Many players in BCL-2 family affairs

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

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The landscape of somatic copy-number alteration across human cancers

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BCL-2 family members and the mitochondria in apoptosisPreprint

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

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A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD

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

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Direct Activation of Bax by p53 Mediates Mitochondrial Membrane Permeabilization and Apoptosis

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Discovering High-Affinity Ligands for Proteins: SAR by NMR

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

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

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X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death

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The BCL-2 Family Reunion

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Cytochrome C -Mediated Apoptosis

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tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome cPreprint

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The BH3 mimetic ABT-737 targets selective Bcl-2 proteins and efficiently induces apoptosis via Bak/Bax if Mcl-1 is neutralized

van Delft, M. F., Wei, A. H., Mason, K. D., Vandenberg, C. J., Chen, L., Czabotar, P. E., Willis, S. N., Scott, C. L., Day, C. L., Cory, S., et al. (2006) · Cancer Cell · doi:10.1016/j.ccr.2006.08.027 · Cited by 1,237 · see citing works

Cell Death

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Cytoplasmic functions of the tumour suppressor p53

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Structure of Bax

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Promoting apoptosis as a strategy for cancer drug discovery

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Pro-apoptotic cascade activates BID, which oligomerizes BAK or BAX into pores that result in the release of cytochrome c

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How do BCL-2 proteins induce mitochondrial outer membrane permeabilization?

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

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Apoptotic Pathways: Ten Minutes to Dead

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Mitochondrial p53 activates Bak and causes disruption of a Bak–Mcl1 complex

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Structural biology of the Bcl-2 family of proteins

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Mechanisms of Action of Bcl-2 Family Proteins

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BAX activation is initiated at a novel interaction site

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Bcl-xL Retrotranslocates Bax from the Mitochondria into the Cytosol

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BCL-2 family antagonists for cancer therapy

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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

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

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Xk-Related Protein 8 and CED-8 Promote Phosphatidylserine Exposure in Apoptotic Cells

Suzuki, J., Denning, D. P., Imanishi, E., Horvitz, H. R., & Nagata, S. (2013) · Science · doi:10.1126/science.1236758 · Cited by 573 · 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

A common BIM deletion polymorphism mediates intrinsic resistance and inferior responses to tyrosine kinase inhibitors in cancer

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PUMA Couples the Nuclear and Cytoplasmic Proapoptotic Function of p53

Chipuk, J. E., Bouchier‐Hayes, L., Kuwana, T., Newmeyer, D. D., & Green, D. R. (2005) · Science · doi:10.1126/science.1114297 · Cited by 547 · see citing works

Solution Structure of BID, an Intracellular Amplifier of Apoptotic Signaling

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

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BID, BIM, and PUMA Are Essential for Activation of the BAX- and BAK-Dependent Cell Death Program

Ren, D., Tu, H.-C., Kim, H., Wang, G. X., Bean, G. R., Takeuchi, O., Jeffers, J. R., Zambetti, G. P., Hsieh, J. J.-D., & Cheng, E. H. Y. (2010) · Science · doi:10.1126/science.1190217 · Cited by 475 · see citing works

Rationale for Bcl-xL/Bad peptide complex formation from structure, mutagenesis, and biophysical studies

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Structure-guided design of a selective BCL-XL inhibitor

Lessène, G., Czabotar, P. E., Sleebs, B. E., Zobel, K., Lowes, K. N., Adams, J. M., Baell, J. B., Colman, P. M., Deshayes, K., Fairbrother, W. J., et al. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1246 · Cited by 381 · 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

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

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

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

Evidence that inhibition of BAX activation by BCL-2 involves its tight and preferential interaction with the BH3 domain of BAX

Ku, B., Liang, C., Jung, J. U., & Oh, B. (2010) · Cell Research · doi:10.1038/cr.2010.149 · Cited by 307 · see citing works

Discovery of Potent Myeloid Cell Leukemia 1 (Mcl-1) Inhibitors Using Fragment-Based Methods and Structure-Based Design

Friberg, A., Vigil, D., Zhao, B., Daniels, R. N., Burke, J. P., García-Barrantes, P. M., Camper, D. V., Chauder, B. A., Lee, T., Olejniczak, E. T., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm301448p · Cited by 306 · see citing works

Pharmacologic activation of p53 elicits Bax-dependent apoptosis in the absence of transcription

Chipuk, J. E., Maurer, U., Green, D. R., & Schüler, M. (2003) · Cancer Cell · doi:10.1016/s1535-6108(03)00272-1 · Cited by 297 · see citing works

The Bcl-2 specific BH3 mimetic ABT-199: a promising targeted therapy for t(11;14) multiple myeloma

Touzeau, C., Dousset, C., Gouill, S. L., Sampath, D., Leverson, J. D., Souers, A. J., Maïga, S., Béné, M. C., Moreau, P., Pellat‐Deceunynck, C., et al. (2013) · Leukemia · doi:10.1038/leu.2013.216 · Cited by 290 · see citing works

Deletion of MCL-1 causes lethal cardiac failure and mitochondrial dysfunctionPreprint

Wang, X., Bathina, M., Lynch, J., Koss, B. S., Calabrese, C. R., Frase, S., Schuetz, J. D., Rehg, J. E., & Opferman, J. T. (2013) · Genes & Development · doi:10.1101/gad.215855.113 · Cited by 284 · 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

Targeting BCL-2 with the BH3 Mimetic ABT-199 in Estrogen Receptor-Positive Breast Cancer

Vaillant, F., Mérino, D., Lee, L., Breslin, K. A., Pal, B., Ritchie, M. E., Smyth, G. K., Christie, M., Phillipson, L. J., Burns, C. J., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.06.002 · Cited by 275 · 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

WT p53, but Not Tumor-derived Mutants, Bind to Bcl2 via the DNA Binding Domain and Induce Mitochondrial Permeabilization

Tomita, Y. A., Marchenko, N. D., Erster, S. H., Nemajerová, A., Dehner, A., Klein, C., Pan, H., Kessler, H., Pančoška, P., & Moll, U. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m507611200 · Cited by 246 · 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

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

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

Structure of the BH3 Domains from the p53-Inducible BH3-Only Proteins Noxa and Puma in Complex with Mcl-1

Day, C. L., Smits, C., Fan, F. C., Lee, E. F., Fairlie, W. D., & Hinds, M. G. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.05.071 · Cited by 204 · see citing works

Activity of the Bcl-2 Family Inhibitor ABT-263 in a Panel of Small Cell Lung Cancer Xenograft Models

Shoemaker, A. R., Mitten, M. J., Adickes, J., Ackler, S., Refici, M. L., Ferguson, D. C., Oleksijew, A., O'Connor, J. M., Wang, B., Frost, D. J., et al. (2008) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-07-4622 · Cited by 203 · see citing works

Cytomegalovirus cell death suppressor vMIA blocks Bax- but not Bak-mediated apoptosis by binding and sequestering Bax at mitochondria

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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

BH3-only proteins in apoptosis at a glance

Happo, L., Strasser, A., & Cory, S. (2012) · Journal of Cell Science · doi:10.1242/jcs.090514 · Cited by 193 · 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

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

A stapled BIM peptide overcomes apoptotic resistance in hematologic cancers

LaBelle, J. L., Katz, S. G., Bird, G. H., Gavathiotis, E., Stewart, M. L., Lawrence, C. E., Fisher, J. K., Godes, M., Pitter, K. L., Kung, A. L., et al. (2012) · Journal of Clinical Investigation · doi:10.1172/jci46231 · Cited by 176 · see citing works

PUMA binding induces partial unfolding within BCL-xL to disrupt p53 binding and promote apoptosis

Follis, A. V., Chipuk, J. E., Fisher, J. C., Yun, M., Grace, C. R., Nourse, A., Baran, K., Ou, L., Min, L., White, S. W., et al. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1166 · Cited by 174 · see citing works

Mitochondria: gatekeepers of response to chemotherapy

Sarosiek, K. A., Chonghaile, T. N., & Letai, A. G. (2013) · Trends in Cell Biology · doi:10.1016/j.tcb.2013.08.003 · Cited by 170 · see citing works

Direct and selective small-molecule activation of proapoptotic BAX

Gavathiotis, E., Reyna, D. E., Bellairs, J. A., Leshchiner, E. S., & Walensky, L. D. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.995 · Cited by 169 · 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

Transcription, apoptosis and p53: catch-22

Schüler, M., & Green, D. R. (2005) · Trends in Genetics · doi:10.1016/j.tig.2005.01.001 · Cited by 161 · see citing works

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

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

The Bcl-2/Bcl-XL/Bcl-w Inhibitor, Navitoclax, Enhances the Activity of Chemotherapeutic Agents In Vitro and In Vivo

Chen, J., Jin, S. S., Abraham, V., Huang, X., Liu, B. A., Mitten, M. J., Nimmer, P. M., Lin, X., Smith, M. L., Shen, Y., et al. (2011) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-11-0415 · Cited by 158 · see citing works

Direct activation of full-length proapoptotic BAK

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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

Structural biology of the Bcl-2 family and its mimicry by viral proteins

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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

Protein–protein interactions as druggable targets: recent technological advances

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Targeting post-mitochondrial effectors of apoptosis for neuroprotection

Galluzzi, L., Morselli, E., Kepp, O., & Kroemer, G. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.09.006 · Cited by 119 · see citing works

ABT ‐199 selectively inhibits BCL 2 but not BCL 2 L 1 and efficiently induces apoptosis of chronic lymphocytic leukaemic cells but not platelets

Vogler, M., Dinsdale, D. D., Dyer, M. J. S., & Cohen, G. M. (2013) · British Journal of Haematology · doi:10.1111/bjh.12457 · Cited by 105 · see citing works

Defining the p53 DNA‐binding domain/Bcl‐xL‐binding interface using NMR

Petros, A. M., Gunasekera, A. H., Xu, N., Olejniczak, E. T., & Fesik, S. W. (2004) · FEBS Letters · doi:10.1016/s0014-5793(04)00059-6 · Cited by 105 · see citing works

Evaluation and critical assessment of putative MCL-1 inhibitors

Varadarajan, S., Vogler, M., Butterworth, M., Dinsdale, D. D., Walensky, L. D., & Cohen, G. M. (2013) · Cell Death and Differentiation · doi:10.1038/cdd.2013.79 · Cited by 101 · see citing works

Oligomerization of BAK by p53 Utilizes Conserved Residues of the p53 DNA Binding Domain

Pietsch, E. C., Perchiniak, E. M., Canutescu, A. A., Wang, G., Dunbrack, R. L., & Murphy, M. E. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m710539200 · Cited by 94 · 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

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The MDM2-Binding Region in the Transactivation Domain of p53 Also Acts as a Bcl-X L -Binding Motif

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Viral Inhibition of BAK Promotes Murine Cytomegalovirus Dissemination to Salivary Glands

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