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.
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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
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Targeting apoptosis in cancer therapy
Carneiro, B. A., & El‐Deiry, W. S. (2020) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-020-0341-y · Cited by 2,676
Regulation of apoptosis in health and disease: the balancing act of BCL-2 family proteins
Singh, R., Letai, A., & Sarosiek, K. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0089-8 · Cited by 2,111
Targeting BCL2 with Venetoclax in Relapsed Chronic Lymphocytic Leukemia
Roberts, A. W., Davids, M. S., Pagel, J. M., Kahl, B. S., Puvvada, S. D., Gerecitano, J. F., Kipps, T. J., Anderson, M. A., Brown, J. R., Gressick, L. A., et al. (2015) · New England Journal of Medicine · doi:10.1056/nejmoa1513257 · Cited by 1,930
Konopleva, M. Y., Pollyea, D. A., Potluri, J., Chyla, B., Hogdal, L. J., Busman, T. A., McKeegan, E. M., Salem, A. H., Zhu, M., Ricker, J. L., et al. (2016) · Cancer Discovery · doi:10.1158/2159-8290.cd-16-0313 · Cited by 1,101
Self-citationCellular senescence: a translational perspective
Kirkland, J. L., & Tchkonia, T. (2017) · EBioMedicine · doi:10.1016/j.ebiom.2017.04.013 · Cited by 1,013
Targeted protein degradation: mechanisms, strategies and application
Zhao, L., Zhao, J., Zhong, K., Tong, A., & Jia, D. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-00966-4 · Cited by 1,035
Venetoclax-Rituximab in Relapsed or Refractory Chronic Lymphocytic Leukemia
Seymour, J. F., Kipps, T. J., Eichhorst, B., Hillmen, P., D’Rozario, J., Assouline, S., Owen, C., Gerecitano, J., Robak, T., De la Serna, J., et al. (2018) · New England Journal of Medicine · doi:10.1056/nejmoa1713976 · Cited by 940
From basic apoptosis discoveries to advanced selective BCL-2 family inhibitors
Ashkenazi, A., Fairbrother, W. J., Leverson, J. D., & Souers, A. J. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.253 · Cited by 903
Self-citationThe promise and peril of chemical probes
Arrowsmith, C. H., Audia, J. E., Austin, C., Baell, J., Bennett, J., Blagg, J., Bountra, C., Brennan, P. E., Brown, P. J., Bunnage, M. E., et al. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1867 · Cited by 839
Self-citationStilgenbauer, S., Eichhorst, B. F., Schetelig, J., Coutre, S. E., Seymour, J. F., Munir, T., Puvvada, S. D., Wendtner, C., Roberts, A. W., Jurczak, W. J., et al. (2016) · The Lancet Oncology · doi:10.1016/s1470-2045(16)30019-5 · Cited by 809
Zhu, Y., Doornebal, E. J., Pirtskhalava, T., Giorgadze, N., Wentworth, M., Fuhrmann-Stroissnigg, H., Niedernhofer, L. J., Robbins, P. D., Tchkonia, T., & Kirkland, J. L. (2017) · Aging · doi:10.18632/aging.101202 · Cited by 757
Davids, M. S., Roberts, A. W., Seymour, J. F., Pagel, J. M., Kahl, B. S., Wierda, W. G., Puvvada, S. D., Kipps, T. J., Anderson, M. A., Salem, A. H., et al. (2017) · Journal of Clinical Oncology · doi:10.1200/jco.2016.70.4320 · Cited by 746
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Warren, C., Wong‐Brown, M. W., & Bowden, N. A. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1407-6 · Cited by 717
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Khan, S., Zhang, X., Lv, D., Zhang, Q., He, Y., Zhang, P., Liu, X., Thummuri, D., Yuan, Y., Wiegand, J. S., et al. (2019) · Nature Medicine · doi:10.1038/s41591-019-0668-z · Cited by 688
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Dale, B., Cheng, M., Park, K., Kanıskan, H. Ü., Xiong, Y., & Jin, J. J. (2021) · Nature reviews. Cancer · doi:10.1038/s41568-021-00365-x · Cited by 697
Targeting cellular senescence with senotherapeutics: senolytics and senomorphics
Zhang, L. J., Pitcher, L. E., Prahalad, V., Niedernhofer, L. J., & Robbins, P. D. (2022) · FEBS Journal · doi:10.1111/febs.16350 · Cited by 674
The BCL-2 arbiters of apoptosis and their growing role as cancer targets
Adams, J. M., & Cory, S. (2018) · Cell Death & Differentiation · doi:10.1038/cdd.2017.161 · Cited by 530
Targeting BCL-2 regulated apoptosis in cancer
Campbell, K. J., & Tait, S. W. G. (2018) · Open Biology · doi:10.1098/rsob.180002 · Cited by 564
BCL-2 protein family: attractive targets for cancer therapy
Kaloni, D., Diepstraten, S. T., Strasser, A., & Kelly, G. L. (2022) · APOPTOSIS · doi:10.1007/s10495-022-01780-7 · Cited by 547
Blombery, P., Anderson, M. A., Gong, J.-N., Thijssen, R., Birkinshaw, R. W., Thompson, E. R., Teh, C. E., Nguyen, T., Xu, Z., Flensburg, C., et al. (2019) · Cancer Discovery · doi:10.1158/2159-8290.cd-18-1119 · Cited by 434
Beyond the Rule of 5: Lessons Learned from AbbVie’s Drugs and Compound Collection
DeGoey, D. A., Chen, H.-J., Cox, P. B., & Wendt, M. D. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00717 · Cited by 390
Self-citationRamsey, H. E., Fischer, M. A., Lee, T., Gorska, A. E., Arrate, M. P., Fuller, L., Boyd, K. L., Strickland, S. A., Sensintaffar, J., Hogdal, L. J., et al. (2018) · Cancer Discovery · doi:10.1158/2159-8290.cd-18-0140 · Cited by 385
The manipulation of apoptosis for cancer therapy using BH3-mimetic drugs
Diepstraten, S. T., Anderson, M. A., Czabotar, P. E., Lessène, G., Strasser, A., & Kelly, G. L. (2021) · Nature reviews. Cancer · doi:10.1038/s41568-021-00407-4 · Cited by 351
Massively parallel assessment of human variants with base editor screens
Hanna, R. E., Hegde, M., Fagre, C. R., DeWeirdt, P. C., Sangree, A. K., Szegletes, Z., Griffith, A., Feeley, M. N., Sanson, K. R., Baidi, Y., et al. (2021) · Cell · doi:10.1016/j.cell.2021.01.012 · Cited by 316
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Najm, F. J., Strand, C., Donovan, K. F., Hegde, M., Sanson, K. R., Vaimberg, E. W., Sullender, M. E., Hartenian, E., Kalani, Z., Fusi, N., et al. (2018) · Nature Biotechnology · doi:10.1038/nbt.4048 · Cited by 279
Punnoose, E. A., Leverson, J. D., Peale, F. V., Jr., Boghaert, E. R., Belmont, L. D., Tan, N., Young, A., Mitten, M. J., Ingalla, E., Darbonne, W. C., et al. (2016) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-15-0730 · Cited by 307
Self-citationMolecular biomarkers in acute myeloid leukemia
Prada‐Arismendy, J., Arroyave-Ospina, J. C., & Röthlisberger, S. (2016) · Blood Reviews · doi:10.1016/j.blre.2016.08.005 · Cited by 317
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Bose, P., Gandhi, V. V., & Konopleva, M. Y. (2017) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.1080/10428194.2017.1283032 · Cited by 311
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Paez‐Ribes, M., González‐Gualda, E., Doherty, G. J., & Muñoz‐Espín, D. (2019) · EMBO Molecular Medicine · doi:10.15252/emmm.201810234 · Cited by 293
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Mérino, D., Kelly, G. L., Lessène, G., Wei, A. H., Roberts, A. W., & Strasser, A. (2018) · Cancer Cell · doi:10.1016/j.ccell.2018.11.004 · Cited by 300
He, Y., Zhang, X., Chang, J., Kim, H.-N., Zhang, P., Wang, Y., Khan, S., Liu, X., Zhang, X., Lv, D., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15838-0 · Cited by 280
Lagoumtzi, S. M., & Chondrogianni, N. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.05.003 · Cited by 279
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Kapoor, I., Bodo, J., Hill, B. T., Hsi, E. D., & Almasan, A. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-03144-y · Cited by 255
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Birkinshaw, R. W., & Czabotar, P. E. (2017) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2017.04.001 · Cited by 229
Singh, P., & Lim, B. (2022) · Current Oncology Reports · doi:10.1007/s11912-022-01199-y · Cited by 222
MCL-1 is a prognostic indicator and drug target in breast cancer
Campbell, K. J., Dhayade, S., Ferrari, N., Sims, A. H., Johnson, E. R., Mason, S. M., Dickson, A., Ryan, K. M., Kalna, G., Edwards, J., et al. (2018) · Cell Death and Disease · doi:10.1038/s41419-017-0035-2 · Cited by 203
Agarwal, R., Chan, Y.-C., Tam, C. S. L., Hunter, T., Vassiliadis, D., Teh, C. E., Thijssen, R., Yeh, P. S.-H., Wong, S. Q., Ftouni, S., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0243-z · Cited by 207
VDAC2 enables BAX to mediate apoptosis and limit tumor development
Chin, H. S., Li, M. X., Tan, I. K. L., Ninnis, R. L., Reljic, B., Scicluna, K., Dagley, L. F., Sandow, J. J., Kelly, G. L., Samson, A. L., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-07309-4 · Cited by 196
Co-targeting of BAX and BCL-XL proteins broadly overcomes resistance to apoptosis in cancer
López, A., Reyna, D. E., Gitego, N., Kopp, F., Zhou, H., Miranda-Román, M. A., Nordstrøm, L. U., Narayanagari, S.-R., Chi, P., Vilar, E., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-28741-7 · Cited by 203
Mérino, D., Whittle, J. R., Vaillant, F., Serrano, A., Gong, J.-N., Giner, G., Maragno, A. L., Chanrion, M., Schneider, E., Pal, B., et al. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aam7049 · Cited by 195
Saleh, T., Carpenter, V. J., Tyutyunyk‐Massey, L., Murray, G., Leverson, J. D., Souers, A. J., Alotaibi, M. R., Faber, A. C., Reed, J., Harada, H., et al. (2020) · Molecular Oncology · doi:10.1002/1878-0261.12761 · Cited by 190
Self-citationTargeting MCL-1/BCL-XL Forestalls the Acquisition of Resistance to ABT-199 in Acute Myeloid Leukemia
Lin, K., Winter, P. S., Xie, A., Roth, C., Martz, C. A., Stein, E. M., Anderson, G. R., Tingley, J. P., & Wood, K. C. (2016) · Scientific Reports · doi:10.1038/srep27696 · Cited by 195
(ECIL), O. B. O. T. E. C. O. I. I. L., Maschmeyer, G., Greef, J. D., Mellinghoff, S. C., Nosari, A., Thiébaut, A., Bergeron, A., Franquet, T., Blijlevens, N. M. A., & Maertens, J. A. (2019) · Leukemia · doi:10.1038/s41375-019-0388-x · Cited by 188
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Inoue‐Yamauchi, A., Jeng, P., Kim, K., Chen, H., Han, S., Ganesan, Y. T., Ishizawa, K., Jebiwott, S., Dong, Y., Pietanza, M. C., et al. (2017) · Nature Communications · doi:10.1038/ncomms16078 · Cited by 180
Moujalled, D. M., Pomilio, G., Ghiurau, C., Ivey, A., Salmon, J. M., Rijal, S., MacRaild, S., Zhang, L., Teh, T., Tiong, I. S., et al. (2018) · Leukemia · doi:10.1038/s41375-018-0261-3 · Cited by 171
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Self-citationBasu, A. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2021.107943 · Cited by 171
Farhang, M., Akbarzadeh, A. R., Rabbani, M., & Ghadiri, A. M. (2022) · Polyhedron · doi:10.1016/j.poly.2022.116124 · Cited by 179
Knight, T. E., Luedtke, D. A., Edwards, H. J., Taub, J. W., & Ge, Y. (2019) · Biochemical Pharmacology · doi:10.1016/j.bcp.2019.01.015 · Cited by 170
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Reyna, D. E., Garner, T. P., López, A., Kopp, F., Choudhary, G. S., Sridharan, A., Narayanagari, S.-R., Mitchell, K., Dong, B., Bartholdy, B., et al. (2017) · Cancer Cell · doi:10.1016/j.ccell.2017.09.001 · Cited by 164
Baltschukat, S., Engstler, B. S., Huang, A., Hao, H.-X., Tam, A., Wang, H. Q., Liang, J., DiMare, M. T., Bhang, H.-E. C., Wang, Y., et al. (2019) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-18-2814 · Cited by 167
Davids, M. S., Hallek, M. J., Wierda, W. G., Roberts, A. W., Stilgenbauer, S., Jones, J. A., Gerecitano, J. F., Kim, S. Y., Potluri, J., Busman, T. A., et al. (2018) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-17-3761 · Cited by 164
Targeting BCL-2 to enhance vulnerability to therapy in estrogen receptor-positive breast cancer
Mérino, D., Lok, S. W., Visvader, J. E., & Lindeman, G. J. (2015) · Oncogene · doi:10.1038/onc.2015.287 · Cited by 164
The rise of apoptosis: targeting apoptosis in hematologic malignancies
Valentin, R., Grabow, S., & Davids, M. S. (2018) · Blood · doi:10.1182/blood-2018-02-791350 · Cited by 163
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Adams, C. M., Clark-Garvey, S., Porcu, P., & Eischen, C. M. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2018.00636 · Cited by 163
Development of a BCL-xL and BCL-2 dual degrader with improved anti-leukemic activity,
Lv, D., Pal, P., Liu, X., Jia, Y., Thummuri, D., Zhang, P., Hu, W., Pei, J., Zhang, Q., Zhou, S., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-27210-x · Cited by 158
Benito, J. M., Godfrey, L., Kojima, K., Hogdal, L. J., Wunderlich, M., Geng, H., Marzo, I., Harutyunyan, K. G., Golfman, L. S., North, P. S., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.12.003 · Cited by 158
Self-citationD’Aguanno, S., & Bufalo, D. D. (2020) · Cells · doi:10.3390/cells9051287 · Cited by 158
Targeting BCL-2-like Proteins to Kill Cancer Cells
Cory, S., Roberts, A. W., Colman, P. M., & Adams, J. M. (2016) · Trends in cancer · doi:10.1016/j.trecan.2016.07.001 · Cited by 148
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Gong, J.-N., Khong, T. T., Segal, D., Yao, Y., Riffkin, C. D., Garnier, J.-M., Khaw, S. L., Lessène, G., Spencer, A. G., Herold, M. J., et al. (2016) · Blood · doi:10.1182/blood-2016-03-704908 · Cited by 150
Roberts, A. W., & Huang, D. (2016) · Clinical Pharmacology & Therapeutics · doi:10.1002/cpt.553 · Cited by 153
Attianese, G. M. P. G., Gaínza, P., Gray-Gaillard, E. F., Cribioli, E., Shui, S., Kim, S., Kwak, M., Vollers, S. S., Osorio, A. D. J. C., Reichenbach, P., et al. (2020) · Nature Biotechnology · doi:10.1038/s41587-019-0403-9 · Cited by 146
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Zhang, S., Zhang, M., Jing, Y., Yin, X., Ma, P., Zhang, Z., Wang, X., Di, W. J., & Zhuang, G. (2018) · Nature Communications · doi:10.1038/s41467-017-02693-9 · Cited by 150
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Wang, L., Doherty, G. A., Judd, A. S., Tao, Z., Hansen, T. M., Frey, R. R., Song, X., Bruncko, M., Kunzer, A. R., Wang, X., et al. (2020) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.9b00568 · Cited by 146
Self-citationMali, R. S., Zhang, Q., DeFilippis, R., Cavazos, A., Kuruvilla, V. M., Raman, J., Mody, V., Choo, E. F., Dail, M., Shah, N. P., et al. (2020) · Haematologica · doi:10.3324/haematol.2019.244020 · Cited by 140
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He, Y., Koch, R., Budamagunta, V., Zhang, P., Zhang, X., Khan, S., Thummuri, D., Ortiz, Y. T., Zhang, X., Lv, D., et al. (2020) · Journal of Hematology & Oncology · doi:10.1186/s13045-020-00928-9 · Cited by 139
Genetic screens in isogenic mammalian cell lines without single cell cloning
DeWeirdt, P. C., Sangree, A. K., Hanna, R. E., Sanson, K. R., Hegde, M., Strand, C., Persky, N. S., & Doench, J. G. (2020) · Nature Communications · doi:10.1038/s41467-020-14620-6 · Cited by 138
Kuusanmäki, H. A., Dufva, O., Vähä-Koskela, M. J. V., Leppä, A., Huuhtanen, J., Vänttinen, I., Nygren, P. J., Klievink, J., Bouhlal, J., Pölönen, P., et al. (2022) · Blood · doi:10.1182/blood.2021011094 · Cited by 135
Moncsek, A., Al‐Suraih, M. S., Trussoni, C. E., O'Hara, S. P., Splinter, P. L., Zuber, C., Patsenker, E., Valli, P. V., Fingas, C. D., Weber, A., et al. (2018) · Hepatology · doi:10.1002/hep.29464 · Cited by 136
Salem, A. H., Agarwal, S. K., Dunbar, M., Enschede, S. H., Humerickhouse, R. A., & Wong, S. L. (2016) · The Journal of Clinical Pharmacology · doi:10.1002/jcph.821 · Cited by 135
Liu, H., Xu, Q., Wufuer, H., Li, Z., Sun, R., Jiang, Z., Dou, X., Fu, Q., Campisi, J., & Sun, Y. (2023) · Aging Cell · doi:10.1111/acel.13921 · Cited by 138
Influenza Virus Infection, Interferon Response, Viral Counter-Response, and Apoptosis
Shim, J. M., Kim, J., Tenson, T., Min, J.-Y., & Kainov, D. E. (2017) · Viruses · doi:10.3390/v9080223 · Cited by 133
BCL-2 family deregulation in colorectal cancer: potential for BH3 mimetics in therapy
Ramesh, P., & Medema, J. P. (2020) · APOPTOSIS · doi:10.1007/s10495-020-01601-9 · Cited by 134
Advances in targeted therapy for acute myeloid leukaemia
Käyser, S., & Levis, M. J. (2017) · British Journal of Haematology · doi:10.1111/bjh.15032 · Cited by 127
Leverson, J. D., Sampath, D., Souers, A. J., Rosenberg, S. H., Fairbrother, W. J., Amiot, M., Konopleva, M. Y., & Letai, A. G. (2017) · Cancer Discovery · doi:10.1158/2159-8290.cd-17-0797 · Cited by 126
Self-citationBCL2 Inhibitors as Anticancer Drugs: A Plethora of Misleading BH3 Mimetics
Soderquist, R. S., & Eastman, A. R. (2016) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-16-0031 · Cited by 124
Boyajian, J. L., Ghebretatios, M., Schaly, S., Islam, P., & Prakash, S. (2021) · Nutrients · doi:10.3390/nu13124550 · Cited by 115
Oppermann, S., Ylanko, J., Shi, Y., Hariharan, S., Oakes, C. C., Brauer, P. M., Zúñiga‐Pflücker, J. C., Leber, B. F., Spaner, D., & Andrews, D. W. (2016) · Blood · doi:10.1182/blood-2015-12-687814 · Cited by 122
Soderquist, R. S., Crawford, L. A., Liu, E., Lu, M., Agarwal, A., Anderson, G. R., Lin, K., Winter, P. S., Çakır, M., & Wood, K. C. (2018) · Nature Communications · doi:10.1038/s41467-018-05815-z · Cited by 122
Casara, P., Davidson, J. E. P., Clapéron, A., Toumelin-Braizat, G. L., Vogler, M., Bruno, A., Chanrion, M., Lysiak-Auvity, G., Diguarher, T. L., Starck, J.-B., et al. (2018) · Oncotarget · doi:10.18632/oncotarget.24744 · Cited by 119
Zhang, X., Thummuri, D., Liu, X., Hu, W., Zhang, P., Khan, S., Yuan, Y., Zhou, D., & Zheng, G. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112186 · Cited by 123
Induction of synthetic lethality in IDH1-mutated gliomas through inhibition of Bcl-xL
Karpel‐Massler, G., Ishida, C. T., Bianchetti, E., Zhang, Y., Shu, C., Tsujiuchi, T., Banu, M. A., Garcia, F., Roth, K. A., Bruce, J. N., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00984-9 · Cited by 121
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Zhang, L., Pitcher, L. E., Prahalad, V., Niedernhofer, L. J., & Robbins, P. D. (2021) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2021.111587 · Cited by 115
Lohard, S., Bourgeois, N., Maillet, L., Gautier, F., Fétiveau, A., Lasla, H., Nguyen, F., Vuillier, C., Dumont, A., Moreau‐Aubry, A., et al. (2020) · Nature Communications · doi:10.1038/s41467-019-13689-y · Cited by 120
Attacking cancer's Achilles heel: antagonism of anti‐apoptotic BCL ‐2 family members
Opferman, J. T. (2015) · FEBS Journal · doi:10.1111/febs.13472 · Cited by 118
Phillips, D. C., Xiao, Y., Lam, L. T., Litvinovich, E., Roberts-Rapp, L. A., Souers, A. J., & Leverson, J. D. (2015) · Blood Cancer Journal · doi:10.1038/bcj.2015.88 · Cited by 114
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Ong, F., Kim, K., & Konopleva, M. Y. (2022) · Cancer Drug Resistance · doi:10.20517/cdr.2021.125 · Cited by 113
Progress in targeting the BCL-2 family of proteins
Garner, T. P., López, A., Reyna, D. E., Spitz, A. Z., & Gavathiotis, E. (2017) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2017.06.014 · Cited by 109
Watt, A. C. S., Cejas, P., DeCristo, M. J., Metzger, O., Lam, E. Y. N., Qiu, X., BrinJones, H., Kesten, N., Coulson, R. S., Font‐Tello, A., et al. (2020) · Nature Cancer · doi:10.1038/s43018-020-00135-y · Cited by 112
Terai, H., Kitajima, S., Potter, D. S., Matsui, Y., Quiceno, L. G., Chen, T., Kim, T. J., Rusan, M., Thai, T. C., Piccioni, F., et al. (2017) · Cancer Research · doi:10.1158/0008-5472.can-17-1904 · Cited by 106
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He, Y., Thummuri, D., Zheng, G., Okunieff, P. G., Citrin, D. E., Vujašković, Ž., & Zhou, D. (2019) · Translational research · doi:10.1016/j.trsl.2019.03.006 · Cited by 107
Whittle, J. R., Vaillant, F., Surgenor, E., Policheni, A. N., Giner, G., Capaldo, B. D., Chen, H.-R., Liu, H. K., Dekkers, J. F., Sachs, N., et al. (2020) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-19-1872 · Cited by 102
Rapidly inducible Cas9 and DSB-ddPCR to probe editing kinetics
Rose, J. C., Stephany, J. J., Valente, W. J., Trevillian, B. M., Dang, H. V., Bielas, J. H., Maly, D. J., & Fowler, D. M. (2017) · Nature Methods · doi:10.1038/nmeth.4368 · Cited by 101
Venetoclax: A new wave in hematooncology
Mihályová, J., Jelı́nek, T., Growková, K., Hrdinka, M., Šimíček, M., & Hájek, R. (2018) · Experimental Hematology · doi:10.1016/j.exphem.2018.02.002 · Cited by 99
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
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