The BCL-2 family of proteins and mitochondrial outer membrane permeabilisation

Hallmarks of Cancer: The Next Generation

Hanahan, D., & Weinberg, R. A. (2011) · Cell · doi:10.1016/j.cell.2011.02.013 · Cited by 66,590 · see citing works

The hallmarks of cancer

Hanahan, D., & Weinberg, R. A. (2000) · Cell · doi:10.1016/s0092-8674(00)81683-9 · Cited by 29,219 · see citing works

Apoptosis: A Basic Biological Phenomenon with Wideranging Implications in Tissue Kinetics

Kerr, J. F. R., Wyllie, A. H., & Currie, A. R. (1972) · British Journal of Cancer · doi:10.1038/bjc.1972.33 · Cited by 15,673 · see citing works

Apoptosis: A Review of Programmed Cell Death

Elmore, S. (2007) · Toxicologic Pathology · doi:10.1080/01926230701320337 · Cited by 13,853 · see citing works

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

Caspases: the executioners of apoptosis

Cohen, G. M. (1997) · Biochemical Journal · doi:10.1042/bj3260001 · Cited by 4,720 · see citing works

The Release of Cytochrome c from Mitochondria: A Primary Site for Bcl-2 Regulation of Apoptosis

Kluck, R. M., Bossy‐Wetzel, E., Green, D. R., & Newmeyer, D. D. (1997) · Science · doi:10.1126/science.275.5303.1132 · Cited by 4,715 · see citing works

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

The landscape of somatic copy-number alteration across human cancers

Beroukhim, R., Mermel, C. H., Porter, D., Wei, G., Raychaudhuri, S., Donovan, J., Barretina, J., Boehm, J. S., Dobson, J., Urashima, M., et al. (2010) · Nature · doi:10.1038/nature08822 · Cited by 4,017 · see citing works

Smac, a Mitochondrial Protein that Promotes Cytochrome c–Dependent Caspase Activation by Eliminating IAP Inhibition

Du, C., Fang, M., Li, Y., Li, L., & Wang, X. (2000) · Cell · doi:10.1016/s0092-8674(00)00008-8 · Cited by 3,513 · see citing works

An inhibitor of Bcl-2 family proteins induces regression of solid tumours

Oltersdorf, T., Elmore, S. W., Shoemaker, A. R., Armstrong, R. C., Augeri, D. J., Belli, B., Bruncko, M., Deckwerth, T. L., Dinges, J., Hajduk, P. J., et al. (2005) · Nature · doi:10.1038/nature03579 · Cited by 3,407 · see citing works

Classification of cell death: recommendations of the Nomenclature Committee on Cell Death 2009

Kroemer, G., Galluzzi, L., Vandenabeele, P., Abrams, J., Alnemri, E. S., Baehrecke, E. H., Blagosklonny, M. V., El-Deiry, W. S., Golstein, P., Green, D. R., et al. (2009) · Cell Death & Differentiation · doi:10.1038/cdd.2008.150 · Cited by 3,399 · see citing works

Bcl-2 gene promotes haemopoietic cell survival and cooperates with c-myc to immortalize pre-B cells

Vaux, D., Cory, S., & Adams, J. (1988) · Nature · doi:10.1038/335440a0 · Cited by 3,355 · 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

Apaf-1, a Human Protein Homologous to C. elegans CED-4, Participates in Cytochrome c–Dependent Activation of Caspase-3

Zou, H., Henzel, W. J., Liu, X., Lutschg, A., & Wang, X. (1997) · Cell · doi:10.1016/s0092-8674(00)80501-2 · Cited by 3,145 · 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

Identification of DIABLO, a Mammalian Protein that Promotes Apoptosis by Binding to and Antagonizing IAP Proteins

Verhagen, A. M., Ekert, P. G., Pakusch, M., Silke, J., Connolly, L. M., Reid, G. E., Moritz, R. L., Simpson, R. J., & Vaux, D. L. (2000) · Cell · doi:10.1016/s0092-8674(00)00009-x · Cited by 2,372 · see citing works

ABT-263: A Potent and Orally Bioavailable Bcl-2 Family Inhibitor

Tse, C., Shoemaker, A. R., Adickes, J., Anderson, M. G., Chen, J., Jin, S., Johnson, E. F., Marsh, K. C., Mitten, M. J., Nimmer, P., et al. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-5836 · Cited by 1,992 · see citing works

X-linked IAP is a direct inhibitor of cell-death proteases

Deveraux, Q. L., Takahashi, R., Salvesen, G. S., & Reed, J. C. (1997) · Nature · doi:10.1038/40901 · Cited by 1,956 · 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

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

Cloning of the Chromosome Breakpoint of Neoplastic B Cells with the t(14;18) Chromosome Translocation

Tsujimoto, Y., Finger, L. R., Yunis, J. J., Nowell̀, P. C., & Croce, C. M. (1984) · Science · doi:10.1126/science.6093263 · Cited by 1,769 · 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

A receptor for phosphatidylserine-specific clearance of apoptotic cells

Fadok, V. A., Bratton, D. L., Rose, D. M., Pearson, A. M., Ezekowitz, R. A. B., & Henson, P. M. (2000) · Nature · doi:10.1038/35011084 · Cited by 1,491 · 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

p53- and Drug-Induced Apoptotic Responses Mediated by BH3-Only Proteins Puma and Noxa

Villunger, A., Michalak, E. M., Coultas, L., Müllauer, F., Böck, G., Ausserlechner, M. J., Adams, J. M., & Strasser, A. (2003) · Science · doi:10.1126/science.1090072 · Cited by 1,327 · 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

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

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

Massive Cell Death of Immature Hematopoietic Cells and Neurons in Bcl-x-Deficient Mice

Motoyama, N., Wang, F., Roth, K. A., Sawa, H., Nakayama, K., Nakayama, K., Negishi, I., Senju, S., Zhang, Q., Fujii, S., et al. (1995) · Science · doi:10.1126/science.7878471 · Cited by 1,164 · 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

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

Autoactivation of Procaspase-9 by Apaf-1-Mediated Oligomerization

Srinivasula, S. M., Ahmad, M., Fernandes‐Alnemri, T., & Alnemri, E. S. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80095-7 · Cited by 1,119 · 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

Genetic Control of Programmed Cell Death in Drosophila

White, K., Grether, M. E., Abrams, J., Young, L. M., Farrell, K., & Steller, H. (1994) · Science · doi:10.1126/science.8171319 · Cited by 1,047 · see citing works

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

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

Programmed Anuclear Cell Death Delimits Platelet Life Span

Mason, K. D., Carpinelli, M. R., Fletcher, J. I., Collinge, J. E., Hilton, A. A., Ellis, S., Kelly, P. N., Ekert, P. G., Metcalf, D., Roberts, A. W., et al. (2007) · Cell · doi:10.1016/j.cell.2007.01.037 · Cited by 1,031 · see citing works

The many roles of FAS receptor signaling in the immune system

Strasser, A., Jost, P. J., & Nagata, S. (2009) · Immunity · doi:10.1016/j.immuni.2009.01.001 · Cited by 968 · 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

Caenorhabditis elegans gene ced-9 protects cells from programmed cell death

Hengartner, M. O., Ellis, R. E., & Horvitz, H. R. (1992) · Nature · doi:10.1038/356494a0 · Cited by 889 · see citing works

Autoimmunity and the Clearance of Dead Cells

Nagata, S., Hanayama, R., & Kawane, K. (2010) · Cell · doi:10.1016/j.cell.2010.02.014 · Cited by 877 · 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

Structural and biochemical basis of apoptotic activation by Smac/DIABLO

Chai, J., Du, C., Wu, J.-W., Kyin, S., Wang, X., & Shi, Y. (2000) · Nature · doi:10.1038/35022514 · Cited by 864 · 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

Cleavage of human inhibitor of apoptosis protein XIAP results in fragments with distinct specificities for caspases

Deveraux, Q. L., Leo, E., Stennicke, H. R., Welsh, K., Salvesen, G. S., & Reed, J. C. (1999) · The EMBO Journal · doi:10.1093/emboj/18.19.5242 · Cited by 751 · 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

The C. elegans Protein EGL-1 Is Required for Programmed Cell Death and Interacts with the Bcl-2–like Protein CED-9

Conradt, B., & Horvitz, H. R. (1998) · Cell · doi:10.1016/s0092-8674(00)81182-4 · Cited by 642 · 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

Interaction of CED-4 with CED-3 and CED-9: A Molecular Framework for Cell Death

Chinnaiyan, A. M., O’Rourke, K. M., Lane, B. R., & Dixit, V. M. (1997) · Science · doi:10.1126/science.275.5303.1122 · Cited by 626 · see citing works

The role of BH3-only proteins in the immune system

Strasser, A. (2005) · Nature reviews. Immunology · doi:10.1038/nri1568 · Cited by 624 · 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

Exploiting selective BCL-2 family inhibitors to dissect cell survival dependencies and define improved strategies for cancer therapy

Leverson, J. D., Phillips, D. C., Mitten, M. J., Boghaert, E. R., Diaz, D., Tahir, S. K., Belmont, L. D., Nimmer, P., Xiao, Y., Ma, X. M., et al. (2015) · Science Translational Medicine · doi:10.1126/scitranslmed.aaa4642 · Cited by 541 · see citing works

Bax in Murine Thymus Is a Soluble Monomeric Protein That Displays Differential Detergent-induced Conformations

Hsu, Y., & Youle, R. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.17.10777 · Cited by 504 · 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

Apoptotic bodies from endothelial cells enhance the number and initiate the differentiation of human endothelial progenitor cells in vitro

Hristov, M., Erl, W., Linder, S., & Weber, P. C. (2004) · Blood · doi:10.1182/blood-2003-10-3614 · Cited by 485 · see citing works

Appearance of Phosphatidylserine on Apoptotic Cells Requires Calcium-mediated Nonspecific Flip-Flop and Is Enhanced by Loss of the Aminophospholipid Translocase

Bratton, D. L., Fadok, V. A., Richter, D., Kailey, J. M., Guthrie, L. A., & Henson, P. M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.42.26159 · Cited by 485 · 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

Bax and Bak Coalesce into Novel Mitochondria-Associated Clusters during Apoptosis

Nechushtan, A., Smith, C. L., Lamensdorf, I., Yoon, S., & Youle, R. J. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.6.1265 · Cited by 477 · see citing works

Building blocks of the apoptotic pore: how Bax and Bak are activated and oligomerize during apoptosis

Westphal, D., Kluck, R. M., & Dewson, G. (2013) · Cell Death and Differentiation · doi:10.1038/cdd.2013.139 · Cited by 437 · see citing works

grim, a novel cell death gene in Drosophila.Preprint

Chen, P., Nordstrom, W., Gish, B., & Abrams, J. (1996) · Genes & Development · doi:10.1101/gad.10.14.1773 · Cited by 428 · see citing works

The structural basis for membrane binding and pore formation by lymphocyte perforin

Law, R. H. P., Lukoyanova, N., Voskoboinik, I., Caradoc-Davies, T. T., Baran, K., Dunstone, M. A., D’Angelo, M. E., Orlova, E. V., Coulibaly, F., Verschoor, S., et al. (2010) · Nature · doi:10.1038/nature09518 · Cited by 418 · see citing works

Mcl-1 deficiency results in peri-implantation embryonic lethality

Rinkenberger, J. L., Horning, S., Klocke, B., Roth, K., & Korsmeyer, S. J. (2000) · Genes & Development · doi:10.1101/gad.14.1.23 · Cited by 397 · 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

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 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

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

Interaction and Regulation of Subcellular Localization of CED-4 by CED-9

Wu, D., Wallen, H. D., & Núñez, G. (1997) · Science · doi:10.1126/science.275.5303.1126 · Cited by 341 · see citing works

Integral role of Noxa in p53-mediated apoptotic responsePreprint

Shibue, T., Takeda, K., Oda, E., Tanaka, H., Murasawa, H., Takaoka, A., Morishita, Y., Akira, S., Taniguchi, T., & Tanaka, N. (2003) · Genes & Development · doi:10.1101/gad.1103603 · Cited by 338 · see citing works

Discovery of a Potent and Selective BCL-X L Inhibitor with in Vivo Activity

Tao, Z., Hasvold, L. A., Wang, L., Wang, X., Petros, A. M., Park, C. H., Boghaert, E. R., Catron, N. D., Chen, J., Colman, P. M., et al. (2014) · ACS Medicinal Chemistry Letters · doi:10.1021/ml5001867 · Cited by 311 · 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

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

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

Crystal structure of ABT-737 complexed with Bcl-xL: implications for selectivity of antagonists of the Bcl-2 family

Lee, E. F., Czabotar, P. E., Smith, B. J., Deshayes, K., Zobel, K., Colman, P. M., & Fairlie, W. D. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402178 · Cited by 280 · 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

The conserved N‐terminal BH4 domain of Bcl‐2 homologues is essential for inhibition of apoptosis and interaction with CED‐4

Huang, D. C. S., Adams, J. M., & Cory, S. (1998) · The EMBO Journal · doi:10.1093/emboj/17.4.1029 · Cited by 250 · 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

Translocation of C. elegans CED-4 to Nuclear Membranes During Programmed Cell Death

Chen, F., Hersh, B. M., Conradt, B., Zhou, Z., Riemer, D., Gruenbaum, Y., & Horvitz, H. R. (2000) · Science · doi:10.1126/science.287.5457.1485 · Cited by 237 · 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

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

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

Decoding and unlocking the BCL-2 dependency of cancer cells

Juin, P. P., Geneste, O., Gautier, F., Depil, S., & Campone, M. (2013) · Nature reviews. Cancer · doi:10.1038/nrc3538 · Cited by 231 · 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

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

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

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

Mutagenesis of the BH3 Domain of BAX Identifies Residues Critical for Dimerization and Killing

Wang, K., Gross, A., Waksman, G., & Korsmeyer, S. J. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.10.6083 · Cited by 216 · see citing works

Conditional deletion of the Bcl-x gene from erythroid cells results in hemolytic anemia and profound splenomegaly

Wagner, K., Claudio, E., Rucker, E. B., Riedlinger, G., Broussard, C., Schwartzberg, P. L., Siebenlist, U. K., & Hennighausen, L. G. (2000) · Development · doi:10.1242/dev.127.22.4949 · Cited by 205 · 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

Accelerated Neutrophil Apoptosis in Mice Lacking A1-a, a Subtype of the bcl-2–related A1 Gene

Hamasaki, A., Sendo, F., Nakayama, K., Ishida, N., Negishi, I., Nakayama, K., & Hatakeyama, S. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.188.11.1985 · Cited by 199 · see citing works

Apoptosis inDrosophila: neither fish nor fowl (nor man, nor worm)

Kornbluth, S. A., & White, K. (2005) · Journal of Cell Science · doi:10.1242/jcs.02377 · Cited by 190 · 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 & Differentiation · doi:10.1038/cdd.2011.138 · Cited by 189 · 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

Debcl, a Proapoptotic Bcl-2 Homologue, Is a Component of the Drosophila melanogaster Cell Death Machinery

Colussi, P. A., Quinn, L. M., Huang, D. C. S., et al. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.148.4.703 · Cited by 179 · see citing works

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

BH3 Domains other than Bim and Bid Can Directly Activate Bax/Bak

Du, H., Wolf, J., Schafer, B., Moldoveanu, T., Chipuk, J. E., & Kuwana, T. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.167148 · 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

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

Vaccinia virus encodes a previously uncharacterized mitochondrial-associated inhibitor of apoptosis

Wasilenko, S. T., Stewart, T. L., Meyers, A. F. A., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2235583100 · Cited by 155 · see citing works

Pro-Apoptotic Apoptosis Protease–Activating Factor 1 (Apaf-1) Has a Cytoplasmic Localization Distinct from Bcl-2 or Bcl-XL

Hausmann, G., O’Reilly, L. A., van Driel, R. R., Beaumont, J. G., Strasser, A., Adams, J. M., & Huang, D. C. S. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.149.3.623 · Cited by 139 · 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

Roles of c-FLIP in Apoptosis, Necroptosis, and Autophagy

Safa, A. R. (2013) · Journal of Carcinogenesis & Mutagenesis · doi:10.4172/2157-2518.s6-003 · Cited by 139 · 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 & 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 & Differentiation · doi:10.1038/cdd.2013.10 · Cited by 137 · 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

BCL-2 family member BOK promotes apoptosis in response to endoplasmic reticulum stress

Carpio, M. A., Michaud, M., Zhou, W., Fisher, J. K., Walensky, L. D., & Katz, S. G. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1421063112 · Cited by 127 · see citing works

The Damage-Responsive Drosophila Gene sickle Encodes a Novel IAP Binding Protein Similar to but Distinct from reaper, grim, and hid

Christich, A., Kauppila, S., Chen, P., Sogame, N., Ho, S. I., & Abrams, J. (2002) · Current Biology · doi:10.1016/s0960-9822(01)00658-3 · Cited by 125 · see citing works

The Drosophila Bcl-2 family member dBorg-1 functions in the apoptotic response to UV-irradiation

Brachmann, C. B., Jassim, O. W., Wachsmuth, B. D., et al. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00474-7 · Cited by 123 · 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

Induction of allogenic T-cell hyporesponsiveness by galectin-1-mediated apoptotic and non-apoptotic mechanisms

Rabinovich, G. A., Ramhorst, R., Rubinstein, N., Corigliano, A., Daroqui, M. C., Joffé, E. B. D. K., & Fainboim, L. (2002) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401009 · Cited by 118 · see citing works

Mutation to Bax beyond the BH3 Domain Disrupts Interactions with Pro-survival Proteins and Promotes Apoptosis

Czabotar, P. E., Lee, E. F., Thompson, G. V., Wardak, A. Z., Fairlie, W. D., & Colman, P. M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.161281 · Cited by 115 · see citing works

BCL-2 family member BOK is widely expressed but its loss has only minimal impact in mice

Ke, F., Voss, A., Kerr, J. B., O'Reilly, L. A., Tai, L., Echeverry, N., Bouillet, P., Strasser, A., & Kaufmann, T. (2012) · Cell Death & Differentiation · doi:10.1038/cdd.2011.210 · Cited by 113 · see citing works

Inhibition of Bak Activation by VDAC2 Is Dependent on the Bak Transmembrane Anchor

Lazarou, M., Stojanovski, D., Frazier, A. E., Kotevski, A., Dewson, G., Craigen, W. J., Kluck, R. M., Vaux, D. L., & Ryan, M. T. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.159301 · Cited by 111 · see citing works

Caenorhabditis elegans EGL-1 Disrupts the Interaction of CED-9 with CED-4 and Promotes CED-3 Activation

del Peso, L., González, V. M., & Núñez, G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.50.33495 · Cited by 105 · see citing works

Where Killers Meet--Permeabilization of the Outer Mitochondrial Membrane during ApoptosisPreprint

Bender, T., & Martinou, J. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a011106 · Cited by 105 · see citing works

Evolution of Bcl-2 homology motifs: homology versus homoplasy

Aouacheria, A., Rech de Laval, V., Combet, C., & Hardwick, J. M. (2013) · Trends in Cell Biology · doi:10.1016/j.tcb.2012.10.010 · Cited by 103 · see citing works

tBid Undergoes Multiple Conformational Changes at the Membrane Required for Bax Activation

Shamas‐Din, A., Bindner, S., Zhu, W., Zaltsman, Y., Campbell, C. J. V., Gross, A., Leber, B. F., Andrews, D. W., & Fradin, C. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.482109 · Cited by 101 · see citing works

The Bcl-2 Protein Family Member Bok Binds to the Coupling Domain of Inositol 1,4,5-Trisphosphate Receptors and Protects Them from Proteolytic Cleavage

Schulman, J. J., Wright, F. A., Kaufmann, T., & Wojcikiewicz, R. J. H. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.496570 · Cited by 98 · see citing works

BH3‐in‐groove dimerization initiates and helix 9 dimerization expands Bax pore assembly in membranes

Zhang, Z., Subramaniam, S., Kale, J., Liao, C., Huang, B., Brahmbhatt, H., Condon, S. G., Lapolla, S. M., Hays, F. A., Ding, J., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201591552 · Cited by 93 · see citing works

The porin VDAC2 is the mitochondrial platform for Bax retrotranslocation

Lauterwasser, J., Todt, F., Zerbes, R. M., Nguyen, T. N., Craigen, W. J., Lazarou, M., van der Laan, M., & Edlich, F. (2016) · Scientific Reports · doi:10.1038/srep32994 · Cited by 92 · see citing works

Bax Activation Initiates the Assembly of a Multimeric Catalyst that Facilitates Bax Pore Formation in Mitochondrial Outer Membranes

Kushnareva, Y., Andreyev, A. Y., Kuwana, T., & Newmeyer, D. D. (2012) · PLoS Biology · doi:10.1371/journal.pbio.1001394 · Cited by 91 · see citing works

Bid chimeras indicate that most BH3-only proteins can directly activate Bak and Bax, and show no preference for Bak versus Bax

Hockings, C., Anwari, K., Ninnis, R. L., Brouwer, J. M., O’Hely, M., Evangelista, M., Hinds, M. G., Czabotar, P. E., Lee, E. F., Fairlie, W. D., et al. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.105 · Cited by 91 · 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

Just So Stories about the Evolution of Apoptosis

Green, D. R., & Fitzgerald, P. (2016) · Current Biology · doi:10.1016/j.cub.2016.05.023 · Cited by 81 · see citing works

BH3-only proteins are tail-anchored in the outer mitochondrial membrane and can initiate the activation of Bax

Wilfling, F., Weber, A., Potthoff, S., Vögtle, F. ‐., Meisinger, C., Paschen, S. A., & Häcker, G. A. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.9 · Cited by 79 · see citing works

Structural Insights of tBid, the Caspase-8-activated Bid, and Its BH3 Domain

Wang, Y., & Tjandra, N. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.503680 · Cited by 77 · see citing works

Caspase cleavage of the nuclear autoantigen LEDGF/p75 abrogates its pro-survival function: implications for autoimmunity in atopic disorders

Wu, X., Daniels‐Wells, T. R., Molinaro, C., Lilly, M. B., & Casiano, C. A. (2002) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401063 · Cited by 77 · see citing works

Crystal structure of Bax bound to the BH3 peptide of Bim identifies important contacts for interaction

Robin, A. Y., Kumar, K. K., Westphal, D., Wardak, A. Z., Thompson, G. V., Dewson, G., Colman, P. M., & Czabotar, P. E. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.141 · Cited by 73 · see citing works

Organization of the Mitochondrial Apoptotic BAK Pore

Aluvila, S., Mandal, T., Hustedt, E., Fajer, P., Choe, J. Y., & Oh, K. J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.526806 · Cited by 71 · see citing works

The molecular cell death machinery in the simple cnidarian Hydra includes an expanded caspase family and pro- and anti-apoptotic Bcl-2 proteins

Lasi, M., Pauly, B. S., Schmidt, N., et al. (2010) · Cell Research · doi:10.1038/cr.2010.66 · Cited by 71 · see citing works

BHRF1, the Epstein-Barr virus (EBV) homologue of the BCL-2 protooncogene, is transcribed in EBV-associated B-cell lymphomas and in reactive lymphocytes

Oudejans, J., van den Brule, A., Jiwa, N., et al. (1995) · Blood · doi:10.1182/blood.v86.5.1893.bloodjournal8651893 · Cited by 68 · see citing works

Drosophila Bcl‐2 proteins participate in stress‐induced apoptosis, but are not required for normal development

Sevrioukov, E. A., Burr, J., Huang, E. W., Assi, H. H., Monserrate, J. P., Purves, D. C., Wu, J. N., Song, E. J., & Brachmann, C. B. (2007) · genesis · doi:10.1002/dvg.20279 · Cited by 67 · 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

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

Programmed cell death in Hydra

Böttger, A., & Alexandrova, O. (2006) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2006.11.008 · Cited by 62 · see citing works

The Stability and Expression Level of Bok Are Governed by Binding to Inositol 1,4,5-Trisphosphate Receptors

Schulman, J. J., Wright, F. A., Han, X., Zluhan, E., Szczesniak, L. M., & Wojcikiewicz, R. J. H. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.711242 · Cited by 59 · see citing works

Dissociation of Bak α1 helix from the core and latch domains is required for apoptosis

Alsop, A. E., Fennell, S. C., Bartolo, R. C., Tan, I. K. L., Dewson, G., & Kluck, R. M. (2015) · Nature Communications · doi:10.1038/ncomms7841 · Cited by 57 · see citing works

Discovery and molecular characterization of a Bcl-2–regulated cell death pathway in schistosomes

Lee, E. F., Clarke, O. B., Evangelista, M., Feng, Z., Speed, T. P., Tchoubrieva, E. B., Strasser, A., Kalinna, B. H., Colman, P. M., & Fairlie, W. D. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1100652108 · Cited by 57 · see citing works

Mitochondrial involvement in cell death of non-mammalian eukaryotes

Abdelwahid, E., Rolland, S. G. M., Teng, X., Conradt, B., Hardwick, J. M., & White, K. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.10.008 · Cited by 55 · see citing works

Bok Is Not Pro-Apoptotic But Suppresses Poly ADP-Ribose Polymerase-Dependent Cell Death Pathways and Protects against Excitotoxic and Seizure-Induced Neuronal Injury

D’Orsi, B., Engel, T., Pfeiffer, S. L., Nandi, S., Kaufmann, T., Henshall, D. C., & Prehn, J. H. M. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.3780-15.2016 · Cited by 53 · see citing works

Solution Structure of Apoptotic BAX Oligomer: Oligomerization Likely Precedes Membrane Insertion

Sung, T.-C., Li, C.-Y., Lai, Y., et al. (2015) · Structure · doi:10.1016/j.str.2015.07.013 · Cited by 50 · see citing works

The membrane activity of <scp>BOK</scp> involves formation of large, stable toroidal pores and is promoted by <scp>cBID</scp>

Fernández‐Marrero, Y., Bleicken, S., Das, K. K., Bachmann, D., Kaufmann, T., & Garcia‐Saez, A. J. (2017) · The FEBS Journal · doi:10.1111/febs.14008 · Cited by 47 · see citing works

Assembly of Bak homodimers into higher order homooligomers in the mitochondrial apoptotic pore

Mandal, T., Shin, S., Aluvila, S., Chen, H., Grieve, C., Choe, J., Cheng, E. H. Y., Hustedt, E. J., & Oh, K. J. (2016) · Scientific Reports · doi:10.1038/srep30763 · Cited by 43 · see citing works

The structure of Boo/Diva reveals a divergent Bcl-2 protein

Rautureau, G. J. P., Day, C. L., & Hinds, M. G. (2010) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22728 · Cited by 35 · 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., et al. (2016) · Journal of Cell Science · doi:10.1242/jcs.193946 · Cited by 35 · see citing works

Structural insight into an evolutionarily ancient programmed cell death regulator – the crystal structure of marine sponge BHP2 bound to LB-Bak-2

Caria, S., Hinds, M. G., & Kvansakul, M. (2017) · Cell Death and Disease · doi:10.1038/cddis.2016.469 · Cited by 28 · see citing works

Oncogenic Mutations Differentially Affect Bax Monomer, Dimer, and Oligomeric Pore Formation in the Membrane

Zhang, M., Zheng, J., Nussinov, R., & Ma, B. (2016) · Scientific Reports · doi:10.1038/srep33340 · Cited by 12 · see citing works

Untitled work

(1998) · doi:10.1002/(sici)1097-0320(19980101)31:1

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 &amp; Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680 · see citing works

Regulation of apoptosis in health and disease: the balancing act of BCL-2 family proteins

Singh, R., Letai, A., & Sarosiek, K. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0089-8 · Cited by 2,111 · 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 &amp; Differentiation · doi:10.1038/cdd.2017.186 · Cited by 1,574 · see citing works

An overview of apoptosis assays detecting DNA fragmentation

Majtnerová, P., & Roušar, T. (2018) · Molecular Biology Reports · doi:10.1007/s11033-018-4258-9 · Cited by 330 · see citing works

Triazole fungicide tebuconazole induces apoptosis through ROS-mediated endoplasmic reticulum stress pathway

Ben Othmène, Y., Monceaux, K., Belhadef, A., Karoui, A., Ben Salem, I., Boussabbeh, M., Abid-Essefi, S., & Lemaire, C. (2022) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2022.103919 · Cited by 43 · see citing works

Bacterial solutions to multicellularity: a tale of biofilms, filaments and fruiting bodies

Claessen, D., Rozen, D. E., Kuipers, O. P., Søgaard‐Andersen, L., & van Wezel, G. P. (2014) · Nature Reviews Microbiology · doi:10.1038/nrmicro3178 · Cited by 476 · see citing works

Transition from one- to two-dimensional development facilitates maintenance of multicellularity

Manjarrez-Casas, A. M., Bagheri, H. C., & Dobay, A. (2016) · Royal Society Open Science · doi:10.1098/rsos.160554

Building a Multicellular Organism

Kaiser, D. (2001) · Annual Review of Genetics · doi:10.1146/annurev.genet.35.102401.090145 · Cited by 205 · see citing works

Programmed cell death in the cellular differentiation of microbial eukaryotes

Ramsdale, M. (2012) · Current Opinion in Microbiology · doi:10.1016/j.mib.2012.09.005 · Cited by 17 · see citing works

Pharmacological manipulation of Bcl-2 family members to control cell death

Letai, A. G. (2005) · Journal of Clinical Investigation · doi:10.1172/jci26250 · Cited by 134 · see citing works