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The Bcl2 family: regulators of the cellular life-or-death switch
Abstract
Tissue homeostasis is regulated by apoptosis, the cell-suicide programme that is executed by proteases called caspases. The Bcl2 family of intracellular proteins is the central regulator of caspase activation, and its opposing factions of anti- and pro-apoptotic members arbitrate the life-or-death decision. Apoptosis is often impaired in cancer and can limit conventional therapy. A better understanding of how the Bcl2 family controls caspase activation should result in new, more effective therapeutic approaches.
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“This family consists of anti-apoptotic and pro-apoptotic proteins that act synergistically as apoptotic switches, ultimately determining the cell’s fate.358–360”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [359]
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Cites
Hanahan, D., & Weinberg, R. A. (2000) · Cell · doi:10.1016/s0092-8674(00)81683-9 · Cited by 29,219
Apoptosis: A Basic Biological Phenomenon with Wideranging Implications in Tissue Kinetics
Kerr, J. F. R., Wyllie, A. H., & Currie, A. R. (1972) · British Journal of Cancer · doi:10.1038/bjc.1972.33 · Cited by 15,673
Green, D. R., & Reed, J. C. (1998) · Science · doi:10.1126/science.281.5381.1309 · Cited by 9,051
Li, P., Nijhawan, D., Budihardjo, I., Srinivasula, S. M., Ahmad, M., Alnemri, E. S., & Wang, X. (1997) · Cell · doi:10.1016/s0092-8674(00)80434-1 · Cited by 7,289
Thornberry, N. A., & Lazebnik, Y. A. (1998) · Science · doi:10.1126/science.281.5381.1312 · Cited by 6,857
Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programed cell death
Oltval, Z. N., Milliman, C. L., & Korsmeyer, S. J. (1993) · Cell · doi:10.1016/0092-8674(93)90509-o · Cited by 6,003
The Bcl-2 Protein Family: Arbiters of Cell Survival
Adams, J. M., & Cory, S. (1998) · Science · doi:10.1126/science.281.5381.1322 · Cited by 5,334
Self-citationPrevention of Apoptosis by Bcl-2: Release of Cytochrome c from Mitochondria Blocked
Yang, J., Liu, X., Bhalla, K. N., Kim, C. N., Ibrado, A. M., Cai, J., Peng, T.-I., Jones, D. P., & Wang, X. (1997) · Science · doi:10.1126/science.275.5303.1129 · Cited by 4,913
The Release of Cytochrome c from Mitochondria: A Primary Site for Bcl-2 Regulation of Apoptosis
Kluck, R. M., Bossy‐Wetzel, E., Green, D. R., & Newmeyer, D. D. (1997) · Science · doi:10.1126/science.275.5303.1132 · Cited by 4,715
Cleavage of BID by Caspase 8 Mediates the Mitochondrial Damage in the Fas Pathway of Apoptosis
Li, H., Zhu, H., Xu, C.-J., & Yuan, J. (1998) · Cell · doi:10.1016/s0092-8674(00)81590-1 · Cited by 4,445
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- Cory, S., Vaux, D. L., Strasser, A., Harris, A. W. & Adams, J. M. Insights from Bcl2 and Myc: malignancy involves abrogation of apoptosis as well as sustained proliferation. Cancer Res. 59, S1685–S1692 (1999).
- Lassus, P., Opitz-Araya, X. & Lazebnik, Y. Caspase-2 is required for stress-induced apoptosis and acts prior to mitochondrial permeabilization. Science (in the press).In certain cell lines, stress stimuli are shown to activate caspase-2 upstream of mitochondrial disruption. Together with other recent findings by Marsden et al . (see text), this work argues strongly that Bcl2 function extends beyond guarding mitochondrial integrity and is likely to involve direct regulation of the activation of several initiator caspases.
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Items 901–1,000 of 1,007
Trisciuoglio, D., Gabellini, C., Desideri, M., Ragazzoni, Y., Luca, T. D., Ziparo, E., & Bufalo, D. D. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2010.175 · Cited by 67
Luster, T. A., Carrell, J. A., McCormick, K., Sun, D. W., & Humphreys, R. C. (2009) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-08-0918 · Cited by 67
Sevrioukov, E. A., Burr, J., Huang, E. W., Assi, H. H., Monserrate, J. P., Purves, D. C., Wu, J. N., Song, E. J., & Brachmann, C. B. (2007) · genesis · doi:10.1002/dvg.20279 · Cited by 67
Maggio, C., Barbante, A., Ferro, F., Frigerio, L., & Pedrazzini, E. (2007) · Journal of Experimental Botany · doi:10.1093/jxb/erl303 · Cited by 67
Mitochondrial proteomic approach reveals galectin-7 as a novel BCL-2 binding protein in human cells
Villeneuve, C., Baricault, L., Canelle, L., Barboule, N., Racca, C., Monsarrat, B., Magnaldo, T., & Larminat, F. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-06-0534 · Cited by 68
Kao, S., Lee, W.-J., Chang, J., Chow, J., Chung, C., Hung, W.-Y., & Chien, M. (2016) · Environmental Toxicology · doi:10.1002/tox.22336 · Cited by 67
MicroRNA-129 in Human Cancers: from Tumorigenesis to Clinical Treatment
Gao, Y., Feng, B., Han, S., Lu, L., Chen, Y., Chu, X., Wang, R., & Chen, L. (2016) · Cellular Physiology and Biochemistry · doi:10.1159/000447913 · Cited by 67
The Stability and Anti-apoptotic Function of A1 Are Controlled by Its C Terminus
Herold, M. J., Zeitz, J., Pelzer, C., Kraus, C., Peters, A., Wohlleben, G., & Berberich, I. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600266200 · Cited by 69
Liu, M., Yue, P. Y., Wang, Z., & Wong, R. N. (2005) · Cancer Letters · doi:10.1016/j.canlet.2004.11.051 · Cited by 67
Runx2-mediated activation of the Bax gene increases osteosarcoma cell sensitivity to apoptosis
Eliseev, R. A., Dong, Y.-F., Sampson, E. R., Zuscik, M. J., Schwarz, E. M., O’Keefe, R. J., Rosier, R. N., & Drissi, H. (2008) · Oncogene · doi:10.1038/sj.onc.1211020 · Cited by 67
Wu, C., Sundararajan, V., Sheu, B., Huang, R. Y., & Wei, L. (2019) · Cancers · doi:10.3390/cancers12010024 · Cited by 66
Thomas, D., Powell, J. A., Vergez, F., Segal, D., Nguyen, N.-Y. N., Baker, A., Teh, T., Barry, E. F., Sarry, J., Lee, E. M., et al. (2013) · Blood · doi:10.1182/blood-2012-08-447441 · Cited by 66
Jarray, R., Allain, B., Borriello, L., Biard, D. S. F., Loukaci, A., Larghero, J., Hadj-Slimane, R., Garbay, C., Lepelletier, Y., & Raynaud, F. (2011) · Biochimie · doi:10.1016/j.biochi.2011.07.010 · Cited by 70
Duval, D., Malaisé, M., Reinhardt, B., Kédinger, C., & Bœuf, H. (2003) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401337 · Cited by 66
A Cleaved Form of MAGE-A4 Binds to Miz-1 and Induces Apoptosis in Human Cells
Sakurai, T., Itoh, K., Higashitsuji, H., Nagao, T., Nonoguchi, K., Chiba, T., & Fujita, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310437200 · Cited by 67
Small molecules, big effects: the role of microRNAs in regulation of cardiomyocyte death
Skommer, J., Rana, I., Marques, F. Z., Zhu, W., Du, Z., & Charchar, F. J. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.287 · Cited by 66
Wendt, M. D. (2008) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.3.9.1123 · Cited by 66
Zheng, Q., Liu, Y., Liu, W., Ma, F., Zhou, Y., Chen, M., Chang, J., Wang, Y., Yang, G., & He, G. (2014) · Molecular Medicine Reports · doi:10.3892/mmr.2014.2175 · Cited by 67
Gao, Q., Chen, W., Xie, J., & Wong, M. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06051.x · Cited by 66
Pivotal role of Harakiri in the induction and prevention of gentamicin-induced hearing loss
Kalinec, G. M., Fernández-Zapico, M. E., Urrutia, R. A., Esteban-Cruciani, N., Chen, S., & Kalinec, F. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508053102 · Cited by 66
KLF6 transcription factor protects hepatocellular carcinoma-derived cells from apoptosis
Sirach, E., Bureau, C., Péron, J., Pradayrol, L., Vinel, J. P., Buscail, L., & Cordelier, P. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402114 · Cited by 66
Li, X., Beau, M. M. L., Ciccone, S. L. M., Yang, F., Freie, B. W., Shi, C., Yuan, J., Hong, P., Orazi, A., Haneline, L. S., et al. (2005) · Blood · doi:10.1182/blood-2004-06-2483 · Cited by 66
Claessens, Y.-É., Park, S., Dubart‐Kupperschmitt, A., Mariot, V., Garrido, C., Chrétien, S., Dreyfus, F., Lacombe, C., Mayeux, P., & Fontenay, M. (2005) · Blood · doi:10.1182/blood-2004-08-3166 · Cited by 66
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Boillée, S., Peschanski, M., & Junier, M. (2003) · Molecular Neurobiology · doi:10.1385/mn:28:1:65 · Cited by 66
Senthilkumar, K., Perumal, E., Arunkumar, R., Banudevi, S., Gunadharini, D. N., Sharmila, G., Selvakumar, K., & Arunakaran, J. (2010) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-010-0540-4 · Cited by 65
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Zain, J. M., & O’Connor, O. A. (2010) · Investigational New Drugs · doi:10.1007/s10637-010-9591-3 · Cited by 65
Aghaei, M., Panjehpour, M., Karami‐Tehrani, F., & Salami, S. (2011) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-011-1031-z · Cited by 65
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Tan, C.-B., Gao, M. H., Xu, W., Yang, X., Zhu, X.-M., & Du, G. (2009) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.32.1359 · Cited by 65
Peyerl, F. W., Dai, S., Murphy, G. A., Crawford, F., White, J., Marrack, P., & Kappler, J. W. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402025 · Cited by 65
Zhao, T., Su, G., Wang, S., Zhang, Q., Zhang, J., Zheng, L. P., Sun, B., & Zhao, M. (2017) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.7b03945 · Cited by 65
Chen, X., Cui, J., Zhai, X., Zhang, J., Gu, Z., Zhi, X., Weng, W., Pan, P., Cao, L., Ji, F., et al. (2018) · Cellular Physiology and Biochemistry · doi:10.1159/000489764 · Cited by 65
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Nicholas, L. M., Nagao, M., Kusinski, L. C., Fernandez‐Twinn, D. S., Eliasson, L., & Ozanne, S. E. (2019) · Diabetologia · doi:10.1007/s00125-019-05037-y · Cited by 69
Liu, Q., & Shio, H. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.1000097 · Cited by 67
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Sugerman, P. B., Faber, S. B., Willis, L. M., Petrović, A., Murphy, G. F., Pappo, J., Silberstein, D. S., & van den Brink, M. R. M. (2004) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63776-5 · Cited by 65
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Patel, J. H., & McMahon, S. B. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m609138200 · Cited by 68
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Moretti, J., Hauet, N., Çağlar, M., Rebillard, O., & Burak, Z. (2005) · European Journal of Nuclear Medicine and Molecular Imaging · doi:10.1007/s00259-005-1840-x · Cited by 65
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O’Shea, C. C. (2005) · Oncogene · doi:10.1038/sj.onc.1209047 · Cited by 65
Ji, Y., Dai, F., & Zhou, B. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.09.017 · Cited by 64
Al‐Owais, M. M., Scragg, J. L., Dallas, M. L., Boycott, H. E., Warburton, P., Chakrabarty, A., Boyle, J. P., & Peers, C. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.357012 · Cited by 64
Ardehali, R., Inlay, M. A., Ali, S. R., Tang, C. Z., Drukker, M., & Weissman, I. L. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1019047108 · Cited by 64
Regulation of ceramide channel formation and disassembly: Insights on the initiation of apoptosis
Abou-Ghali, M., & Stiban, J. (2015) · Saudi Journal of Biological Sciences · doi:10.1016/j.sjbs.2015.03.005 · Cited by 64
Ellis, L., & Пили, Р. (2010) · Pharmaceuticals · doi:10.3390/ph3082441 · Cited by 65
Umesalma, S., Nagendraprabhu, P., & Sudhandiran, G. (2014) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-014-2257-2 · Cited by 64
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Ide, T., Uchida, K., Kikuta, F., Suzuki, K., & Nakayama, H. (2010) · Veterinary Pathology · doi:10.1177/0300985810363486 · Cited by 64
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Emeterio, E. P.-S., Tramullas, M., & Hurlé, M. A. (2006) · Journal of Neuroscience Research · doi:10.1002/jnr.20812 · Cited by 64
Gou, Y., Qi, J., Ajayi, J.-P., Zhang, Y., Zhou, Z., Wu, X., Yang, F., & Liang, H. (2015) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.5b00314 · Cited by 64
Achour, I., Arel-Dubeau, A.-M., Renaud, J., Legrand, M., Attard, E., Germain, M., & Martinoli, M. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17081293 · Cited by 64
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Zeng, Y., Ma, J., Xu, L., & Wu, D. (2017) · Current Medicinal Chemistry · doi:10.2174/0929867324666170523123655 · Cited by 64
Zhao, Z., Gao, P., You, Y., & Chen, T. (2017) · Chemistry - A European Journal · doi:10.1002/chem.201705561 · Cited by 64
Takahashi, K., Nakagawasai, O., Nemoto, W., Kadota, S., Isono, J., Odaira, T., Sakuma, W., Arai, Y., Tadano, T., & Tan–No, K. (2018) · Neuropharmacology · doi:10.1016/j.neuropharm.2018.04.013 · Cited by 64
Girisha, K. M., von Elsner, L., Kausthubham, N., Muranjan, M. N., Shukla, A., Bhavani, G. S., Nishimura, G., Kutsche, K., & Mortier, G. R. (2018) · Human Mutation · doi:10.1002/humu.23693 · Cited by 65
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Mao, X., Orchard, G. E., Lillington, D. M., Child, F. J., Vonderheid, E. C., Nowell̀, P. C., Bagot, M., Bensussan, A., Russell‐Jones, R., Young, B. D., et al. (2004) · British Journal of Dermatology · doi:10.1111/j.1365-2133.2004.06106.x · Cited by 64
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Moreno, R. D., Lizama, C. O., Urzúa, N., Vergara, S. P., & Reyes, J. G. (2006) · Cell and Tissue Research · doi:10.1007/s00441-006-0186-4 · Cited by 64
Chen, Y.-C., Lu, P., Pan, S., Teng, C., Kuo, S., Lin, T. P., Ho, Y., Huang, Y.-C., & Guh, J. (2007) · Biochemical Pharmacology · doi:10.1016/j.bcp.2007.03.015 · Cited by 64
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Fulda, S. (2007) · Expert Review of Anticancer Therapy · doi:10.1586/14737140.7.9.1255 · Cited by 64
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The DNA double-strand break response in the nervous system
Abner, C. W., & McKinnon, P. J. (2004) · DNA repair · doi:10.1016/j.dnarep.2004.03.009 · Cited by 67
Zeng, X., Jiang, W., Du, Z., & Kokini, J. L. (2022) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2022.2075313 · Cited by 64
Lin, S.-Y., Lai, W.-W., Chou, C., Kuo, H., Li, T., Chung, J., & Yang, J. (2006) · Melanoma Research · doi:10.1097/01.cmr.0000232297.99160.9e · Cited by 63
Chang, H.-L., Chen, C., Hsu, Y.-F., Kuo, W.-S., Ou, G., Chiu, P.-T., Huang, Y., & Hsu, M. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.04.011 · Cited by 68
Liu, X., Shi, Y., Giranda, V. L., & Luo, Y. (2006) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-05-0049 · Cited by 63
BH3‐only proteins: The death‐puppeteer's wires
Ghiotto, F., Fais, F., & Bruno, S. (2009) · Cytometry Part A · doi:10.1002/cyto.a.20819 · Cited by 65
The emergence of DNA methylation as a key modulator of aberrant cell death in prostate cancer
Murphy, T. M., Perry, A. S., & Lawler, M. (2008) · Endocrine Related Cancer · doi:10.1677/erc-07-0208 · Cited by 63
Guo, H., Cui, H., Peng, X., Fang, J. S., Zuo, Z., Deng, J., Wang, X., Wu, B., Chen, K., & Deng, J. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms160922989 · Cited by 63
(2015) · Biochemistry & Analytical Biochemistry · doi:10.4172/2161-1009.1000211 · Cited by 63
Guo, Z., Hu, G., Wang, H., Li, Z., & Liu, N. (2019) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.12.136 · Cited by 64
Sitailo, L. A., Tibudan, S. S., & Denning, M. F. (2004) · Journal of Investigative Dermatology · doi:10.1111/j.0022-202x.2004.23403.x · Cited by 63
Harnois, C., Demers, M., Bouchard, V., Vallée, K., Gagné, D., Fujita, N., Tsuruo, T., Vézina, A., Beaulieu, J., Côté, A., et al. (2003) · Journal of Cellular Physiology · doi:10.1002/jcp.10399 · Cited by 63
Duan, H., Chai, J., Sheng, Z., Yao, Y.-M., Yin, H., Liang, L., Shen, C., & Lin, J. (2008) · APOPTOSIS · doi:10.1007/s10495-008-0277-7 · Cited by 65
Animal cell technology: from biopharmaceuticals to gene therapy
(2008) · Choice Reviews Online · doi:10.5860/choice.46-1453 · Cited by 64
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Hroudová, J., & Fišar, Z. (2011) · Psychiatry and Clinical Neurosciences · doi:10.1111/j.1440-1819.2010.02178.x · Cited by 63
Wong, J. C., Bathina, M., & Fiscus, R. R. (2012) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24237 · Cited by 62
Ling, Y., Li, T., Perez-Soler, R., & Haigentz, M. (2009) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-008-0902-8 · Cited by 62
Kumar, P., Coltas, I. K., Kumar, B., Chepeha, D. B., Bradford, C. R., & Polverini, P. J. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-2265 · Cited by 62
Kim, J. H., Go, H. Y., Jin, D. H., Kim, H., Hong, M. H., Chung, W.-Y., Park, J., Jang, J. B., Jung, H. J., Shin, Y. C., et al. (2008) · Cancer Letters · doi:10.1016/j.canlet.2008.02.039 · Cited by 62
Fan, C., Li, Y., Fu, X., Wu, Q., Hou, Y., Yang, M., Sun, J., Fu, X., Zheng, Z., & Sun, B. (2016) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-016-0362-3 · Cited by 62
Xu, J., Huai, Y., Meng, N., Dong, Y., Liu, Z., Qi, Q., Hu, M. C., Fan, M., Jin, W., & Lv, P. (2017) · Neurochemical Research · doi:10.1007/s11064-017-2328-3 · Cited by 62
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Lee, K. H., & Kang, T. (2019) · Cells · doi:10.3390/cells8091057 · Cited by 65
APO2 ligand/tumor necrosis factor-related apoptosis-inducing ligand in prostate cancer therapy
Bucur, O. (2006) · Frontiers in bioscience · doi:10.2741/1903 · Cited by 62
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Tanel, A., & Averill‐Bates, D. A. (2007) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.106.114678 · Cited by 62
Cellular Distribution of Bcl-2 Family Proteins
Germain, M., & Shore, G. C. (2003) · Science Signaling · doi:10.1126/scisignal.1732003pe10 · Cited by 62
Exploiting death receptor signaling pathways for tumor therapy
Fulda, S., & Debatin, K. (2004) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2004.09.003 · Cited by 64
Bilotas, M. A., Barañao, R. I., Buquet, R. A., Sueldo, C. E., Tesone, M., & Meresman, G. F. (2006) · Human Reproduction · doi:10.1093/humrep/del423 · Cited by 62
There is more to life and death than mitochondria: Bcl-2 proteins at the endoplasmic reticulum
Annis, M. G., Yethon, J. A., Leber, B. F., & Andrews, D. W. (2003) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2003.07.001 · Cited by 62
Li, L., Cao, W., Zheng, W., Fan, C., & Chen, T. (2012) · Dalton Transactions · doi:10.1039/c2dt30665d · Cited by 62
Zhang, L., & Zhang, S. (2011) · Phytotherapy Research · doi:10.1002/ptr.3534 · Cited by 61
Liu, Q., Zhou, T., Zhao, Y., Chen, L., Gong, M.-W., Xia, Q., Ying, M., Zheng, Q., & Zhang, Q. (2015) · Marine Drugs · doi:10.3390/md13084733 · Cited by 61
Chung, H. J., Choi, Y. E., Kim, E., Han, Y.-H., Park, M., & Bae, I. H. (2015) · Oncotarget · doi:10.18632/oncotarget.4384 · Cited by 61
Milner, R. J., Farese, J. P., Henry, C. J., Selting, K. A., Fan, T. M., & de Lorimier, L. (2004) · Journal of Veterinary Internal Medicine · doi:10.1111/j.1939-1676.2004.tb02593.x · Cited by 61
Bim Protein Degradation Contributes to Cisplatin Resistance
Wang, J., Zhou, J.-Y., & Wu, G. S. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.239566 · Cited by 63
Mäkelä, J., Koivuniemi, R., Korhonen, L., & Lindholm, D. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011091 · Cited by 65
S6 Kinase 2 Promotes Breast Cancer Cell Survival via Akt
Sridharan, S., & Basu, A. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-3253 · Cited by 63
Hematologic malignancies: newer strategies to counter the BCL-2 protein
Ebrahim, A. S., Sabbagh, H., Liddane, A., Raufi, A. M., Kandouz, M., & Al-Katib, A. M. (2016) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-016-2144-1 · Cited by 61
Khan, S., Ansari, A. A., Khan, A. A., Abdulla, M., Al-Obeed, O. A., & Ahmad, R. (2016) · MedChemComm · doi:10.1039/c6md00219f · Cited by 62
Deng, J., Liu, A., Hou, G., Zhang, X., Ren, K., Chen, X.-Z., Li, S. S. ‐., Wu, Y., & Cao, X. (2019) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-018-1016-8 · Cited by 62
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Metadata
- Authors
- Cory, S., & Adams, J. M.
- Affiliations
- The Royal Melbourne Hospital (AU)
- Venue
- Nature Reviews Cancer
- Published
- 2002-09-01
- Volume
- 2
- Issue
- 9
- Pages
- 647-656
- ISSN
- 1474-175X (ISSN-L)
- 1474-1768
- OpenAlex
- W2087877138
- Cited by
- 4,032
- References
- 155
- Citations by year
- 2026: 118 · 2025: 111 · 2024: 115 · 2023: 115 · 2022: 132 · 2021: 143 · 2020: 133 · 2019: 155 · 2018: 171 · 2017: 174 · 2016: 189 · 2015: 165 · 2014: 194 · 2013: 214 · 2012: 188
- FWCI
- 12.89
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature reviews. Cancer (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Leukemia and Lymphoma Society
- National Institutes of Health
- National Health and Medical Research Council
- National Medical Research Council
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- Bcl-2 family proteins, apoptosis, caspase activation, anti-apoptotic proteins, pro-apoptotic proteins, life-or-death decisions, cancer therapy, tissue homeostasis
- MeSH terms
- Animals, Humans, Models, Molecular, Neoplasms, Protein Conformation, Apoptosis, Proto-Oncogene Proteins c-bcl-2, Caspases
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