The DOI matches its Crossref record; 120 of the 120 references it cites were found in a registry or an index.
BCL-2 family proteins: changing partners in the dance towards death
Open accessAbstract
The BCL-2 family of proteins controls cell death primarily by direct binding interactions that regulate mitochondrial outer membrane permeabilization (MOMP) leading to the irreversible release of intermembrane space proteins, subsequent caspase activation and apoptosis. The affinities and relative abundance of the BCL-2 family proteins dictate the predominate interactions between anti-apoptotic and pro-apoptotic BCL-2 family proteins that regulate MOMP. We highlight the core mechanisms of BCL-2 family regulation of MOMP with an emphasis on how the interactions between the BCL-2 family proteins govern cell fate. We address the critical importance of both the concentration and affinities of BCL-2 family proteins and show how differences in either can greatly change the outcome. Further, we explain the importance of using full-length BCL-2 family proteins (versus truncated versions or peptides) to parse out the core mechanisms of MOMP regulation by the BCL-2 family. Finally, we discuss how post-translational modifications and differing intracellular localizations alter the mechanisms of apoptosis regulation by BCL-2 family proteins. Successful therapeutic intervention of MOMP regulation in human disease requires an understanding of the factors that mediate the major binding interactions between BCL-2 family proteins in cells.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
In the citing paper
“Bcl-2 family plays a crucial role in the endogenous apoptosis signal transduction pathway by regulating the mitochondrial/cytochrome C-mediated apoptosis process.356,357”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [357]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
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
Caspase Functions in Cell Death and DiseasePreprint
McIlwain, D. R., Berger, T., & Mak, T. W. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008656 · Cited by 2,702
Mitochondria and cell death: outer membrane permeabilization and beyond
Tait, S. W. G., & Green, D. R. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2952 · Cited by 2,593
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
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
Bid, Bax, and Lipids Cooperate to Form Supramolecular Openings in the Outer Mitochondrial Membrane
Kuwana, T., Mackey, M. R., Perkins, G. A., Ellisman, M. H., Latterich, M., Schneiter, R., Green, D. R., & Newmeyer, D. D. (2002) · Cell · doi:10.1016/s0092-8674(02)01036-x · Cited by 1,513
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
BAX and BAK Regulation of Endoplasmic Reticulum Ca 2+ : A Control Point for Apoptosis
Scorrano, L., Oakes, S. A., Opferman, J. T., Cheng, E. H. Y., Sorcinelli, M. D., Pozzan, T., & Korsmeyer, S. J. (2003) · Science · doi:10.1126/science.1081208 · Cited by 1,387
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
Certo, M. V., Moore, V. D. G., Nishino, M., Wei, G., Korsmeyer, S. J., Armstrong, S. A., & Letai, A. G. (2006) · Cancer Cell · doi:10.1016/j.ccr.2006.03.027 · Cited by 1,278
Flagged first, then by citations
Cited by
Sorted by citations
Items 901–1,000 of 1,000
Drozdowska, M., Leszczyńska, T., Piasna-Słupecka, E., Domagała, D., & Koronowicz, A. A. (2021) · Applied Sciences · doi:10.3390/app112311507 · Cited by 7
Mestrum, S. G. C., Vanblarcum, R. B. Y., Drent, R. J. M., Boonen, B., van Hemert, W. L. W., Ramaekers, F. C. S., Hopman, A. H. N., & Leers, M. P. G. (2022) · Cytometry Part A · doi:10.1002/cyto.a.24558 · Cited by 7
Li, H., Zhang, W., Zhang, H., Xie, Y., Sun, C., Di, C., Si, J., Gan, L., & Yan, J. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.28808 · Cited by 7
Pennec, G. L., & Gardères, J. (2019) · Genes · doi:10.3390/genes10070485 · Cited by 7
Almansour, N. M., Allemailem, K. S., Aty, A. A. A. E., Boussoufa, D., Ismail, E. I. F., & Ibrahim, M. A. A. (2023) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2023.2180668 · Cited by 6
Malard, F., Sizun, C., Thureau, A., Carlier, L., & Lescop, E. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104830 · Cited by 6
High incidence of imperforate vagina in ADGRA3-deficient mice
Kvam, J. M., Nybo, M. L., Torz, L., Sustarsic, R. K., Jensen, K. H. R., Nielsen, J. E., Frederiksen, H. W., Gadgaard, S., Spieß, K., Poulsen, S. S., et al. (2024) · BMC Biology · doi:10.1186/s12915-024-01873-6 · Cited by 6
Korelin, K., Oostveen, M., Wahbi, W., Ianevski, F., Cavalcante, B., Turunen, L., Belevich, I. N., Al‐Samadi, A., & Salo, T. A. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116719 · Cited by 6
Jian, Y., Han, F., Zhu, Y., Geng, C., Zhang, Y., Wu, Y., Leng, Y., Chen, W.-M., An, Z., & Zhu, H. (2024) · Clinical and Translational Science · doi:10.1111/cts.70006 · Cited by 6
Protection of beta cells against cytokine‐induced apoptosis by the gut microbial metabolite butyrate
Jørgensen, K. S., Pedersen, S. S., Hjorth, S. A., Billestrup, N., & Prause, M. C. B. (2024) · FEBS Journal · doi:10.1111/febs.17334 · Cited by 6
Yang, X., Li, K., Chen, L., Wang, L., Wang, X., Lu, K., Bai, Y., Hou, Y., Hou, J., Wang, C., et al. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05061-7 · Cited by 6
Effect of Apoptosis and Autophagy on Recombinant Protein Expression in Chinese Hamster Ovary Cells
Zhang, H., Zhao, Q., Abiti, J., Gao, Y., Han, M., Wang, H., Zhang, X., Wang, J., Guo, J., Wang, X., et al. (2025) · Biotechnology Journal · doi:10.1002/biot.70069 · Cited by 6
Wang, W., Yue, W., Shao, L., Liu, T., Xiao, J., Chu, Q., & Wu, S. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.149096 · Cited by 6
Maillet, L., Fétiveau, A., Lalier-Bretaudeau, L., Martin, N., Barillé‐Nion, S., Guette, C., Gautier, F., Télétchéa, S., & Juin, P. P. (2025) · Nature Communications · doi:10.1038/s41467-025-65509-1 · Cited by 6
Liu, Y., Ullah, I., Yuan, Y., & Wang, J. (2026) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2026.115776 · Cited by 6
Fueling the fire: metabolic dysfunction and senescence as drivers of lung aging and disease
Kliment, C. R., Gurkar, A. U., Cárdenes, N., Ramonell, R. P., Finkel, T., & Königshoff, M. (2026) · Physiological Reviews · doi:10.1152/physrev.00024.2025 · Cited by 6
Chen, X., Li, Z., Yang, S., & Zhang, Y. (2023) · Food Bioscience · doi:10.1016/j.fbio.2023.103088 · Cited by 6
Dong, L., Zhang, L., Zhao, X., Zou, H., Lin, S., Zhu, X., Cao, J., Zhou, C. H., Yu, Z., Zhu, Y., et al. (2023) · Cancer Cell International · doi:10.1186/s12935-023-03036-z · Cited by 6
To be or not to be: The active inference of suicide
Krupnik, V., & Danilova, N. (2024) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2023.105531 · Cited by 6
Li, M., Zhang, X., Wang, Y., Xiang, B., Liu, Z., Zhang, W., Liu, X., & Guo, R. (2024) · ACS Omega · doi:10.1021/acsomega.3c09648 · Cited by 6
Rigo, A., Vaisitti, T., Laudanna, C., Terrabuio, E., Micillo, M., Frusteri, C., D’Ulivo, B., Merigo, F., Sbarbati, A., Mellert, K., et al. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06707-5 · Cited by 6
Müstakim, K. R., Eo, M. Y., Seo, M. H., Yang, H., Kim, M.-K., Myoung, H., & Kim, S. M. (2024) · Scientific Reports · doi:10.1038/s41598-024-60474-z · Cited by 6
Zhao, H., Yang, M., Han, Y., Jiang, N., Liu, Y., Li, C., Yang, J., Luo, S., Liu, C., Sun, L., et al. (2024) · Antioxidants and Redox Signaling · doi:10.1089/ars.2023.0467 · Cited by 9
Ven the dose matters: Venetoclax dosing in the frontline treatment of AML
Sastow, D. L., Levavi, H., Wagner, N., Pratz, K. W., & Tremblay, D. A. (2024) · Blood Reviews · doi:10.1016/j.blre.2024.101238 · Cited by 6
Zohar, H., Lindenboim, L., Gozlan, O., Gundersen, G. G., Worman, H. J., & Stein, R. (2024) · Nucleus · doi:10.1080/19491034.2024.2413501 · Cited by 6
Mifepristone potentiates etoposide toxicity in Hep G2 cells by modulating drug transport
Dostál, Z., Kosina, P., Mlejnek, P., Kikalová, K., & Modrianský, M. (2018) · Toxicology in Vitro · doi:10.1016/j.tiv.2018.09.005 · Cited by 6
B-cell lymphoma-2 inhibition and resistance in acute myeloid leukemia
Wilde, L. R., Ramanathan, S., & Kasner, M. T. (2020) · World Journal of Clinical Oncology · doi:10.5306/wjco.v11.i8.528 · Cited by 6
Sun, F., Zhang, J., Chen, L., Yuan, Y., Guo, X., Dong, L., & Sun, J. (2021) · Neuroscience · doi:10.1016/j.neuroscience.2021.03.032 · Cited by 6
Nica, I. C., Stan, M. S., Popescu, R. G., Nicula, N.-O., Ducu, R., Diamandescu, L., & Dinischiotu, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179627 · Cited by 6
González, J. R., Wilkins‐Rodríguez, A. A., & Gutiérrez‐Kobeh, L. (2022) · Parasite Immunology · doi:10.1111/pim.12917 · Cited by 6
Song, P., Choi, S. Y., Hwang, J. S., Park, H. C., Kim, K. K., Son, H., Hong, C., Kim, Y., Kim, W., & Lee, K. M. (2022) · Molecules · doi:10.3390/molecules27175498 · Cited by 6
Chen, L., Chan, A. M., Wilder, P. T., & Fletcher, S. (2022) · Drug Development Research · doi:10.1002/ddr.22004 · Cited by 6
THE GROWING ROLE OF THE BH3 MIMETIC DRUG VENETOCLAX IN THE THERAPY OF ACUTE MYELOID LEUKEMIA
Pelosi, E., Castelli, G., & Testa, U. (2022) · Mediterranean Journal of Hematology and Infectious Diseases · doi:10.4084/mjhid.2022.080 · Cited by 6
Recent Advances in Nanomaterials of Group XIV Elements of Periodic Table in Breast Cancer Treatment
Hekmat, A., Saso, L., Lather, V., Pandita, D., Kostova, I. P., & Saboury, A. A. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14122640 · Cited by 6
Augmenting Venetoclax Activity Through Signal Transduction in AML
Bouligny, I. M., Maher, K. R., & Grant, S. (2023) · Journal of Cellular Signaling · doi:10.33696/signaling.4.085 · Cited by 7
Dương, M. Q., Gadet, R., Treilleux, I., Borel, S., Nougarède, A., Marcillat, O., Gonzalo, P., Mikaélian, I., Popgeorgiev, N., Rimokh, R., et al. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-05917-7 · Cited by 6
BH3 Mimetic Peptides: An Effective Strategy to Complement Anticancer Therapy
Saraswathy, S. D., Mirunalini, A., Karthikeyan, K., & Premkumar, K. (2023) · Current Protein and Peptide Science · doi:10.2174/1389203724666230822100131 · Cited by 6
Cai, Y., Lai, Q., Zhang, X., Zhang, Y., Zhang, M., Gu, S., Qin, Y., Hou, J., & Zhao, L. (2023) · Korean Journal of Physiology and Pharmacology · doi:10.4196/kjpp.2023.27.5.457 · Cited by 6
Design, molecular modelling and synthesis of novel benzothiazole derivatives as BCL-2 inhibitors
Ismail, H. S., Khalil, A. I., Taha, R. A., Lasheen, D. S., & Ella, D. A. A. E. (2023) · Scientific Reports · doi:10.1038/s41598-023-41783-1 · Cited by 6
Chen, L., Lowe, B. D., & Fletcher, S. (2023) · RSC Advances · doi:10.1039/d3ra05711a · Cited by 6
Mittal, A., Mahala, N., Dhanawade, N. H., Dubey, S. K., & Dubey, U. S. (2024) · Biotechnology Journal · doi:10.1002/biot.202300449 · Cited by 6
Kumari, R., Pandey, S. K., Patel, A. K., Kushwaha, D., Acharya, A., & Bharty, M. K. (2024) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2024.138422 · Cited by 6
Braga, C. B., Milan, J. C., Meirelles, M. A., Zavan, B., Ferreira‐Silva, G. Á., Caixeta, E. S., Ionta, M., & Pilli, R. A. (2024) · RSC Medicinal Chemistry · doi:10.1039/d4md00281d · Cited by 6
Cho, H., Yadav, A. K., Do, Y.-R., Heo, M., Bishop‐Bailey, D., Lee, J., & Jang, B. (2019) · International Journal of Oncology · doi:10.3892/ijo.2019.4925 · Cited by 6
MiR-449a-5p regulates the proliferation of esophageal carcinoma cell by targeting B-cell lymphoma 2
Jiang, T., Zhao, R., Du, Y., Shi, Z., & Cheng, H. (2020) · Translational Cancer Research · doi:10.21037/tcr-20-2869 · Cited by 6
Apoptosis, guardian of the genome: Review
Khalil, A. M. (2021) · World Journal of Biology Pharmacy and Health Sciences · doi:10.30574/wjbphs.2021.5.1.0003 · Cited by 6
Bui, I., Baritaki, S., Libra, M., Zaravinos, A., & Bonavida, B. (2023) · Antioxidants and Redox Signaling · doi:10.1089/ars.2023.0250 · Cited by 6
Zhang, X., Chen, X., Wang, A., Wang, L., He, C., Shi, Z., Zhang, S., Fu, Q., Xu, W., Li, W., et al. (2023) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2023.116903 · Cited by 6
Cross-talk reduction in a multiplexed synchroscan streak camera with simultaneous calibration
Hirmiz, N., Tsikouras, A., Osterlund, E. J., Richards, M., Andrews, D. W., & Fang, Q. (2019) · Optics Express · doi:10.1364/oe.27.022602 · Cited by 6
Self-citationA Probabilistic Approach to Explore Signal Execution Mechanisms With Limited Experimental Data
Kochen, M. A., & Lopez, C. F. (2020) · Frontiers in Genetics · doi:10.3389/fgene.2020.00686 · Cited by 6
Frenster, J. D., Babin, S., Garcia, J. B. J., Casani-Galdon, P., Pascual-Mas, P., Robertson, G., Ojalvo, J. G., & Arias, A. M. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.01.25.634859 · Cited by 6
Ubiquitin-independent mitophagy: mechanisms and pathophysiological functions
Tang, C., & Dong, Z. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-15260-3.00012-0 · Cited by 5
Kudo, S., Hikita, H., Saito, Y., Murai, K., Kodama, T., Tatsumi, T., & Takehara, T. (2025) · Cell Death and Differentiation · doi:10.1038/s41418-025-01458-y · Cited by 5
Jang, J. H., Kim, H.-I., Jun, H., Park, C.-Y., Kim, J., Yeo, M., Kim, H.-C., Shin, Y., Kang, S., Kim, E. H., et al. (2025) · Biochemical Pharmacology · doi:10.1016/j.bcp.2025.116877 · Cited by 6
Regulation of Apoptotic Pathways by MicroRNAs: A Therapeutic Strategy for Alzheimer’s Disease
Saadh, M. J., Muhammad, F. A., Alazzawi, T. S., Fahdil, A. A., Athab, Z. H., Tuxtayev, J., Alsaikhan, F., & Farhood, B. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-04833-5 · Cited by 5
Bilden, A., Sabancılar, İ., Azarkan, S. Y., Kaçak, K., Kaya, S., Kahraman, M., & Çiçek, M. (2025) · Current Issues in Molecular Biology · doi:10.3390/cimb47050328 · Cited by 5
Gong, X., Ogino, N., Leite, M. F., Zhang, D., Chen, Z., Nguyen, R. Y., Liu, R., Kruglov, E. A., Flores, K. M., Cabral, A. T., et al. (2025) · Cancer Research · doi:10.1158/0008-5472.can-24-0859 · Cited by 6
Chai, J., Wen, Z., Chen, L., Pu, Q., Luo, T., Wu, X., Ma, Z., Luo, Z., Luo, J., & Wang, J. (2025) · Antioxidants · doi:10.3390/antiox14060623 · Cited by 5
Gu, H., You, W., Zhou, X., Wang, Z., Huo, S., Nie, X., Feng, Y., You, Y., Zhan, X., & Xia, L. (2025) · ACS Omega · doi:10.1021/acsomega.5c01251 · Cited by 5
Mazzeo, P., Penir, S. M. U., Shumilov, E., Wolf, S., Häupl, B., Markus, K., Shirneshan, K., Rittscher, K., Brzuszkiewicz, E., Aydilek, E., et al. (2025) · Leukemia · doi:10.1038/s41375-025-02756-7 · Cited by 5
Molecular Cell Biology of Apoptosis in Health and Disease
Ahmed, A. S., & Tait, S. W. G. (2025) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-92785-0_1 · Cited by 6
Gan, H., Gong, M., Wang, L., Huang, X., Yuxing, C., Hu, Z., Li, X., & Zeng, Q. (2025) · Food Science & Nutrition · doi:10.1002/fsn3.71064 · Cited by 5
Bukhari, S. N. A., & Yogesh, R. (2022) · Letters in Drug Design & Discovery · doi:10.2174/1570180819666220405232333 · Cited by 5
Krishna, S., Murthy, T. P. K., Divyashri, G., Murahari, M., Shukla, R., Kumar, S. B., & Singh, T. R. (2022) · Journal of Molecular Liquids · doi:10.1016/j.molliq.2022.120250 · Cited by 5
Yuan, S., Zuo, W., Liu, T., & Fu, H. (2023) · Technology in Cancer Research & Treatment · doi:10.1177/15330338231208608 · Cited by 5
The broad impact of cell death genes on the human disease phenome
Rich, A., Lin, P., Gamazon, E. R., & Zinkel, S. S. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06632-7 · Cited by 6
Malla, S., Nyinawabera, A., Neupane, R., Pathak, R., Lee, D., Abou-Dahech, M. S., Kumari, S., Sinha, S., Tang, Y., Ray, A., et al. (2024) · Cancers · doi:10.3390/cancers16152621 · Cited by 5
Porphyromonas gingivalis affects neutrophil pro-inflammatory activities
Zimny, A., Płonczyńska, A., Jakubowski, W., Zubrzycka, N., Potempa, J., & Sochalska, M. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1419651 · Cited by 5
Chemotherapeutic Drug—Antibody Conjugates (ChemoBodies): Recent Advances and Future Directions
Tiwatane, A. K., Khandave, P. Y., Kulkarni, S. S., Oisaki, K., & Pande, A. H. (2025) · Current Oncology Reports · doi:10.1007/s11912-025-01713-y · Cited by 6
Bacterial effector OspB hijacks apoptosis through peptide-bond recombination of BH3 domain proteins
Shao, Y., Yang, D., Gao, X., Wang, M., Meng, L., Niu, T., Li, X., Ding, J., Shao, F., & Xu, Y. (2025) · Cell Host & Microbe · doi:10.1016/j.chom.2025.09.018 · Cited by 5
Anticancer tendency of aflatoxin B1 in 4T1 breast cancer cell line
Mousazadeh, R., Hesaraki, S., Bayat, M., Jahandideh, A., & Hashemi, J. (2019) · Gene Reports · doi:10.1016/j.genrep.2019.100442 · Cited by 5
Linking hyperosmotic stress and apoptotic sensitivity
Stöhr, D., & Rehm, M. (2020) · FEBS Journal · doi:10.1111/febs.15520 · Cited by 5
Apoptosis-inducing effects of Terminalia phanerophlebia leaf extracts on human renal cells
Mposula, S., Amoako, D. G., Somboro, A. M., Arhin, I., Kumalo, H. M., & Khan, R. B. (2021) · South African Journal of Botany · doi:10.1016/j.sajb.2021.03.009 · Cited by 5
Testicular Nuclear Receptor 4 Regulates Proliferation and Apoptosis of Bladder Cancer via Bcl-2
Wang, H., Luo, W., Wang, X., Xue, D., Ren, L., Xu, L. L., Ge, G., Xia, L., Yu, S., Wang, M., et al. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.670409 · Cited by 5
Deepak Shyl, E. S., Beutline Malgija, M., Iniyan, A. M., & Vincent, S. G. P. (2022) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26347 · Cited by 5
Amare, M., Westrick, N. M., Keller, N. P., & Kabbage, M. (2022) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2022.103730 · Cited by 5
Zolottsev, V. А., Latysheva, А. S., Khan, I. I., Pokrovsky, V. S., & Misharin, A. Y. (2022) · ChemistrySelect · doi:10.1002/slct.202203393 · Cited by 5
Bowman, K. E. R., Ahne, L., O’Brien, L., Mause, E. R. V., Lu, P., Wallis, B., Evason, K. J., & Lim, C. S. (2022) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.2c00665 · Cited by 5
Bayram, N. N., Ulu, G. T., Abdulhadi, N. A., Gürdap, S., İşoğlu, İ. A., Baran, Y., & Dinçer, S. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15030733 · Cited by 5
Parekh, S., Arkatkar, A., Soni, A., Patel, P., & Mishra, K. K. (2023) · 3 Biotech · doi:10.1007/s13205-023-03594-z · Cited by 5
Ranson, A. J., Carneiro, M. B. H., Perks, B., Penner, R., Melo, L. D., Canton, J., Egen, J. G., & Peters, N. C. (2023) · The Journal of Immunology · doi:10.4049/jimmunol.2200720 · Cited by 5
The inhibitory function of GDF11/BMP11 in liver cancer by inducing apoptosis and ROS–JNK pathway
Zhang, Y., Wang, C., Li, J., Jin, L., Ding, W., Liu, H., Zhou, N., Ren, Z., Zhang, J., Wei, Y. S., et al. (2023) · ONCOLOGIE · doi:10.1515/oncologie-2023-0001 · Cited by 5
Spectroscopically Orthogonal Spin Labels in Structural Biology at Physiological Temperatures
Teucher, M., Kucher, S., Timachi, M. H., Wilson, C. B., Śmiłowicz, D., Stoll, R., Metzler‐Nolte, N., Sherwin, M. S., Han, S., & Bordignon, E. (2023) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.3c04497 · Cited by 5
El‐Fakharany, E. M., El‐Gendi, H., Abdel-Wahhab, K. G., Abu-Serie, M. M., El-Sahra, D. G., & Ashry, M. (2023) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2023.2250452 · Cited by 5
Xu, J., Hashino, T., Tanaka, R., Kawaguchi, K., Yoshida, H., & Kataoka, T. (2023) · Scientific Reports · doi:10.1038/s41598-023-41196-0 · Cited by 5
Correlation of ultrasound features with Bcl‐2 protein expression in basal cell carcinomas ( BCCs )
Luo, P., Chen, Y., Zhong, Z., Feng, M., Wang, J., & Liang, J. (2023) · Journal of Clinical Ultrasound · doi:10.1002/jcu.23554 · Cited by 5
Yang, N., Jia, X., Yang, Y., Niu, J., Wu, X., Ding, F., Tian, M., & Tang, D. (2023) · Arabian Journal of Chemistry · doi:10.1016/j.arabjc.2023.105409 · Cited by 5
Seymour, D. J., Kim, J. J. M., Doelman, J., & Cant, J. P. (2024) · Journal of Dairy Science · doi:10.3168/jds.2023-24478 · Cited by 4
Phenotyping of cancer-associated somatic mutations in the BCL2 transmembrane domain
Leiva, D., Lucendo, E., García-Jareño, A. B., Sancho, M., & Orzáez, M. (2024) · Oncogenesis · doi:10.1038/s41389-024-00516-3 · Cited by 5
Wang, F., Zeng, L., Chi, Y., Yao, S., Zheng, Z., Peng, S., Wang, X., & Chen, K. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.112679 · Cited by 5
Luković, D., Franich, A. A., Živković, M. D., Rajković, S., Stojanović, B., Gajović, N., Jurišević, M., Pavlovic, S. M., Marković, B. S., Jovanović, M., et al. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25158525 · Cited by 5
Wei, S., Mao, Y., Sokolova, I. M., Li, Z., Li, L., Khalid, M. S., Tu, Z., Zhong, Z., Hu, M., & Wang, Y. (2024) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2024.176916 · Cited by 5
Antiviral efficacy of dictamnine against nervous necrosis virus in Epinephelus coioides
Liu, Q., Liu, X., Wang, M., Zhou, J.-L., Liu, T., Yu, Q. C., Ling, F., & Wang, G. (2025) · Aquaculture · doi:10.1016/j.aquaculture.2025.742363 · Cited by 5
Seo, H. W., Park, J.-H., Lee, J. Y., Park, H., & Kim, J. (2018) · Journal of Experimental & Biomedical Sciences/Biomedical Science Letters · doi:10.15616/bsl.2018.24.1.15 · Cited by 5
Nutrient Deprivation Promotes MCL-1 Degradation in an Autophagy-Independent Manner
Pervushin, N. V., Senichkin, V. V., Kapusta, A. A., Gorbunova, A. S., Kaminskyy, V. O., Zhivotovsky, B., & Kopeina, G. S. (2020) · Biochemistry (Moscow) · doi:10.1134/s0006297920100119 · Cited by 5
Wang, Z., Song, T., Guo, Z., Cao, K., Chen, C., Feng, Y., Wang, H., Yin, F., Zhou, S. D., Dai, J., et al. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01290 · Cited by 5
Susceptibility of multiple myeloma to B-cell lymphoma 2 family inhibitors
Lernoux, M., Schnekenburger, M., Dicato, M. A., & Diederich, M. F. (2021) · Biochemical Pharmacology · doi:10.1016/j.bcp.2021.114526 · Cited by 5
Contribution of Yeast Studies to the Understanding of BCL-2 Family Intracellular Trafficking
Eyitayo, A. R., Gonin, M., Arokium, H., & Manon, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22084086 · Cited by 5
Wooten, J. V., Mavingire, N., Araújo, C., Aja, J., Wauchope, S., Delgoda, R., & Brantley, E. J. (2022) · Fitoterapia · doi:10.1016/j.fitote.2022.105203 · Cited by 5
Domain-specific insight into the recognition of BH3-death motifs by the pro-survival Bcl-2 protein
Mushtaq, A. U., Ådén, J., Ali, K., & Gröbner, G. (2022) · Biophysical Journal · doi:10.1016/j.bpj.2022.10.041 · Cited by 5
Metadata
- Authors
- Kale, J., Osterlund, E. J., & Andrews, D. W.
- Affiliations
- Sunnybrook Hospital (CA)
- University of Toronto (CA)
- Corresponding author
- Andrews, David W
- Venue
- Cell Death & Differentiation
- Published
- 2017-11-17
- Volume
- 25
- Issue
- 1
- Pages
- 65-80
- ISSN
- 1350-9047 (ISSN-L)
- 1476-5403
- PMC
- PMC5729540
- OpenAlex
- W2769631482
- Cited by
- 1,574
- References
- 120
- Citations by year
- 2026: 123 · 2025: 189 · 2024: 225 · 2023: 231 · 2022: 242 · 2021: 228 · 2020: 155 · 2019: 123 · 2018: 52 · 2017: 3
- FWCI
- 8.52
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Cell Death and Differentiation (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- Canadian Institutes of Health Research ((FDN143312))
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Keywords
- Bcl-2 family proteins, mitochondrial outer membrane permeabilization, apoptosis, anti-apoptotic proteins, pro-apoptotic proteins, protein-protein interaction, binding affinity, protein concentration, post-translational modification, subcellular localization, caspase activation, cell fate regulation
- MeSH terms
- Cell Membrane Permeability, Protein Processing, Post-Translational, Apoptosis, Proto-Oncogene Proteins c-bcl-2, bcl-2 Homologous Antagonist-Killer Protein, Apoptosis Regulatory Proteins, bcl-2-Associated X Protein, Mitochondrial Membranes
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