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 801–900 of 918
Apoptosis, necroptosis, and pyroptosis in health and disease
Liao, D. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-814208-0.00008-7
Jiang, J., Sun, B., Zhu, X., Zhang, Y., Xiong, J., Zhang, M., Qian, Y., Liu, R., & Yang, W. (2020) · doi:10.21203/rs.3.rs-67782/v1
刘晓岗 (2010) · 视听界
Preparation and Evaluation of Supramolecular Hydrogels for Localized Sustained Gene Delivery
Ke, L., Wu, Y., & Tian, H. (2021) · Biomaterial engineering · doi:10.1007/978-981-33-6198-0_13-1
Effect of VirD4 on gastric epithelial-1 cells and its mechanism
Yang, Y., You, B., & Zhou, C. (2022) · Biocell · doi:10.32604/biocell.2022.018326
Davidson, B. (2018) · Springer eBooks · doi:10.1007/978-3-319-76478-8_9
Rahman, S. F. A., & Mohana‐Kumaran, N. (2020) · Malaysian Applied Biology · doi:10.55230/mabjournal.v49i1.1674
Park, E., Lee, C., Park, J., Liu, J., Hong, J., Shin, D., Byun, J. M., Yun, H., Koh, Y., & Yoon, S. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.03.28.486020
Che, Y. (2020) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.737014723.793569231
Jafari, M., Motamedi, P., & Khaledi, N. (2021) · مجله علمی پزشکی جندی شاپور · doi:10.32598/jsmj.20.4.2475
Fu, Y., Zhu, F., Ma, Z., Lv, B., Wang, X., Dai, C., Ma, X., Liu, P., Lv, H., Chen, X., et al. (2020) · doi:10.21203/rs.3.rs-35356/v1
Research Progress of Venetoclax for the Treatment of Multiple Myeloma
夏, 静. (2022) · Advances in Clinical Medicine · doi:10.12677/acm.2022.127911
Chun, C., & Yoon, T. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.21203/rs.3.rs-1849067/v1
Research on the role of microRNA in neuron apoptosis
Wang, Y., Yuan, X., & Shi, L. (2022) · AIP conference proceedings · doi:10.1063/5.0094317
Gahl, R. F. (2022) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.2c04581
Yee, A. J., Hideshima, T., Raje, N. S., & Anderson, K. C. (2022) · Wiley eBooks · doi:10.1002/9781119000822.hfcm122.pub2
Bcl-2, JAK and mTOR Inhibitors
Mueller, N. J., & Burkhard, S. (2022) · Springer eBooks · doi:10.1007/978-3-031-11363-5_16
Targeted Therapies: A Molecular Overview
Özveren, B., & Narter, F. (2023) · Bulletin of Urooncology · doi:10.4274/uob.galenos.2022.2022.4.1
Zhang, J., & Tian, Y. (2023) · Reproduction Fertility and Development · doi:10.1071/rd23050
Xue, H. Y., Li, S., Yan-jun, T., Cao, J., Hou, W.-S., Wang, A., Ren, W.-X., & Jin, C. (2024) · Research Square · doi:10.21203/rs.3.rs-3796020/v1
Yang, B., & Yang, Z. (2024) · Mathematical Biosciences & Engineering · doi:10.3934/mbe.2024142
Bartošová, O., Bielčiková, Z., Štursa, J., Pešta, M., Neužil, J., Bursová, M., Slanař, O., Netikova, I. S., & Werner, L. (2024) · Research Square · doi:10.21203/rs.3.rs-4669827/v1
Luteolin ve Apigenin Fitokimyasallarının Meme Kanseri Üzerine Etkileri
Yeler, G. U., & Göktaş, Z. (2024) · Journal of Nutrition and Dietetics · doi:10.33076/2024.bdd.1877
Zhu, Y., Xiao, M., Zhao, R., Yang, X., Wu, K., Liu, X., Chen, X. X., Guo, L., Liu, J., Chen, X., et al. (2024) · Human & Experimental Toxicology · doi:10.1177/09603271241279166
RetractedEffect of sea cucumber glycosides on ovarian cancer cell line SKOV3: an in vitro and in silico study
Ding, C. (2024) · International Journal of Clinical and Experimental Medicine · doi:10.62347/cjjd5502
Liu, T., Zhang, E., Cui, S., Dai, H., Yang, X., & Lin, C. (2024) · Lasers in Medical Science · doi:10.1007/s10103-024-04176-y
Ashfira, Ilyas, S., & Tanjung, M. (2024) · Jurnal Penelitian Pendidikan IPA · doi:10.29303/jppipa.v10i9.8371
Structure-based Design, Synthesis, And Evaluation of a New Bcl-2/Mcl-1 Inhibitor
Zhang, X. (2025) · Highlights in Science Engineering and Technology · doi:10.54097/fywa0t44
Mangrove Microbiome as a Source of Antiviral Drugs
Sonavale, R. M., & Pathade, G. R. (2025) · Springer eBooks · doi:10.1007/978-981-96-2602-1_21
Harnessing proteomics for precision medicine in lung cancer
Berkovska, O. (2025) · doi:10.69622/28563788
Jia, W.-H., Huang, C.-L., Zhang, W.-L., He, Y.-Q., Xue, W.-Q., Liao, Y., Yang, M., Yang, M., Pei, L., Jia, W., et al. (2025) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-025-06224-8
Sim, D. Y., Hwang, J. W., Park, S. Y., Shim, B. S., Kim, S. H., & Koo, J. S. (2025) · Journal of Agriculture & Life Science · doi:10.14397/jals.2025.59.2.59
Rahimi, A., Karimipoor, M., Mahdian, R., Alipour, A., Hosseini, S., Mohammadi, M., Kaghazian, H., Shahsavarani, H., & Shokrgozar, M. A. (2025) · Iranian Biomedical Journal · doi:10.61882/ibj.4934
Benedi, A., Beltrán‐Visiedo, M., Jiménez‐Alduán, N., del Valle, A. S., Anel, A., Naval, J., & Marzo, I. (2025) · Cancers · doi:10.3390/cancers17142290 · Cited by 2
Zhang, Y., Liu, M., Wang, X., Li, N., Chang, X., Xu, J., Tian, F., Wen, X., Liu, C., & Li, Y. (2025) · Journal of Inflammation Research · doi:10.2147/jir.s520179
The current report on drug development focuses on “The new dimension” of cancer hallmarks
Ucche, S., Larasati, Y. A., Maharani, D., Widyardhita, M. H., Widayanti, W. R., & Hermawan, A. (2025) · Gene · doi:10.1016/j.gene.2025.149750
Fang, H. J., Li, Q., Chen, L., & Ding, G. (2025) · Journal of Fungi · doi:10.3390/jof11100712
BCL ‐2 inhibition in Waldenström macroglobulinaemia and marginal zone lymphoma
Sarosiek, S., Suárez, U. B., Fernández, M. J., Sarosiek, K. A., & Castillo, J. J. (2025) · British Journal of Haematology · doi:10.1111/bjh.70208
Guo, Y., Zhang, T., Tang, X., Mao, B., Zhang, Q., Zhao, J., & Cui, S. (2025) · Probiotics and Antimicrobial Proteins · doi:10.1007/s12602-025-10830-w
miR-107 targets WNT3A and BTRC to promote bovine endometrial epithelial cells receptivity
Wang, Y., Bao, B., Wang, X., & Luoreng, Z. (2025) · Genomics · doi:10.1016/j.ygeno.2025.111177
Yu, W., Zhang, X., Zhang, W., Xiong, M., Lin, Y., Chang, M., Xu, L., Lu, Y., Liu, Y., & Zhang, J. (2021) · Figshare · doi:10.6084/m9.figshare.16869842
Li, C., Deng, C., Pan, G., Wang, X., Zhang, K., Dong, Z., Zhao, G., Tan, M., Hu, X., Shi, S., et al. (2020) · Figshare · doi:10.6084/m9.figshare.13173162
Li, C., Deng, C., Pan, G., Wang, X., Zhang, K., Dong, Z., Zhao, G., Tan, M., Hu, X., Shi, S., et al. (2020) · Figshare · doi:10.6084/m9.figshare.13173153
Li, C., Deng, C., Pan, G., Wang, X., Zhang, K., Dong, Z., Zhao, G., Tan, M., Hu, X., Shi, S., et al. (2020) · Figshare · doi:10.6084/m9.figshare.13173150
Li, C., Deng, C., Pan, G., Wang, X., Zhang, K., Dong, Z., Zhao, G., Tan, M., Hu, X., Shi, S., et al. (2020) · Figshare · doi:10.6084/m9.figshare.13173159
Wang, W., Mai, H., Xu, H., Jing, B., Yu, C., Li, X., Chen, D., Huang, Y., Shao, M., & Pan, T. (2023) · Figshare · doi:10.6084/m9.figshare.24792294
Zhang, D., Yang, Z.-C., Chen, J.-Q., Jin, X.-X., Qiu, Y.-D., Chen, X.-J., Shi, H.-Y., Liu, Z.-G., Wang, M.-S., Liang, G., et al. (2021) · Figshare · doi:10.6084/m9.figshare.14920905
Zhang, D., Yang, Z.-C., Chen, J.-Q., Jin, X.-X., Qiu, Y.-D., Chen, X.-J., Shi, H.-Y., Liu, Z.-G., Wang, M.-S., Liang, G., et al. (2021) · Figshare · doi:10.6084/m9.figshare.14920902
Li, C., Deng, C., Pan, G., Wang, X., Zhang, K., Dong, Z., Zhao, G., Tan, M., Hu, X., Shi, S., et al. (2020) · Figshare · doi:10.6084/m9.figshare.13173156
Human Longevity: Bringing Radical Disruptive Ideas into Light
Tiwary, V., Kovvali, B., Umair, M. B., & Peleg, S. (2025) · Springer eBooks · doi:10.1007/978-3-031-93623-4_7
Capicua regulates the survival of Cajal-Retzius cells in the postnatal hippocampus
Patel, Z. H., van Bruggen, R., Wang, M., & Tan, Q. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-08206-7
Yi, S., Lin, S., Xie, J., Yang, Z., You, J., Zhong, X., Yang, H., Lin, H., Wang, Q., Gong, Y., et al. (2025) · Toxics · doi:10.3390/toxics14010050
Yuan, K., Bai, Y., Chen, S., Shi, Y., Yu, M., Zhang, K., Zhu, L. J., & Li, S. (2026) · Medicine · doi:10.1097/md.0000000000046783
Chen, X., Li, R., Ruan, Z., & Chen, Q. (2025) · Letters in Drug Design & Discovery · doi:10.1016/j.lddd.2025.100244
Jiang, M., Sun, C., Wang, B. T., Huang, Q., Hu, Q., & Che, X. (2026) · Medicine · doi:10.1097/md.0000000000047378
Sirtuin1 modulates P53/Nrf2 pathway to promote spinal cord injury repair
Huang, X., Shi, S., Zhang, Z., Zhao, Z., Gao, J., Zhang, M., Qin, L., & Yu, X. (2026) · Neurological Sciences · doi:10.1007/s10072-025-08604-x
MiR-1202 increases radioresistance in nasopharyngeal carcinoma by targeting NAIF1/MAPK/ERK pathway
Chen, X., Du, Y., Chen, W., Yang, X., Fang, J., & Qu, S. (2026) · iScience · doi:10.1016/j.isci.2026.115135
Régulation de la stabilité de la protéine anti-apoptotique BCL2A1
Lionnard, L. (2018) · theses.fr (ABES) · doi:10.70675/1eec02ffz98dez4a56z98e2z389a2cd8558d
Les méthyltransférases de la coiffe du MERS-CoV : étude fonctionnelle et recherches d'inhibiteurs
Aouadi, W. (2017) · theses.fr (ABES) · doi:10.70675/8e1435e3zc63az4f17z8e10zc76c0a7a533b
Dissecting the impact of cellular senescence on muscle regeneration
Cazin, C. (2020) · theses.fr (ABES) · doi:10.70675/42a7ff38zb338z4eb8za925z2ce0a01ee74e
Analyse du rôle des protéines FAK et CD47 dans l'invasion tumorale du mélanome
Mousson, A. (2020) · theses.fr (ABES) · doi:10.70675/fe000e00ze698z4536za6b1z7b9986716e1f
Etude de la structure et la dynamique de Mcl-1 : application en cancérologie
Benabderrahmane, M. B. (2020) · theses.fr (ABES) · doi:10.70675/bfeb5608zf944z4b23zbb2bzd3f959a16cd3
Thomine, C. (2023) · theses.fr (ABES) · doi:10.70675/d1e538f7z6e75z441az8e0fza6253fc7ebf8
Eyitayo, A. R. (2023) · theses.fr (ABES) · doi:10.70675/5ffd7262za032z4230zbbaaz9d8a596af7fc
The Role of Regnase-1 in Autoimmune Diseases – A Future Therapeutic Target for Clinical Use
Wang, M., Huang, Z., Gong, X., Rui, K., Tian, J., & Liu, M. (2026) · Clinical Reviews in Allergy & Immunology · doi:10.1007/s12016-026-09156-4
Wang, Y., Fan, F., Yang, X., Li, Y., Li, L., Lei, Q., Xiang, L., Zhang, X., Cao, Y., & Li, X. (2026) · Chinese Journal of Natural Medicines · doi:10.1016/s1875-5364(26)61084-9
Alsharksi, A. N., Salim, A. A., Mustapha, A., Abudabbous, A. A., & Mustapha3, A. M. (2026) · Scientific Journal of Faculty of Education Misurata University · doi:10.36602/sjfe.2026.v13.i01.03
ANRIL in Cardiovascular Diseases: Expression, Mechanism and Therapeutic Implications
Yang, H., Li, Y., 蔡秋霜, Hua, H., Liu, X., Liu, Y. C., Qin, W., & Mao, R. (2026) · Cardiovascular Drugs and Therapy · doi:10.1007/s10557-026-07884-5
Ning, D.-Y., Luo, R.-Y., Cen, L.-F., Wang, F., Liu, Y.-H., Liu, Y., Huang, Y.-N., Liang, H., & Chen, Z. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c03796
Inhibitory effects of mycosubtilin on proliferation of colon cancer SW480 cells
Yang, J., Wu, Q., Zhou, Q., Yin, L., Zhao, H., & Li, J. (2026) · PLoS ONE · doi:10.1371/journal.pone.0348056
Yi, S., Li, J., Zhang, X., & Zhao, S. (2026) · Scientific Reports · doi:10.1038/s41598-026-55771-8
Nuzhath, S., Vasanthi, C., S., S. K., Matta, S., Keerthana, M., Charitha, A., Saimanjunath, C., & Vilangalil, A. (2026) · International Journal of Drug Delivery Technology · doi:10.25258/ijddt.16.54s.117
Structure-driven steric occlusion of BCL-2 by an RNA origami Traptamer
Elsisi, M., & Labib, M. M. (2026) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2026.2688522
Li, B., Yang, J., Cai, M., Yee, S. K., Carlson, D. M., Smoot, R. L., Baker, D. J., & Ilyas, S. I. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.24.734341
Mechanism and Clinical Translation of BCL-2–Targeted Antitumor Therapy
Xie, R. (2026) · International Journal of Biology and Life Sciences · doi:10.54097/5q155127
Nasiri, M. A., Ahmadi, I., & Fekrat, N. (2026) · Journal of Natural Science Review · doi:10.62810/jnsr.v4i2.523
Holasová, J., Vranovský, A., Demitrovičová, Ĺ., Chudej, J., Flochová, E., Váleková, Ľ., Stecova, N., Hlebasková, M., Uzikova, K., Sajgalikova, H., et al. (2026) · Lymphatics · doi:10.3390/lymphatics4030035
Canty, J., Marsters, S. A., Lawrence, D., Lee, S., Koeppen, H., & Ashkenazi, A. (2026) · Cell Death and Differentiation · doi:10.1038/s41418-026-01798-3
Self-citationZhao, Z., Cai, Y., Li, C. J., Du, C., & Zhang, S. (2026) · International Journal of Gynecology & Obstetrics · doi:10.1002/ijgo.71206
Pioger, A., Martin, N., Abbadie, C., & Dehennaut, V. (2026) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2026.189665
Niu, S.-X., Fan, L.-S., Cheng, J.-Y., Xu, L., Yang, L., Sheng-Nan, X., Sun, R.-R., Qin, S., Xiao, B., Fan, H.-J., et al. (2026) · Chinese Journal of Integrative Medicine · doi:10.1007/s11655-026-4160-6
Cell Death, Survival, and Recycling Mechanisms; Apoptosis, Necrosis, and Autophagy
Minden, A. (2026) · Springer eBooks · doi:10.1007/978-3-032-20529-2_22
Wu, L., Budak, B., Ofogo, O., Jouneghani, A. J., JeanRichard, P., Bachmann, D., & Kaufmann, T. (2026) · Cell Death and Differentiation · doi:10.1038/s41418-026-01829-z
Lassoued, A., Mkacher, H., Messaoudi, S., Arnoux, P., Roisnel, T., Turowska‐Tyrk, I., Acherar, S., & Nasri, H. (2026) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2026.147259
Hussin, N. M. H., Mediani, A., Latip, N. A., Fenech, M. F., Widyanto, R. M., & Sharif, R. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27167181
Development of a high-throughput assay format to identify inhibitors of HAX1–CLPB interaction
Fan, Y., Dahiya, V., Chatterjee, D., Fleck, M., Aretz, J., Nagel, F., Maskos, K., Makino, D. L., Noeske, J., Pangratz-Fuehrer, S., et al. (2026) · Results in Chemistry · doi:10.1016/j.rechem.2026.103765
Nagalakshmamma, V., Mallepogu, V., Pothuraju, S., Pasala, C., Poreddy, S., Amineni, U. M., Reddy, C. S., & Meriga, B. (2026) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.71025
Mudda, R. R., Gundla, R., Basava, V., Shaik, B. B., Velavalapalli, V. M., Chennuru, R., Gurská, S., Das, V., & Katari, N. K. (2026) · ChemistrySelect · doi:10.1002/slct.74187
Kim, H., Jang, A., Hong, S., Ryu, S. E., & Park, H. (2026) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2026.109642
Encapsulation of navitoclax in non-folate and in folate targeted comb-shaped polymer nanoparticles
Alrosan, K., Alsuraifi, A., Hoskins, C., & Richardson, A. (2026) · Next research. · doi:10.1016/j.nexres.2026.102365
Ge, F., Yang, H., Wang, X.-Z., Liu, Z., Shao, D., & Liu, H.-X. (2026) · Frontiers in Oncology · doi:10.3389/fonc.2026.1926287
Ozli, G., Sakagami, H., Polat, M. F., Kazaz, C., Kurosaki, K., Uesawa, Y., Inden, K., & Gul, H. I. (2026) · Medicinal Chemistry Research · doi:10.1007/s00044-026-03624-4
Wei, H., Wang, J., Jiang, J., & Dai, S. (2026) · Medicinal Research Reviews · doi:10.1002/med.70108
Sonntag, J., Preugschas, R.-L., Jazmati, D., Qin, N., Neuwahl, J., Matuschek, C., Remke, M., Budach, W., Hörner‐Rieber, J., & Sohn, D. (2026) · Cell Death Discovery · doi:10.1038/s41420-026-03404-4
Snake venom in oncology: Breakthroughs in anticancer therapies
Addoum, B., Sakoui, S., Merrouni, I. A., Derdak, R., Ainane, T., Benbacer, L., & Dalli, M. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-44394-7.00016-0
Li, Y., 屠厚泽, 刘子菡, Wu, T., & Lu, B. (2026) · Food Bioscience · doi:10.1016/j.fbio.2026.110351
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
