The DOI matches its Crossref record; 103 of the 105 references it cites were found in a registry or an index.
From basic apoptosis discoveries to advanced selective BCL-2 family inhibitors
Abstract
Members of the B cell lymphoma 2 (BCL-2) gene family have a central role in regulating programmed cell death by controlling pro-apoptotic and anti-apoptotic intracellular signals. In cancer, apoptosis evasion through dysregulation of specific BCL-2 family genes is a recurring event; accordingly, selective inhibition of specific anti-apoptotic BCL-2 family proteins represents an exciting therapeutic opportunity. A combination of nuclear magnetic resonance (NMR)-based screening and structure-based drug design has yielded the first bona fide BCL-2 homology 3 (BH3) mimetics, including the BCL-2 and BCL-X L dual antagonist navitoclax, which is the first BCL-2 family inhibitor to show efficacy in patients with cancer. Clinical experience with navitoclax prompted the generation of the highly selective BCL-2 inhibitor venetoclax, which is now approved in the United States for the treatment of patients with chronic lymphocytic leukaemia with 17p deletion who have received at least one prior therapy. Recent advances have also been made in the development of potent and selective inhibitors of BCL-X L and myeloid cell leukaemia 1 (MCL1), which are additional BCL-2 family members with established anti-apoptotic roles in cancer. Here we review the latest progress in direct and selective targeting of BCL-2 family proteins for cancer therapy.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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
“Conversely, the BCL2 inhibitor venetoclax is currently available for the treatment of CLL patients who fail to obtain clinical benefit from conventional therapies [1046], and several other molecules with a similar mechanism of action are currently in clinical development [118] (source https://clinicaltrials.gov/).”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [1046]
In the citing paper
“The use of Bcl-xl inhibitors as senolytics is largely limited by their on-target and dose-limiting platelet toxicity.”
From Using proteolysis-targeting chimera technology to reduce navitoclax platelet toxicity and improve its senolytic activity (2020) · cites this paper as [24]
In the citing paper
“Bcl-xl inhibition with ABT263 and other small molecular inhibitors induces platelet apoptosis and results in severe thrombocytopenia, which prevents the use of ABT263 and other Bcl-xl specific inhibitors in the clinic—even for cancer patients—because platelets solely depend on Bcl-xl for survival24–27.”
From Using proteolysis-targeting chimera technology to reduce navitoclax platelet toxicity and improve its senolytic activity (2020) · cites this paper as [24]
In the citing paper
“ABT263 (also known as navitoclax), a Bcl-2 and Bcl-xl dual inhibitor23,24, is one of the most potent and broad-spectrum senolytic agents identified to date16–18.”
From Using proteolysis-targeting chimera technology to reduce navitoclax platelet toxicity and improve its senolytic activity (2020) · cites this paper as [24]
In the citing paper
“Because both SCs and platelets, but not NCs, are primarily dependent on Bcl-xl for survival16–18,24–27 (Supplementary Fig. 1h), we evaluated the effects of PZ compared with ABT263 on the viability of WI38 NCs (Fig. 1g, left panel), IR-SCs (Fig. 1g, middle panel), and platelets (Fig. 1g, right panel).”
From Using proteolysis-targeting chimera technology to reduce navitoclax platelet toxicity and improve its senolytic activity (2020) · cites this paper as [24]
In the citing paper
“As reported, ABT263 was highly toxic to both WI38 IR-SCs (Fig. 1g, middle panel) and platelets16–18,24–27 (Fig. 1g, right panel; Supplementary Fig. 2).”
From Using proteolysis-targeting chimera technology to reduce navitoclax platelet toxicity and improve its senolytic activity (2020) · cites this paper as [24]
In the citing paper
“Therefore, PZ can selectively induce apoptosis in SCs, but not platelets, which are dependent on Bcl-xl for survival while having minimal toxicity to NCs that are less sensitive to Bcl-xl inhibition than SCs16–18,24–27.”
From Using proteolysis-targeting chimera technology to reduce navitoclax platelet toxicity and improve its senolytic activity (2020) · cites this paper as [24]
In the citing paper
“the BCL2 inhibitor venetoclax has been approved by regulatory agencies for use in patients with CLL or small lymphocytic lymphoma (SLL) (Ashkenazi et al., 2017)”
From Immunomodulation by targeted anticancer agents (2021) · cites this paper as Ashkenazi et al., 2017
Citations
Cites
Hallmarks of Cancer: The Next Generation
Hanahan, D., & Weinberg, R. A. (2011) · Cell · doi:10.1016/j.cell.2011.02.013 · Cited by 66,590
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
Death Receptors: Signaling and Modulation
Ashkenazi, A., & Dixit, V. M. (1998) · Science · doi:10.1126/science.281.5381.1305 · Cited by 5,866
Self-citationDanial, N. N., & Korsmeyer, S. J. (2004) · Cell · doi:10.1016/s0092-8674(04)00046-7 · Cited by 4,651
The landscape of somatic copy-number alteration across human cancers
Beroukhim, R., Mermel, C. H., Porter, D., Wei, G., Raychaudhuri, S., Donovan, J., Barretina, J., Boehm, J. S., Dobson, J., Urashima, M., et al. (2010) · Nature · doi:10.1038/nature08822 · Cited by 4,017
An inhibitor of Bcl-2 family proteins induces regression of solid tumours
Oltersdorf, T., Elmore, S. W., Shoemaker, A. R., Armstrong, R. C., Augeri, D. J., Belli, B., Bruncko, M., Deckwerth, T. L., Dinges, J., Hajduk, P. J., et al. (2005) · Nature · doi:10.1038/nature03579 · Cited by 3,407
Bcl-2 gene promotes haemopoietic cell survival and cooperates with c-myc to immortalize pre-B cells
Vaux, D., Cory, S., & Adams, J. (1988) · Nature · doi:10.1038/335440a0 · Cited by 3,355
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-citationDiscovering High-Affinity Ligands for Proteins: SAR by NMR
Shuker, S. B., Hajduk, P. J., Meadows, R. P., & Fesik, S. W. (1996) · Science · doi:10.1126/science.274.5292.1531 · Cited by 2,045
Flagged first, then by citations
2 of the 105 references couldn’t be matched to a known paper.
Research works printed but not linked: 1
- Seymour, J. F. et al. Reduction of tumor lysis syndrome (TLS) risk in chronic lymphocytic leukemia (CLL) patients treated with ABT-199 (GDC-0199): results of modifications to dosing schedule and TLS prophylaxis [abstract P868]. Haematologica 99 (Suppl. 1), 321 (2014).
Cited by
Sorted by citations
Items 501–600 of 918
Molaei, P., Vaseghi, S., Entezari, M., Hashemi, M., & Nasehi, M. (2021) · Neurochemical Research · doi:10.1007/s11064-021-03353-7 · Cited by 10
Reddy, C. N., & Sankararamakrishnan, R. (2021) · ACS Omega · doi:10.1021/acsomega.1c03385 · Cited by 10
Su, H., Wen, T., Liu, D., Shao, J., Zhao, L., & Gao, Q. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.811369 · Cited by 10
Jiang, S., Wang, Y.-Q., Tang, Y., Lu, X., & Guo, D. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/6208872 · Cited by 10
Li, Q., Pang, L., Shi, H., Yang, W., Liu, X., Su, G., & Dong, Y. (2018) · Europe PMC (PubMed Central) · Cited by 10
Wu, Z., Yang, Y., & Wang, M. (2024) · Journal of Orthopaedic Surgery and Research · doi:10.1186/s13018-024-04653-8 · Cited by 9
In situ proximity labeling of proteins associated with circRNA and RNA G-quadruplexes
Mo, J., Chen, Z., Cui, M., Fang, X., Li, R., Qin, S., Zhou, Z., Sun, M., Wu, J., He, C., et al. (2025) · Nature Chemical Biology · doi:10.1038/s41589-025-01993-2 · Cited by 9
Xiong, W., Chen, H., Lu, J., Ren, J., Nie, C., Liang, R., Liu, F., Huang, B., & Luo, Y. (2021) · Folia Histochemica et Cytobiologica · doi:10.5603/fhc.a2021.0019 · Cited by 9
Noncoding RNAs in Drug Resistance of Gastrointestinal Stromal Tumor
Li, J., Guo, S., Sun, Z., & Fu, Y. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.808591 · Cited by 10
iPCD: A Comprehensive Data Resource of Regulatory Proteins in Programmed Cell Death
Tang, D., Han, C., Lin, S., Tan, X., Zhang, W., Peng, D., Wang, C., & Xue, Y. (2022) · Cells · doi:10.3390/cells11132018 · Cited by 9
Gyebi, G. A., Ogunyemi, O. M., Ibrahim, I. M., Afolabi, S. O., Johnson, O. R., Ejike, U. D., & Adebayo, J. O. (2022) · Egyptian Journal of Basic and Applied Sciences · doi:10.1080/2314808x.2022.2106095 · Cited by 9
Pan, D., Zheng, M., Liu, J., Sun, Z., & Shi, X. (2023) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2023/4025734 · Cited by 9
Mouratidou, C., Pavlidis, T., Katsanos, G., Kotoulas, S., Mouloudi, E. K., Tsoulfas, G., Galanis, I. N., & Pavlidis, T. (2023) · World Journal of Gastrointestinal Surgery · doi:10.4240/wjgs.v15.i9.1858 · Cited by 9
Li, X., Ma, R., Ni, Z., Wang, W., Thakur, K., Zhang, J., & Wei, Z. (2023) · Food Science and Human Wellness · doi:10.26599/fshw.2022.9250209 · Cited by 9
Lou, J., Zhou, Q., Lyu, X., Cen, X., Liu, C., Yan, Z., Li, Y., Tang, H., Liu, Q., Ding, J., et al. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c00291 · Cited by 9
Ghrelin, MicroRNAs, and Critical Limb Ischemia: Hungering for a Novel Treatment Option
Neale, J. P. H., Pearson, J. T., Katare, R., & Schwenke, D. O. (2017) · Frontiers in Endocrinology · doi:10.3389/fendo.2017.00350 · Cited by 9
Methods to Detect Immunogenic Cell Death In Vivo
Yamazaki, T., Buqué, A., Rybstein, M. D., Chen, J., Sato, A., & Galluzzi, L. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9773-2_20 · Cited by 9
Gastroprotective Activity of the Total Flavones from Abelmoschus manihot (L.) Medic Flowers
Jun, Z., Fu, Z., Chu, Z., & Bi-wei, S. (2020) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2020/6584945 · Cited by 9
Guo, J., Cao, W., Chen, C., & Chen, X. (2020) · Annals of Translational Medicine · doi:10.21037/atm-20-6598 · Cited by 9
Liu, Y., Zhou, W., Chen, F., Xiao, F., Zhu, H., Zhou, Y., & Guo, G. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/8189706 · Cited by 9
Bioactive recombinant human oncostatin M for NMR-based screening in drug discovery
Mass, O. A., Tuccinardi, J. P., Woodbury, L. G., Wolf, C. L., Grantham, B., Holdaway, K. A., Pu, X., King, M. D., Warner, D. L., Jorcyk, C. L., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-95424-6 · Cited by 9
Chen, J., Nie, W., Hu, Y., Shen, Y., Lin, Y., Wang, B., Qian, Z., & Gao, X. (2021) · Applied Materials Today · doi:10.1016/j.apmt.2021.101277 · Cited by 9
Ruan, Y., XIE, Z., LIU, Q., ZHANG, L., HAN, X., LIAO, X., Liu, J., & Gao, F. (2021) · Biocell · doi:10.32604/biocell.2021.015261 · Cited by 9
Liu, Z., Luo, X., Mo, Y., Zhao, P., Wang, H., Fang, Y., & Xu, Y. (2022) · Pharmaceuticals · doi:10.3390/ph15101244 · Cited by 9
Targeting Mcl-1 by a small molecule NSC260594 for triple-negative breast cancer therapy
Dong, S., Matossian, M. D., Yousefi, H., Khosla, M., Collins‐Burow, B. M., Burow, M. E., & Alahari, S. K. (2023) · Scientific Reports · doi:10.1038/s41598-023-37058-4 · Cited by 9
Cao, A., & Li, X. (2019) · PubMed · doi:10.1080/21691401.2019.1640708 · Cited by 9
RetractedLiu, A., Yu, H., Yang, Y., Xue, F.-Y., Chen, X., Zhang, Y., Zhou, Z.-Y., Zhang, B., Li, L., Sun, C., et al. (2019) · OncoTargets and Therapy · doi:10.2147/ott.s231125 · Cited by 9
Reddy, C. N., Manzar, N., Ateeq, B., & Sankararamakrishnan, R. (2020) · Biochemistry · doi:10.1021/acs.biochem.0c00661 · Cited by 9
Discovery of potent and selective Bcl-2 inhibitors with acyl sulfonamide skeleton
Wang, B., Feng, W., Wang, J., Dong, Y., Liu, Y., Yao, Y., Zhang, J., Shi, W. Q., Liu, L., Zhang, H., et al. (2021) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2021.116350 · Cited by 9
Bufarenogin induces intrinsic apoptosis via Bax and ANT cooperation
Han, Q., Zhang, C., Zhang, Y., Li, Y., Wu, L., & Sun, X. (2021) · Pharmacology Research & Perspectives · doi:10.1002/prp2.694 · Cited by 9
Sinularin stabilizes FOXO3 protein to trigger prostate cancer cell intrinsic apoptosis
Meng, X., Wang, K., Ye, S., Chen, J., Chen, Z.-Y., Zhang, Z., Yin, W.-Q., Jia, X.-L., Li, Y., Yu, R., et al. (2023) · Biochemical Pharmacology · doi:10.1016/j.bcp.2023.116011 · Cited by 8
Jiang, P., Zhao, Y., Jia, Y., Ma, H., Guo, Y., Yan, W., & Xi, X. (2025) · Journal of Translational Medicine · doi:10.1186/s12967-025-06288-7 · Cited by 8
Zou, C., Yang, H., Cui, L., Cao, X., Huang, H., & Chen, T. (2020) · Molecular Medicine Reports · doi:10.3892/mmr.2020.11399 · Cited by 8
Zhao, S., Nan, L., Wang, Y., Wei, L., & Mo, S. (2021) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2021.4858 · Cited by 8
Drug Repurposing: Deferasirox Inhibits the Anti-Apoptotic Activity of Mcl-1
Bourafai-Aziez, A., Benabderrahmane, M. B., Paysant, H., Weiswald, L., Poulain, L., Carlier, L., Ravault, D., Jouanne, M., Coadou, G., Oulyadi, H., et al. (2021) · Drug Design Development and Therapy · doi:10.2147/dddt.s323077 · Cited by 8
Al-shuwaili, Z. A. H., Tabrizi, M. H., & Ghobeh, M. (2023) · Journal of Drug Delivery Science and Technology · doi:10.1016/j.jddst.2023.104303 · Cited by 8
Ren, Q., Zhang, G., Yan, R., Zhou, D., Huang, L., Zhang, Q., Li, W., Huang, G., Li, Z., & Yan, J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241914508 · Cited by 8
Zhang, X., Zhang, Q., Yu, M., Zhang, Y., He, T., Qiu, Z., Qiu, Y., & Wang, W. (2023) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2023.117349 · Cited by 8
Koyuncu, İ., Temiz, E., Güler, E. M., Durgun, M., Yüksekdağ, Ö., Giovannuzzi, S., & Supuran, C. T. (2024) · ChemMedChem · doi:10.1002/cmdc.202300680 · Cited by 8
Fu, R., Dou, Z., Li, N., Fan, X., Amin, S., Zhang, J., Wang, Y., Li, Z., Li, Z., & Yang, P. (2024) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2024.07.018 · Cited by 8
Røsand, Ø., Wang, J., Scrimgeour, N. R., Marwarha, G., & Høydal, M. A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25158460 · Cited by 8
“Examining RAS pathway rewiring with a chemically inducible activator of RAS”
Rose, J. C., Dieter, E. M., Cunningham‐Bryant, D., & Maly, D. J. (2018) · Small GTPases · doi:10.1080/21541248.2018.1446697 · Cited by 8
Baltzer, S., & Klußmann, E. (2019) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-019-01686-3 · Cited by 8
Cao, Y.-Q., Chen, Y. X., Wang, F., Wang, Y.-G., & Long, J. (2020) · Folia Neuropathologica · doi:10.5114/fn.2020.94006 · Cited by 6
FRA-1 suppresses apoptosis of Helicobacter pylori infected MGC-803 cells
Yang, Y., You, B., Dong, S., & Zhou, C. (2021) · Molecular Biology Reports · doi:10.1007/s11033-020-06105-y · Cited by 8
Wu, Y., Wu, T., Hu, X., Xu, S., Xiao, D., Wu, J., Yan, X., Yang, X., & Li, G. (2022) · International Journal of Medical Sciences · doi:10.7150/ijms.67027 · Cited by 8
The effect and mechanisms of melatonin on the proliferation and apoptosis of lung cancer cells
Liu, H., Wang, F., Zhao, J., Zhang, X., Zeng, Z., Wang, S., Guan, J., & Qin, H. (2022) · Bioengineered · doi:10.1080/21655979.2021.2023803 · Cited by 8
Recent advances of bioactive proteins/polypeptides in the treatment of breast cancer
Li, Q., Zhou, Z., Hu, C., Li, X., Chang, Y., Liu, Y., Wang, Y., & Zhou, X. (2023) · Food Science and Biotechnology · doi:10.1007/s10068-022-01233-6 · Cited by 8
Abdel‐Wahed, H. M., & Fadda, A. A. (2023) · ChemistrySelect · doi:10.1002/slct.202300107 · Cited by 8
RetractedOne-step synthesis of gene carrier via gamma irradiation and its application in tumor gene therapy
Jeong, S. I., Park, S., Park, S.-J., Kim, E., Heo, H., Park, J. S., Gwon, H., Lim, Y., & Jang, M.-K. (2018) · International Journal of Nanomedicine · doi:10.2147/ijn.s149532 · Cited by 8
Expression profile of long non‑coding RNAs in cardiomyocytes exposed to acute ischemic hypoxia
Li, H., Cheng, Z., Tang, Y., Feng, M., Yin, A., Zhang, H., Xu, J. M., Zhang, Q., Zhang, J., & Qian, L. (2018) · Molecular Medicine Reports · doi:10.3892/mmr.2018.9658 · Cited by 8
Tian, R., Guo, K., Wu, B., & Wang, H. (2019) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-019-03634-4 · Cited by 8
Kirchhofer, D., Burdick, D. J., Skelton, N. J., Zhang, Y., & Ultsch, M. H. (2020) · Biochemical Society Transactions · doi:10.1042/bst20190672 · Cited by 8
The Design and Application of Bioisosteres in Drug Design
Meanwell, N. A. (2021) · Wiley eBooks · doi:10.1002/0471266949.bmc259 · Cited by 8
Li, J., Li, W., Wang, S., Zheng, H., Bao, J., Wang, Y., & Jin, H. (2025) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2025.119916 · Cited by 7
Bhusare, N., Gade, A., & Kumar, M. S. (2024) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.23732 · Cited by 7
Eugenol suppresses VEGF-dependent angiogenesis by JAK2/STAT3 pathway in non-small cell lung cancer
Su, Y., Wang, Y., Yu, Q., Wu, Z., Zhang, D., & Yan, C. (2024) · Guidelines and Standards of Chinese Medicine · doi:10.1097/gscm.0000000000000021 · Cited by 7
Ung, J., Kassai, M., Tan, S., Loughran, T. P., Feith, D. J., & Cabot, M. C. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25189825 · Cited by 7
Wu, R. J., Li, P., Hao, B., Fredimoses, M., Ge, Y., Zhou, Y., Tang, L., Li, Y., Liu, H., Janson, V., et al. (2024) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2024.107878 · Cited by 7
Pro-apoptotic carboxamide analogues of natural fislatifolic acid targeting Mcl-1 and Bcl-2
Tiamas, S. G., Daressy, F., Samra, A. A., Bignon, J. S., Steinmetz, V., Litaudon, M., Fourneau, C., Leong, K. H., Ariffin, A., Awang, K., et al. (2020) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2020.127003 · Cited by 7
Recent Advances in β-catenin/BCL9 protein–protein Interaction Inhibitors
Zhang, H., Bao, Y., Liu, C., Li, J., Zhu, D., & Zhang, Q. (2021) · Future Medicinal Chemistry · doi:10.4155/fmc-2020-0357 · Cited by 7
Santos, D., Rafacho, B. P. M., Gonçalves, A., Pires, V. C., Roscani, M. G., Azevedo, P. S., Polegato, B. F., Minicucci, M. F., Fernandes, A. A. H., Tanni, S. É., et al. (2021) · Arquivos Brasileiros de Cardiologia · doi:10.36660/abc.20190633 · Cited by 7
Functional Diversity of Mitochondrial Peptidyl-tRNA Hydrolase ICT1 in Human Cells
Chicherin, I., Dukhalin, S., Khannanov, R. A., Baleva, M. V., Левицкий, С. А., Patrushev, M. V., Владимирович, С. П., & Kamenski, P. A. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.716885 · Cited by 7
Murthy, A. V. R., Narendar, V., Kumar, N. S., Aparna, P., Bhavani, A. K. D., Solhi, H., Guével, R. L., Roul, J., Gautier, F., Juin, P. P., et al. (2021) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2021.128390 · Cited by 7
Siddiqui, M. T., & Konopleva, M. Y. (2021) · Expert Review of Clinical Pharmacology · doi:10.1080/17512433.2021.2008239 · Cited by 7
Eddinger, G. A., & Gellman, S. H. (2018) · Angewandte Chemie · doi:10.1002/ange.201806909 · Cited by 7
Wang, D., Xu, M., Li, F., Gao, Y., & Sun, H. (2022) · Natural Product Communications · doi:10.1177/1934578x221115528 · Cited by 7
Rational design of Harakiri (HRK)-derived constrained peptides as BCL-x L inhibitors
Zhang, P., Walko, M., & Wilson, A. J. (2023) · Chemical Communications · doi:10.1039/d2cc06029a · Cited by 7
Hu, X., Zhang, J., Xiang, Q., Huang, G., Yuan, Q., Wang, Y., & Shen, Z. (2023) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2023.02.009 · Cited by 7
Recent Updates in Venetoclax Combination Therapies in Pediatric Hematological Malignancies
Leśniak, M., Lipniarska, J., Majka, P., Lejman, M., & Zawitkowska, J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242316708 · Cited by 7
Mani‐Varnosfaderani, A., Neiband, M. S., & Benvidi, A. (2018) · Molecular Diversity · doi:10.1007/s11030-018-9856-x · Cited by 7
Wei, R., Wu, W., Pan, C., Yu, C., Li, C., Chen, L., Liang, S., & Shiue, Y. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.27643 · Cited by 7
Methods to Probe Conformational Activation and Mitochondrial Activity of Proapoptotic BAK
Singh, G., & Moldoveanu, T. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-8861-7_13 · Cited by 7
Wong, S., Ninomiya, M., Koketsu, M., & Hasbullah, S. A. (2019) · Arabian Journal of Chemistry · doi:10.1016/j.arabjc.2019.02.002 · Cited by 7
5-FU preferably induces apoptosis in BRAF V600E colorectal cancer cells via downregulation of Bcl-xL
Shi, T., Gao, M., He, M., Yue, F., Zhao, Y., Sun, M., He, K., & Chen, L. (2019) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-019-03598-5 · Cited by 7
Kuo, Y., & Rajesh, R. (2020) · Journal of the Taiwan Institute of Chemical Engineers · doi:10.1016/j.jtice.2020.05.011 · Cited by 7
Narendar, K., Rao, B. S., Tirunavalli, S. K., Jadav, S. S., Andugulapati, S. B., Ramalingam, V., & Babu, K. S. (2023) · Natural Product Research · doi:10.1080/14786419.2023.2166042 · Cited by 7
The miR-1204 regulates apoptosis in NSCLC cells by targeting DEK
Qian, Z. Y., Yang, J., Liu, H., Yin, Y., Hou, L., & Hu, H. (2019) · Folia Histochemica et Cytobiologica · doi:10.5603/fhc.a2019.0009 · Cited by 7
Nie, D., Liu, X., Wang, Y., He, W., Li, M., Peng, Y., Zhang, J., Sun, L., Yan, Z., & Ye, L. (2020) · In Vitro Cellular & Developmental Biology - Animal · doi:10.1007/s11626-019-00424-6 · Cited by 7
Technical aspects of megaureter repair.
Hendren, W. H. (1977) · PubMed · Cited by 7
Philadelpho, B. O., Santiago, V. G., dos Santos, J. E. M., Silva, M., Grandis, R. A. D., Cilli, E. M., Pavan, F. R., Castilho, M. S., Scarafoni, A., de Souza, C. O., et al. (2024) · Foods · doi:10.3390/foods13213508 · Cited by 6
Luo, W., Li, N., Liu, J., Li, D., Li, Y., Ma, Q., Lin, C., Lu, L., & Lin, S. (2024) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.70319 · Cited by 6
A novel FOXM1–BCL2A1 axis determines unfavorable response to venetoclax in AML
Raghuwanshi, S., Magdy, A., Hay, N., & Gartel, A. L. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108240 · Cited by 6
Sherif, M. M., El-Abhar, H. S., Fawzy, H. M., Gad, A. M., & Abdallah, D. M. (2025) · Future Journal of Pharmaceutical Sciences · doi:10.1186/s43094-025-00781-y · Cited by 6
Advancements in breast cancer therapy: Integrating AI tools for drug discovery and clinical trials
Pandey, V., Verma, P., Natesan, G., & Chaube, U. (2025) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2025.111067 · 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
Yang, P., ZOU, Z., & GAO, X. (2021) · Biocell · doi:10.32604/biocell.2021.014728 · Cited by 6
Lv, X.-L., Li, W., Sun, F., An, Y.-Z., Sun, N., Lv, X.-P., & Gao, X. (2024) · BioMetals · doi:10.1007/s10534-024-00588-z · Cited by 6
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
The protective role of vagus nerve stimulation in ischemia-reperfusion injury
Zhang, Q., Zhang, L., Lin, G., & Luo, F. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e30952 · Cited by 6
Tryggestad, S. S., Roseth, I. A., Aass, K. R., Ørning, N. E. H., Mjelle, R., Hella, H., & Standal, T. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1393906 · Cited by 6
Prenatal exposure to Benzo[a]pyrene affects maternal–fetal outcomes via placental apoptosis
Zhao, N., Chu, J., Liu, J., Ma, L., Ma, N., Song, W. D., & Sun, T. (2024) · Scientific Reports · doi:10.1038/s41598-024-68029-y · Cited by 6
Apoptotic signaling pathways in bone metastatic lung cancer: a comprehensive analysis
Zhang, Y., Zheng, Y., Zhang, J., Xu, C., & Wu, J. (2024) · Discover Oncology · doi:10.1007/s12672-024-01151-5 · Cited by 6
The function and mechanism of clinical trial agent CPI-613 in multiple myeloma
Wang, H., Zhang, Y., Xiang, R., Xiang, R., Gong, H., Gong, Y., Xu, H., Ma, Z., Xie, Y., Hu, B., et al. (2024) · Biochemical Pharmacology · doi:10.1016/j.bcp.2024.116717 · Cited by 6
The phosphodiesterase-4 inhibitor Zl-n-91 suppresses glioblastoma growth via EGR1/PTEN/AKT pathway
Li, Y., He, X., Li, S., Chen, S., Zhao, Z., Mu, Y., Zhao, A. Z., Zhou, S., & Li, F. (2024) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2024.177230 · Cited by 6
Tang, S., Yan, G., Kong, L. D., Sun, H. J., Liu, C., Han, Y. M., & Wang, X. (2025) · Acupuncture and Herbal Medicine · doi:10.1097/hm9.0000000000000160 · Cited by 6
Li, X., Hua, D., Wu, D., Hong, W., Kang, Y., Tang, L., Yang, Q., Wang, X., Li, B., Li, R., et al. (2025) · Cancer Medicine · doi:10.1002/cam4.70987 · Cited by 6
Gravitational and mechanical forces shape mitochondrial translation
Wakigawa, T., Kimura, Y., Mito, M., Tsubaki, T., Lee, M., Nakamura, K., Khan, A. H., Saito, H., Yamamori, T., Yamazaki, T., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-74493-z · Cited by 6
Bourafai-Aziez, A., Sebban, M., Benabderrahmane, M. B., Marekha, B., Denis, C., Paysant, H., Weiswald, L., Carlier, L., Bureau, R., Coadou, G., et al. (2019) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2019.1680434 · Cited by 6
Wu, X. F., Zhao, H., Lai, J., Zhang, N., Shi, J., Zhou, R., Su, Q., Zheng, E., Xu, Z., Huang, S., et al. (2021) · Animals · doi:10.3390/ani11113062 · Cited by 6
Metadata
- Authors
- Ashkenazi, A., Fairbrother, W. J., Leverson, J. D., & Souers, A. J.
- Affiliations
- Genentech (US)
- AbbVie (United States) (US)
- Corresponding author
- Ashkenazi, Avi
- Venue
- Nature Reviews Drug Discovery
- Published
- 2017-02-17
- Volume
- 16
- Issue
- 4
- Pages
- 273-284
- ISSN
- 1474-1776 (ISSN-L)
- 1474-1784
- OpenAlex
- W2589060305
- Cited by
- 903
- References
- 105
- Citations by year
- 2026: 49 · 2025: 87 · 2024: 99 · 2023: 90 · 2022: 94 · 2021: 120 · 2020: 116 · 2019: 93 · 2018: 100 · 2017: 51
- FWCI
- 9.25
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Drug Discovery (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Health Sciences › Medicine › Hematology › Chronic Lymphocytic Leukemia Research
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Keywords
- Bcl-2 family proteins, apoptosis, BH3 mimetics, BCL-2 inhibitor, venetoclax, navitoclax, Bcl-xL, Mcl-1, small molecule inhibitors, structure-based drug design, NMR-based screening, apoptosis evasion, chronic lymphocytic leukemia, 17p deletion, cancer therapy
- MeSH terms
- Antineoplastic Agents, Humans, Neoplasms, Molecular Structure, Apoptosis, Proto-Oncogene Proteins c-bcl-2, Protein Interaction Domains and Motifs, Molecular Targeted Therapy
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
