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

Comparison of simple potential functions for simulating liquid water

Jorgensen, W. L., Chandrasekhar, J., Madura, J., Impey, R., & Klein, M. (1983) · The Journal of Chemical Physics · doi:10.1063/1.445869 · Cited by 38,335 · see citing works

Molecular dynamics with coupling to an external bath

Berendsen, H. J. C., Postma, J. P. M., van Gunsteren, W. F., DiNola, A., & Haak, J. R. (1984) · The Journal of Chemical Physics · doi:10.1063/1.448118 · Cited by 30,626 · see citing works

Particle mesh Ewald: An N⋅log(N) method for Ewald sums in large systems

Darden, T., York, D., & Pedersen, L. (1993) · The Journal of Chemical Physics · doi:10.1063/1.464397 · Cited by 29,588 · see citing works

The Amber biomolecular simulation programs

Case, D. A., Cheatham, T. E., Darden, T., Gohlke, H., Luo, R., Merz, K. M., Onufriev, A., Simmerling, C., Wang, B., & Woods, R. J. (2005) · Journal of Computational Chemistry · doi:10.1002/jcc.20290 · Cited by 9,535 · see citing works

Comparison of multiple Amber force fields and development of improved protein backbone parameters

Horn̆ák, V., Abel, R., Okur, A., Strockbine, B., Roitberg, A. E., & Simmerling, C. L. (2006) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21123 · Cited by 6,903 · see citing works

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

The Bcl2 family: regulators of the cellular life-or-death switch

Cory, S., & Adams, J. M. (2002) · Nature Reviews Cancer · doi:10.1038/nrc883 · Cited by 4,032 · see citing works

Proapoptotic BAX and BAK: A Requisite Gateway to Mitochondrial Dysfunction and Death

Wei, M. C., Zong, W.-X., Cheng, E. H.-Y., Lindsten, T., Panoutsakopoulou, V., Ross, A. J., Roth, K. A., MacGregor, G. R., Thompson, C. B., & Korsmeyer, S. J. (2001) · Science · doi:10.1126/science.1059108 · Cited by 3,988 · see citing works

Mitochondrial membrane permeabilization in cell death

Kroemer, G., Galluzzi, L., & Brenner, C. (2007) · Physiological Reviews · doi:10.1152/physrev.00013.2006 · Cited by 3,598 · see citing works

AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules

Pearlman, D. A., Case, D. A., Caldwell, J. W., Ross, W. S., Cheatham, T. E., DeBolt, S., Ferguson, D. M., Seibel, G., & Kollman, P. A. (1995) · Computer Physics Communications · doi:10.1016/0010-4655(95)00041-d · Cited by 3,129 · see citing works

Noxa, a BH3-Only Member of the Bcl-2 Family and Candidate Mediator of p53-Induced Apoptosis

Oda, E., Ohki, R., Murasawa, H., Nemoto, J., Shibue, T., Yamashita, T., Tokino, T., Taniguchi, T., & Tanaka, †. N. (2000) · Science · doi:10.1126/science.288.5468.1053 · Cited by 2,112 · see citing works

The SWISS-MODEL Repository and associated resources

Kiefer, F., Arnold, K., Künzli, M., Bordoli, L., & Schwede, T. F. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn750 · Cited by 2,003 · 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

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

The BCL-2 Family Reunion

Chipuk, J. E., Moldoveanu, T., Llambi, F., Parsons, M. J., & Green, D. R. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.01.025 · Cited by 1,432 · see citing works

Cytochrome C -Mediated Apoptosis

Jiang, X., & Wang, X. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073706 · Cited by 1,359 · 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

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

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

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

Clustering Molecular Dynamics Trajectories: 1. Characterizing the Performance of Different Clustering Algorithms

Shao, J., Tanner, S. W., Thompson, N., & Cheatham, T. E. (2007) · Journal of Chemical Theory and Computation · doi:10.1021/ct700119m · Cited by 832 · see citing works

Methods for the detection and analysis of protein–protein interactions

Berggård, T., Linse, S. S., & James, P. (2007) · PROTEOMICS · doi:10.1002/pmic.200700131 · Cited by 714 · 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

Bax Is Present as a High Molecular Weight Oligomer/Complex in the Mitochondrial Membrane of Apoptotic Cells

Antonsson, B. E., Montessuit, S., Sanchez, B., & Martinou, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010810200 · Cited by 676 · see citing works

Regulated Targeting of BAX to Mitochondria

Goping, I. S., Gross, A., Lavoie, J. N., Nguyen, M., Jemmerson, R., Roth, K. A., Korsmeyer, S. J., & Shore, G. C. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.1.207 · Cited by 611 · 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

Membrane Binding by tBid Initiates an Ordered Series of Events Culminating in Membrane Permeabilization by Bax

Lovell, J. F., Billen, L. P., Bindner, S., Shamas‐Din, A., Fradin, C., Leber, B. F., & Andrews, D. W. (2008) · Cell · doi:10.1016/j.cell.2008.11.010 · Cited by 565 · see citing works

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

Proapoptotic multidomain Bcl-2/Bax-family proteins: mechanisms, physiological roles, and therapeutic opportunities

Reed, J. C. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401975 · Cited by 474 · see citing works

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

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

A Stapled BID BH3 Helix Directly Binds and Activates BAX

Walensky, L. D., Pitter, K., Morash, J., Oh, K. J., Barbuto, S., Fisher, J., Smith, E., Verdine, G. L., & Korsmeyer, S. J. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.08.020 · Cited by 383 · see citing works

Mechanisms by which Bak and Bax permeabilise mitochondria during apoptosis

Dewson, G., & Kluck, R. M. (2009) · Journal of Cell Science · doi:10.1242/jcs.038166 · Cited by 360 · 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

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

Evaluating the Performance of the ff99SB Force Field Based on NMR Scalar Coupling Data

Wickstrom, L., Okur, A., & Simmerling, C. L. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2009.04.063 · Cited by 211 · 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

Overview of Biacore Systems and Their Applications

Jason‐Moller, L., Murphy, M. B., & Bruno, J. (2006) · Current Protocols in Protein Science · doi:10.1002/0471140864.ps1913s45 · Cited by 155 · see citing works

MCL-1 as a Buffer for Proapoptotic BCL-2 Family Members during TRAIL-induced Apoptosis

Meng, X. W., Lee, S. H., Dai, H., Loegering, D. A., Yu, C., Flatten, K. S., Schneider, P. A., Dai, N. T., Kumar, S. K., Smith, B. D., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706110200 · Cited by 108 · see citing works

Noxa/Bcl-2 Protein Interactions Contribute to Bortezomib Resistance in Human Lymphoid Cells

Smith, A. J., Dai, H., Correia, C., Takahashi, R., Lee, S. H., Schmitz, I., & Kaufmann, S. H. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.189092 · Cited by 96 · 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

Structure of HI-6•Sarin-Acetylcholinesterase Determined by X-Ray Crystallography and Molecular Dynamics Simulation: Reactivator Mechanism and Design

Ekström, F., Hörnberg, A., Artursson, E., Hammarström, L., Schneider, G., & Pang, Y. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005957 · Cited by 83 · see citing works

Cellular damage signals promote sequential changes at the N-terminus and BH-1 domain of the pro-apoptotic protein Bak

Griffiths, G. J., Corfe, B. M., Savory, P., Leech, S. H., Esposti, M. D., Hickman, J. A., & Dive, C. (2001) · Oncogene · doi:10.1038/sj.onc.1204995 · Cited by 82 · see citing works

Molecular cloning and characterization of a cDNA for a novel phorbol-12-myristate-13-acetate-responsive gene that is highly expressed in an adult T-cell leukemia cell line

Hijikata, M., Kato, N., Sato, T., Kagami, Y., & Shimotohno, K. (1990) · Journal of Virology · doi:10.1128/jvi.64.10.4632-4639.1990 · Cited by 65 · see citing works

Chapter 23 Dissection of the BCL‐2 Family Signaling Network with Stabilized α‐Helices of BCL‐2 Domains

Pitter, K. L., Bernal, F., LaBelle, J. L., & Walensky, L. D. (2008) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(08)01623-6 · Cited by 46 · see citing works

Three‐dimensional model of a substrate‐bound SARS chymotrypsin‐like cysteine proteinase predicted by multiple molecular dynamics simulations: Catalytic efficiency regulated by substrate binding

Pang, Y. (2004) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20249 · Cited by 45 · see citing works

S-peptide epitope tagging for protein purification, expression monitoring, and localization in mammalian cells.

Hackbarth, J. S., Lee, S. H., Meng, X. W., Vroman, B. T., Kaufmann, S. H., & Karnitz, L. M. (2004) · PubMed · Cited by 39 · see citing works

Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018.

Galluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death & Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680 · see citing works

Control of apoptosis by the BCL-2 protein family: implications for physiology and therapy

Czabotar, P. E., Lessene, G., Strasser, A., & Adams, J. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3722 · Cited by 3,219 · see citing works

Targeting apoptosis in cancer therapy

Carneiro, B. A., & El‐Deiry, W. S. (2020) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-020-0341-y · Cited by 2,594 · 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

The role of BCL-2 family proteins in regulating apoptosis and cancer therapy

Qian, S., Wei, Z., Yang, W., Huang, J., Yang, Y., & Wang, J. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.985363 · Cited by 1,011 · see citing works

Bax, Bak and beyond — mitochondrial performance in apoptosis

Peña‐Blanco, A., & García‐Sáez, A. J. (2017) · FEBS Journal · doi:10.1111/febs.14186 · Cited by 939 · see citing works

Mechanisms of BCL-2 family proteins in mitochondrial apoptosis

Czabotar, P. E., & García‐Sáez, A. J. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00629-4 · Cited by 718 · 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

Deciphering the rules of programmed cell death to improve therapy of cancer and other diseases

Strasser, A., Cory, S., & Adams, J. M. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.307 · Cited by 530 · 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

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

Apoptotic cell death in disease—Current understanding of the NCCD 2023

Vitale, I., Pietrocola, F., Guilbaud, E., Aaronson, S. A., Abrams, J., Adam, D., Agostini, M., Agostinis, P., Alnemri, E. S., Altucci, L., et al. (2023) · Cell Death and Differentiation · doi:10.1038/s41418-023-01153-w · Cited by 359 · see citing works

Mitochondria—Judges and Executioners of Cell Death Sentences

Bhola, P. D., & Letai, A. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.02.019 · Cited by 326 · see citing works

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

O'Neill, K. L., Huang, K., Zhang, J., Chen, Y., & Luo, X. (2016) · Genes & Development · doi:10.1101/gad.276725.115 · Cited by 323 · see citing works

Why do BCL-2 inhibitors work and where should we use them in the clinic?

Montero, J., & Letai, A. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.183 · Cited by 325 · 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 rheostat in the membrane: BCL-2 family proteins and apoptosis

Volkmann, N., Marassi, F. M., Newmeyer, D. D., & Hanein, D. (2013) · Cell Death and Differentiation · doi:10.1038/cdd.2013.153 · Cited by 224 · see citing works

COMMD1 is linked to the WASH complex and regulates endosomal trafficking of the copper transporter ATP7A

Phillips-Krawczak, C. A., Singla, A., Starokadomskyy, P., Deng, Z.-H., Osborne, D. G., Li, H., Dick, C. J., Gomez, T. S., Koenecke, M., Zhang, J., et al. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-06-1073 · Cited by 217 · 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

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

BCL-XL and MCL-1 are the key BCL-2 family proteins in melanoma cell survival

Lee, E. F., Harris, T. J., Tran, S. H., Evangelista, M., Arulananda, S., John, T., Ramnac, C., Hobbs, C., Zhu, H., Gunasingh, G. P., et al. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1568-3 · Cited by 188 · 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

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

Flores‐Romero, H., Hohorst, L., John, M. D., Albert, M., King, L., Beckmann, L., Szabó, T. G., Hertlein, V., Luo, X., Villunger, A., et al. (2021) · The EMBO Journal · doi:10.15252/embj.2021108690 · Cited by 172 · see citing works

The Bcl-2 family: structures, interactions and targets for drug discovery

Kvansakul, M., & Hinds, M. G. (2014) · APOPTOSIS · doi:10.1007/s10495-014-1051-7 · Cited by 168 · see citing works

Emerging understanding of Bcl-2 biology: Implications for neoplastic progression and treatment

Correia, C., Lee, S. H., Meng, X. W., Vincelette, N. D., Knorr, K. L. B., Ding, H., Nowakowski, G. S., Dai, H., & Kaufmann, S. H. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.03.012 · Cited by 167 · see citing works

Direct activation of full-length proapoptotic BAK

Leshchiner, E. S., Braun, C. R., Bird, G. H., & Walensky, L. D. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1214313110 · Cited by 157 · 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

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

BH3-only proteins target BCL-xL/MCL-1, not BAX/BAK, to initiate apoptosis

Huang, K., O’Neill, K. L., Li, J., Zhou, W., Han, N., Pang, X., Wu, W., Struble, L. R., Borgstahl, G., Liu, Z., et al. (2019) · Cell Research · doi:10.1038/s41422-019-0231-y · Cited by 140 · see citing works

Stabilizing the Pro-Apoptotic BimBH3 Helix (BimSAHB) Does Not Necessarily Enhance Affinity or Biological Activity

Okamoto, T., Zobel, K., Fedorova, A., Quan, C., Yang, H., Fairbrother, W. J., Huang, D. C. S., Smith, B. J., Deshayes, K., & Czabotar, P. E. (2013) · ACS Chemical Biology · doi:10.1021/cb3005403 · Cited by 136 · see citing works

BCL-2 family deregulation in colorectal cancer: potential for BH3 mimetics in therapy

Ramesh, P., & Medema, J. P. (2020) · APOPTOSIS · doi:10.1007/s10495-020-01601-9 · Cited by 131 · see citing works

Mcl-1 Phosphorylation Defines ABT-737 Resistance That Can Be Overcome by Increased NOXA Expression in Leukemic B cells

Mazumder, S., Choudhary, G. S., Al-harbi, S., & Almasan, A. (2012) · Cancer Research · doi:10.1158/0008-5472.can-11-4106 · Cited by 117 · 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

Prime, Shock, and Kill: Priming CD4 T Cells from HIV Patients with a BCL-2 Antagonist before HIV Reactivation Reduces HIV Reservoir Size

Cummins, N. W., Sainski, A. M., Dai, H., Natesampillai, S., Pang, Y., Bren, G. D., Correia, M. C. M. D. A., Sampath, R., Rizza, S. A., O’Brien, D. R., et al. (2016) · Journal of Virology · doi:10.1128/jvi.03179-15 · Cited by 102 · see citing works

New dimension in therapeutic targeting of BCL-2 family proteins

Besbes, S., Mirshahi, M., Pocard, M. D., & Billard, C. (2015) · Oncotarget · doi:10.18632/oncotarget.3868 · Cited by 101 · see citing works

Targeting BAX to drug death directly

Walensky, L. D. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0306-6 · Cited by 95 · see citing works

Mitochondria and apoptosis: emerging concepts

Li, X., & Dewson, G. (2015) · F1000Prime Reports · doi:10.12703/p7-42 · Cited by 98 · see citing works

Selectively targeting Mcl-1 for the treatment of acute myelogenous leukemia and solid tumors: Figure 1.Preprint

Gores, G. J., & Kaufmann, S. H. (2012) · Genes & Development · doi:10.1101/gad.186189.111 · Cited by 99 · see citing works

MLN4924 induces Noxa upregulation in acute myelogenous leukemia and synergizes with Bcl-2 inhibitors

Knorr, K. L. B., Schneider, P., Meng, X. W., Dai, H., Smith, B. D., Hess, A. D., Karp, J. E., & Kaufmann, S. H. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2015.74 · Cited by 98 · see citing works

Contribution of Bcl-2 Phosphorylation to Bak Binding and Drug Resistance

Dai, H., Ding, H., Meng, X. W., Lee, S. H., Schneider, P. A., & Kaufmann, S. H. (2013) · Cancer Research · doi:10.1158/0008-5472.can-13-0940 · Cited by 98 · see citing works

Disordered clusters of Bak dimers rupture mitochondria during apoptosis

Uren, R. T., O’Hely, M., Iyer, S., Bartolo, R. C., Shi, M. X., Brouwer, J. M., Alsop, A. E., Dewson, G., & Kluck, R. M. (2017) · eLife · doi:10.7554/elife.19944 · Cited by 97 · 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

Computationally designed high specificity inhibitors delineate the roles of BCL2 family proteins in cancer

Berger, S., Procko, E., Margineantu, D. H., Lee, E. F., Shen, B. W., Zelter, A., Silva, D., Chawla, K., Herold, M. J., Garnier, J.-M., et al. (2016) · eLife · doi:10.7554/elife.20352 · Cited by 93 · see citing works

BH3-dependent and independent activation of BAX and BAK in mitochondrial apoptosis

Jeng, P., Inoue‐Yamauchi, A., Hsieh, J. J.-D., & Cheng, E. H. Y. (2018) · Current Opinion in Physiology · doi:10.1016/j.cophys.2018.03.005 · Cited by 93 · see citing works

Direct Interaction of Bax and Bak Proteins with Bcl-2 Homology Domain 3 (BH3)-only Proteins in Living Cells Revealed by Fluorescence Complementation

Vela, L., Gonzalo, Ó., Naval, J., & Marzo, I. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.422204 · Cited by 90 · see citing works

Kill one or kill the many: interplay between mitophagy and apoptosis

Wanderoy, S., Hees, J. T., Klesse, R., Edlich, F., & Harbauer, A. B. (2020) · Biological Chemistry · doi:10.1515/hsz-2020-0231 · Cited by 91 · see citing works

Current overview on the clinical update of Bcl-2 anti-apoptotic inhibitors for cancer therapy

Suvarna, V., Singh, V., & Murahari, M. (2019) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2019.172655 · Cited by 89 · see citing works

Exploiting the pro-apoptotic function of NOXA as a therapeutic modality in cancer

Guikema, J. E. J., Amiot, M., & Eldering, E. (2017) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2017.1349754 · Cited by 80 · see citing works

CXCR4 Chemokine Receptor Signaling Induces Apoptosis in Acute Myeloid Leukemia Cells via Regulation of the Bcl-2 Family Members Bcl-XL, Noxa, and Bak

Kremer, K. N., Peterson, K. L., Schneider, P. A., Meng, X. W., Dai, H., Hess, A. D., Smith, B. D., Rodriguez-Ramirez, C., Karp, J. E., Kaufmann, S. H., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.449926 · Cited by 81 · see citing works

The third model of Bax/Bak activation: a Bcl-2 family feud finally resolved?

Luo, X., O’Neill, K. L., & Huang, K. (2020) · F1000Research · doi:10.12688/f1000research.25607.1 · Cited by 75 · see citing works

Novel Small-Molecule Inhibitors of Bcl-XL to Treat Lung Cancer

Park, D., Magis, A. T., Li, R., Owonikoko, T. K., Sica, G., Sun, S., Ramalingam, S. S., Khuri, F. R., Curran, W. J., & Deng, X. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-2272 · Cited by 74 · see citing works

Chitosan magnetic nanoparticles for pH responsive Bortezomib release in cancer therapy

Ünsoy, G., Yalçın, S., Khodadust, R., Mutlu, P., Öngürü, Ö., & Gündüz, U. (2014) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2014.04.003 · Cited by 73 · see citing works

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

Dai, H., Pang, Y., Ramı́rez-Alvarado, M., & Kaufmann, S. H. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.505701 · Cited by 73 · 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

Proteotoxic Stress and Cell Death in Cancer Cells

Brancolini, C., & Iuliano, L. (2020) · Cancers · doi:10.3390/cancers12092385 · Cited by 70 · 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

BCL2 Family, Mitochondrial Apoptosis, and Beyond

Dai, H., Meng, W., & Kaufmann, S. H. (2016) · Cancer translational medicine · doi:10.4103/2395-3977.177558 · Cited by 69 · see citing works

Multimodal Interaction with BCL-2 Family Proteins Underlies the Proapoptotic Activity of PUMA BH3

Edwards, A., Gavathiotis, E., LaBelle, J. L., Braun, C. R., Opoku-Nsiah, K., Bird, G. H., & Walensky, L. D. (2013) · Chemistry & Biology · doi:10.1016/j.chembiol.2013.06.007 · Cited by 68 · see citing works

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

BCL2L13: physiological and pathological meanings

Meng, F., Sun, N., Liu, D., Jia, J., Xiao, J., & Dai, H. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03702-9 · Cited by 63 · 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

Platelet-derived Growth Factor Primes Cancer-associated Fibroblasts for Apoptosis

Ilyas, S. I., Mertens, J. C., Bronk, S. F., Hirsova, P., Dai, H., Roberts, L. R., Kaufmann, S. H., & Gores, G. J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.563064 · Cited by 56 · see citing works

Translocation of a Bak C-Terminus Mutant from Cytosol to Mitochondria to Mediate Cytochrome c Release: Implications for Bak and Bax Apoptotic Function

Ferrer, P. E., Frederick, P., Gulbis, J. M., Dewson, G., & Kluck, R. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031510 · Cited by 53 · 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

Ensemble Properties of Bax Determine Its Function

Robin, A. Y., Iyer, S., Birkinshaw, R. W., Sandow, J. J., Wardak, A. Z., Luo, C. S., Shi, M. X., Webb, A. I., Czabotar, P. E., Kluck, R. M., et al. (2018) · Structure · doi:10.1016/j.str.2018.07.006 · Cited by 49 · see citing works

Bak Conformational Changes Induced by Ligand Binding: Insight into BH3 Domain Binding and Bak Homo-Oligomerization

Pang, Y., Dai, H., Smith, A. J., Meng, X. W., Schneider, P. A., & Kaufmann, S. H. (2012) · Scientific Reports · doi:10.1038/srep00257 · Cited by 47 · 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

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

Separase-triggered apoptosis enforces minimal length of mitosis

Hellmuth, S., & Stemmann, O. (2020) · Nature · doi:10.1038/s41586-020-2187-y · 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

Toxoplasma gondii isolate with genotype Chinese 1 triggers trophoblast apoptosis through oxidative stress and mitochondrial dysfunction in mice

Xu, X., He, L., Zhang, A., Li, Q., Hu, W., Chen, H., Du, J., & Shen, J. (2015) · Experimental Parasitology · doi:10.1016/j.exppara.2015.04.008 · Cited by 37 · see citing works

Beta-Amyloid Oligomers Activate Apoptotic BAK Pore for Cytochrome c Release

Kim, J., Yang, Y., Song, S. S., Na, J., Oh, K. J., Jeong, C., Yu, Y. G., & Shin, Y. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2014.07.074 · Cited by 37 · 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

Discovery of Small Molecule Bak Activator for Lung Cancer Therapy

Park, D., Anisuzzaman, A. S. M., Magis, A. T., Chen, G., Xie, M., Zhang, G., Behera, M., Sica, G., Ramalingam, S. S., Owonikoko, T. K., et al. (2021) · Theranostics · doi:10.7150/thno.60349 · Cited by 32 · see citing works

Casp8p41 generated by HIV protease kills CD4 T cells through direct Bak activation

Sainski, A. M., Dai, H., Natesampillai, S., Pang, Y., Bren, G. D., Cummins, N. W., Correia, C., Meng, X. W., Tarara, J. E., Ramı́rez-Alvarado, M., et al. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201405051 · 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

P53 Regulates Rapid Apoptosis in Human Pluripotent Stem Cells

Setoguchi, K., TeSlaa, T. A., Koehler, C. M., & Teitell, M. A. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.07.019 · Cited by 31 · see citing works

Farnesyltransferase inhibitor tipifarnib inhibits Rheb prenylation and stabilizes Bax in acute myelogenous leukemia cells

Ding, H., McDonald, J. S., Yun, S., Schneider, P. A., Peterson, K. L., Flatten, K. S., Loegering, D. A., Oberg, A. L., Riska, S. M., Huang, S., et al. (2013) · Haematologica · doi:10.3324/haematol.2013.087734 · Cited by 29 · see citing works

Bik reduces hyperplastic cells by increasing Bak and activating DAPk1 to juxtapose ER and mitochondria

Mebratu, Y. A., Leyva-Baca, I., Wathelet, M. G., Lacey, N. E., Chand, H. S., Choi, A. M. K., & Tesfaigzi, Y. (2017) · Nature Communications · doi:10.1038/s41467-017-00975-w · Cited by 28 · see citing works

Mitochondria in Human Pluripotent Stem Cell Apoptosis

TeSlaa, T. A., Setoguchi, K., & Teitell, M. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.01.027 · Cited by 31 · 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

miR‐125b lowers sensitivity to apoptosis following mitotic arrest: Implications for breast cancer therapy

Matuszyk, J., & Kłopotowska, D. (2020) · Journal of Cellular Physiology · doi:10.1002/jcp.29610 · Cited by 26 · see citing works

Measurement of BH3-only protein tolerance

Dai, H., Ding, H., Peterson, K. L., Meng, X. W., Schneider, P. A., Knorr, K. L. B., & Kaufmann, S. H. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.156 · Cited by 26 · see citing works

HIV Protease-Generated Casp8p41, When Bound and Inactivated by Bcl2, Is Degraded by the Proteasome

Natesampillai, S., Cummins, N. W., Nie, Z., Sampath, R., Baker, J. V., Henry, K., Pinzone, M. R., O’Doherty, U., Polley, E. C., Bren, G. D., et al. (2018) · Journal of Virology · doi:10.1128/jvi.00037-18 · 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

Analysis of the Binding Sites on BAX and the Mechanism of BAX Activators through Extensive Molecular Dynamics Simulations

Feng, G., Zhang, X., Li, Y., & Wang, R. (2021) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.0c01420 · Cited by 20 · see citing works

The fourth dimension in immunological space: how the struggle for nutrients selects high‐affinity lymphocytes

Wensveen, F. M., van Gisbergen, K. P. J. M., & Eldering, E. (2012) · Immunological Reviews · doi:10.1111/j.1600-065x.2012.01156.x · Cited by 20 · see citing works

MicroRNA Function Can Be Reversed by Altering Target Gene Expression Levels

Svoronos, A. A., Campbell, S. G., & Engelman, D. M. (2021) · iScience · doi:10.1016/j.isci.2021.103208 · Cited by 19 · 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

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

Bak apoptotic function is not directly regulated by phosphorylation

Tran, V., Bartolo, R. C., Westphal, D., Alsop, A. E., Dewson, G., & Kluck, R. M. (2013) · Cell Death and Disease · doi:10.1038/cddis.2012.191 · Cited by 16 · see citing works

Ligand Binding and Membrane Insertion Compete with Oligomerization of the BclXL Apoptotic Repressor

Bhat, V. S., McDonald, C. B., Mikles, D. C., Deegan, B. J., Seldeen, K. L., Bates, M. L., & Farooq, A. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.12.015 · 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

Charge Profile Analysis Reveals That Activation of Pro-apoptotic Regulators Bax and Bak Relies on Charge Transfer Mediated Allosteric Regulation

Ionescu, C.-M., Vařeková, R. S., Prehn, J. H. M., Huber, H. J., & Koča, J. (2012) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1002565 · Cited by 15 · see citing works

β,β-Dimethylacrylshikonin Induces Apoptosis in Melanoma Cell Lines by NOXA Upregulation

Stallinger, A., Kretschmer, N., Kleinegger, F., Brvar, L., Liegl‐Atzwanger, B., Prokesch, A., Durchschein, C., Bauer, R., Deutsch, A. J. A., & Rinner, B. (2020) · Journal of Natural Products · doi:10.1021/acs.jnatprod.9b00719 · Cited by 15 · see citing works

THE JOURNAL OF CELL BIOLOGY

Oligomerization, B., Dai, H., Smith, A., Meng, X. W., Schneider, P. A., Pang, Y., & Kaufmann, S. H. (2013)

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

I want you BAK

Finkelstein, J. M. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1267

Direct binding of the C-terminal sequences of Bim and Bak contributes to efficient Bak activation

Nguyen, D., Trebinjac, S., Beigl, T. B., Eßmann, F., Murphy, K. M., & Andrews, D. W. (2026) · Cell Death and Differentiation · doi:10.1038/s41418-026-01848-w

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