Cited by 4,032Cell death mechanisms and regulationCancer-related Molecular PathwaysUbiquitin and proteasome pathways

The DOI matches its Crossref record; 153 of the 155 references it cites were found in a registry or an index.

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

Cory, Suzanne, Adams, Jerry M.·2002·Nature Reviews Cancer

Open this paper in CoChat — free account

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.

Integrity signals

Registry

Crossref · 10.1038/nrc883

Cites

153 of 153 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

The hallmarks of cancer
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
Mitochondria and Apoptosis
Green, D. R., & Reed, J. C. (1998) · Science · doi:10.1126/science.281.5381.1309 · Cited by 9,051
Cytochrome c and dATP-Dependent Formation of Apaf-1/Caspase-9 Complex Initiates an Apoptotic Protease Cascade
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
Caspases: Enemies Within
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-citation
Prevention 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

Flagged first, then by citations

Show all 155 references

2 of the 155 references couldn’t be matched to a known paper.

Research works printed but not linked: 2

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.

Sorted by citations

Items 201–300 of 1,007

Nrf2-induced antiapoptotic Bcl-xL protein enhances cell survival and drug resistance
Niture, S. K., & Jaiswal, A. K. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.12.014 · Cited by 220
Metabolic Cooperation and Competition in the Tumor Microenvironment: Implications for Therapy
Gupta, S., Roy, A., & Dwarakanath, B. S. R. (2017) · Frontiers in Oncology · doi:10.3389/fonc.2017.00068 · Cited by 225
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
Self-citation
Resolution of inflammation: Mechanisms and opportunity for drug development
Alessandri, A. L., Sousa, L. P., Lucas, C. D., Rossi, A. G., Pinho, V., & Teixeira, M. M. (2013) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2013.04.006 · Cited by 219
Current concepts in apoptosis: The physiological suicide program revisited
Chowdhury, I., Tharakan, B., & Bhat, G. K. (2006) · Cellular & Molecular Biology Letters · doi:10.2478/s11658-006-0041-3 · Cited by 223
Apoptosis versus necrosis in acute pancreatitis
Bhatia, M. (2004) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00304.2003 · Cited by 216
A dual role for the anti-apoptotic Bcl-2 protein in cancer: Mitochondria versus endoplasmic reticulum
Akl, H., Vervloessem, T., Kiviluoto, S., Bittremieux, M., Parys, J. B., SMEDT, H. D., & Bultynck, G. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.04.017 · Cited by 225
The oncogenic and tumour suppressive roles of microRNAs in cancer and apoptosis
Babashah, S., & Soleimani, M. (2011) · European Journal of Cancer · doi:10.1016/j.ejca.2011.02.008 · Cited by 220
Role of peroxynitrite in the redox regulation of cell signal transduction pathways
Liaudet, L. (2009) · Frontiers in bioscience · doi:10.2741/3569 · Cited by 219
MiR-148a promotes apoptosis by targeting Bcl-2 in colorectal cancer
Zhang, H., Li, Y., Huang, Q., Ren, X., Hu, H., Sheng, H., & Lai, M. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.28 · Cited by 214
Delivery of CRISPR/Cas systems for cancer gene therapy and immunotherapy
Song, X., Liu, C., Wang, N., Huang, H., He, S., Gong, C., & Wei, Y. (2020) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2020.04.010 · Cited by 217
Circadian gene mPer2 overexpression induces cancer cell apoptosis
Hua, H., Wang, Y., Wan, C., Liu, Y., Zhu, B., Yang, C., Wang, X., Wang, Z., Cornélissen, G., & Franz Halberg, A. (2006) · Cancer Science · doi:10.1111/j.1349-7006.2006.00225.x · Cited by 222
Death receptor signals to the mitochondria
Khosravi‐Far, R. (2004) · Cancer Biology & Therapy · doi:10.4161/cbt.3.11.1173 · Cited by 219
Apoptosis and Autophagy: Decoding Calcium Signals that Mediate Life or DeathPreprint
Harr, M. W., & Distelhorst, C. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005579 · Cited by 217
Neuronal damage and protection in the pathophysiology and treatment of psychiatric illness: stress and depression
Duman, R. S. (2009) · Dialogues in Clinical Neuroscience · doi:10.31887/dcns.2009.11.3/rsduman · Cited by 210
MECHANISMS OF APOPTOSIS THROUGH STRUCTURAL BIOLOGY
Yan, N., & Shi, Y. (2005) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.21.012704.131040 · Cited by 212
Mitochondrial and Cell Death Mechanisms in Neurodegenerative Diseases
Martin, L. J. (2010) · Pharmaceuticals · doi:10.3390/ph3040839 · Cited by 213
Inhibition of Mcl-1 through covalent modification of a noncatalytic lysine side chain
Akçay, G., Belmonte, M. A., Aquila, B., Chuaqui, C., Hird, A. W., Lamb, M. L., Rawlins, P. B., Su, N., Tentarelli, S., Grimster, N. P., et al. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2174 · Cited by 207
Cardioprotective Effect of Paeonol and Danshensu Combination on Isoproterenol-Induced Myocardial Injury in Rats
Li, H., Xie, Y., Yang, Q., Wang, S., Zhang, B., Wang, J., Cao, W., Bi, L., Sun, J., Miao, S., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0048872 · Cited by 206
Sensitization for anticancer drug-induced apoptosis by the chemopreventive agent resveratrol
Fulda, S., & Debatin, K. (2004) · Oncogene · doi:10.1038/sj.onc.1207630 · Cited by 205
The Mitochondrial Pathway of Anesthetic Isoflurane-induced Apoptosis
Zhang, Y., Dong, Y., Wu, X., Lu, Y., Xu, Z., Knapp, A., Yue, Y., Xu, T., & Xie, Z. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.065664 · Cited by 204
Dietary exposure to soy or whey proteins alters colonic global gene expression profiles during rat colon tumorigenesis.
Xiao, R., Badger, T. M., & Simmen, F. A. (2005) · Molecular Cancer · doi:10.1186/1476-4598-4-1 · Cited by 205
Life and Death Decisions
Nicholson, D. W., & Thornberry, N. A. (2003) · Science · doi:10.1126/science.1081274 · Cited by 207
Interaction with a Membrane Surface Triggers a Reversible Conformational Change in Bax Normally Associated with Induction of Apoptosis
Yethon, J. A., Epand, R. F., Leber, B. F., Epand, R. M., & Andrews, D. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306289200 · Cited by 203
BCL2 and MCL1 inhibitors for hematologic malignancies
Roberts, A. W., Wei, A. H., & Huang, D. C. S. (2021) · Blood · doi:10.1182/blood.2020006785 · Cited by 211
Mcl-1, Bcl-XL and Stat3 expression are associated with progression of melanoma whereas Bcl-2, AP-2 and MITF levels decrease during progression of melanoma
Zhuang, L., Lee, C. S., Scolyer, R. A., McCarthy, S. W., Zhang, X. D., Thompson, J. F., & Hersey, P. (2007) · Modern Pathology · doi:10.1038/modpathol.3800750 · Cited by 202
Essential role of the voltage-dependent anion channel (VDAC) in mitochondrial permeability transition pore opening and cytochrome c release induced by arsenic trioxide
Zheng, Y., Shi, Y., Tian, C., Jiang, C., Jin, H., Chen, J., Almasan, A., Tang, H., & Chen, Q. (2003) · Oncogene · doi:10.1038/sj.onc.1207205 · Cited by 206
Oncogenic potential of Nrf2 and its principal target protein heme oxygenase-1
Na, H., & Surh, Y. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.10.819 · Cited by 203
BH3 profiling – Measuring integrated function of the mitochondrial apoptotic pathway to predict cell fate decisions
Moore, V. D. G., & Letai, A. G. (2012) · Cancer Letters · doi:10.1016/j.canlet.2011.12.021 · Cited by 201
Dieldrin-Induced Neurotoxicity: Relevance to Parkinson's Disease Pathogenesis
Kanthasamy, A. G., Kitazawa, M., Kanthasamy, A., & Anantharam, V. (2004) · NeuroToxicology · doi:10.1016/j.neuro.2004.07.010 · Cited by 201
The effects of bioactive compounds from plant foods on mitochondrial function: A focus on apoptotic mechanisms
Forbes-Hernández, T. Y., Giampieri, F., Gasparrini, M., Mazzoni, L., Quiles, J. L., Álvarez-Suárez, J. M., & Battino, M. A. (2014) · Food and Chemical Toxicology · doi:10.1016/j.fct.2014.03.017 · Cited by 202
Betulinic acid, a natural compound with potent anticancer effects
Mullauer, F. B., Kessler, J. H., & Medema, J. P. (2010) · Anti-Cancer Drugs · doi:10.1097/cad.0b013e3283357c62 · Cited by 199
Apoptosis and lung cancer: A review
Shivapurkar, N., Reddy, J., Chaudhary, P. M., & Gazdar, A. F. (2003) · Journal of Cellular Biochemistry · doi:10.1002/jcb.10440 · Cited by 195
Lithium neuroprotection: molecular mechanisms and clinical implications
Rowe, M. K., & Chuang, D. (2004) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399404008385 · Cited by 195
Finding the right organelle
Rapaport, D. (2003) · EMBO Reports · doi:10.1038/sj.embor.embor937 · Cited by 194
Extracellular Signal-regulated Kinases 1/2 Are Serum-stimulated “BimEL Kinases” That Bind to the BH3-only Protein BimEL Causing Its Phosphorylation and Turnover
Ley, R., Ewings, K. E., Hadfield, K., Howes, E. A., Balmanno, K., & Cook, S. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311578200 · Cited by 193
Enhancement of auranofin-induced lung cancer cell apoptosis by selenocystine, a natural inhibitor of TrxR1 in vitro and in vivo
Fan, C., Zheng, W., Fu, X., Li, X., Wong, Y.-S., & Chen, T. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.132 · Cited by 193
VDAC1: from structure to cancer therapy
Shoshan‐Barmatz, V., & Mizrachi, D. (2012) · Frontiers in Oncology · doi:10.3389/fonc.2012.00164 · Cited by 200
Exosomes Derived From Bone Mesenchymal Stem Cells Ameliorate Early Inflammatory Responses Following Traumatic Brain Injury
Ni, H., Yang, S., Siaw-Debrah, F., Hu, J., Wu, K., He, Z., Yang, J., Pan, S., Lin, X., Ye, H., et al. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00014 · Cited by 197
Mitochondrial membrane permeabilisation by Bax/Bak
Esposti, M. D., & Dive, C. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00617-x · Cited by 193
miR-129 promotes apoptosis and enhances chemosensitivity to 5-fluorouracil in colorectal cancer
Karaayvaz, M., Zhai, H., & Ju, J. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.193 · Cited by 192
Regulation of apoptosis during homeostasis and disease in the intestinal epithelium
Edelblum, K. L., Yan, F., Yamaoka, T., & Polk, D. B. (2006) · Inflammatory Bowel Diseases · doi:10.1097/01.mib.0000217334.30689.3e · Cited by 192
Integrin signaling in epithelial cells
Gilcrease, M. Z. (2006) · Cancer Letters · doi:10.1016/j.canlet.2006.03.031 · Cited by 204
Multiple paths to a drug resistance phenotype: Mutations, translocations, deletions and amplification of coding genes or promoter regions, epigenetic changes and microRNAs☆
Fojo, T. (2007) · Drug Resistance Updates · doi:10.1016/j.drup.2007.02.002 · Cited by 191
The BH3-mimetic GX15-070 synergizes with bortezomib in mantle cell lymphoma by enhancing Noxa-mediated activation of Bak
Pérez‐Galán, P., Roué, G., Villamor, N., Campo, E., & Colomer, D. (2007) · Blood · doi:10.1182/blood-2006-07-034173 · Cited by 188
Targeting Programmed Cell Death Using Small‐Molecule Compounds to Improve Potential Cancer Therapy
Ke, B., Tian, M., Li, J., Liu, B., & He, G. (2016) · Medicinal Research Reviews · doi:10.1002/med.21398 · Cited by 190
Acquired mutations in BCL2 family proteins conferring resistance to the BH3 mimetic ABT-199 in lymphoma
Fresquet, V., Rieger, M., Carolis, C., Garcia-Barchino, M. J., & Martinez-Climent, J. A. (2014) · Blood · doi:10.1182/blood-2014-03-560284 · Cited by 190
Complicating the complexity of p53
Yee, K. S. Y., & Vousden, K. H. (2005) · Carcinogenesis · doi:10.1093/carcin/bgi122 · Cited by 190
Promise for plant pest control: root-associated pseudomonads with insecticidal activities
Kupferschmied, P., Maurhofer, M., & Keel, C. (2013) · Frontiers in Plant Science · doi:10.3389/fpls.2013.00287 · Cited by 190
In vitro acute and developmental neurotoxicity screening: an overview of cellular platforms and high-throughput technical possibilities
Schmidt, B. Z., Lehmann, M., Gutbier, S., Nembo, E. N., Noël, S., Smirnova, L., Forsby, A., Hescheler, J., Avci, H. X., Härtung, T., et al. (2016) · Archives of Toxicology · doi:10.1007/s00204-016-1805-9 · Cited by 191
Neuroprotection via pro‐survival protein kinase C isoforms associated with Bcl‐2 family members
Weinreb, O., Bar‐Am, O., Amit, T., Chillag-Talmor, O., & Youdim, M. B. H. (2004) · The FASEB Journal · doi:10.1096/fj.04-1916fje · Cited by 184
Apoptotic signaling cascades
Ashe, P. C., & Berry, M. D. (2003) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/s0278-5846(03)00016-2 · Cited by 186
PUMA Dissociates Bax and Bcl-XL to Induce Apoptosis in Colon Cancer Cells
Ming, L., Wang, P., Bank, A., Yu, J., & Zhang, L. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513587200 · Cited by 183
T-lymphocyte death during shutdown of an immune response
Strasser, A., & Pellegrini, M. (2004) · Trends in Immunology · doi:10.1016/j.it.2004.08.012 · Cited by 186
Protective Effects of Resveratrol and Quercetin Against MPP+ -Induced Oxidative Stress Act by Modulating Markers of Apoptotic Death in Dopaminergic Neurons
Bournival, J., Quessy, P., & Martinoli, M. (2009) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-009-9411-5 · Cited by 182
Cell metabolism: An essential link between cell growth and apoptosis
Mason, E. F., & Rathmell, J. C. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.08.011 · Cited by 192
Mcl-1 Interacts with Truncated Bid and Inhibits Its Induction of Cytochrome c Release and Its Role in Receptor-mediated Apoptosis
Clohessy, J. G., Zhuang, J., de Boer, J., Gil‐Gómez, G., & Brady, H. J. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505688200 · Cited by 182
Combined microarray analysis of small cell lung cancer reveals altered apoptotic balance and distinct expression signatures of MYC family gene amplification
Kim, Y. H., Girard, L., Giacomini, C. P., Wang, P., Hernandez‐Boussard, T., Tibshirani, R. J., Minna, J. D., & Pollack, J. R. (2005) · Oncogene · doi:10.1038/sj.onc.1208997 · Cited by 184
Diosgenin induces cell cycle arrest and apoptosis in human leukemia K562 cells with the disruption of Ca2+ homeostasis
Liu, M., Wang, Z., Ju, Y., Wong, R. N., & Wu, Q. (2004) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-004-0849-3 · Cited by 181
Regulation of survivin expression by IGF-1/mTOR signaling
Vaira, V., Lee, C. W., Goel, H. L., Bòsari, S., Languino, L. R., & Altieri, D. C. (2006) · Oncogene · doi:10.1038/sj.onc.1210094 · Cited by 180
Venetoclax-based therapies for acute myeloid leukemia
Guerra, V. A., Dinardo, C. D., & Konopleva, M. Y. (2019) · Best Practice & Research Clinical Haematology · doi:10.1016/j.beha.2019.05.008 · Cited by 183
Exosomes Derived from miR-126-modified MSCs Promote Angiogenesis and Neurogenesis and Attenuate Apoptosis after Spinal Cord Injury in Rats
Huang, J., Xu, Y., Yin, X.-M., & Lin, F. (2019) · Neuroscience · doi:10.1016/j.neuroscience.2019.10.043 · Cited by 180
Cell death regulation: A new way for natural products to treat osteoporosis
Li, Z., Li, D., Chen, R., Gao, S., Xu, Z., & Li, N. (2022) · Pharmacological Research · doi:10.1016/j.phrs.2022.106635 · Cited by 183
Mediation of the antiapoptotic activity of Bcl-xL protein upon interaction with VDAC1 protein
Arbel, N., Ben-Hail, D., & Shoshan-Barmatz, V. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.345918 · Cited by 179
Mitochondrial dynamics and cancer
Grandemange, S., Herzig, S., & Martinou, J. (2008) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2008.12.001 · Cited by 180
Cleavage of Mcl-1 by caspases impaired its ability to counteract Bim-induced apoptosis
Herrant, M., Jacquel, A., Marchetti, S., Belhacène, N., Colosetti, P., Luciano, F., & Auberger, P. (2004) · Oncogene · doi:10.1038/sj.onc.1208069 · Cited by 179
Specific downregulation of bcl-2 and xIAP by RNAi enhances the effects of chemotherapeutic agents in MCF-7 human breast cancer cells
Lima, R. T., Martins, L. M., Guimarães, J. E., Sambade, C., & Vasconcelos, M. H. (2004) · Cancer Gene Therapy · doi:10.1038/sj.cgt.7700706 · Cited by 179
Green tea polyphenols: biology and therapeutic implications in cancer
Shankar, S. (2007) · Frontiers in bioscience · doi:10.2741/2435 · Cited by 180
Targeting specific cell signaling transduction pathways by dietary and medicinal phytochemicals in cancer chemoprevention
Neergheen, V. S., Bahorun, T., Taylor, E. W., Jen, L., & Aruoma, O. I. (2009) · Toxicology · doi:10.1016/j.tox.2009.10.010 · Cited by 180
ERK1/2‐dependent phosphorylation of BimEL promotes its rapid dissociation from Mcl‐1 and Bcl‐xL
Ewings, K. E., Hadfield‐Moorhouse, K., Wiggins, C. M., Wickenden, J. A., Balmanno, K., Gilley, R., Degenhardt, K., White, E., & Cook, S. J. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601723 · Cited by 176
Molecular Details of Bax Activation, Oligomerization, and Membrane Insertion
Bleicken, S., Classen, M., Padmavathi, P. V. L., Ishikawa, T., Zeth, K., Steinhoff, H., & Bordignon, E. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.081539 · Cited by 176
The structure of Bcl‐w reveals a role for the C‐terminal residues in modulating biological activity
Hinds, M. G., Lackmann, M., Skea, G. L., Harrison, P. J., Huang, D. C. S., & Day, C. L. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg144 · Cited by 175
The role of ATF/CREB family members in cell growth, survival and apoptosis
Persengiev, S. P., & Green, M. R. (2003) · APOPTOSIS · doi:10.1023/a:1023633704132 · Cited by 175
Bax inhibition protects against free fatty acid-induced lysosomal permeabilization
Feldstein, A. E., Werneburg, N. W., Li, Z., Bronk, S. F., & Gores, G. J. (2006) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00509.2005 · Cited by 174
Identification of a novel Bcl‐xL phosphorylation site regulating the sensitivity of taxol‐ or 2‐methoxyestradiol‐induced apoptosis
Basu, A., & Haldar, S. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00131-5 · Cited by 174
Genetic Control of Programmed Cell Death During Animal Development
Conradt, B. (2009) · Annual Review of Genetics · doi:10.1146/annurev.genet.42.110807.091533 · Cited by 173
Inhibition of IκB Kinase Activity by Acetyl-boswellic Acids Promotes Apoptosis in Androgen-independent PC-3 Prostate Cancer Cells in Vitro and in Vivo
Syrovets, T., Gschwend, J. E., Büchele, B., Laumonnier, Y., Zugmaier, W., Genze, F., & Simmet, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409477200 · Cited by 176
Critical role of pro-apoptotic Bcl-2 family members in andrographolide-induced apoptosis in human cancer cells
Zhou, J., Zhang, S., Choon-Nam, O., & Shen, H. (2006) · Biochemical Pharmacology · doi:10.1016/j.bcp.2006.04.019 · Cited by 172
Worms, Life, and Death (Nobel Lecture)
Horvitz, H. R. (2003) · ChemBioChem · doi:10.1002/cbic.200300614 · Cited by 171
Iron and α-Synuclein in the Substantia Nigra of MPTP-Treated Mice: Effect of Neuroprotective Drugs R-Apomorphine and Green Tea Polyphenol (-)-Epigallocatechin-3-Gallate
Mandel, S. A., Maor, G., & Youdim, M. B. H. (2004) · Journal of Molecular Neuroscience · doi:10.1385/jmn:24:3:401 · Cited by 171
Immunomodulatory function and anti-tumor mechanism of natural polysaccharides: A review
Yang, Y., & Wu, H. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1147641 · Cited by 171
BH3-only proteins in cell death initiation, malignant disease and anticancer therapy
Labi, V., Erlacher, M., Kießling, S., & Villunger, A. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401940 · Cited by 172
Selenocystine induces apoptosis of A375 human melanoma cells by activating ROS-mediated mitochondrial pathway and p53 phosphorylation
Chen, T., & Wong, Y. S. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8329-2 · Cited by 170
Loss of XIAP protein expression by RNAi and antisense approaches sensitizes cancer cells to functionally diverse chemotherapeutics
McManus, D. C., Lefebvre, C. A., Cherton-Horvat, G., St-Jean, M., Kandimalla, E. R., Agrawal, S., Morris, S. J., Durkin, J. P., & LaCasse, E. C. (2004) · Oncogene · doi:10.1038/sj.onc.1207967 · Cited by 169
MicroRNAs in cancer cell death pathways: Apoptosis and necroptosis
Shirjang, S., Mansoori, B., Asghari, S., Duijf, P. H. G., Mohammadi, A., Gjerstorff, M. F., & Baradaran, B. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.05.017 · Cited by 172
Voltage-dependent anion channel 1-based peptides interact with Bcl-2 to prevent antiapoptotic activity
Arbel, N., & Shoshan-Barmatz, V. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.082990 · Cited by 168
Neuroprotection with metformin and thymoquinone against ethanol-induced apoptotic neurodegeneration in prenatal rat cortical neurons
Ullah, I., Ullah, N., Naseer, M. I., Lee, H., & Kim, M. (2012) · BMC Neuroscience · doi:10.1186/1471-2202-13-11 · Cited by 170
Annona muricata leaves induce G1 cell cycle arrest and apoptosis through mitochondria-mediated pathway in human HCT-116 and HT-29 colon cancer cells
Moghadamtousi, S. Z., Karimian, H., Rouhollahi, E., Paydar, M., Fadaeinasab, M., & Kadir, H. A. (2014) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2014.08.011 · Cited by 171
Aptamer-Functionalized DNA Origami for Targeted Codelivery of Antisense Oligonucleotides and Doxorubicin to Enhance Therapy in Drug-Resistant Cancer Cells
Pan, Q., Nie, C., Hu, Y., Yi, J., Liu, C., Zhang, J., He, M., He, M., Chen, T., & Chu, X. (2019) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.9b20707 · Cited by 167
PROTEINS OF THE BCL‐2 FAMILY IN APOPTOSIS SIGNALLING: FROM MECHANISTIC INSIGHTS TO THERAPEUTIC OPPORTUNITIES
Chan, S. L., & Yu, V. C. K. (2004) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/j.1440-1681.2004.03975.x · Cited by 168
Rasagiline: Neurodegeneration, neuroprotection, and mitochondrial permeability transition
Youdim, M. B. H., Bar‐Am, O., Yogev‐Falach, M., Weinreb, O., Maruyama, W., Naoi, M., & Amit, T. (2004) · Journal of Neuroscience Research · doi:10.1002/jnr.20350 · Cited by 166
Immunotherapy: A promising approach to reverse sepsis-induced immunosuppression
Patil, N. K., Bohannon, J. K., & Sherwood, E. R. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.07.019 · Cited by 173
Nanoparticles of Titanium and Zinc Oxides as Novel Agents in Tumor Treatment: a Review
Bogdan, J., Pławińska-Czarnak, J., & Zarzynska, J. M. (2017) · Nanoscale Research Letters · doi:10.1186/s11671-017-2007-y · Cited by 165
BCL2: A promising cancer therapeutic target
Radha, G., & Raghavan, S. C. (2017) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2017.06.004 · Cited by 165
Granzyme B activates procaspase-3 which signals a mitochondrial amplification loop for maximal apoptosis
Metkar, S. S., Wang, B., Ebbs, M. L., Kim, J. H., Lee, Y. J., Raja, S. M., & Froelich, C. J. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200210158 · Cited by 165
Proteasome inhibitor therapy in multiple myeloma
Chauhan, D., Hideshima, T., Mitsiades, C. S., Richardson, P. G. G., & Anderson, K. C. (2005) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-04-0338 · Cited by 167
Repeated Unpredictable Stress and Antidepressants Differentially Regulate Expression of the Bcl-2 Family of Apoptotic Genes in Rat Cortical, Hippocampal, and Limbic Brain Structures
Kosten, T. A., Galloway, M. P., Duman, R. S., Russell, D. S., & D'Sa, C. (2008) · Neuropsychopharmacology · doi:10.1038/sj.npp.1301527 · Cited by 165
Cell survival and metastasis regulation by Akt signaling in colorectal cancer
Agarwal, E., Brattain, M. G., & Chowdhury, S. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2013.03.025 · Cited by 164
The mammalian START domain protein family in lipid transport in health and disease
Clark, B. J. (2011) · Journal of Endocrinology · doi:10.1530/joe-11-0313 · Cited by 174
Cytosolic factor‐ and TOM‐independent import of C‐tail‐anchored mitochondrial outer membrane proteins
Setoguchi, K., Otera, H., & Mihara, K. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601438 · Cited by 163

Authors: Cory, S., & Adams, J. M.
Affiliations: The Royal Melbourne Hospital (AU)
ORCID: Cory, Suzanne
Adams, Jerry M.
Venue: Nature Reviews Cancer
Publisher: Springer Science and Business Media LLC
Published: 2002-09-01
Volume: 2
Issue: 9
Pages: 647-656
ISSN: 1474-175X (ISSN-L)
1474-1768
DOI: 10.1038/nrc883
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
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
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

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

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

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks