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

<i>Coot</i> : model-building tools for molecular graphics

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<i>PHENIX</i> : a comprehensive Python-based system for macromolecular structure solution

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Linking Crystallographic Model and Data Quality

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Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics

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Bax-Deficient Mice with Lymphoid Hyperplasia and Male Germ Cell Death

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Proapoptotic Bak is sequestered by Mcl-1 and Bcl-x L , but not Bcl-2, until displaced by BH3-only proteinsPreprint

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Structure of Bax

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

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

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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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Relationship of Membrane Curvature to the Formation of Pores by Magainin 2

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To Trigger Apoptosis, Bak Exposes Its BH3 Domain and Homodimerizes via BH3:Groove Interactions

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BID Preferentially Activates BAK while BIM Preferentially Activates BAX, Affecting Chemotherapy Response

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

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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

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Bak Activation for Apoptosis Involves Oligomerization of Dimers via Their α6 Helices

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BID-induced structural changes in BAK promote apoptosis

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Bax dimerizes via a symmetric BH3:groove interface during apoptosis

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

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Direct activation of full-length proapoptotic BAK

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

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A three-helix homo-oligomerization domain containing BH3 and BH1 is responsible for the apoptotic activity of BaxPreprint

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

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Evaluation of the BH3-only Protein Puma as a Direct Bak Activator

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Assembly of the Bak Apoptotic Pore

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Transbilayer Lipid Diffusion Promoted by Bax: Implications for Apoptosis

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BIM-mediated membrane insertion of the BAK pore domain is an essential requirement for apoptosis

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Bax, Bak and beyond — mitochondrial performance in apoptosis

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

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BAX, BAK, and BOK: A Coming of Age for the BCL-2 Family Effector ProteinsPreprint

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BCL‐2‐family protein tBID can act as a BAX‐like effector of apoptosis

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Apoptosis and Cancer

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Targeting BCL-2-like Proteins to Kill Cancer Cells

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

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Parkin inhibits BAK and BAX apoptotic function by distinct mechanisms during mitophagy

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Structures of p53/BCL-2 complex suggest a mechanism for p53 to antagonize BCL-2 activity

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Disordered clusters of Bak dimers rupture mitochondria during apoptosis

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

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Crosstalk between apoptosis and autophagy signaling pathways

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VDAC2 and the BCL-2 family of proteins

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BAK core dimers bind lipids and can be bridged by them

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BCL2 Family, Mitochondrial Apoptosis, and Beyond

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Conversion of Bim-BH3 from Activator to Inhibitor of Bak through Structure-Based Design

Brouwer, J. M., Lan, P., Cowan, A. D., Bernardini, J. P., Birkinshaw, R. W., van Delft, M. F., Sleebs, B. E., Robin, A. Y., Wardak, A. Z., Tan, I. K. L., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.11.001 · Cited by 64 · 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

Epigenetic control of mitochondrial cell death through PACS1-mediated regulation of BAX/BAK oligomerization

Brasacchio, D., Alsop, A. E., Noori, T., Lufti, M., Iyer, S., Simpson, K. J., Bird, P. I., Kluck, R. M., Johnstone, R. W., & Trapani, J. A. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2016.119 · Cited by 63 · see citing works

Expanding roles of BCL-2 proteins in apoptosis execution and beyond

King, L., Hohorst, L., & García‐Sáez, A. J. (2023) · Journal of Cell Science · doi:10.1242/jcs.260790 · Cited by 65 · see citing works

A small molecule interacts with VDAC2 to block mouse BAK-driven apoptosis

van Delft, M. F., Chappaz, S., Khakham, Y., Bui, C. T., Debrincat, M. A., Lowes, K. N., Brouwer, J. M., Grohmann, C., Sharp, P. P., Dagley, L. F., et al. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0365-8 · Cited by 59 · see citing works

Constitutive BAK activation as a determinant of drug sensitivity in malignant lymphohematopoietic cellsPreprint

Dai, H., Ding, H., Meng, X. W., Peterson, K. L., Schneider, P. A., Karp, J. E., & Kaufmann, S. H. (2015) · Genes & Development · doi:10.1101/gad.267997.115 · Cited by 60 · see citing works

Identification of an activation site in Bak and mitochondrial Bax triggered by antibodies

Iyer, S., Anwari, K., Alsop, A. E., Yuen, W. S., Huang, D. C. S., Carroll, J., Smith, N. A., Smith, B. J., Dewson, G., & Kluck, R. M. (2016) · Nature Communications · doi:10.1038/ncomms11734 · Cited by 58 · 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

BAX Activation: Mutations Near Its Proposed Non-canonical BH3 Binding Site Reveal Allosteric Changes Controlling Mitochondrial Association

Dengler, M. A., Robin, A. Y., Gibson, L., Li, X., Sandow, J. J., Iyer, S., Webb, A. I., Westphal, D., Dewson, G., & Adams, J. M. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.03.040 · Cited by 56 · see citing works

The BCL-2 protein family: from discovery to drug development

Croce, C. M., Vaux, D. L., Strasser, A., Opferman, J. T., Czabotar, P. E., & Fesik, S. W. (2025) · Cell Death and Differentiation · doi:10.1038/s41418-025-01481-z · Cited by 53 · see citing works

Topology of active, membrane-embedded Bax in the context of a toroidal pore

Bleicken, S., Assafa, T. E., Stegmueller, C., Wittig, A., García‐Sáez, A. J., & Bordignon, E. (2018) · Cell Death and Differentiation · doi:10.1038/s41418-018-0184-6 · Cited by 60 · see citing works

Robust autoactivation for apoptosis by BAK but not BAX highlights BAK as an important therapeutic target

Iyer, S., Uren, R. T., Dengler, M. A., Shi, M. X., Uno, E., Adams, J. M., Dewson, G., & Kluck, R. M. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-2463-7 · Cited by 45 · 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

Mitochondrial apoptosis and BH3 mimetics

Dai, H., Meng, X. W., & Kaufmann, S. H. (2016) · F1000Research · doi:10.12688/f1000research.9629.1 · Cited by 42 · see citing works

Characterization of an alternative BAK-binding site for BH3 peptides

Ye, K., Meng, W. X., Sun, H., Wu, B., Chen, M., Pang, Y., Gao, J., Wang, H., Wang, J., Kaufmann, S. H., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-17074-y · Cited by 42 · see citing works

BAK α6 permits activation by BH3-only proteins and homooligomerization via the canonical hydrophobic groove

Li, X., Tan, I. K. L., Ma, S. B., Hockings, C., Kratina, T., Dengler, M. A., Alsop, A. E., Kluck, R. M., & Dewson, G. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1702453114 · Cited by 41 · see citing works

Structural basis of BAX pore formation

Zhang, Y., Tian, L., Huang, G., Ge, X., Kong, F., Wang, P., Xu, Y., & Shi, Y. (2025) · Science · doi:10.1126/science.adv4314 · Cited by 40 · see citing works

Histone deacetylase inhibitors interrupt HSP90•RASGRP1 and HSP90•CRAF interactions to upregulate BIM and circumvent drug resistance in lymphoma cells

Ding, H., Peterson, K. L., Correia, C., Koh, B. D., Schneider, P., Nowakowski, G. S., & Kaufmann, S. H. (2016) · Leukemia · doi:10.1038/leu.2016.357 · Cited by 40 · see citing works

The Functional Differences between Pro-survival and Pro-apoptotic B Cell Lymphoma 2 (Bcl-2) Proteins Depend on Structural Differences in Their Bcl-2 Homology 3 (BH3) Domains

Lee, E. F., Dewson, G., Evangelista, M., Pettikiriarachchi, A., Gold, G., Zhu, H., Colman, P. M., & Fairlie, W. D. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.610758 · Cited by 39 · see citing works

Structure of detergent-activated BAK dimers derived from the inert monomer

Birkinshaw, R. W., Iyer, S., Lio, D. S. S., Luo, C. S., Brouwer, J. M., Miller, M. S., Robin, A. Y., Uren, R. T., Dewson, G., Kluck, R. M., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.03.014 · Cited by 39 · see citing works

Directly targeting BAX for drug discovery: Therapeutic opportunities and challenges

Zhang, Z., Hou, L., Liu, D., Luan, S., Huang, M., & Zhao, L. (2024) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2024.02.010 · Cited by 41 · see citing works

Structural basis of BAK activation in mitochondrial apoptosis initiation

Singh, G., Guibao, C. D., Seetharaman, J., Aggarwal, A., Grace, C. R., McNamara, D. E., Vaithiyalingam, S., Waddell, M. B., & Moldoveanu, T. (2022) · Nature Communications · doi:10.1038/s41467-021-27851-y · Cited by 36 · see citing works

Dying to protect: cell death and the control of T‐cell homeostasis

Li, K., Shanmuganad, S., Carroll, K. R., Katz, J. D., Jordan, M. B., & Hildeman, D. A. (2017) · Immunological Reviews · doi:10.1111/imr.12538 · Cited by 34 · see citing works

Mitochondria: A Galaxy in the Hematopoietic and Leukemic Stem Cell Universe

Panuzzo, C., Jovanovski, A., Pergolizzi, B., Pironi, L., Stanga, S., Fava, C., & Cilloni, D. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21113928 · Cited by 34 · see citing works

An amphipathic Bax core dimer forms part of the apoptotic pore wall in the mitochondrial␣membrane

Lv, F., Qi, F., Zhang, Z., Wen, M., Kale, J., Piai, A., Du, L., Wang, S., Zhou, L., Yang, Y., et al. (2021) · The EMBO Journal · doi:10.15252/embj.2020106438 · Cited by 34 · see citing works

Grouper iridovirus GIV66 is a Bcl-2 protein that inhibits apoptosis by exclusively sequestering Bim

Banjara, S., Mao, J., Ryan, T. M., Caria, S., & Kvansakul, M. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.000591 · Cited by 33 · see citing works

Structural Details of BH3 Motifs and BH3-Mediated Interactions: an Updated Perspective

Sora, V., & Papaleo, E. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.864874 · Cited by 32 · see citing works

Dynamic reconfiguration of pro‐apoptotic BAK on membranes

Sandow, J. J., Tan, I. K. L., Huang, A. S., Masaldan, S., Bernardini, J. P., Wardak, A. Z., Birkinshaw, R. W., Ninnis, R. L., Liu, Z., Dalseno, D., et al. (2021) · The EMBO Journal · doi:10.15252/embj.2020107237 · Cited by 41 · see citing works

Protein–protein and protein–lipid interactions of pore-forming BCL-2 family proteins in apoptosis initiation

Sekar, G., Ojoawo, A. M., & Moldoveanu, T. (2022) · Biochemical Society Transactions · doi:10.1042/bst20220323 · Cited by 31 · see citing works

Pharmacological Targeting of Executioner Proteins: Controlling Life and Death

Pogmore, J. P., Uehling, D., & Andrews, D. W. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c02200 · Cited by 28 · see citing works

Bax retrotranslocation potentiates Bcl-xL’s antiapoptotic activity and is essential for switch-like transitions between MOMP competency and resistance

Hantusch, A., Das, K. K., García‐Sáez, A. J., Brunner, T., & Rehm, M. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0464-6 · Cited by 27 · see citing works

Cellular demolition: Proteins as molecular players of programmed cell death

Dhuriya, Y. K., Sharma, D., & Naik, A. A. (2019) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2019.07.113 · Cited by 26 · see citing works

High‐resolution analysis of the conformational transition of pro‐apoptotic Bak at the lipid membrane

Sperl, L. E., Rührnößl, F., Schiller, A., Haslbeck, M., & Hagn, F. (2021) · The EMBO Journal · doi:10.15252/embj.2020107159 · Cited by 25 · see citing works

Structural transition in Bcl-xL and its potential association with mitochondrial calcium ion transport

Rajan, S. S., Choi, M., Nguyen, Q. T., Ye, H., Liu, W., Toh, H. T., Kang, C., Kamariah, N., Li, C., Huang, H., et al. (2015) · Scientific Reports · doi:10.1038/srep10609 · Cited by 24 · see citing works

Truncated Bid Regulates Cisplatin Response via Activation of Mitochondrial Apoptosis Pathway in Ovarian Cancer

Dai, Y., Zhao, X., Li, F., Yuan, Y., Yan, D., Cao, H., Huang, X., Hu, Z., Ma, D., & Gao, Q. (2020) · Human Gene Therapy · doi:10.1089/hum.2019.206 · Cited by 24 · see citing works

Structural basis for dimerization of the death effector domain of the F122A mutant of Caspase-8

Shen, C., Pei, J., Guo, X., Zhou, L., Li, Q., & Quan, J. (2018) · Scientific Reports · doi:10.1038/s41598-018-35153-5 · Cited by 21 · see citing works

Key residues in the VDAC2-BAK complex can be targeted to modulate apoptosis

Yuan, Z., van Delft, M. F., Li, X., Sumardy, F., Smith, B. J., Huang, D. C. S., Lessène, G., Khakam, Y., Jin, R., He, S., et al. (2024) · PLoS Biology · doi:10.1371/journal.pbio.3002617 · Cited by 18 · see citing works

The C-terminal sequences of Bcl-2 family proteins mediate interactions that regulate cell death

Nguyen, D. Q., Osterlund, E. J., Kale, J., & Andrews, D. W. (2024) · Biochemical Journal · doi:10.1042/bcj20210352 · Cited by 20 · see citing works

A BAK subdomain that binds mitochondrial lipids selectively and releases cytochrome C

Dai, H., Peterson, K. L., Flatten, K. S., Meng, X. W., Venkatachalam, A., Correia, C., Ramı́rez-Alvarado, M., Pang, Y., & Kaufmann, S. H. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-01083-z · Cited by 19 · see citing works

Cell death classification: A new insight based on molecular mechanisms

Dehghan, S., Kheshtchin, N., Hassannezhad, S., & Soleimani, M. (2023) · Experimental Cell Research · doi:10.1016/j.yexcr.2023.113860 · Cited by 18 · see citing works

Anti-apoptotic A1 is not essential for lymphoma development in Eµ-Myc mice but helps sustain transplanted Eµ-Myc tumour cells

Mensink, M., Anstee, N. S., Robati, M., Schenk, R. L., Herold, M. J., Cory, S., & Vandenberg, C. J. (2018) · Cell Death and Differentiation · doi:10.1038/s41418-017-0045-8 · Cited by 17 · see citing works

Apoptotic mitochondrial poration by a growing list of pore‐forming BCL‐2 family proteins

Moldoveanu, T. (2023) · BioEssays · doi:10.1002/bies.202200221 · Cited by 16 · see citing works

Preparing Samples for Crystallization of Bcl-2 Family Complexes

Kvansakul, M., & Czabotar, P. E. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-3581-9_16 · Cited by 17 · see citing works

Counting on Death – Quantitative aspects of Bcl‐2 family regulation

Hantusch, A., Rehm, M., & Brunner, T. (2018) · FEBS Journal · doi:10.1111/febs.14516 · Cited by 17 · see citing works

BCL-XL directly retrotranslocates the monomeric BAK

Wang, B., Mai, Z., Du, M., Wang, L., Yang, F., Ma, Y., Wang, X., & Chen, T. (2019) · Cellular Signalling · doi:10.1016/j.cellsig.2019.05.001 · Cited by 17 · see citing works

Structural basis of BAK sequestration by MCL-1 in apoptosis

Srivastava, S., Sekar, G., Ojoawo, A. M., Aggarwal, A., Ferreira, E., Uchikawa, E., Yang, M., Grace, C. R., Dey, R., Lin, Y.-L., et al. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.03.013 · Cited by 17 · see citing works

Discovery, development and application of drugs targeting BCL-2 pro-survival proteins in cancer

Lee, E. F., & Fairlie, W. D. (2021) · Biochemical Society Transactions · doi:10.1042/bst20210749 · Cited by 18 · see citing works

Small molecule SJ572946 activates BAK to initiate apoptosis

Sekar, G., Singh, G., Qin, X., Guibao, C. D., Schwam, B., Inde, Z., Grace, C. R., Zhang, W., Slavish, P. J., Lin, W., et al. (2022) · iScience · doi:10.1016/j.isci.2022.105064 · Cited by 15 · see citing works

Sequence differences between BAX and BAK core domains manifest as differences in their interactions with lipids

Miller, M. S., Cowan, A. D., Brouwer, J. M., Smyth, S. T., Peng, L., Wardak, A. Z., Uren, R. T., Luo, C. S., Roy, M. J., Shah, S., et al. (2023) · FEBS Journal · doi:10.1111/febs.17031 · Cited by 16 · see citing works

Probing BAK and BAX Activation and Pore Assembly with Cytochrome c Release, Limited Proteolysis, and Oxidant-Induced Linkage

Iyer, S., Uren, R. T., & Kluck, R. M. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-8861-7_14 · Cited by 16 · see citing works

An unconventional autophagic pathway that inhibits ATP secretion during apoptotic cell death

Terraza-Silvestre, E., Villamuera, R., Bandera-Linero, J., Letek, M., Oña-Sánchez, D., Ramón-Barros, C., Moyano-Jimeno, C., & Pimentel‐Muiños, F. X. (2025) · Nature Communications · doi:10.1038/s41467-025-58619-3 · Cited by 17 · see citing works

DIDS inhibits overexpression BAK1‐induced mitochondrial apoptosis through GSK3β/β‐catenin signaling pathway

Yang, X., Tang, S., Li, D., Yu, X., Wang, F., & Xiao, X. (2017) · Journal of Cellular Physiology · doi:10.1002/jcp.26396 · Cited by 15 · see citing works

Structural Insights into Bak Activation and Oligomerisation

Brouwer, J. M., Robin, A. Y., Thompson, G. V., Wardak, A. Z., Kluck, R. M., Colman, P. M., & Czabotar, P. E. (2014) · Acta Crystallographica Section A Foundations and Advances · doi:10.1107/s2053273314088330

Crystal structures of Bax and Bak Reveal Molecular Events Initiating Apoptosis

Czabotar, P. E., Brouwer, J. M., Westphal, D., Thompson, G. V., & Colman, P. M. (2014) · Acta Crystallographica Section A Foundations and Advances · doi:10.1107/s205327331408509x

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

Assembly of the Bak Apoptotic Pore

Ma, S., Hockings, C., Anwari, K., Kratina, T., Fennell, S., Lazarou, M., Ryan, M. T., Kluck, R. M., & Dewson, G. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.490094 · Cited by 71 · see citing works

BAK α6 permits activation by BH3-only proteins and homooligomerization via the canonical hydrophobic groove

Li, X., Tan, I. K. L., Ma, S. B., Hockings, C., Kratina, T., Dengler, M. A., Alsop, A. E., Kluck, R. M., & Dewson, G. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1702453114 · Cited by 41 · see citing works