The Structure of a Bcl-xL/Bim Fragment Complex

Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC

Shimizu, S., Narita, M., Tsujimoto, Y., & Tsujimoto, Y. (1999) · Nature · doi:10.1038/20959 · Cited by 2,178

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

The Combined Functions of Proapoptotic Bcl-2 Family Members Bak and Bax Are Essential for Normal Development of Multiple Tissues

Lindsten, T., Ross, A. J., King, A., Zong, W.-X., Rathmell, J. C., Shiels, H. A., Ulrich, E., Waymire, K. G., Mahar, P., Frauwirth, K., et al. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00136-2 · Cited by 1,489

BH3-only Bcl-2 family member Bim is required for apoptosis of autoreactive thymocytes

Bouillet, P., Purton, J. F., Godfrey, D. I., Zhang, L.-C., Coultas, L., Puthalakath, H., Pellegrini, M., Cory, S., Adams, J. M., & Strasser, A. (2002) · Nature · doi:10.1038/415922a · Cited by 782

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

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

Small molecules, big targets: drug discovery faces the protein–protein interaction challenge

Scott, D. E., Bayly, A. R., Abell, C., & Skidmore, J. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.29 · Cited by 1,137

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

Thirty years of BCL-2: translating cell death discoveries into novel cancer therapies

Delbridge, A. R. D., Grabow, S., Strasser, A., & Vaux, D. L. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2015.17 · Cited by 752

Life in the balance: how BH3-only proteins induce apoptosis

Willis, S. N., & Adams, J. M. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.10.001 · Cited by 743

Inhibition of α-helix-mediated protein–protein interactions using designed molecules

Azzarito, V., Long, K., Murphy, N. S., & Wilson, A. J. (2013) · Nature Chemistry · doi:10.1038/nchem.1568 · Cited by 727

Mechanisms of Action of Bcl-2 Family Proteins

Shamas-Din, A., Kale, J., Leber, B., & Andrews, D. W. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008714 · Cited by 705

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

The BCL-2 arbiters of apoptosis and their growing role as cancer targets

Adams, J. M., & Cory, S. (2018) · Cell Death & Differentiation · doi:10.1038/cdd.2017.161 · Cited by 530

Molecular biology of Bax and Bak activation and action

Westphal, D., Dewson, G., Czabotar, P. E., & Kluck, R. M. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.12.019 · Cited by 453

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

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

Birkinshaw, R. W., & Czabotar, P. E. (2017) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2017.04.001 · Cited by 229

Killing cancer cells by flipping the Bcl-2/Bax switch

Cory, S., & Adams, J. M. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.06.012 · Cited by 217

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

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

Hydrophobic Binding Hot Spots of Bcl-xL Protein−Protein Interfaces by Cosolvent Molecular Dynamics Simulation

Yang, C.-Y., & Wang, S. (2011) · ACS Medicinal Chemistry Letters · doi:10.1021/ml100276b · Cited by 57

NMR Solution Structure of a Photoswitchable Apoptosis Activating Bak Peptide Bound to Bcl-xL

Wysoczanski, P., Mart, R. J., Loveridge, E. J., Williams, C., Whittaker, S. B.-M., Crump, M. P., & Allemann, R. K. (2012) · Journal of the American Chemical Society · doi:10.1021/ja302390a · Cited by 47

Genome-wide prediction and validation of peptides that bind human prosurvival Bcl-2 proteins

DeBartolo, J., Taipale, M., & Keating, A. E. (2014) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003693 · Cited by 39

BH3 Mimetics in Hematologic Malignancies

Klener, P., Sovilj, D., Renesova, N., & Andera, L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221810157 · Cited by 31