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

Oltersdorf, Tilman, Elmore, Steven W., Shoemaker, Alexander R., Armstrong, Robert C., Augeri, David J., Belli, Barbara A., Bruncko, Milan, Deckwerth, Thomas L., Dinges, Jurgen, Hajduk, Philip J., Joseph, Mary K., Kitada, Shinichi, Korsmeyer, Stanley J., Kunzer, Aaron R., Letai, Anthony, Li, Chi, Mitten, Michael J., Nettesheim, David G., Ng, ShiChung, Nimmer, Paul M., O'Connor, Jacqueline M., Oleksijew, Anatol, Petros, Andrew M., Reed, John C., Shen, Wang, Tahir, Stephen K., Thompson, Craig B., Tomaselli, Kevin J., Wang, Baole, Wendt, Michael D., Zhang, Haichao, Fesik, Stephen W., Rosenberg, Saul H.·2005·Nature

DOI 10.1038/nature03579

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Danial, N. N., & Korsmeyer, S. J. (2004) · Cell · doi:10.1016/s0092-8674(04)00046-7 · Cited by 4,651
Self-citation
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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
Self-citation
Activation of Apoptosis in Vivo by a Hydrocarbon-Stapled BH3 Helix
Walensky, L. D., Kung, A. L., Escher, I., Malia, T. J., Barbuto, S., Wright, R. D., Wagner, G., Verdine, G. L., & Korsmeyer, S. J. (2004) · Science · doi:10.1126/science.1099191 · Cited by 1,349
Self-citation
Structural biology of the Bcl-2 family of proteins
Petros, A. M., Olejniczak, E. T., & Fesik, S. W. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2003.08.012 · Cited by 745
Self-citation

Show all 4 references

Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition).
Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, M. J., Abeliovich, H., Acevedo Arozena, A., Adachi, H., Adams, C. M., Adams, P. D., Adeli, K., et al. (2016) · Autophagy · doi:10.1080/15548627.2015.1100356 · Cited by 5,894
Self-citation
Cancer drug resistance: an evolving paradigm
Holohan, C., Van Schaeybroeck, S., Longley, D. B., & Johnston, P. G. (2013) · Nature Reviews Cancer · doi:10.1038/nrc3599 · Cited by 4,681
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
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
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
Self-citation
Apoptosis in cancer: from pathogenesis to treatment
Wong, R. S. (2011) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/1756-9966-30-87 · Cited by 2,836
Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1
Klionsky, D. J., Abdel-Aziz, A. K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M. H., Abudu, Y. P., Acevedo-Arozena, A., et al. (2021) · Autophagy · doi:10.1080/15548627.2020.1797280 · Cited by 2,897
Self-citation
Extrinsic versus intrinsic apoptosis pathways in anticancer chemotherapy
Fulda, S., & Debatin, K.-M. (2006) · Oncogene · doi:10.1038/sj.onc.1209608 · Cited by 2,312
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
Self-citation
Essential role for Nix in autophagic maturation of erythroid cells
Sandoval, H., Thiagarajan, P., Dasgupta, S. K., Schumacher, A., Prchal, J. T., Chen, M., & Wang, J. (2008) · Nature · doi:10.1038/nature07006 · Cited by 1,185
Small-Molecule Inhibitors of Protein-Protein Interactions: Progressing toward the Reality
Arkin, M. R., Tang, Y., & Wells, J. A. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2014.09.001 · Cited by 1,065
BAK/BAX macropores facilitate mitochondrial herniation and mtDNA efflux during apoptosis
McArthur, K., Whitehead, L. W., Heddleston, J. M., Li, L., Padman, B. S., Oorschot, V., Geoghegan, N. D., Chappaz, S., Davidson, S., San Chin, H., et al. (2018) · Science · doi:10.1126/science.aao6047 · Cited by 1,072
Directed elimination of senescent cells by inhibition of BCL-W and BCL-XL
Yosef, R., Pilpel, N., Tokarsky-Amiel, R., Biran, A., Ovadya, Y., Cohen, S., Vadai, E., Dassa, L., Shahar, E., Condiotti, R., et al. (2016) · Nature Communications · doi:10.1038/ncomms11190 · Cited by 1,032
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
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
Twenty years on: the impact of fragments on drug discovery
Erlanson, D. A., Fesik, S. W., Hubbard, R. E., Jahnke, W., & Jhoti, H. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.109 · Cited by 1,000
Self-citation
Apoptotic Caspases Suppress mtDNA-Induced STING-Mediated Type I IFN Production
White, M. J., McArthur, K., Metcalf, D., Lane, R. M., Cambier, J. C., Herold, M. J., van Delft, M. F., Bedoui, S., Lessene, G., Ritchie, M. E., et al. (2014) · Cell · doi:10.1016/j.cell.2014.11.036 · Cited by 983
“To test this, we treated WT murine splenocytes with the proapoptotic BH3 mimetic drug ABT-737, which targets the prosurvival proteins Bcl-xL and Bcl-2 (Oltersdorf et al., 2005).”
Recent advances in the development of protein–protein interactions modulators: mechanisms and clinical trials
Lu, H., Zhou, Q., He, J., Jiang, Z., Peng, C., Tong, R., & Shi, J. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00315-3 · Cited by 891
Awakening guardian angels: drugging the p53 pathway
Brown, C. J., Lain, S., Verma, C. S., Fersht, A. R., & Lane, D. P. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2763 · Cited by 881
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
Targeting the RAS/RAF/MAPK pathway for cancer therapy: from mechanism to clinical studies
Bahar, M. E., Kim, H. J., & Kim, D. R. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01705-z · Cited by 888
Navitoclax, a targeted high-affinity inhibitor of BCL-2, in lymphoid malignancies: a phase 1 dose-escalation study of safety, pharmacokinetics, pharmacodynamics, and antitumour activity
Wilson, W. H., O'Connor, O. A., Czuczman, M. S., LaCasce, A. S., Gerecitano, J. F., Leonard, J. P., Tulpule, A., Dunleavy, K., Xiong, H., Chiu, Y.-L., et al. (2010) · The Lancet Oncology · doi:10.1016/s1470-2045(10)70261-8 · Cited by 876
Self-citation
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
Potential therapeutic applications of autophagy
Rubinsztein, D. C., Gestwicki, J. E., Murphy, L. O., & Klionsky, D. J. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2272 · Cited by 862
Apoptotic Caspases Prevent the Induction of Type I Interferons by Mitochondrial DNA
Rongvaux, A., Jackson, R., Harman, C. C. D., Li, T., West, A. P., de Zoete, M. R., Wu, Y., Yordy, B., Lakhani, S. A., Kuan, C.-Y., et al. (2014) · Cell · doi:10.1016/j.cell.2014.11.037 · Cited by 847
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
Structure-Based Design of Spiro-oxindoles as Potent, Specific Small-Molecule Inhibitors of the MDM2−p53 Interaction
Ding, K., Lu, Y., Nikolovska-Coleska, Z., Wang, G., Qiu, S., Shangary, S., Gao, W., Qin, D., Stuckey, J., Krajewski, K., et al. (2006) · Journal of Medicinal Chemistry · doi:10.1021/jm051122a · Cited by 702
Self-citation
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
A selective BCL-XL PROTAC degrader achieves safe and potent antitumor activity
Khan, S., Zhang, X., Lv, D., Zhang, Q., He, Y., Zhang, P., Liu, X., Thummuri, D., Yuan, Y., Wiegand, J. S., et al. (2019) · Nature Medicine · doi:10.1038/s41591-019-0668-z · Cited by 688
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
Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival
Schwickart, M., Huang, X., Lill, J. R., Liu, J., Ferrando, R., French, D. M., Maecker, H., O’Rourke, K., Bazan, F., Eastham-Anderson, J., et al. (2010) · Nature · doi:10.1038/nature08646 · Cited by 628
The BCL2 Family: Key Mediators of the Apoptotic Response to Targeted Anticancer Therapeutics
Hata, A. N., Engelman, J. A., & Faber, A. C. (2015) · Cancer Discovery · doi:10.1158/2159-8290.cd-15-0011 · Cited by 619
Phase I Study of Navitoclax (ABT-263), a Novel Bcl-2 Family Inhibitor, in Patients With Small-Cell Lung Cancer and Other Solid Tumors
Gandhi, L., Camidge, D. R., Ribeiro de Oliveira, M., Bonomi, P., Gandara, D., Khaira, D., Hann, C. L., McKeegan, E. M., Litvinovich, E., Hemken, P. M., et al. (2011) · Journal of Clinical Oncology · doi:10.1200/jco.2010.31.6208 · Cited by 603
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
Multiple Functions of BCL-2 Family Proteins
Hardwick, J. M., & Soane, L. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008722 · Cited by 564
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
Self-citation
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
Mitochondrial inner membrane permeabilisation enables mtDNA release during apoptosis
Riley, J. S., Quarato, G., Cloix, C., Lopez, J., O'Prey, J., Pearson, M., Chapman, J., Sesaki, H., Carlin, L. M., Passos, J. F., et al. (2018) · The EMBO Journal · doi:10.15252/embj.201899238 · Cited by 551
Limited Mitochondrial Permeabilization Causes DNA Damage and Genomic Instability in the Absence of Cell Death
Ichim, G., Lopez, J., Ahmed, S. U., Muthalagu, N., Giampazolias, E., Delgado, M. E., Haller, M., Riley, J. S., Mason, S. M., Athineos, D., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.01.018 · Cited by 479
A fate worse than death: apoptosis as an oncogenic process
Ichim, G., & Tait, S. W. G. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2016.58 · Cited by 451
The BCL2 family: from apoptosis mechanisms to new advances in targeted therapy
Vogler, M., Braun, Y., Smith, V. M., Westhoff, M.-A., Pereira, R. S., Pieper, N. M., Anders, M., Callens, M., Vervliet, T., Abbas, M., et al. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02176-0 · Cited by 462
Potent and selective small-molecule MCL-1 inhibitors demonstrate on-target cancer cell killing activity as single agents and in combination with ABT-263 (navitoclax)
Leverson, J. D., Zhang, H., Chen, J., Tahir, S. K., Phillips, D. C., Xue, J., Nimmer, P., Jin, S., Smith, M., Xiao, Y., et al. (2015) · Cell Death & Disease · doi:10.1038/cddis.2014.561 · Cited by 440
Self-citation
Bcl-2 family proteins are essential for platelet survival
Zhang, H., Nimmer, P. M., Tahir, S. K., Chen, J., Fryer, R. M., Hahn, K. R., Iciek, L. A., Morgan, S. J., Nasarre, M. C., Nelson, R., et al. (2007) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4402081 · Cited by 427
Self-citation
Acquisition of the Recurrent Gly101Val Mutation in BCL2 Confers Resistance to Venetoclax in Patients with Progressive Chronic Lymphocytic Leukemia
Blombery, P., Anderson, M. A., Gong, J.-N., Thijssen, R., Birkinshaw, R. W., Thompson, E. R., Teh, C. E., Nguyen, T., Xu, Z., Flensburg, C., et al. (2019) · Cancer Discovery · doi:10.1158/2159-8290.cd-18-1119 · Cited by 434
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
The MCL-1 BH3 helix is an exclusive MCL-1 inhibitor and apoptosis sensitizer
Stewart, M. L., Fire, E., Keating, A. E., & Walensky, L. D. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.391 · Cited by 418
Targeting protein–protein interactions as an anticancer strategy
Ivanov, A. A., Khuri, F. R., & Fu, H. (2013) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2013.04.007 · Cited by 401
Pomegranate fruit juice for chemoprevention and chemotherapy of prostate cancer
Malik, A., Afaq, F., Sarfaraz, S., Adhami, V. M., Syed, D. N., & Mukhtar, H. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505870102 · Cited by 401
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
Self-citation
Interactive Association of Drugs Binding to Human Serum Albumin
Yang, F., Zhang, Y., & Liang, H. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms15033580 · Cited by 376
Hypoxia increases the expression of stem-cell markers and promotes clonogenicity in glioblastoma neurospheres
Bar, E. E., Lin, A., Mahairaki, V., Matsui, W., & Eberhart, C. G. (2010) · The American Journal of Pathology · doi:10.2353/ajpath.2010.091021 · Cited by 373
Bcl-xL–inhibitory BH3 mimetics can induce a transient thrombocytopathy that undermines the hemostatic function of platelets
Schoenwaelder, S. M., Jarman, K. E., Gardiner, E. E., Hua, M., Qiao, J., White, M. J., Josefsson, E. C., Alwis, I., Ono, A., Willcox, A., et al. (2011) · Blood · doi:10.1182/blood-2011-04-347849 · Cited by 351
SAR405838: An Optimized Inhibitor of MDM2–p53 Interaction That Induces Complete and Durable Tumor Regression
Wang, S., Sun, W., Zhao, Y., McEachern, D., Meaux, I., Barrière, C., Stuckey, J. A., Meagher, J. L., Bai, L., Liu, L., et al. (2014) · Cancer Research · doi:10.1158/0008-5472.can-14-0799 · Cited by 328
Dual or multi-targeting inhibitors: The next generation anticancer agents
Raghavendra, N. M., Pingili, D., Kadasi, S., Mettu, A., & Prasad, S. V. U. M. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.10.021 · Cited by 333
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
Gut bacteria signaling to mitochondria in intestinal inflammation and cancer
Jackson, D. N., & Theiss, A. L. (2020) · Gut Microbes · doi:10.1080/19490976.2019.1592421 · Cited by 312
Orthologous CRISPR–Cas9 enzymes for combinatorial genetic screens
Najm, F. J., Strand, C., Donovan, K. F., Hegde, M., Sanson, K. R., Vaimberg, E. W., Sullender, M. E., Hartenian, E., Kalani, Z., Fusi, N., et al. (2018) · Nature Biotechnology · doi:10.1038/nbt.4048 · Cited by 279
EGFR family: Structure physiology signalling and therapeutic targets †
Burgess, A. W. (2008) · Growth Factors · doi:10.1080/08977190802312844 · Cited by 288
ABT-199 mediated inhibition of BCL-2 as a novel therapeutic strategy in T-cell acute lymphoblastic leukemia
Peirs, S., Matthijssens, F., Goossens, S., Van de Walle, I., Ruggero, K., de Bock, C. E., Degryse, S., Canté-Barrett, K., Briot, D., Clappier, E., et al. (2014) · Blood · doi:10.1182/blood-2014-05-574566 · Cited by 264
Senolytics and senomorphics: Natural and synthetic therapeutics in the treatment of aging and chronic diseases
Lagoumtzi, S. M., & Chondrogianni, N. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.05.003 · Cited by 279
Mitochondrial permeabilization engages NF-κB-dependent anti-tumour activity under caspase deficiency
Giampazolias, E., Zunino, B., Dhayade, S., Bock, F., Cloix, C., Cao, K., Roca, A., Lopez, J., Ichim, G., Proïcs, E., et al. (2017) · Nature Cell Biology · doi:10.1038/ncb3596 · Cited by 258
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
Targeted apoptosis of myofibroblasts with the BH3 mimetic ABT-263 reverses established fibrosis
Lagares, D., Santos, A., Grasberger, P. E., Liu, F., Probst, C. K., Rahimi, R. A., Sakai, N., Kuehl, T., Ryan, J., Bhola, P., et al. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aal3765 · Cited by 246
Self-citation
Inhibition of pluripotent stem cell-derived teratoma formation by small molecules
Lee, M.-O., Moon, S. H., Jeong, H.-C., Yi, J.-Y., Lee, T.-H., Shim, S. H., Rhee, Y.-H., Lee, S.-H., Oh, S.-J., Lee, M.-Y., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1303669110 · Cited by 246
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
Structural Biology and Drug Discovery of Difficult Targets: The Limits of Ligandability
Surade, S., & Blundell, T. L. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.12.013 · Cited by 230
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
Mitochondrial Shape Governs BAX-Induced Membrane Permeabilization and Apoptosis
Renault, T. T., Floros, K. V., Elkholi, R., Corrigan, K.-A., Kushnareva, Y., Wieder, S. Y., Lindtner, C., Serasinghe, M. N., Asciolla, J. J., Buettner, C., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2014.10.028 · Cited by 217
Role of Platelet Mitochondria: Life in a Nucleus-Free Zone
Melchinger, H., Jain, K., Tyagi, T., & Hwa, J. (2019) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2019.00153 · Cited by 208
Treatment of B-RAF mutant human tumor cells with a MEK inhibitor requires Bim and is enhanced by a BH3 mimetic
Cragg, M. S., Jansen, E. S., Cook, M., Harris, C., Strasser, A., & Scott, C. L. (2008) · Journal of Clinical Investigation · doi:10.1172/jci35437 · Cited by 207
Metabolic reprogramming of pancreatic cancer mediated by CDK4/6 inhibition elicits unique vulnerabilities
Franco, J., Balaji, U., Freinkman, E., Witkiewicz, A. K., & Knudsen, E. S. (2016) · Cell Reports · doi:10.1016/j.celrep.2015.12.094 · Cited by 199
VDAC2 enables BAX to mediate apoptosis and limit tumor development
Chin, H. S., Li, M. X., Tan, I. K. L., Ninnis, R. L., Reljic, B., Scicluna, K., Dagley, L. F., Sandow, J. J., Kelly, G. L., Samson, A. L., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-07309-4 · Cited by 196
Strategies targeting cellular senescence
Ovadya, Y., & Krizhanovsky, V. (2018) · Journal of Clinical Investigation · doi:10.1172/jci95149 · Cited by 200
Systematic Targeting of Protein–Protein Interactions
Modell, A. E., Blosser, S. L., & Arora, P. S. (2016) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2016.05.008 · Cited by 184
Targeting Protein-Protein Interaction by Small Molecules
Jin, L., Wang, W., & Fang, G. (2014) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-011613-140028 · Cited by 195
Systematic Analysis of Helical Protein Interfaces Reveals Targets for Synthetic Inhibitors
Jochim, A. L., & Arora, P. S. (2010) · ACS Chemical Biology · doi:10.1021/cb1001747 · Cited by 191
Unleashing the power of inhibitors of oncogenic kinases through BH3 mimetics
Cragg, M. S., Harris, C., Strasser, A., & Scott, C. L. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2615 · Cited by 185
Drug Insight: cancer therapy strategies based on restoration of endogenous cell death mechanisms
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Muppidi, A., Doi, K., Edwardraja, S., Drake, E. J., Gulick, A. M., Wang, H.-G., & Lin, Q. (2012) · Journal of the American Chemical Society · doi:10.1021/ja306864v · Cited by 156
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Physiological and Pharmacological Control of BAK, BAX, and Beyond
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Molecular and cellular mechanisms of CLL: novel therapeutic approaches.
Pleyer, L., Egle, A., Hartmann, T. N., & Greil, R. (2009) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2009.72 · Cited by 125
Protein–protein interactions as targets for small-molecule therapeutics in cancer
White, A. W., Westwell, A. D., & Brahemi, G. (2008) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399408000641 · Cited by 122
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Kile, B. T. (2014) · British Journal of Haematology · doi:10.1111/bjh.12757 · Cited by 122
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Zhang, X., Thummuri, D., Liu, X., Hu, W., Zhang, P., Khan, S., Yuan, Y., Zhou, D., & Zheng, G. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112186 · Cited by 123
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Anders, C., Higuchi, Y., Koschinsky, K., Bartel, M., Schumacher, B., Thiel, P., Nitta, H., Preisig-Müller, R., Schlichthörl, G., Renigunta, V., et al. (2013) · Chemistry & Biology · doi:10.1016/j.chembiol.2013.03.015 · Cited by 106
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Yip, K. W., Mao, X., Au, P. Y. B., Hedley, D. W., Chow, S., Dalili, S., Mocanu, J. D., Bastianutto, C., Schimmer, A., & Liu, F.-F. (2006) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-06-0536 · Cited by 99
Does vitamin D protect against DNA damage?
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Authors: Oltersdorf, T., Elmore, S. W., Shoemaker, A. R., Armstrong, R. C., Augeri, D. J., Belli, B. A., Bruncko, M., Deckwerth, T. L., Dinges, J., Hajduk, P. J., Joseph, M. K., Kitada, S., Korsmeyer, S. J., Kunzer, A. R., Letai, A., Li, C., Mitten, M. J., Nettesheim, D. G., Ng, S., Nimmer, P. M., O'Connor, J. M., Oleksijew, A., Petros, A. M., Reed, J. C., Shen, W., Tahir, S. K., Thompson, C. B., Tomaselli, K. J., Wang, B., Wendt, M. D., Zhang, H., Fesik, S. W., & Rosenberg, S. H.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2005-05-15
Volume: 435
Issue: 7042
Pages: 677-681
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature03579
OpenAlex: W2085419794
Cited by: 3,416
References: 4
FWCI: 64.42
Type: journal article
Language: en
Open access: closed

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

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