The DOI matches its Crossref record; 51 of the 51 references it cites were found in a registry or an index.
Exploiting selective BCL-2 family inhibitors to dissect cell survival dependencies and define improved strategies for cancer therapy
Abstract
Selective inhibition of BCL-X L synergizes with docetaxel to inhibit the growth of solid tumors but does not inhibit granulopoiesis.
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
“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 [25]
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 [25]
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 [25]
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 [25]
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 [25]
In the citing paper
“The inability of PZ to efficiently induce Bcl-2 degradation may provide additional advantages for using PROTAC technology to reduce ABT263 on-target toxicity because Bcl-2 inhibition with a high dose or an intensive treatment regimen of ABT263 can lead to neutropenia and lymphocytopenia25.”
From Using proteolysis-targeting chimera technology to reduce navitoclax platelet toxicity and improve its senolytic activity (2020) · cites this paper as [25]
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
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
Self-citationControl 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-citationClinical development success rates for investigational drugs
Hay, M., Thomas, D. W., Craighead, J. L., Economides, C., & Rosenthal, J. (2014) · Nature Biotechnology · doi:10.1038/nbt.2786 · Cited by 2,536
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
Self-citationNovack, D. V., Sorenson, C. M., Shutter, J. R., & Korsmeyer, S. J. (1993) · Cell · doi:10.1016/0092-8674(93)80065-m · Cited by 1,637
Chipuk, J. E., Moldoveanu, T., Llambi, F., Parsons, M. J., & Green, D. R. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.01.025 · Cited by 1,476
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
van Delft, M. F., Wei, A. H., Mason, K. D., Vandenberg, C. J., Chen, L., Czabotar, P. E., Willis, S. N., Scott, C. L., Day, C. L., Cory, S., et al. (2006) · Cancer Cell · doi:10.1016/j.ccr.2006.08.027 · Cited by 1,271
Flagged first, then by citations
Cited by
Sorted by citations
Items 201–300 of 548
Interorganellar calcium signaling in the regulation of cell metabolism: A cancer perspective
Rimessi, A., Pedriali, G., Vezzani, B., Tarocco, A., Marchi, S., Wieckowski, M. R., Giorgi, C., & Pinton, P. (2019) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2019.05.015 · Cited by 48
Seiller, C., Maïga, S., Touzeau, C., Bellanger, C., Kervoëlen, C., Descamps, G., Maillet, L., Moreau, P., Pellat‐Deceunynck, C., Gomez‐Bougie, P., et al. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-2505-1 · Cited by 45
Langerbeins, P., & Eichhorst, B. F. (2021) · Acta Haematologica · doi:10.1159/000514071 · Cited by 45
A recent development of new therapeutic agents and novel drug targets for cancer treatment
Kifle, Z. D., Tadele, M., Alemu, E., Gedamu, T., & Ayele, A. G. (2021) · SAGE Open Medicine · doi:10.1177/20503121211067083 · Cited by 44
FGFR1 inhibition in lung squamous cell carcinoma: questions and controversies
Weeden, C. E., Solomon, B., & Asselin-Labat, M.-L. (2015) · Cell Death Discovery · doi:10.1038/cddiscovery.2015.49 · Cited by 44
Overview of BCL-2 Family Proteins and Therapeutic Potentials
Huska, J. D., Lamb, H. M., & Hardwick, J. M. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-8861-7_1 · Cited by 44
Side-by-side comparison of BH3-mimetics identifies MCL-1 as a key therapeutic target in AML
Ewald, L., Dittmann, J., Vogler, M., & Fulda, S. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-2156-2 · Cited by 42
Targeting Cellular Senescence for Age-Related Diseases: Path to Clinical Translation
Wyles, S. P., Tchkonia, T., & Kirkland, J. L. (2021) · Plastic & Reconstructive Surgery · doi:10.1097/prs.0000000000009669 · Cited by 42
Arandjelovic, P., Kim, Y., Cooney, J. P., Preston, S., Doerflinger, M., McMahon, J. H., Garner, S. E., Zerbato, J. M., Roche, M., Tumpach, C., et al. (2023) · Cell Reports Medicine · doi:10.1016/j.xcrm.2023.101178 · Cited by 41
BH3 profiling and a toolkit of BH3-mimetic drugs predict anti-apoptotic dependence of cancer cells
Butterworth, M., Pettitt, A. R., Varadarajan, S., & Cohen, G. M. (2016) · British Journal of Cancer · doi:10.1038/bjc.2016.49 · Cited by 41
Kabir, S., Cidado, J. R., Andersen, C. L., Dick, C., Lin, P., Mitros, T., Ma, H., Baik, R., Belmonte, M. A., Drew, L., et al. (2019) · eLife · doi:10.7554/elife.44288 · Cited by 43
Co-Operativity between MYC and BCL-2 Pro-Survival Proteins in Cancer
Fairlie, W. D., & Lee, E. F. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22062841 · Cited by 45
Wakui, N., Yoshino, R., Yasuo, N., Ohue, M., & Sekijima, M. (2017) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2017.11.011 · Cited by 44
Venetoclax: A First-in-Class Oral BCL-2 Inhibitor for the Management of Lymphoid Malignancies
King, A. C., Peterson, T. J., Horvat, T. Z., Rodríguez, M., & Tang, L. A. (2017) · Annals of Pharmacotherapy · doi:10.1177/1060028016685803 · Cited by 41
Deng, L., Wan, H., Zhou, H., Yu, L., & He, Y. T. (2018) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2018.02.011 · Cited by 41
Infection with flaviviruses requires BCLXL for cell survival
Suzuki, T., Okamoto, T., Katoh, H., Sugiyama, Y., Kusakabe, S., Tokunaga, M., Hirano, J., Miyata, Y., Fukuhara, T., Ikawa, M., et al. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1007299 · Cited by 40
Venetoclax for the treatment of multiple myeloma
Vaxman, I., Sidiqi, M. H., & Gertz, M. A. (2018) · Expert Review of Hematology · doi:10.1080/17474086.2018.1548931 · Cited by 40
Tumor-targeted nanoparticles improve the therapeutic index of BCL2 and MCL1 dual inhibition
Tannan, N. B., Manzari, M. T., Herviou, L., Ferreira, M. D. S., Hagen, C. J., Kiguchi, H., Manova-Todorova, K. O., Seshan, V., de Stanchina, E., Heller, D. A., et al. (2020) · Blood · doi:10.1182/blood.2020008017 · Cited by 41
Scherr, A., Möck, A., Gdynia, G., Schmitt, N., Heilig, C. E., Korell, F., Rhadakrishnan, P., Hoffmeister‐Wittmann, P., Metzeler, K. H., Schulze‐Osthoff, K., et al. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-03092-7 · Cited by 41
Regulation of stressed-induced cell death by the Bcl-2 family of apoptotic proteins
Roufayel, R. (2016) · Molecular Membrane Biology · doi:10.1080/09687688.2017.1400600 · Cited by 41
Bierbrauer, A., Jacob, M., Vogler, M., & Fulda, S. (2020) · British Journal of Cancer · doi:10.1038/s41416-020-0795-9 · Cited by 41
A guide to senolytic intervention in neurodegenerative disease
Lee, S., Wang, E. Y., Steinberg, A. B., Walton, C. C., Chinta, S. J., & Andersen, J. K. (2021) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2021.111585 · Cited by 43
Rosa, N., Speelman-Rooms, F., Parys, J. B., & Bultynck, G. (2022) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2022.188791 · Cited by 43
Targeting Anti-Apoptotic BCL-2 Family Proteins for Cancer Treatment
Zhang, X., Liu, X., Zhou, D., & Zheng, G. (2020) · Future Medicinal Chemistry · doi:10.4155/fmc-2020-0004 · Cited by 40
Selective inhibitors of Bcl-2 and Bcl-xL: Balancing antitumor activity with on-target toxicity
Hennessy, E. J. (2016) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2016.03.032 · Cited by 40
Inhibition of Bcl-xL sensitizes cells to mitotic blockers, but not mitotic drivers
Bennett, A., Sloss, O., Topham, C. H., Nelson, L., Tighe, A., & Taylor, S. S. (2016) · Open Biology · doi:10.1098/rsob.160134 · Cited by 35
Human placental extract: a potential therapeutic in treating osteoarthritis
Gwam, C. U., Ohanele, C., Hamby, J., Chughtai, N., Mufti, Z., & Ma, X. (2021) · Annals of Translational Medicine · doi:10.21037/atm.2019.10.20 · Cited by 37
Self-citationThe Ewing Family of Tumors Relies on BCL-2 and BCL-XL to Escape PARP Inhibitor Toxicity
Heisey, D. A. R., Lochmann, T. L., Floros, K. V., Coon, C. M., Powell, K. M., Jacob, S., Calbert, M. L., Ghotra, M. S., Stein, G. T., Maves, Y. K., et al. (2018) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-18-0277 · Cited by 35
Self-citationTeh, C. E., Gong, J., Segal, D., Tan, T., Vandenberg, C. J., Fedele, P. L., Low, M. S. Y., Grigoriadis, G., Harrison, S. J., Strasser, A., et al. (2020) · Cell Death and Differentiation · doi:10.1038/s41418-020-0498-z · Cited by 38
Recent trends and advances in novel formulations as an armament in Bcl-2/Bax targeted breast cancer
Samia, S., Chary, P. S., Khan, O., & Mehra, N. K. (2024) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2024.123889 · Cited by 39
Neutralization of BCL-2/XL Enhances the Cytotoxicity of T-DM1 In Vivo
Zoeller, J. J., Vagodny, A., Taneja, K. L., Tan, B. Y., O’Brien, N. A., Slamon, D. J., Sampath, D., Leverson, J. D., Bronson, R. T., Dillon, D. A. R., et al. (2019) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-18-0743 · Cited by 37
Self-citationAlsuraih, M., O’Hara, S. P., Woodrum, J. E., Pirius, N., & LaRusso, N. F. (2021) · JHEP Reports · doi:10.1016/j.jhepr.2021.100250 · Cited by 38
Resistance to apoptosis and autophagy leads to enhanced survival in Sertoli cells
Aslani, F., Sebastian, T., Keidel, M., Fröhlich, S., Elsässer, H., Schuppe, H.-C., Klug, J., Mahavadi, P., Fijak, M., Bergmann, M., et al. (2017) · Molecular Human Reproduction · doi:10.1093/molehr/gax022 · Cited by 37
Bavachinin Ameliorates Rheumatoid Arthritis Inflammation via PPARG/PI3K/AKT Signaling Pathway
Deng, H., Jiang, J., Shu, J., Huang, M., Zhang, Q., Wu, L., & Sun, W. (2023) · Inflammation · doi:10.1007/s10753-023-01855-w · Cited by 36
Bcl-xL targeting eliminates ageing tumor-promoting neutrophils and inhibits lung tumor growth
Bodac, A., Mayet, A., Rana, S., Pascual, J., Bowler, A. D., Roh, V., Fournier, N., Craciun, L., Demetter, P., Radtke, F., et al. (2023) · EMBO Molecular Medicine · doi:10.1038/s44321-023-00013-x · Cited by 37
Targeting Bcl-2 Family Proteins: What, Where, When?
Senichkin, V. V., Pervushin, N. V., Zuev, A. P., Zhivotovsky, B., & Kopeina, G. S. (2020) · Biochemistry (Moscow) · doi:10.1134/s0006297920100090 · Cited by 37
Mukherjee, N., Lü, Y., Almeida, A. R., Lambert, K. A., Shiau, C., Su, J.-C., Luo, Y., Fujita, M., Robinson, W. A., Robinson, S. E., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.8695 · Cited by 37
Defining specificity and on-target activity of BH3-mimetics using engineered B-ALL cell lines
Koss, B. S., Ryan, J. A., Budhraja, A., Szarama, K. B., Yang, X., Bathina, M., Cardone, M. H., Nikolovska‐Coleska, Z., Letai, A. G., & Opferman, J. T. (2016) · Oncotarget · doi:10.18632/oncotarget.7204 · Cited by 36
Senotherapy: growing old and staying young?
Schmitt, R. (2017) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-017-1972-4 · Cited by 36
The chemical biology of apoptosis: Revisited after 17 years
Yang, S., Mao, Y., Zhang, H., Xu, Y., An, J., & Huang, Z. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.05.019 · Cited by 35
Self-citationArulananda, S., O’Brien, M., Evangelista, M., Jenkins, L. J., Poh, A. R., Walkiewicz, M., Leong, T. Y.-M., Mariadason, J. M., Cebon, J. S., Balachander, S. B., et al. (2021) · Cell Death Discovery · doi:10.1038/s41420-021-00505-0 · Cited by 35
Adaptive immunity and atherosclerosis: aging at its crossroads
Snijckers, R., & Foks, A. C. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1350471 · Cited by 40
A concise review of BCL-2 inhibition in acute myeloid leukemia
Yogarajah, M., & Stone, R. M. (2017) · Expert Review of Hematology · doi:10.1080/17474086.2018.1420474 · Cited by 34
Talukdar, A., Mukherjee, A., & Bhattacharya, D. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01208 · Cited by 33
Freise, K. J., Jones, A. K., Verdugo, M. E., Menon, R. M., Maciag, P., & Salem, A. H. (2017) · Clinical Pharmacology & Therapeutics · doi:10.1002/cpt.712 · Cited by 34
Wang, M., Chen, L., Xiong, Y., Xu, J., Wang, J., & Meng, Z. (2017) · International Journal of Nanomedicine · doi:10.2147/ijn.s127549 · Cited by 34
Dambach, D. M., Misner, D., Brock, M., Fullerton, A. M., Proctor, W. R., Maher, J. M., Lee, D. H., Ford, K. A., & Diaz, D. (2015) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.5b00396 · Cited by 35
Self-citationDRP-1 is required for BH3 mimetic-mediated mitochondrial fragmentation and apoptosis
Milani, M., Byrne, D. P., Greaves, G., Butterworth, M., Cohen, G. M., Eyers, P. A., & Varadarajan, S. (2017) · Cell Death and Disease · doi:10.1038/cddis.2016.485 · Cited by 33
Non-Hodgkin and Hodgkin Lymphomas Select for Overexpression of BCLW
Adams, C. M., Mitra, R., Gong, J. Z., & Eischen, C. M. (2017) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-17-1144 · Cited by 33
Guo, X.-F., Liu, J., Ma, S., Zhang, P., & Sun, W.-D. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.03.110 · Cited by 33
BCL-2 Inhibitors, Present and Future
Ryan, C. E., & Davids, M. S. (2019) · The Cancer Journal · doi:10.1097/ppo.0000000000000408 · Cited by 33
Waggoner, M. S., Katsetos, J., Emilee Thomas, M., Galinsky, I., & Fox, H. R. (2022) · Journal of the Advanced Practitioner in Oncology · doi:10.6004/jadpro.2022.13.4.4 · Cited by 35
Puglisi, M., Molife, L. R., Jonge, M. J. D., Khan, K. H., van Doorn, L., Forster, M. D., Blanco, M., Gutierrez, M. E., Franklin, C. A., Busman, T. A., et al. (2021) · Future Oncology · doi:10.2217/fon-2021-0140 · Cited by 33
Osterlund, E. J., Hirmiz, N., Pemberton, J. M., Nougarède, A., Liu, Q., Leber, B. F., Fang, Q., & Andrews, D. W. (2022) · Science Advances · doi:10.1126/sciadv.abm7375 · Cited by 32
Levesley, J., Steele, L. P., Brüning‐Richardson, A., Davison, A., Zhou, J., Ding, C., Lawler, S. E., & Short, S. C. (2017) · Neuro-Oncology · doi:10.1093/neuonc/nox134 · Cited by 30
Liu, J., Bhadra, M., Sinnakannu, J. R., Yue, W. L., Tan, C. W., Rigo, F., Ong, S. T., & Roca, X. (2017) · Oncotarget · doi:10.18632/oncotarget.20658 · Cited by 30
Coamplification of miR-4728 protects HER2 -amplified breast cancers from targeted therapy
Floros, K. V., Lochmann, T. L., Hu, B., Monterrubio, C., Hughes, M. T., Wells, J. D., Morales, C. B., Ghotra, M. S., Costa, C., Souers, A. J., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1717820115 · Cited by 30
Self-citationMilani, M., Beckett, A. J., Al-Zebeeby, A., Luo, X., Prior, I. A., Cohen, G. M., & Varadarajan, S. (2019) · Cell Death Discovery · doi:10.1038/s41420-019-0199-x · Cited by 32
Exploring the potential of BH3 mimetic therapy in squamous cell carcinoma of the head and neck
Carter, R. J., Milani, M., Butterworth, M., Alotibi, A., Harper, N. W., Yedida, G., Greaves, G., Al-Zebeeby, A., Jorgensen, A., Schache, A. G., et al. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-2150-8 · Cited by 31
ER+ Breast Cancer Strongly Depends on MCL-1 and BCL-xL Anti-Apoptotic Proteins
Alcon, C., Zañudo, J. G. T., Albert, R., Wagle, N., Scaltriti, M., Letai, A. G., Samitier, J., & Montero, J. (2021) · Cells · doi:10.3390/cells10071659 · Cited by 32
Development of venetoclax for therapy of lymphoid malignancies
Zhu, H., & Almasan, A. (2017) · Drug Design Development and Therapy · doi:10.2147/dddt.s109325 · Cited by 31
Protein isoform-centric therapeutics: expanding targets and increasing specificity
Kjer-Hansen, P., Phan, T. G., & Weatheritt, R. J. (2024) · Nature Reviews Drug Discovery · doi:10.1038/s41573-024-01025-z · Cited by 27
Sensitizing non-small cell lung cancer to BCL-xL-targeted apoptosis
Shen, Q., Li, J., Mai, J., Zhang, Z., Fisher, A., Wu, X., Li, Z., Ramirez, M., Chen, S., & Shen, H. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-1040-9 · Cited by 30
BH3 Mimetics in AML Therapy: Death and Beyond?
Cerella, C., Dicato, M. A., & Diederich, M. F. (2020) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2020.09.004 · Cited by 31
BH3 Mimetics in Hematologic Malignancies
Klener, P., Sovilj, D., Renesova, N., & Andera, L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221810157 · Cited by 31
Cucarull, B., Tutusaus, A., Subías, M., Stefanović, M., Hernáez-Alsina, T., Boix, L., Reig, M., de Frutos, P. G., Marı́, M., Colell, A., et al. (2020) · Cancers · doi:10.3390/cancers12020332 · Cited by 28
Alcon, C., Manzano-Muñoz, A., Prada, E., Mora, J., Soriano, A., Guillén, G., Gallego, S., Roma, J. M., Samitier, J., Villanueva, A., et al. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-02887-y · Cited by 29
Ionic liquid-mediated delivery of a BCL-2 inhibitor for topical treatment of skin melanoma
Huda, M. N., Deaguero, I. G., Borrego, E. A., Kumar, R., Islam, T., Afrin, H., Varela-Ramı́rez, A., Aguilera, R. J., Tanner, E. E. L., & Nurunnabi, M. (2022) · Journal of Controlled Release · doi:10.1016/j.jconrel.2022.07.035 · Cited by 28
Sela, Y., Li, J., Maheswaran, S., Norgard, R. J., Yuan, S., Hubbi, M. E., Doepner, M., Xu, J. P., Ho, E. S., Mesaros, C., et al. (2022) · Cancer Research · doi:10.1158/0008-5472.can-22-0431 · Cited by 27
Feng, Y., Hu, X., & Wang, X. (2024) · Biomarker Research · doi:10.1186/s40364-024-00638-1 · Cited by 30
Targeting CDKs in cancer therapy: advances in PROTACs and molecular glues
Marei, H. E. S., Bedair, K., Hasan, A., Al-Mansoori, L., Gaiba, A., Morrione, A., Cenciarelli, C., & Giordano, A. (2025) · npj Precision Oncology · doi:10.1038/s41698-025-00931-8 · Cited by 31
Faqar-Uz-Zaman, S. F., Heinicke, U., Meister, M. T., Vogler, M., & Fulda, S. (2017) · Cancer Letters · doi:10.1016/j.canlet.2017.09.025 · Cited by 27
Increased apoptotic sensitivity of glioblastoma enables therapeutic targeting by BH3-mimetics
Koessinger, A. L., Cloix, C., Koessinger, D., Heiland, D. H., Bock, F. J., Strathdee, K. E., Kinch, K., Martínez‐Escardó, L., Paul, N. R., Nixon, C., et al. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-01001-3 · Cited by 30
Li, H., Zheng, H., Li, L., Shen, X., Zang, W., & Sun, Y. (2016) · PLoS ONE · doi:10.1371/journal.pone.0160989 · Cited by 27
RetractedPanayotopoulou, E. G., Müller, A., Börries, M., Busch, H. S., Hu, G., & Lev, S. (2017) · Oncotarget · doi:10.18632/oncotarget.15125 · Cited by 27
Leto, S. M., Ferri, M., Sassi, F. P., Zanella, E. R., Cottino, F., Vurchio, V., Catalano, I., Ferrero, A., Zingaretti, C. C., Marchiò, C., et al. (2023) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-22-2550 · Cited by 28
Newell, S., van der Watt, P. J., & Leaner, V. D. (2023) · IUBMB Life · doi:10.1002/iub.2773 · Cited by 25
Judd, A. S., Bawa, B., Buck, W. R., Tao, Z., Li, Y., Mitten, M. J., Bruncko, M., Catron, N. D., Doherty, G. A., Durbin, K. R., et al. (2024) · Science Advances · doi:10.1126/sciadv.ado7120 · Cited by 28
Self-citationTargeting the BCL-2-regulated apoptotic pathway for the treatment of solid cancers
Fairlie, W. D., & Lee, E. F. (2021) · Biochemical Society Transactions · doi:10.1042/bst20210750 · Cited by 28
Chen, Y., Zou, J., Cheng, F., & Li, W. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.769730 · Cited by 29
MCL1 nuclear translocation induces chemoresistance in colorectal carcinoma
Fu, D., Pfannenstiel, L., Demelash, A., Phoon, Y. P., Mayell, C., Cabrera, C., Liu, C., Zhao, J., Dermawan, J. K. T. K., Patil, D. T., et al. (2022) · Cell Death and Disease · doi:10.1038/s41419-021-04334-y · Cited by 28
Self-citationLakhani, N. J., Rasco, D. W., Wang, H., Men, L., Liang, E., Fu, T., Collins, M. C., Min, P., Yin, Y., Davids, M. S., et al. (2023) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-23-1525 · Cited by 28
Lucas, C., Milani, M., Butterworth, M., Carmell, N., Scott, L. J., Clark, R. E., Cohen, G. M., & Varadarajan, S. (2016) · Leukemia · doi:10.1038/leu.2016.42 · Cited by 27
Uchida, A., Isobe, Y., Asano, J., Uemura, Y., Hoshikawa, M., Takagi, M., & Miura, I. (2018) · Haematologica · doi:10.3324/haematol.2018.204958 · Cited by 26
Potent efficacy of MCL-1 inhibitor-based therapies in preclinical models of mantle cell lymphoma
Dengler, M. A., Teh, C. E., Thijssen, R., Gangoda, L., Lan, P., Herold, M. J., Gray, D. H. D., Kelly, G. L., Roberts, A. W., & Adams, J. M. (2019) · Oncogene · doi:10.1038/s41388-019-1122-x · Cited by 25
Overcoming MCL-1-driven adaptive resistance to targeted therapies
Wood, K. C. (2020) · Nature Communications · doi:10.1038/s41467-020-14392-z · Cited by 25
BCL2 Family Inhibitors in the Biology and Treatment of Multiple Myeloma
Gupta, V. A., Ackley, J. C., Kaufman, J. L., & Boise, L. (2021) · Blood and Lymphatic Cancer Targets and Therapy · doi:10.2147/blctt.s245191 · Cited by 27
Jackson, M. R., Ashton, M., Koessinger, A. L., Dick, C., Verheij, M., & Chalmers, A. J. (2019) · International Journal of Radiation Oncology*Biology*Physics · doi:10.1016/j.ijrobp.2019.11.029 · Cited by 24
PROTACs are effective in addressing the platelet toxicity associated with BCL-XL inhibitors
Zhang, P., Zhang, X., Liu, X., Khan, S. U., Zhou, D., & Zheng, G. (2020) · Exploration of Targeted Anti-tumor Therapy · doi:10.37349/etat.2020.00017 · Cited by 27
Antileukemic efficacy of a potent artemisinin combined with sorafenib and venetoclax
Moses, B. S., McCullough, S., Fox, J. M., Mott, B. T., Bentzen, S. M., Kim, M.-J., Tyner, J. W., Lapidus, R. G., Emadi, A., Rudek, M. A., et al. (2021) · Blood Advances · doi:10.1182/bloodadvances.2020003429 · Cited by 24
Tahir, S. K., Calvo, E., Carneiro, B. A., Yuda, J., Shreenivas, A. V., Jongen‐Lavrencic, M., Gort, E. H., Ishizawa, K., Morillo, D., Biesdorf, C., et al. (2023) · Blood · doi:10.1182/blood.2022017333 · Cited by 26
Self-citationHLA susceptibility genes in rheumatoid factor positive juvenile rheumatoid arthritis.
Vehe, R. K., Begovich, A. B., & Nepom, B. S. (1990) · PubMed · Cited by 24
Al-Zebeeby, A., Vogler, M., Milani, M., Richards, C., Alotibi, A., Greaves, G., Dyer, M. J. S., Cohen, G. M., & Varadarajan, S. (2018) · Haematologica · doi:10.3324/haematol.2018.204701 · Cited by 22
Cucarull, B., Tutusaus, A., Hernáez-Alsina, T., de Frutos, P. G., Reig, M., Colell, A., Marı́, M., & Morales, A. (2021) · Antioxidants · doi:10.3390/antiox10091336 · Cited by 23
Synergistic activity of combined inhibition of anti-apoptotic molecules in B-cell precursor ALL
Seyfried, F., Stirnweiß, F. U., Niedermayer, A., Enzenmüller, S., Hörl, R. L., Münch, V., Köhrer, S., Debatin, K., & Meyer, L. H. (2022) · Leukemia · doi:10.1038/s41375-021-01502-z · Cited by 24
Särchen, V., Shanmugalingam, S., Kehr, S., Reindl, L. M., Grèze, V., Wiedemann, S., Boedicker, C., Jacob, M., Bankov, K., Becker, N., et al. (2022) · Cell Death Discovery · doi:10.1038/s41420-021-00812-6 · Cited by 25
Mancuso, S., Mattana, M., Carlisi, M., Santoro, M., & Siragusa, S. M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23063368 · Cited by 27
Zhang, S., Chen, Y., Xu, Z., Yang, J., Sun, R., Wang, J., Sun, Y., Jiang, B., Yang, X., & Tan, W. (2022) · Theranostics · doi:10.7150/thno.75421 · Cited by 23
Involvement of Bcl-2 Family Proteins in Tetraploidization-Related Senescence
Barriuso, D., Alvarez-Frutos, L., Gutiérrez, L. G., Motiño, O., Kroemer, G., Palacios, R., & Senovilla, L. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24076374 · Cited by 23
Britt, E., Raman, S., Leek, K., Sheehy, C. H., Kim, S. W., & Harada, H. (2019) · PLoS ONE · doi:10.1371/journal.pone.0219398 · Cited by 22
Metadata
- Authors
- Leverson, J. D., Phillips, D. C., Mitten, M. J., Boghaert, E. R., Diaz, D., Tahir, S. K., Belmont, L. D., Nimmer, P., Xiao, Y., Ma, X. M., Lowes, K. N., Kovar, P., Chen, J., Jin, S., Smith, M., Xue, J., Zhang, H., Oleksijew, A., Magoc, T. J., Vaidya, K. S., Albert, D. H., Tarrant, J. M., La, N., Wang, L., Tao, Z.-F., Wendt, M. D., Sampath, D., Rosenberg, S. H., Tse, C., S. Huang, D. C., Fairbrother, W. J., Elmore, S. W., & Souers, A. J.
- Affiliations
- AbbVie (United States) (US)
- Genentech (US)
- AbbVie Inc., North Chicago, IL 60064, USA.
- The University of Melbourne (AU)
- Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria 3052, Australia.
- Corresponding author
- Leverson, Joel D.
- Ma, Xiaoju Max
- ORCID
- Venue
- Science Translational Medicine
- Published
- 2015-03-18
- Volume
- 7
- Issue
- 279
- Pages
- 279ra40-279ra40
- ISSN
- 1946-6234 (ISSN-L)
- 1946-6242
- OpenAlex
- W2110525250
- Cited by
- 541
- References
- 51
- Citations by year
- 2026: 22 · 2025: 33 · 2024: 34 · 2023: 38 · 2022: 58 · 2021: 56 · 2020: 69 · 2019: 49 · 2018: 58 · 2017: 65 · 2016: 43 · 2015: 12
- FWCI
- 25.92
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science Translational Medicine (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Leukemia and Lymphoma Society
- Medical Research Council (461219, 461221, 1016701)
- Australian Cancer Research Foundation
- Cancer Council Victoria
- Australian National Health
- Independent Research Institutes Infrastructure Support Scheme (361646)
- Victorian State Government Operational Infrastructure Support
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Health Sciences › Medicine › Hematology › Chronic Lymphocytic Leukemia Research
- Keywords
- BCL-2 inhibitor, venetoclax, navitoclax, BCL-XL inhibition, A-1331852, docetaxel combination, neutropenia, thrombocytopenia, granulopoiesis, solid tumors, chronic lymphocytic leukemia
- MeSH terms
- Docetaxel, Administration, Oral, Aniline Compounds, Animals, Antineoplastic Agents, Cell Survival, Granulocytes, Humans, Isoquinolines, Kinetics, Neoplasm Transplantation, Neoplasms, Neutropenia, Neutrophils, Sulfonamides, Thrombocytopenia, Gene Expression Regulation, Neoplastic, Bridged Bicyclo Compounds, Heterocyclic, Proto-Oncogene Proteins c-bcl-2, Gene Expression Profiling, Taxoids, Cell Line, Tumor, bcl-X Protein, Mice, Benzothiazoles
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