The Incomplete Puzzle of the BCL2 Proteins

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

Youle, R. J., & Strasser, A. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2308 · Cited by 4,704 · see citing works

Bcl-2 Antiapoptotic Proteins Inhibit Beclin 1-Dependent Autophagy

Pattingre, S., Tassa, A., Qu, X., Garuti, R., Liang, X. H., Mizushima, N., Packer, M., Schneider, M. D., & Levine, B. (2005) · Cell · doi:10.1016/j.cell.2005.07.002 · Cited by 3,536 · see citing works

ABT-199, a potent and selective BCL-2 inhibitor, achieves antitumor activity while sparing platelets

Souers, A. J., Leverson, J. D., Boghaert, E. R., Ackler, S. L., Catron, N. D., Chen, J., Dayton, B. D., Ding, H., Enschede, S. H., Fairbrother, W. J., et al. (2013) · Nature Medicine · doi:10.1038/nm.3048 · Cited by 3,058 · see citing works

ER Tubules Mark Sites of Mitochondrial Division

Friedman, J. R., Lackner, L. L., West, M., DiBenedetto, J. R., Nunnari, J., & Voeltz, G. K. (2011) · Science · doi:10.1126/science.1207385 · Cited by 2,072 · see citing works

Targeting BCL2 with Venetoclax in Relapsed Chronic Lymphocytic Leukemia

Roberts, A. W., Davids, M. S., Pagel, J. M., Kahl, B. S., Puvvada, S. D., Gerecitano, J. F., Kipps, T. J., Anderson, M. A., Brown, J. R., Gressick, L. A., et al. (2015) · New England Journal of Medicine · doi:10.1056/nejmoa1513257 · Cited by 1,901 · see citing works

Venetoclax combined with decitabine or azacitidine in treatment-naive, elderly patients with acute myeloid leukemia

DiNardo, C. D., Pratz, K., Pullarkat, V., Jonas, B. A., Arellano, M., Becker, P. S., Frankfurt, O., Konopleva, M., Wei, A. H., Kantarjian, H. M., et al. (2019) · Blood · doi:10.1182/blood-2018-08-868752 · Cited by 1,825 · 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

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

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

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

Cytochrome c acts as a cardiolipin oxygenase required for release of proapoptotic factors

Kagan, V. E., Tyurin, V. A., Jiang, J., Tyurina, Y. Y., Ritov, V. B., Amoscato, A. A., Osipov, A. N., Belikova, N. A., Kapralov, A. A., Kini, V., et al. (2005) · Nature Chemical Biology · doi:10.1038/nchembio727 · Cited by 1,256 · see citing works

Apoptosis Initiated When BH3 Ligands Engage Multiple Bcl-2 Homologs, Not Bax or Bak

Willis, S. N., Fletcher, J. I., Kaufmann, T., van Delft, M. F., Chen, L., Czabotar, P. E., Ierino, H., Lee, E. F., Fairlie, W. D., Bouillet, P., et al. (2007) · Science · doi:10.1126/science.1133289 · Cited by 1,125 · see citing works

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 · 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

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

BAK/BAX macropores facilitate mitochondrial herniation and mtDNA efflux during apoptosis

McArthur, K., Whitehead, L. W., Heddleston, J. M., Li, L., Padman, B. S., Oorschot, V., Geoghegan, N. D., Chappaz, S., Davidson, S., San Chin, H., et al. (2018) · Science · doi:10.1126/science.aao6047 · Cited by 1,072 · see citing works

The MCL1 inhibitor S63845 is tolerable and effective in diverse cancer models

Kotschy, A., Szlavik, Z., Murray, J., Davidson, J., Maragno, A. L., Le Toumelin-Braizat, G., Chanrion, M., Kelly, G. L., Gong, J.-N., Moujalled, D. M., et al. (2016) · Nature · doi:10.1038/nature19830 · Cited by 1,047 · see citing works

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 · see citing works

From basic apoptosis discoveries to advanced selective BCL-2 family inhibitors

Ashkenazi, A., Fairbrother, W. J., Leverson, J. D., & Souers, A. J. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.253 · Cited by 903 · 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

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 735 · 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

Conversion of Bcl-2 from Protector to Killer by Interaction with Nuclear Orphan Receptor Nur77/TR3

Lin, B., Kolluri, S. K., Lin, F., Liu, W., Han, Y.-H., Cao, X., Dawson, M. I., Reed, J. C., & Zhang, X.-K. (2004) · Cell · doi:10.1016/s0092-8674(04)00162-x · Cited by 672 · 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

MOMP, cell suicide as a BCL-2 family business

Kalkavan, H., & Green, D. R. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.179 · Cited by 667 · 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

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

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

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

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

The rise of mitochondria in medicine

Picard, M. A., Wallace, D. C., & Burelle, Y. (2016) · Mitochondrion · doi:10.1016/j.mito.2016.07.003 · Cited by 454 · 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

Acquired resistance to ABT-737 in lymphoma cells that up-regulate MCL-1 and BFL-1

Yecies, D. W., Carlson, N. E., Deng, J., & Letai, A. G. (2010) · Blood · doi:10.1182/blood-2009-07-233304 · Cited by 362 · see citing works

Mitochondrial fission requires DRP1 but not dynamins

Fonseca, T. B., Sánchez-Guerrero, Á., Milošević, I., & Raimundo, N. (2019) · Nature · doi:10.1038/s41586-019-1296-y · Cited by 355 · 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

Oxidative lipidomics of apoptosis: redox catalytic interactions of cytochrome c with cardiolipin and phosphatidylserine

Kagan, V. E., Borisenko, G. G., Tyurina, Y. Y., Tyurin, V. A., Jiang, J., Potapovich, A. I., Kini, V., Amoscato, A. A., & Fujii, Y. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.08.016 · Cited by 342 · 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 assembles into large ring‐like structures remodeling the mitochondrial outer membrane in apoptosis

Große, L., Wurm, C. A., Brüser, C., Neumann, D., Jans, D. C., & Jakobs, S. (2016) · The EMBO Journal · doi:10.15252/embj.201592789 · Cited by 281 · see citing works

Cardiolipin Domains in Bacillus subtilis Marburg Membranes

Kawai, F., Shoda, M., Harashima, R., Sadaie, Y., Hara, H., & Matsumoto, K. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.5.1475-1483.2004 · Cited by 274 · see citing works

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 270 · 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

The role of cardiolipin in the structural organization of mitochondrial membranes

Schlame, M., & Ren, M. (2009) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2009.04.019 · Cited by 248 · see citing works

Lipidic Pore Formation by the Concerted Action of Proapoptotic BAX and tBID

Terrones, O., Antonsson, B. E., Yamaguchi, H., Wang, H., Liu, J., Lee, R. M., Herrmann, A., & Basáñez, G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313420200 · Cited by 243 · 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

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 · 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

OPA1 disease alleles causing dominant optic atrophy have defects in cardiolipin-stimulated GTP hydrolysis and membrane tubulation

Ban, T., Heymann, J. A. W., Song, Z., Hinshaw, J. E., & Chan, D. C. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq088 · Cited by 222 · 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

BID-induced structural changes in BAK promote apoptosis

Moldoveanu, T., Grace, C. R., Llambi, F., Nourse, A., Fitzgerald, P., Gehring, K., Kriwacki, R. W., & Green, D. R. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2563 · Cited by 201 · see citing works

Non-apoptotic functions of BCL-2 family proteins

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

Apoptosis is triggered when prosurvival Bcl-2 proteins cannot restrain Bax

Fletcher, J. I., Meusburger, S., Hawkins, C. J., Riglar, D. T., Lee, E. F., Fairlie, W. D., Huang, D. C. S., & Adams, J. M. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808691105 · Cited by 193 · see citing works

Bax monomers form dimer units in the membrane that further self-assemble into multiple oligomeric species

Subburaj, Y., Cosentino, K., Axmann, M., Pedrueza-Villalmanzo, E., Hermann, E., Bleicken, S., Spatz, J., & García-Sáez, A. J. (2015) · Nature Communications · doi:10.1038/ncomms9042 · Cited by 181 · see citing works

Ups1p and Ups2p antagonistically regulate cardiolipin metabolism in mitochondria

Tamura, Y., Endo, T., Iijima, M., & Sesaki, H. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200812018 · Cited by 181 · 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

Ca2+-Induced Increased Lipid Packing and Domain Formation in Submitochondrial Particles. A Possible Early Step in the Mechanism of Ca2+-Stimulated Generation of Reactive Oxygen Species by the Respiratory Chain

Grijalba, M. T., Vercesi, A. E., & Schreier, S. (1999) · Biochemistry · doi:10.1021/bi9828674 · Cited by 168 · see citing works

Proapoptotic Bax and Bak Proteins Form Stable Protein-permeable Pores of Tunable Size

Bleicken, S., Landeta, O., Landajuela, A., Basáñez, G., & García‐Sáez, A. J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.512087 · Cited by 153 · see citing works

Cardiolipin Effects on Membrane Structure and Dynamics

Unsay, J. D., Cosentino, K., Subburaj, Y., & García‐Sáez, A. J. (2013) · Langmuir · doi:10.1021/la402669z · Cited by 151 · see citing works

Pro-apoptotic Cleavage Products of Bcl-xL Form Cytochrome c-conducting Pores in Pure Lipid Membranes

Basáñez, G., Zhang, J., Chau, B. N., Maksaev, G. I., Frolov, V. A., Brandt, T. A., BURCH, J. B., Hardwick, J. M., & Zimmerberg, J. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103879200 · Cited by 144 · see citing works

Post-Transcriptional Regulation of Anti-Apoptotic BCL2 Family Members

Cui, J., & Placzek, W. J. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19010308 · Cited by 135 · see citing works

Inhibition of Pro-Apoptotic BAX by a Noncanonical Interaction Mechanism

Barclay, L. A., Wales, T. E., Garner, T. P., Wachter, F., Lee, S., Guerra, R. M., Stewart, M. L., Braun, C. R., Bird, G. H., Gavathiotis, E., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.01.014 · Cited by 134 · see citing works

Membrane Fusion and the Lamellar-to-Inverted-Hexagonal Phase Transition in Cardiolipin Vesicle Systems Induced by Divalent Cations

Ortiz, A., Killian, J. A., Verkleij, A. J., & Wilschut, J. (1999) · Biophysical Journal · doi:10.1016/s0006-3495(99)77041-4 · Cited by 133 · 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

Membrane-Insertion Fragments of Bcl-xL, Bax, and Bid

García‐Sáez, A. J., Mingarro, I., Pérez‐Payá, E., & Salgado, J. (2004) · Biochemistry · doi:10.1021/bi036044c · Cited by 130 · see citing works

The C-terminal helix of Bcl-xL mediates Bax retrotranslocation from the mitochondria

Todt, F., Cakir, Z., Reichenbach, F., Youle, R. J., & Edlich, F. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.131 · Cited by 129 · see citing works

Apoptotic pore formation is associated with in-plane insertion of Bak or Bax central helices into the mitochondrial outer membrane

Westphal, D., Dewson, G., Menard, M. J., Frederick, P., Iyer, S., Bartolo, R. C., Gibson, L., Czabotar, P. E., Smith, B. J., Adams, J. M., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1415142111 · Cited by 121 · see citing works

Cardiolipin‐enriched raft‐like microdomains are essential activating platforms for apoptotic signals on mitochondria

Sorice, M., Manganelli, V., Matarrese, P., Tinari, A., Misasi, R., Malorni, W., & Garofalo, T. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.07.018 · Cited by 114 · see citing works

Viewing BCL2 and cell death control from an evolutionary perspective

Strasser, A., & Vaux, D. L. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.145 · Cited by 114 · 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

Bcl-2 family interaction with the mitochondrial morphogenesis machinery

Harwig, M. C., Norris, K. L., Karbowski, M., Wang, C., Suen, D., Jiao, S., George, N. M., Luo, X., Li, Z., & Youle, R. J. (2010) · Cell Death and Differentiation · doi:10.1038/cdd.2010.89 · Cited by 106 · see citing works

Bax transmembrane domain interacts with prosurvival Bcl-2 proteins in biological membranes

Andreu-Férnández, V., Sancho, M., Genovés, A., Lucendo, E., Todt, F., Lauterwasser, J., Funk, K., Jahreis, G., Pérez‐Payá, E., Mingarro, I., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1612322114 · Cited by 100 · see citing works

Phosphorylation switches Bax from promoting to inhibiting apoptosis thereby increasing drug resistance

Kale, J., Kütük, Ö., Brito, G. C., Andrews, T. S., Leber, B. F., Letai, A. G., & Andrews, D. W. (2018) · EMBO Reports · doi:10.15252/embr.201745235 · Cited by 100 · see citing works

The role of Bcl-2 family proteins in chronic lymphocytic leukaemia

Buggins, A. G. S., & Pepper, C. J. (2010) · Leukemia Research · doi:10.1016/j.leukres.2010.03.011 · Cited by 99 · see citing works

Distinct Domains Control the Addressing and the Insertion of Bax into Mitochondria

Cartron, P., Arokium, H., Oliver, L., Méflah, K., Manon, S., & Vallette, F. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409714200 · Cited by 95 · see citing works

Apoptosis-related BCL2-family members: Key players in chemotherapy.

Kontos, C., Christodoulou, M., & Scorilas, A. (2014) · Anti-Cancer Agents in Medicinal Chemistry · doi:10.2174/18715206113139990091 · Cited by 94 · see citing works

Acidic pH Promotes Dimerization of Bcl-2 Family Proteins

Xie, Z., Schendel, S. L., Matsuyama, S., & Reed, J. C. (1998) · Biochemistry · doi:10.1021/bi973052i · Cited by 87 · 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

Connecting mitochondrial dynamics and life-or-death events via Bcl-2 family proteins

Aouacheria, A., Baghdiguian, S., Lamb, H. M., Huska, J. D., Pineda, F. J., & Hardwick, J. M. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.04.009 · Cited by 81 · see citing works

BH3 profiling discriminates on-target small molecule BH3 mimetics from putative mimetics

Villalobos-Ortiz, M., Ryan, J. A., Mashaka, T., Opferman, J. T., & Letai, A. G. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0391-9 · Cited by 72 · see citing works

Quantitative interactome of a membrane Bcl-2 network identifies a hierarchy of complexes for apoptosis regulation

Bleicken, S., Hantusch, A., Das, K. K., Frickey, T., & Garcia-Saez, A. J. (2017) · Nature Communications · doi:10.1038/s41467-017-00086-6 · Cited by 70 · 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

Bak apoptotic pores involve a flexible C-terminal region and juxtaposition of the C-terminal transmembrane domains

Iyer, S., Bell, F., Westphal, D., Anwari, K., Gulbis, J. M., Smith, B. J., Dewson, G., & Kluck, R. M. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2015.15 · Cited by 64 · see citing works

Bok regulates mitochondrial fusion and morphology

Schulman, J. J., Szczesniak, L. M., Bunker, E. N., Nelson, H. A., Roe, M. W., Wagner, L. E., Yule, D. I., & Wojcikiewicz, R. J. H. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0327-4 · Cited by 64 · see citing works

Multifaceted anticancer activity of BH3 mimetics: Current evidence and future prospects

Opydo‐Chanek, M., Gonzalo, Ó., & Marzo, I. (2017) · Biochemical Pharmacology · doi:10.1016/j.bcp.2017.03.006 · Cited by 60 · see citing works

Apoptotic foci at mitochondria: in and around Bax pores

Ugarte‐Uribe, B., & García‐Sáez, A. J. (2017) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2016.0217 · Cited by 59 · see citing works

Venetoclax for the treatment of chronic lymphocytic leukemia

Gentile, M., Petrungaro, A., Uccello, G., Vigna, E., Recchia, A. G., Caruso, N., Bossio, S., Stefano, L. D., Palummo, A., Storino, F., et al. (2017) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2017.1386173 · Cited by 55 · see citing works

Posttranslational modifications of Bcl2 family members-a potential therapeutic target for human malignancy

Basu, A. (2006) · Frontiers in bioscience · doi:10.2741/1900 · Cited by 51 · see citing works

The anti-apoptotic members of the Bcl-2 family are attractive tumor-associated antigens

Straten, P. T., & Andersen, M. H. (2010) · Oncotarget · doi:10.18632/oncotarget.134 · Cited by 45 · see citing works

Surface-Binding to Cardiolipin Nanodomains Triggers Cytochrome c Pro-apoptotic Peroxidase Activity via Localized Dynamics

Li, M., Mandal, A., Tyurin, V. A., DeLucia, M., Ahn, J., Kagan, V. E., & van der Wel, P. C. A. (2019) · Structure · doi:10.1016/j.str.2019.02.007 · Cited by 41 · see citing works

BCL-2 family protein BOK is a positive regulator of uridine metabolism in mammals

Srivastava, R., Cao, Z., Nedeva, C., Naim, S., Bachmann, D., Rabachini, T., Gangoda, L., Shahi, S. K., Glab, J., Menassa, J., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1904523116 · Cited by 41 · see citing works

Venetoclax in the treatment of chronic lymphocytic leukemia

Korycka, A., Wołowiec, D., Kubiak-Mlonka, A., & Robak, T. (2019) · Expert Opinion on Drug Metabolism & Toxicology · doi:10.1080/17425255.2019.1606211 · Cited by 40 · see citing works

cBid, Bax and Bcl-xL exhibit opposite membrane remodeling activities

Bleicken, S., Hofhaus, G., Ugarte‐Uribe, B., Schröder, R. R., & García‐Sáez, A. J. (2016) · Cell Death and Disease · doi:10.1038/cddis.2016.34 · Cited by 38 · see citing works

BFL1 modulates apoptosis at the membrane level through a bifunctional and multimodal mechanism showing key differences with BCLXL

Flores‐Romero, H., Landeta, O., Ugarte‐Uribe, B., Cosentino, K., García‐Porras, M., García‐Sáez, A. J., & Basáñez, G. (2018) · Cell Death and Differentiation · doi:10.1038/s41418-018-0258-5 · Cited by 33 · see citing works

µ-Calpain Conversion of Antiapoptotic Bfl-1 (BCL2A1) into a Prodeath Factor Reveals Two Distinct alpha-Helices Inducing Mitochondria-Mediated Apoptosis

Valero, J. G., Cornut-Thibaut, A., Jugé, R., Mathieu, A., Giménez, D., Gillet, G., Bonnefoy, N., Salgado, J., Salles, G., Aouacheria, A., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0038620 · Cited by 26 · see citing works

Measuring Mitochondrial Shape Changes and Their Consequences on Mitochondrial Involvement During Apoptosis

Frezza, C., Cipolat, S., & Scorrano, L. (2007) · Methods in molecular biology · doi:10.1007/978-1-59745-365-3_29 · Cited by 24 · see citing works

Lipid-modulation of membrane insertion and refolding of the apoptotic inhibitor Bcl-xL

Vasquez‐Montes, V., Vargas‐Uribe, M., PANDEY, N. K., Rodnin, M. V., Langen, R., & Ladokhin, A. S. (2019) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2019.04.006 · Cited by 23 · see citing works

The great migration of Bax and Bak

Edlich, F. (2015) · Molecular & Cellular Oncology · doi:10.4161/23723556.2014.995029 · Cited by 16 · see citing works

Membrane insertion of the BAX core, but not latch domain, drives apoptotic pore formation

Flores‐Romero, H., García‐Porras, M., & Basáñez, G. (2017) · Scientific Reports · doi:10.1038/s41598-017-16384-4 · Cited by 14 · see citing works

Molecular Effects of Treatment of Human Colorectal Cancer Cells with Natural and Classical Chemotherapeutic Drugs: Alterations in the Expression of Apoptosis-related BCL2 Family Members, Including BCL2L12

Kontos, C. K., Avgeris, M., Vassilacopoulou, D., Ardavanis, A. S., & Scorilas, A. (2018) · Current Pharmaceutical Biotechnology · doi:10.2174/1389201019666181112101410 · Cited by 11 · see citing works

A literature review of the patent publications on venetoclax – a selective Bcl-2 inhibitor: discovering the therapeutic potential of a novel chemotherapeutic agent

Žigart, N., & Časar, Z. (2019) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2019.1627327 · Cited by 11 · see citing works

Lipid-Dependent Bimodal MCL1 Membrane Activity

Landeta, O., Valero, J. G., Flores‐Romero, H., Zabalbeitia, I. B., Landajuela, A., García‐Porras, M., Terrones, O., & Basáñez, G. (2014) · ACS Chemical Biology · doi:10.1021/cb500592e · Cited by 10 · see citing works

Venetoclax: A Novel Treatment for Patients With del(17p) Chronic Lymphocytic Leukemia

Borg, M. A., & Clemmons, A. B. (2017) · Journal of the Advanced Practitioner in Oncology · doi:10.6004/jadpro.2017.8.6.8 · Cited by 5 · see citing works

MAVS ‐induced mitochondrial membrane remodeling

Flores‐Romero, H., & García‐Sáez, A. J. (2019) · FEBS Journal · doi:10.1111/febs.14822 · Cited by 5 · see citing works

Apoptosis, Pyroptosis, and Necroptosis—Oh My! The Many Ways a Cell Can Die

Ketelut-Carneiro, N., & Fitzgerald, K. A. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167378 · Cited by 418 · see citing works

Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials

Xie, X., Yu, T., Li, X., Zhang, N., Foster, L. J., Peng, C., Huang, W., & He, G. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01589-z · Cited by 396 · see citing works

Pore formation in regulated cell death

Flores‐Romero, H., Ros, U., & García‐Sáez, A. J. (2020) · The EMBO Journal · doi:10.15252/embj.2020105753 · Cited by 183 · see citing works

Oxidative stress and mitochondrial dysfunction following traumatic brain injury: From mechanistic view to targeted therapeutic opportunities

Hakiminia, B., Alikiaii, B., Khorvash, F., & Mousavi, S. (2022) · Fundamental and Clinical Pharmacology · doi:10.1111/fcp.12767 · Cited by 104 · see citing works

Crosstalk between mitochondria–ER contact sites and the apoptotic machinery as a novel health meter

Larrañaga-SanMiguel, A., Bengoa‐Vergniory, N., & Flores‐Romero, H. (2024) · Trends in Cell Biology · doi:10.1016/j.tcb.2024.08.007 · Cited by 93 · see citing works

Targeting Mitochondrial Apoptosis to Overcome Treatment Resistance in Cancer

Ngoi, N. Y. L., Choong, C. S. H., Lee, J., Bellot, G. L., Wong, A. L. A., Goh, B. C., & Pervaiz, S. (2020) · Cancers · doi:10.3390/cancers12030574 · Cited by 72 · see citing works

The role of apoptosis in the pathogenesis of osteoarthritis

Xiao, S., Cheng, M., Wang, L., Cao, J., Fang, L., Zhou, X.-P., He, X.-J., & Hu, Y.-F. (2023) · International Orthopaedics · doi:10.1007/s00264-023-05847-1 · Cited by 63 · see citing works

Regulation of Apoptosis by the Bcl-2 Family of Proteins: Field on a Brink

Ladokhin, A. S. (2020) · Cells · doi:10.3390/cells9092121 · Cited by 31 · see citing works

A lipid perspective on regulated cell death

Flores‐Romero, H., Ros, U., & García‐Sáez, A. J. (2019) · International review of cytology · doi:10.1016/bs.ircmb.2019.11.004 · Cited by 30 · see citing works

Visualization of BOK pores independent of BAX and BAK reveals a similar mechanism with differing regulation

Shalaby, R., Diwan, A., Flores‐Romero, H., Hertlein, V., & García‐Sáez, A. J. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-01078-w · Cited by 30 · see citing works

METTL3 Affects Spinal Cord Neuronal Apoptosis by Regulating Bcl-2 m6A Modifications After Spinal Cord Injury

Guo, S., Lin, T., Chen, G., Shangguan, Z., Zhou, L., Chen, Z., Shi, T., Chen, D., Wang, Z., & Liu, W. (2023) · Neurospine · doi:10.14245/ns.2346170.085 · Cited by 25 · see citing works

REPIN1 regulates iron metabolism and osteoblast apoptosis in osteoporosis

Xia, Y., Ge, G., Xiao, H., Wu, M., Wang, T., Gu, C., Yang, H., & Geng, D. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-06160-w · Cited by 24 · see citing works

Nuclear‐mitochondrial crosstalk: On the role of the nuclear receptor liver receptor homolog‐1 ( NR5A2 ) in the regulation of mitochondrial metabolism, cell survival, and cancer

Michalek, S., & Brunner, T. (2020) · IUBMB Life · doi:10.1002/iub.2386 · Cited by 24 · see citing works

The Mysteries around the BCL-2 Family Member BOK

Shalaby, R., Flores‐Romero, H., & García‐Sáez, A. J. (2020) · Biomolecules · doi:10.3390/biom10121638 · Cited by 24 · see citing works

Mechanisms of Panax Ginseng on Treating Sepsis by RNA-Seq Technology

Wang, C., Li, S., Shen, Y., Li, Y., Chen, M., Wang, Y., Lan, Y., & Hu, Y. (2022) · Infection and Drug Resistance · doi:10.2147/idr.s393654 · Cited by 18 · see citing works

Senolytic and senomorphic interventions to defy senescence-associated mitochondrial dysfunction

Nehlin, J. O. (2023) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2023.02.020 · Cited by 16 · see citing works

Fenofibrate Ameliorates Hepatic Ischemia/Reperfusion Injury in Mice: Involvements of Apoptosis, Autophagy, and PPAR-α Activation

Zhang, J., Cheng, P., Dai, W., Ji, J., Wu, L., Feng, J., Wu, J., Yu, Q., Li, J., & Guo, C. (2021) · PPAR Research · doi:10.1155/2021/6658944 · Cited by 16 · see citing works

Peptides: A Supercilious Candidate for Activating Intrinsic Apoptosis by Targeting Mitochondrial Membrane Permeability for Cancer Therapy

Aslam, M., Kanthlal, S. K., & Panonnummal, R. (2021) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-021-10297-7 · Cited by 14 · see citing works

Phenolic‐rich extract of avocado Persea americana (var. Colinred) peel blunts paraquat/maneb‐induced apoptosis through blocking phosphorylation of LRRK2 kinase in human nerve‐like cells

Quintero-Espinosa, D. A., Ortega‐Arellano, H. F., Velez‐Pardo, C., & Jiménez-Del-Río, M. (2021) · Environmental Toxicology · doi:10.1002/tox.23433 · Cited by 14 · see citing works

Benomyl-induced development and cardiac toxicity in zebrafish embryos

Luo, Q., Tang, S., Xiao, X., Wei, Y., Cheng, B., Huang, Y., Zhong, K., Tian, G., & Lu, H. (2022) · Environmental Science and Pollution Research · doi:10.1007/s11356-022-24213-z · Cited by 12 · see citing works

Ubiquitination of Ku70 by Parkin promotes apoptosis of lens epithelial cells

Zhang, W., Wu, A., Zhang, G., Ding, X., Kang, L., Zhou, T., Ji, M. J., & Guan, H. (2023) · FEBS Journal · doi:10.1111/febs.16784 · Cited by 12 · see citing works

Glutamine supplementation improves the activity and immunosuppressive action of induced regulatory T cells in vitro and in vivo

Zhang, L., Xu, Z., Li, Y., Wu, K., Yu, C., Zhu, W., Sun, D., Zhu, L., & Zhou, J. (2024) · Transplant Immunology · doi:10.1016/j.trim.2024.102044 · Cited by 9 · see citing works

Comparison of BH3-dependent and BH3-independent membrane interactions of pro-apoptotic factor BAX

Rodnin, M. V., Vasquez‐Montes, V., O’Neil, P. T., Kyrychenko, A. V., & Ladokhin, A. S. (2025) · Biophysical Journal · doi:10.1016/j.bpj.2025.03.034 · Cited by 6 · see citing works

Identification of iron metabolism-related genes as diagnostic signatures in sepsis by blood transcriptomic analysis

Li, H., Wang, X., Yang, Q., Cheng, L., & Zeng, H. (2023) · Open Life Sciences · doi:10.1515/biol-2022-0549 · Cited by 8 · see citing works

Mechanism of ligusticum cycloprolactam against neuroinflammation based on network pharmacology and experimental verification

Gao, J., Su, G., Chen, W., Wu, Q., Liu, J., Liu, J., Chai, M., Dong, Y., Wang, H., Chen, L., et al. (2023) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/1440-1681.13784 · Cited by 5 · see citing works

MAVS ‐induced mitochondrial membrane remodeling

Flores‐Romero, H., & García‐Sáez, A. J. (2019) · FEBS Journal · doi:10.1111/febs.14822 · Cited by 5 · see citing works

Domain-specific insight into the recognition of BH3-death motifs by the pro-survival Bcl-2 protein

Mushtaq, A. U., Ådén, J., Ali, K., & Gröbner, G. (2022) · Biophysical Journal · doi:10.1016/j.bpj.2022.10.041 · Cited by 5 · see citing works

Unraveling the mystery: How bad is BAG3 in hematological malignancies?

Liu, Q., Liu, J., & Huang, X. (2022) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2022.188781 · Cited by 3 · see citing works

The expression of BECN1, LC3B , and BCL2 genes in eutopic endometrium of patients with adenomyosis: A cross-sectional study

Tantanavipas, S., Aojanepong, T., Waiyaput, W., & Sophonsritsuk, A. (2021) · Journal of Endometriosis and Pelvic Pain Disorders · doi:10.1177/22840265211046750 · Cited by 2 · see citing works

Redesigning apoptotic regulator Bid for thrombin activation

Rodnin, M. V., Kyrychenko, A. V., Vasquez‐Montes, V., & Ladokhin, A. S. (2023) · Biopolymers and Cell · doi:10.7124/bc.000aa3 · Cited by 2 · see citing works

Determination of Apoptotic Pathways in Ovarian Folicular Fluid of Infertile Patients With Endometrioma in Relation to Follicular Atresia

Soykan, Y., Sağlam, A. S. Y., Dikmen, A. U., Erdem, M., & Erdem, A. (2025) · American Journal of Reproductive Immunology · doi:10.1111/aji.70164 · Cited by 2 · see citing works

Bioinformatics analysis reveals CTSF suppresses tumor cell malignant phenotype and CD8 + T cell exhaustion by downregulating Bcl- 2 protein in the microenvironment of bladder cancer

Gao, D., Yin, J., Tie, P., Liu, Q., & Xue, M. (2025) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-025-04189-6 · Cited by 1 · see citing works

Apoptotic Switch in Cancer Stem Cells: A Potential Approach for Cancer Treatment

Gunasekaran, V. P., Sivaraman, T., & Ganeshan, M. (2023) · Current Protein and Peptide Science · doi:10.2174/1389203724666230512111755 · Cited by 1 · see citing works

[Therapeutic mechanism of Guizhi Gancao Decoction for heart failure: a network pharmacology-based analysis].

Zhao, Y., Zhao, X., Zhu, Q., Zhu, B., Zhang, Z., & Chen, J. (2023) · PubMed Central · doi:10.12122/j.issn.1673-4254.2023.05.13

Integrated network pharmacology, molecular docking analysis and experimental validation to reveal the mechanisms of Jinglian Hexiao formula in the treatment of adenoid hypertrophy

Li, N., Li, X., Guo, Y.-N., Gu, J.-Y., Zhang, B., Zheng, F., Pi, Z., & Yue, H. (2024) · Proceedings of the 2024 3rd International Conference on Public Health and Data Science · doi:10.1145/3718677.3718702

Therapeutic Evaluation of Tanshinone IIA on Tibial Dyschondroplasia in Broilers

Xu, W., Wang, B., Mehmood, K., Xu, W., Yang, H., & Zhang, H. (2025) · IOP Conference Series Earth and Environmental Science · doi:10.1088/1755-1315/1549/1/012085

Integrated Serum Pharmacochemistry, Metabolomics, and Network Pharmacology to Reveal the Material Basis and Mechanism of Juan-tong-yin in the Treatment of Endometriosis

Guo, P., Liu, Q., Li, J., Li, S., Ding, W., Zhao, Q., Zhou, S., Meng, F., Tang, Z., & Li, W. (2026) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-025-05523-7

Regulating cell death at, on, and in membranes

Chi, X., Kale, J., Leber, B. F., & Andrews, D. W. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.06.002 · Cited by 70 · see citing works

Structural Perspectives on BCL-2 Family of Proteins

Gavathiotis, E. (2013) · Springer eBooks · doi:10.1007/978-1-4614-9302-0_11 · Cited by 1 · see citing works

The secrets of the Bcl-2 family

Sáez, A. J. G. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.105 · Cited by 228 · 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

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