by 418 · see citing works

Solution Structure of the Proapoptotic Molecule BID

McDonnell, J. M., Fushman, D., Milliman, C. L., Korsmeyer, S. J., & Cowburn, D. (1999) · Cell · doi:10.1016/s0092-8674(00)80573-5 · Cited by 396 · see citing works

Targeting of Bcl-2 to the mitochondrial outer membrane by a COOH-terminal signal anchor sequence.

Nguyen, M., Millar, D. G., Yong, V. W., Korsmeyer, S. J., & Shore, G. C. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74386-5 · Cited by 393 · see citing works

harakiri, a novel regulator of cell death, encodes a protein that activates apoptosis and interacts selectively with survival‐promoting proteins Bcl‐2 and Bcl‐XL

Inohara, N., Ding, L., Chen, S., & Núñez, G. (1997) · The EMBO Journal · doi:10.1093/emboj/16.7.1686 · Cited by 392 · see citing works

Embedded together: The life and death consequences of interaction of the Bcl-2 family with membranes

Leber, B. F., Lin, J., & Andrews, D. W. (2007) · APOPTOSIS · doi:10.1007/s10495-007-0746-4 · Cited by 378 · see citing works

Bax forms multispanning monomers that oligomerize to permeabilize membranes during apoptosis

Annis, M. G., Soucie, E. L., Dlugosz, P. J., Cruz-Aguado, J. A., Penn, L. Z., Leber, B. F., & Andrews, D. W. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600675 · Cited by 377 · see citing works

The autophagy effector Beclin 1: a novel BH3-only protein

Sinha, S. C., & Levine, B. (2008) · Oncogene · doi:10.1038/onc.2009.51 · Cited by 376 · see citing works

BH3-only proteins: Orchestrators of apoptosis

Shamas‐Din, A., Brahmbhatt, H., Leber, B. F., & Andrews, D. W. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.11.024 · Cited by 368 · see citing works

The Structure of a Bcl-xL/Bim Fragment Complex

Liu, X., Dai, S., Zhu, Y., Marrack, P., & Kappler, J. W. (2003) · Immunity · doi:10.1016/s1074-7613(03)00234-6 · Cited by 358 · 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

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 · see citing works

Measuring and Modeling Apoptosis in Single Cells

Spencer, S. L., & Sorger, P. K. (2011) · Cell · doi:10.1016/j.cell.2011.03.002 · Cited by 333 · see citing works

Bcl-XL Inhibits Membrane Permeabilization by Competing with Bax

Billen, L. P., Kokoski, C., Lovell, J. F., Leber, B. F., & Andrews, D. W. (2008) · PLoS Biology · doi:10.1371/journal.pbio.0060147 · Cited by 317 · 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

BH3 Domain of BAD Is Required for Heterodimerization with BCL-XL and Pro-apoptotic Activity

Zha, J., Harada, H., Osipov, K. A., Jockel, J., Waksman, G., & Korsmeyer, S. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.39.24101 · Cited by 309 · see citing works

The BH4 domain of Bcl-2 inhibits ER calcium release and apoptosis by binding the regulatory and coupling domain of the IP3 receptor

Rong, Y.-P., Bultynck, G., Aromolaran, A. S., Zhong, F., Parys, J. B., SMEDT, H. D., Mignery, G. A., Roderick, H. L., Bootman, M. D., & Distelhorst, C. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907555106 · Cited by 306 · see citing works

Noxa: at the tip of the balance between life and death

Ploner, C., Kofler, R., & Villunger, A. (2008) · Oncogene · doi:10.1038/onc.2009.46 · Cited by 286 · see citing works

Bid: a Bax-like BH3 protein

Billen, L. P., Shamas‐Din, A., & Andrews, D. W. (2008) · Oncogene · doi:10.1038/onc.2009.47 · Cited by 278 · see citing works

A novel, high conductance channel of mitochondria linked to apoptosis in mammalian cells and Bax expression in yeast

Pavlov, E. V., Priault, M., Pietkiewicz, D., Cheng, E. H. Y., Antonsson, B. E., Manon, S., Korsmeyer, S. J., Mannella, C. A., & Kinnally, K. W. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200107057 · Cited by 273 · see citing works

Bcl‐2 changes conformation to inhibit Bax oligomerization

Dlugosz, P. J., Billen, L. P., Annis, M. G., Zhu, W., Zhang, Z., Lin, J., Leber, B. F., & Andrews, D. W. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601126 · Cited by 262 · see citing works

The First α Helix of Bax Plays a Necessary Role in Its Ligand-Induced Activation by the BH3-Only Proteins Bid and PUMA

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

BAD: undertaker by night, candyman by day

Danial, N. N. (2008) · Oncogene · doi:10.1038/onc.2009.44 · Cited by 252 · see citing works

Mechanism of apoptosis induction by inhibition of the anti-apoptotic BCL-2 proteins

Chipuk, J. E., Fisher, J. C., Dillon, C. P., Kriwacki, R. W., Kuwana, T., & Green, D. R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808036105 · Cited by 246 · see citing works

The Soluble Form of Bax Regulates Mitochondrial Fusion via MFN2 Homotypic Complexes

Hoppins, S. C., Edlich, F., Harwig, M. C., Banerjee, S., McCaffery, J. M., Youle, R. J., & Nunnari, J. M. (2011) · Molecular Cell · doi:10.1016/j.molcel.2010.11.030 · Cited by 243 · 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

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 · see citing works

Vaccinia virus anti-apoptotic F1L is a novel Bcl-2-like domain-swapped dimer that binds a highly selective subset of BH3-containing death ligands

Kvansakul, M., Yang, H. J., Fairlie, W. D., Czabotar, P. E., Fischer, S. F., Perugini, M. A., Huang, D. C. S., & Colman, P. M. (2008) · Cell Death and Differentiation · doi:10.1038/cdd.2008.83 · Cited by 235 · see citing works

Regulation of Bcl-xL: a little bit of this and a little bit of STAT

Grad, J. M., Zeng, X., & Boise, L. (2000) · Current Opinion in Oncology · doi:10.1097/00001622-200011000-00006 · Cited by 231 · see citing works

Structure of transmembrane pore induced by Bax-derived peptide: Evidence for lipidic pores

Qian, S., Wang, W., Yang, L., & Huang, H. W. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0807764105 · Cited by 227 · 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

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 · see citing works

The permeability transition pore complex in cancer cell death

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

BNIP3 subfamily BH3-only proteins: mitochondrial stress sensors in normal and pathological functions

Chinnadurai, G., Vijayalingam, S., & Gibson, S. B. (2008) · Oncogene · doi:10.1038/onc.2009.49 · Cited by 219 · 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

Oligomeric Bax Is a Component of the Putative Cytochrome c Release Channel MAC, Mitochondrial Apoptosis-induced Channel

Dejean, L. M., Martinez‐Caballero, S., Guo, L., Hughes, C., Teijido, Ó., Ducret, T., Ichas, F., Korsmeyer, S. J., Antonsson, B. E., Jonas, E. A., et al. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-12-1111 · Cited by 218 · see citing works

Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets

Hinds, M. G., Smits, C., Fredericks-Short, R., Risk, J. M., Bailey, M., Huang, D. C. S., & Day, C. L. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401934 · Cited by 217 · see citing works

Metabolic Regulation of Protein N-Alpha-Acetylation by Bcl-xL Promotes Cell Survival

Yi, C. H., Pan, H., Seebacher, J., Jang, I. H., Hyberts, S. G., Heffron, G. J., Heiden, M. G. V., Yang, R., Li, F., Locasale, J. W., et al. (2011) · Cell · doi:10.1016/j.cell.2011.06.050 · Cited by 204 · see citing works

Interaction with a Membrane Surface Triggers a Reversible Conformational Change in Bax Normally Associated with Induction of Apoptosis

Yethon, J. A., Epand, R. F., Leber, B. F., Epand, R. M., & Andrews, D. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306289200 · Cited by 203 · see citing works

Bcl‐xL regulates apoptosis by heterodimerization‐dependent and ‐independent mechanisms

Minn, A. J., Kettlun, C. S., Liang, H., Kelekar, A., Heiden, M. G. V., Chang, B. S., Fesik, S. W., Fill, M., & Thompson, C. B. (1999) · The EMBO Journal · doi:10.1093/emboj/18.3.632 · Cited by 195 · see citing works

Selective regulation of IP3-receptor-mediated Ca2+ signaling and apoptosis by the BH4 domain of Bcl-2 versus Bcl-Xl

Monaco, G., Decrock, E., Akl, H., Ponsaerts, R., Vervliet, T., Luyten, T., Maeyer, M. D., Missiaen, L., Distelhorst, C., SMEDT, H. D., et al. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.97 · Cited by 183 · see citing works

Autophagy and Neuronal Cell Death in Neurological DisordersPreprint

Nixon, R. A., & Yang, D.-S. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008839 · Cited by 179 · see citing works

Molecular Details of Bax Activation, Oligomerization, and Membrane Insertion

Bleicken, S., Classen, M., Padmavathi, P. V. L., Ishikawa, T., Zeth, K., Steinhoff, H., & Bordignon, E. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.081539 · Cited by 176 · see citing works

The structure of Bcl‐w reveals a role for the C‐terminal residues in modulating biological activity

Hinds, M. G., Lackmann, M., Skea, G. L., Harrison, P. J., Huang, D. C. S., & Day, C. L. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg144 · Cited by 175 · see citing works

Still embedded together binding to membranes regulates Bcl-2 protein interactions

Leber, B. F., Lin, J., & Andrews, D. W. (2010) · Oncogene · doi:10.1038/onc.2010.283 · Cited by 167 · see citing works

Autophagy and CancerPreprint

Mah, L. Y., & Ryan, K. M. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008821 · Cited by 167 · see citing works

Cytosolic factor‐ and TOM‐independent import of C‐tail‐anchored mitochondrial outer membrane proteins

Setoguchi, K., Otera, H., & Mihara, K. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601438 · Cited by 163 · see citing works

Bcl‐xL sequesters its C‐terminal membrane anchor in soluble, cytosolic homodimers

Jeong, S., Gaume, B. R., Lee, Y.-J., Hsu, Y., Ryu, S., Yoon, S., & Youle, R. J. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600225 · Cited by 162 · see citing works

Human Embryonic Stem Cells Have Constitutively Active Bax at the Golgi and Are Primed to Undergo Rapid Apoptosis

Dumitru, R., Gama, V., Fagan, B. M., Bower, J. J., Swahari, V., Pevny, L., & Deshmukh, M. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.04.002 · Cited by 157 · see citing works

BH-3-only BIK Functions at the Endoplasmic Reticulum to Stimulate Cytochrome c Release from Mitochondria

Germain, M., Mathai, J. P., & Shore, G. C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201235200 · Cited by 153 · see citing works

Bax activation by the BH3-only protein Puma promotes cell dependence on antiapoptotic Bcl-2 family members

Gallenne, T., Gautier, F., Oliver, L., Hervouet, É., Noël, B., Hickman, J. A., Geneste, O., Cartron, P., Vallette, F. M., Manon, S., et al. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200809153 · Cited by 147 · see citing works

The Molecular Mechanism of Noxa-induced Mitochondrial Dysfunction in p53-Mediated Cell Death

Seo, Y.-W., Shin, J. N., Ko, K. H., Cha, J. H., Park, J. Y., Lee, B. R., Yun, C., Kim, Y., Seol, D., Kim, D., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308785200 · Cited by 139 · see citing works

Bax activation and stress-induced apoptosis delayed by the accumulation of cholesterol in mitochondrial membranes

Lucken‐Ardjomande, S., Montessuit, S., & Martinou, J. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402280 · Cited by 134 · see citing works

Membrane promotes tBID interaction with BCLXL

García‐Sáez, A. J., Ries, J., Orzáez, M., Pérez‐Payá, E., & Schwille, P. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1671 · Cited by 132 · see citing works

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 132 · see citing works

Phylogenomics of Life-Or-Death Switches in Multicellular Animals: Bcl-2, BH3-Only, and BNip Families of Apoptotic Regulators

Aouacheria, A., Brunet, F., & Gouy, M. (2005) · Molecular Biology and Evolution · doi:10.1093/molbev/msi234 · Cited by 125 · see citing works

Assembly of Bcl-2 into microsomal and outer mitochondrial membranes

Janiak, F., Leber, B. F., & Andrews, D. W. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36960-0 · Cited by 123 · see citing works

Non-apoptotic role of BID in inflammation and innate immunity

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

Proapoptotic BH3-only proteins trigger membrane integration of prosurvival Bcl-w and neutralize its activity

Wilson-Annan, J., O’Reilly, L. A., Crawford, S., Hausmann, G., Beaumont, J. G., Parma, L. P., Chen, L., Lackmann, M., Lithgow, T. J., Hinds, M. G., et al. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200302144 · Cited by 118 · see citing works

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 118 · see citing works

Bcl-XL is qualitatively different from and ten times more effective than Bcl-2 when expressed in a breast cancer cell line

Fiebig‐Comyn, A., Zhu, W., Hollerbach, C., Leber, B. F., & Andrews, D. W. (2006) · BMC Cancer · doi:10.1186/1471-2407-6-213 · Cited by 111 · see citing works

Regulation of Bcl-2 Family Proteins by Posttranslational Modifications

Letai, A. G., & Kütük, Ö. (2008) · Current Molecular Medicine · doi:10.2174/156652408783769599 · Cited by 108 · see citing works

During Apoptosis Bcl-2 Changes Membrane Topology at Both the Endoplasmic Reticulum and Mitochondria

Kim, P. K., Annis, M. G., Dlugosz, P. J., et al. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00263-1 · Cited by 104 · see citing works

Differences in the Mechanisms of Proapoptotic BH3 Proteins Binding to Bcl-XL and Bcl-2 Quantified in Live MCF-7 Cells

Aranovich, A., Liu, Q., Collins, T., Geng, F., Dixit, S., Leber, B. F., & Andrews, D. W. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.01.030 · Cited by 103 · see citing works

Mcl‐1–Bim complexes accommodate surprising point mutations via minor structural changes

Fire, E., Gullà, S. V., Grant, R. A., et al. (2010) · Protein Science · doi:10.1002/pro.329 · Cited by 102 · see citing works

Conformational Changes in BAK, a Pore-forming Proapoptotic Bcl-2 Family Member, upon Membrane Insertion and Direct Evidence for the Existence of BH3-BH3 Contact Interface in BAK Homo-oligomers

Oh, K. J., Singh, P., Lee, K., Foss, K., Lee, S., Park, M., Lee, S., Aluvila, S., Park, M., Singh, P., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.135293 · Cited by 87 · see citing works

Conformational Changes in Bcl-2 Pro-survival Proteins Determine Their Capacity to Bind Ligands

Lee, E. F., Czabotar, P. E., Yang, H. J., Sleebs, B. E., Lessène, G., Colman, P. M., Smith, B. J., & Fairlie, W. D. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.040725 · Cited by 87 · see citing works

Post-transcriptional and post-translational regulation of Bcl2

Willimott, S., & Wagner, S. D. (2010) · Biochemical Society Transactions · doi:10.1042/bst0381571 · Cited by 86 · see citing works

BimS-induced apoptosis requires mitochondrial localization but not interaction with anti-apoptotic Bcl-2 proteins

Weber, A., Paschen, S. A., Heger, K., Wilfling, F., Frankenberg, T., Bauerschmitt, H., Seiffert, B. M., Kirschnek, S., Wagner, H., & Häcker, G. A. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200610148 · Cited by 86 · see citing works

Bfl-1/A1 functions, similar to Mcl-1, as a selective tBid and Bak antagonist

Simmons, M. J., Fan, G., Zong, W.-X., Degenhardt, K., White, E., & Gélinas, C. (2007) · Oncogene · doi:10.1038/sj.onc.1210771 · Cited by 79 · see citing works

Bax Forms an Oligomer via Separate, Yet Interdependent, Surfaces

Zhang, Z., Zhu, W., Lapolla, S. M., Miao, Y., Shao, Y., Falcone, M., Boreham, D., McFarlane, N. M., Ding, J., Johnson, A. E., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.113456 · Cited by 77 · see citing works

Puma indirectly activates Bax to cause apoptosis in the absence of Bid or Bim

Jabbour, A. M., Heraud-Farlow, J. E., Daunt, C. P., Kaufmann, T., Sandow, J., O’Reilly, L. A., Callus, B. A., Lopez, A. F., Strasser, A., Vaux, D. L., et al. (2008) · Cell Death and Differentiation · doi:10.1038/cdd.2008.179 · Cited by 76 · see citing works

Mitochondrial carriers and pores: Key regulators of the mitochondrial apoptotic program?

Schwarz, M., Andrade-Navarro, M. A., & Gross, A. (2007) · APOPTOSIS · doi:10.1007/s10495-007-0748-2 · Cited by 69 · see citing works

Reconstitution of Proapoptotic BAK Function in Liposomes Reveals a Dual Role for Mitochondrial Lipids in the BAK-driven Membrane Permeabilization Process

Landeta, O., Landajuela, A., Gil‐Carton, D., Taneva, S. G., Primo, C. D., Sot, B., Valle, M., Frolov, V. A., & Basáñez, G. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.165852 · Cited by 68 · see citing works

Reversible Membrane Interaction of BAD Requires two C-terminal Lipid Binding Domains in Conjunction with 14-3-3 Protein Binding

Hekman, M., Albert, S., Galmiche, A., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600292200 · Cited by 67 · see citing works

Pivotal role of Harakiri in the induction and prevention of gentamicin-induced hearing loss

Kalinec, G. M., Fernández-Zapico, M. E., Urrutia, R. A., Esteban-Cruciani, N., Chen, S., & Kalinec, F. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508053102 · Cited by 66 · see citing works

Elucidation of some Bax conformational changes through crystallization of an antibody–peptide complex

Peyerl, F. W., Dai, S., Murphy, G. A., Crawford, F., White, J., Marrack, P., & Kappler, J. W. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402025 · Cited by 65 · see citing works

An Internal EELD Domain Facilitates Mitochondrial Targeting of Mcl-1 via a Tom70-dependent Pathway

Chou, C.-H., Lee, R.-S., & Yang‐Yen, H. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-04-0319 · Cited by 44 · see citing works

The Super Anti-apoptotic Factor Bcl-xFNK Constructed by Disturbing Intramolecular Polar Interactions in Rat Bcl-xL

Asoh, S., Ohtsu, T., & Ohta, S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005841200 · Cited by 41 · see citing works

C-terminal Residues Regulate Localization and Function of the Antiapoptotic Protein Bfl-1

Brien, G., Mathieu, A., Robert, X., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.040824 · Cited by 36 · see citing works

Helix 6 of tBid is necessary but not sufficient for mitochondrial binding activity

Hu, X., Han, Z., Wyche, J. H., et al. (2003) · APOPTOSIS · doi:10.1023/a:1023676906857 · Cited by 26 · see citing works

The Bax carboxy-terminal hydrophobic helix does not determine organelle-specific targeting but is essential for maintaining Bax in an inactive state and for stable mitochondrial membrane insertion

Brock, S. E., Li, C., & Wattenberg, B. W. (2009) · APOPTOSIS · doi:10.1007/s10495-009-0410-2 · Cited by 15 · see citing works

Bax activation by the BH3-only protein Puma promotes cell dependence on antiapoptotic Bcl-2 family members

Gallenne, T., Gautier, F., Oliver, L., et al. (2009) · The Journal of Experimental Medicine · doi:10.1084/jem2065oia8 · Cited by 8 · see citing works

Reconstitution of Proapoptotic Bak Function in Liposomes Reveals a Dual Role for Mitochondrial Lipids in the Bak-Driven Membrane Permeabilization Process

Landeta, O., Landajuela, A., Bustillo, I., et al. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2010.12.299 · Cited by 4 · see citing works

Structure assembly of Bcl-xL through α5–α5 and α6–α6 interhelix interactions in lipid membranes

Feng, Y., Liu, D., Shen, X., et al. (2009) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2009.09.006 · Cited by 3 · 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

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

BCL-2 family proteins: changing partners in the dance towards death

Kale, J., Osterlund, E. J., & Andrews, D. W. (2018) · Cell Death & Differentiation · doi:10.1038/cdd.2017.186 · Cited by 1,574 · see citing works

P53 in survival, death and metabolic health: a lifeguard with a licence to kill.

Kruiswijk, F., Labuschagne, C. F., & Vousden, K. H. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm4007 · Cited by 1,080 · 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

Many players in BCL-2 family affairs

Moldoveanu, T., Follis, A. V., Kriwacki, R. W., & Green, D. R. (2014) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2013.12.006 · Cited by 421 · 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

An Autoinhibited Dimeric Form of BAX Regulates the BAX Activation Pathway

Garner, T. P., Reyna, D. E., Priyadarshi, A., Chen, H.-C., Li, S., Wu, Y., Ganesan, Y. T., Malashkevich, V. N., Cheng, E. H., & Gavathiotis, E. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.06.010 · Cited by 108 · see citing works

Mutant p53 drives cancer chemotherapy resistance due to loss of function on activating transcription of PUMA

Huang, Y., Liu, N., Liu, J., Liu, Y., Zhang, C., Long, S., Luo, G., Zhang, L., & Zhang, Y. (2019) · Cell Cycle · doi:10.1080/15384101.2019.1688951 · Cited by 94 · see citing works

Bok is a genuine multi-BH-domain protein that triggers apoptosis in the absence of Bax and Bak

Einsele-Scholz, S., Malmsheimer, S., Bertram, K., Stehle, D., Johänning, J., Manz, M., Daniel, P. T., Gillissen, B. F., Schulze-Osthoff, K., & Essmann, F. (2016) · Journal of Cell Science · doi:10.1242/jcs.181727 · Cited by 65 · see citing works

Regulation of apoptosis by an intrinsically disordered region of Bcl-xL

Follis, A. V., Llambi, F., Kalkavan, H., Yao, Y., Phillips, A. H., Park, C.-G., Marassi, F. M., Green, D. R., & Kriwacki, R. W. (2018) · Nature Chemical Biology · doi:10.1038/s41589-018-0011-x · Cited by 47 · see citing works

Combined inhibition of KRASG12C and mTORC1 kinase is synergistic in non-small cell lung cancer

Kitai, H., Choi, P. H., Yang, Y. C., Boyer, J. A., Whaley, A., Pancholi, P., Thant, C., Reiter, J., Chen, K., Markov, V., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-50063-z · Cited by 41 · see citing works

Roles of HIF1α- and HIF2α-regulated BNIP3 in hypoxia-induced injury of neurons

Zhu, L., Qi, B., & Hou, D. (2019) · Pathology - Research and Practice · doi:10.1016/j.prp.2019.01.022 · Cited by 20 · see citing works

Postnatal developmental regulation of Bcl‐2 family proteins in brain mitochondria

Soane, L., Siegel, Z. T. G., Schuh, R. A., & Fiskum, G. M. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21584 · Cited by 36 · see citing works

BCL-2 family proteins as regulators of mitochondria metabolism

Gross, A. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.01.017 · Cited by 128 · see citing works

Describing BCL- Family

Mishra, C. K., & Lomte, R. (2013)

BCL-2 family proteins: changing partners in the dance towards death

Kale, J., Osterlund, E. J., & Andrews, D. W. (2018) · Cell Death & Differentiation · doi:10.1038/cdd.2017.186 · Cited by 1,574 · see citing works

[Progress in small-molecule inhibitors of Bcl-2 family proteins].

Tang, Y. H., Zhang, D., & Wu, X. (2008) · PubMed