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Phase I Study of Navitoclax (ABT-263), a Novel Bcl-2 Family Inhibitor, in Patients With Small-Cell Lung Cancer and Other Solid Tumors
Open accessAbstract
Purpose: Resistance to chemotherapy-induced apoptosis represents a major obstacle to cancer control. Overexpression of Bcl-2 is seen in multiple tumor types and targeting Bcl-2 may provide therapeutic benefit. A phase I study of navitoclax, a novel inhibitor of Bcl-2 family proteins, was conducted to evaluate safety, pharmacokinetics, and preliminary efficacy in patients with solid tumors. Patients and Methods: Patients enrolled to intermittent dosing cohorts received navitoclax on day −3, followed by dosing on days 1 to 14 of a 21-day cycle. Patients on continuous dosing received a 1-week lead-in dose of 150 mg followed by continuous daily administration. Blood samples were collected for pharmacokinetic analyses, biomarker analyses, and platelet monitoring. Results: Forty-seven patients, including 29 with small-cell lung cancer (SCLC) or pulmonary carcinoid, were enrolled between 2007 and 2008, 35 on intermittent and 12 on continuous dosing cohorts. Primary toxicities included diarrhea (40%), nausea (34%), vomiting (36%), and fatigue (34%); most were grade 1 or 2. Dose- and schedule-dependent thrombocytopenia was seen in all patients. One patient with SCLC had a confirmed partial response lasting longer than 2 years, and eight patients with SCLC or carcinoid had stable disease (one remained on study for 13 months). Pro-gastrin releasing peptide (pro-GRP) was identified as a surrogate marker of Bcl-2 amplification and changes correlated with changes in tumor volume. Conclusion: Navitoclax is safe and well tolerated, with dose-dependent thrombocytopenia as the major adverse effect. Preliminary efficacy data are encouraging in SCLC. Efficacy in SCLC and the utility of pro-GRP as a marker of treatment response will be further evaluated in phase II studies.
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In the citing paper
“clinical trial data suggest that the dose-limiting toxicities of obatoclax may preclude sufficient target inhibition, in contrast to ABT-263 (30, 34, 35).”
From mTOR Inhibition Specifically Sensitizes Colorectal Cancers with KRAS or BRAF Mutations to BCL-2/BCL-XL Inhibition by Suppressing MCL-1 (2014) · cites this paper as [30]
Experimental — accuracy not yet measuredIn 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 [26]
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 [26]
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 [26]
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 [26]
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 [26]
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2 retracted
Pardo, O. E., Arcaro, A., Salerno, G., Raguz, S., Downward, J., & Seckl, M. J. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.a115.109006 · Cited by 153
RetractedPardo, O. E., Arcaro, A., Salerno, G., Raguz, S., Downward, J., & Seckl, M. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109006200 · Cited by 145
RetractedAn 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
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
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
Programmed Anuclear Cell Death Delimits Platelet Life Span
Mason, K. D., Carpinelli, M. R., Fletcher, J. I., Collinge, J. E., Hilton, A. A., Ellis, S., Kelly, P. N., Ekert, P. G., Metcalf, D., Roberts, A. W., et al. (2007) · Cell · doi:10.1016/j.cell.2007.01.037 · Cited by 1,031 · cited 1×
“This is a mechanism-based toxicity induced by inhibition of Bcl-xL in circulating platelets,(13,18) which is required for platelet survival.(19,20) Here we describe a phase I dose-escalation study to evaluate the safety (with particular attention to platelet dynamics), pharmacokinetics, and preliminary efficacy of nav…”
BackgroundThe role of Bcl-2 family members in tumorigenesis
Kirkin, V., Joos, S., & Zörnig, M. (2003) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2003.08.009 · Cited by 567
Some practical improvements in the continual reassessment method for phase I studies
Goodman, S. N., ZAHURAK, M. L., & Piantadosi, S. (1995) · Statistics in Medicine · doi:10.1002/sim.4780141102 · Cited by 475
Bcl-2 family proteins are essential for platelet survival
Zhang, H., Nimmer, P. M., Tahir, S. K., Chen, J., Fryer, R. M., Hahn, K. R., Iciek, L. A., Morgan, S. J., Nasarre, M. C., Nelson, R., et al. (2007) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4402081 · Cited by 427
Flagged first, then by citations
1 of the 39 references couldn’t be matched to a known paper.
Research works printed but not linked: 2
- Ben-Ezra JM, 1994, Am J Pathol, 145, 1036
- Brambilla E, 1996, Am J Pathol, 149, 1941
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Sorted by citations
Items 201–300 of 616
Targeted therapies for small cell lung cancer: Where do we stand?
Arcaro, A. (2015) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2015.03.001 · Cited by 51
Combination treatment with ABT-737 and chloroquine in preclinical models of small cell lung cancer
Zinn, R. L., Gardner, E. E., Dobromilskaya, I., Murphy, S., Marchionni, L., Hann, C. L., & Rudin, C. M. (2013) · Molecular Cancer · doi:10.1186/1476-4598-12-16 · Cited by 51
Self-citationGreenberg, E. F., McColl, K. S., Zhong, F., Wildey, G. M., Dowlati, A., & Distelhorst, C. W. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.355 · Cited by 51
Mcl-1 inhibitors: a patent review
Chen, L., & Fletcher, S. (2016) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2017.1249848 · Cited by 51
Iavarone, C., Zervantonakis, I. K., Selfors, L. M., Palakurthi, S. S., Liu, J. F., Drapkin, R., Matulonis, U. A., Hallberg, D. L., Velculescu, V. E., Leverson, J. D., et al. (2019) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-18-0413 · Cited by 52
Novel Therapies for Small Cell Lung Cancer
Koczywas, M., & Amanam, I. U. (2019) · Current cancer research · doi:10.1007/978-3-030-17832-1_8 · Cited by 51
Aging and Mesenchymal Stem Cells: Therapeutic Opportunities and Challenges in the Older Group
Chen, H., Liu, O., Chen, S., & Zhou, Y. (2021) · Gerontology · doi:10.1159/000516668 · Cited by 52
Alam, S., Mohammad, T., Padder, R. A., Hassan, M. I., & Husain, M. (2021) · Journal of Cellular Biochemistry · doi:10.1002/jcb.30162 · Cited by 50
Chiappori, A., Schreeder, M. T., Moezi, M. M., Stephenson, J., Blakely, J., Salgia, R., Chu, Q. S.-C., Ross, H. J., Subramaniam, D. S., Schnyder, J., et al. (2012) · British Journal of Cancer · doi:10.1038/bjc.2012.21 · Cited by 50
Lanning, M. E., Yu, W., Yap, J. L., Chauhan, J., Chen, L., Whiting, E., Pidugu, L. S. M., Atkinson, T., Bailey, H., Li, W., et al. (2016) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2016.02.006 · Cited by 50
Targeting Bcl-2/Bcl-XL Induces Antitumor Activity in Uveal Melanoma Patient-Derived Xenografts
Némati, F., de Montrion, C., Lang, G., Kraus‐Berthier, L., Carita, G., Sastre‐Garau, X., Berniard, A., Vallerand, D., Geneste, O., de Plater, L., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0080836 · Cited by 49
Kühl, T., & Lagares, D. (2018) · Matrix Biology · doi:10.1016/j.matbio.2018.01.020 · Cited by 49
Bertino, E. M., Gentzler, R. D., Clifford, S. E., Kolesar, J., Muzikansky, A., Haura, E. B., Piotrowska, Z., Camidge, D. R., Stinchcombe, T. E., Hann, C. L., et al. (2020) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-20-4084 · Cited by 48
Self-citationThe Role of Inhibition of Apoptosis in Acute Leukemias and Myelodysplastic Syndrome
McBride, A., Houtmann, S., Wilde, L. R., Vigil, C. E., Eischen, C. M., Kasner, M. T., & Palmisiano, N. D. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.00192 · Cited by 49
Luo, Q., Pan, W., Zhou, S., Wang, G., Yi, H., Zhang, L., Yan, X., Yuan, L., Liu, Z., Wang, J., et al. (2020) · Oncology Research Featuring Preclinical and Clinical Cancer Therapeutics · doi:10.3727/096504020x15825405463920 · Cited by 48
Beurlet, S., Omidvar, N., Gorombei, P., Krief, P., Pogam, C. L., Setterblad, N., de la Grange, P., Lebœuf, C., Janin, A., Noguera, M., et al. (2013) · Blood · doi:10.1182/blood-2012-07-445635 · Cited by 48
Zhao, X., Ogunwobi, O. O., & Liu, C. (2011) · PLoS ONE · doi:10.1371/journal.pone.0021980 · Cited by 48
Recent Advances in Cancer Therapeutics
Chessum, N. E. A., Jones, K., Pasqua, E., & Tucker, M. (2015) · Progress in medicinal chemistry · doi:10.1016/bs.pmch.2014.11.002 · Cited by 49
THE ROLE OF MITOCHONDRIA IN THE DEVELOPMENT AND PROGRESSION OF LUNG CANCER
Roberts, E., & Craig, K. J. T. (2013) · Computational and Structural Biotechnology Journal · doi:10.5936/csbj.201303019 · Cited by 50
Mukherjee, N., Schwan, J. V., Fujita, M., Norris, D. A., & Shellman, Y. G. (2015) · Journal of Investigative Dermatology · doi:10.1038/jid.2015.145 · Cited by 46
Radiosensitization by a novel Bcl-2 and Bcl-XL inhibitor S44563 in small-cell lung cancer
Loriot, Y., Mordant, P., Dugué, D., Geneste, O., Gombos, A., Opolon, P., Guégan, J., Perfettini, J., Pierré, A., Kraus‐Berthier, L., et al. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.365 · Cited by 46
Mitochondria: An intriguing target for killing tumour-initiating cells
Yan, B., Dong, L., & Neužil, J. (2015) · Mitochondrion · doi:10.1016/j.mito.2015.12.007 · Cited by 46
Venetoclax: Targeting BCL2 in Hematological Cancers
Scheffold, A., Jebaraj, B. M. C., & Stilgenbauer, S. (2018) · Recent results in cancer research/Recent Results in Cancer Research · doi:10.1007/978-3-319-91439-8_11 · Cited by 45
Romashkan, S., Chang, H., & Hadley, E. C. (2021) · The Journals of Gerontology Series A · doi:10.1093/gerona/glab028 · Cited by 46
Bcl-2 inhibitors as anti-cancer therapeutics: The impact of and on calcium signaling
Vervloessem, T., Kerkhofs, M., Rovere, R. M. L. L., Sneyers, F., Parys, J. B., & Bultynck, G. (2017) · Cell Calcium · doi:10.1016/j.ceca.2017.05.014 · Cited by 46
Taghizadeh, M. S., Taherishirazi, M., Niazi, A., Afsharifar, A., & Moghadam, A. A. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1327820 · 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
Hisam, N. S. N., Ugusman, A., Rajab, N. F., Ahmad, M. F., Fenech, M. F., Liew, S. L., & Anuar, N. N. M. (2021) · Pharmaceutics · doi:10.3390/pharmaceutics13091353 · 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
Chen, Q., Song, S., Wei, S., Liu, B., Honjo, S., Scott, A. W., Jin, J., Ma, L., Zhu, H., Skinner, H. D., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.4540 · Cited by 42
Mitochondrial apoptosis and BH3 mimetics
Dai, H., Meng, X. W., & Kaufmann, S. H. (2016) · F1000Research · doi:10.12688/f1000research.9629.1 · Cited by 43
Drugs and Clinical Approaches Targeting the Antiapoptotic Protein: A Review
Han, Z., Liang, J., Li, Y., & He, J. (2019) · BioMed Research International · doi:10.1155/2019/1212369 · Cited by 42
Soderquist, R. S., Danilov, A. V., & Eastman, A. R. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.562900 · Cited by 42
Ishitsuka, K., Kunami, N., Katsuya, H., Nogami, R., Ishikawa, C., Yotsumoto, F., Tanji, H., Mori, N., Takeshita, M., Miyamoto, S., et al. (2011) · Cancer Letters · doi:10.1016/j.canlet.2011.11.030 · Cited by 42
Combination with vorinostat overcomes ABT-263 (navitoclax) resistance of small cell lung cancer
Nakajima, W., Sharma, K., Hicks, M. A., Le, N., Brown, R., Krystal, G. W., & Harada, H. (2015) · Cancer Biology & Therapy · doi:10.1080/15384047.2015.1108485 · Cited by 42
Targeted drugs in small-cell lung cancer.
Santarpía, M., Daffinà, M. G., Karachaliou, N., González‐Cao, M., Lazzari, C., Altavilla, G., & Rosell, R. (2016) · Europe PMC (PubMed Central) · doi:10.3978/j.issn.2218-6751.2016.01.12 · Cited by 41
Zhang, X., Betzi, S., Morelli, X., & Roche, P. (2014) · Future Medicinal Chemistry · doi:10.4155/fmc.14.57 · Cited by 42
Current Management of Small Cell Lung Cancer
Neal, J. W., Gubens, M. A., & Wakelee, H. A. (2011) · Clinics in Chest Medicine · doi:10.1016/j.ccm.2011.07.002 · Cited by 41
Corcoran, R. B., Do, K. T., Kim, J. E., Cleary, J. M., Parikh, A. R., Yeku, O., Xiong, N., Weekes, C. D., Veneris, J. T., Ahronian, L. G., et al. (2024) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-23-3135 · Cited by 41
Self-citationMulti-level evidence that circulating CK18 is a biomarker of tumour burden in colorectal cancer
Greystoke, A., Dean, E. J., Saunders, M. P., Cummings, J., Hughes, A. M., Ranson, M., Dive, C., & Renehan, A. G. (2012) · British Journal of Cancer · doi:10.1038/bjc.2012.416 · Cited by 40
Self-citationTolcher, A. W., LoRusso, P. M., Arzt, J. A., Busman, T. A., Lian, G., Rudersdorf, N. S., Vanderwal, C. A., Waring, J. F., Yang, J., Holen, K. D., et al. (2015) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-015-2882-9 · Cited by 40
Self-citationSelective 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
Targeting the Akt, GSK-3, Bcl-2 axis in acute myeloid leukemia
Ricciardi, M. R., Mirabilii, S., Licchetta, R., Piedimonte, M., & Tafuri, A. (2017) · Advances in Biological Regulation · doi:10.1016/j.jbior.2017.05.002 · 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
Franzin, R., Stasi, A., Ranieri, E., Netti, G. S., Cantaluppi, V., Gesualdo, L., Stallone, G., & Castellano, G. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.630419 · Cited by 41
Bcl-2 antagonists: a proof of concept for CLL therapy
Balakrishnan, K., & Gandhi, V. V. (2013) · Investigational New Drugs · doi:10.1007/s10637-013-0002-4 · Cited by 39
Overcoming blocks in apoptosis with BH3-mimetic therapy in haematological malignancies
Khaw, S. L., Huang, D. C. S., & Roberts, A. W. (2011) · Pathology · doi:10.1097/pat.0b013e32834b1b34 · Cited by 42
Transcription factors and chromatin proteins as therapeutic targets in cancer
Johnston, S. J., & Carroll, J. S. (2015) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2015.02.002 · Cited by 41
Reddy, T. R. K., Li, C., Fischer, P. M., & Dekker, L. V. (2012) · ChemMedChem · doi:10.1002/cmdc.201200107 · Cited by 40
Select Bcl-2 antagonism restores chemotherapy sensitivity in high-risk neuroblastoma
Tanos, R., Karmali, D., Nalluri, S., & Goldsmith, K. C. (2016) · BMC Cancer · doi:10.1186/s12885-016-2129-0 · Cited by 39
Wu, H., Schiff, D. S., Lin, Y., Neboori, H. J., Goyal, S., Feng, Z., & Haffty, B. G. (2014) · Radiation Research · doi:10.1667/rr13856.1 · Cited by 39
Increased MCL-1 expression predicts poor prognosis and disease recurrence in acute myeloid leukemia
Li, X., Zhou, J., Wen, X., Zhang, T., Wu, D., Deng, Z., Zhang, Z., Lian, X., He, P.-F., Yao, X., et al. (2019) · OncoTargets and Therapy · doi:10.2147/ott.s194549 · Cited by 40
Role of mitochondria in carcinogenesis.
Tokarz, P., & Błasiak, J. (2014) · Acta Biochimica Polonica · doi:10.18388/abp.2014_1829 · Cited by 38
Maritoclax induces apoptosis in acute myeloid leukemia cells with elevated Mcl-1 expression
Doi, K., Liu, Q., Gowda, K., Barth, B. M., Claxton, D. F., Amin, S., Loughran, T. P., & Wang, H. (2014) · Cancer Biology & Therapy · doi:10.4161/cbt.29186 · Cited by 38
Bates, D. J. P., Danilov, A. V., Lowrey, C. H., & Eastman, A. R. (2013) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-12-1197 · Cited by 38
Reddy, T. R. K., Li, C., Guo, X., Fischer, P. M., & Dekker, L. V. (2014) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2014.07.043 · Cited by 38
Denèfle, T., Boullet, H., Herbi, L., Newton, C., Martínez‐Torres, A. C., Guez, A., Pramil, É., Quiney, C., Pourcelot, M., Levasseur, M. D., et al. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00781 · Cited by 44
Pleines, I., Lebois, M., Gangatirkar, P., Au, A. E., Lane, R. M., Henley, K. J., Kauppi, M., Corbin, J. E., Cannon, P., Bernardini, J. P., et al. (2018) · Blood · doi:10.1182/blood-2017-11-816355 · Cited by 38
Single and dual target inhibitors based on Bcl-2: Promising anti-tumor agents for cancer therapy
Liu, T., Wu, Z., He, Y., Xiao, Y., & Xia, C. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112446 · Cited by 39
SS18-SSX2 and the mitochondrial apoptosis pathway in mouse and human synovial sarcomas
Jones, K. B., Su, L., Jin, H., Lenz, C., Randall, R. L., Underhill, T. M., Nielsen, T. O., Sharma, S., & Capecchi, M. R. (2012) · Oncogene · doi:10.1038/onc.2012.247 · Cited by 38
Cellular senescence as a therapeutic target to improve renal transplantation outcome
van Willigenburg, H., de Keizer, P. L. J., & de Bruin, R. W. F. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.02.015 · Cited by 38
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
Fang, H., Harned, T. M., Kalous, O., Maldonado, V., DeClerck, Y. A., & Reynolds, C. P. (2011) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-11-0578 · Cited by 38
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
Dual targeting of MDM2 and BCL2 as a therapeutic strategy in neuroblastoma
Goethem, A. V., Yigit, N., Moreno‐Smith, M., Vasudevan, S. A., Barbieri, E., Speleman, F., Shohet, J. M., Vandesompele, J., & Maerken, T. V. (2017) · Oncotarget · doi:10.18632/oncotarget.18982 · Cited by 36
P2Y12 protects platelets from apoptosis via PI3k‐dependent Bak/Bax inactivation
Zhang, S., Ye, J. H., Zhang, Y., Xu, X., Liu, J.-X., ZHANG, S. H., Kunapuli, S. P., & Ding, Z. (2012) · Journal of Thrombosis and Haemostasis · doi:10.1111/jth.12063 · Cited by 36
From Mitochondrial Biology to Magic Bullet: Navitoclax Disarms BCL-2 in Chronic Lymphocytic Leukemia
Walensky, L. D. (2011) · Journal of Clinical Oncology · doi:10.1200/jco.2011.37.9339 · Cited by 36
The Application of Nanoparticles Targeting Cancer-Associated Fibroblasts
Huang, Q., Ge, Y., He, Y. T., Wu, J., Tong, Y., Shang, H., Liu, X., Ba, X., Xia, D., Peng, E., et al. (2024) · International Journal of Nanomedicine · doi:10.2147/ijn.s447350 · Cited by 35
Camps-Fajol, C., Cavero, D., Minguillón, J., & Surrallés, J. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107544 · Cited by 36
MicroRNAs and Glucocorticoid-Induced Apoptosis in Lymphoid Malignancies
Sionov, R. V. (2013) · ISRN Hematology · doi:10.1155/2013/348212 · Cited by 35
The 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
Iketani, M., Sekimoto, K., Igarashi, T., Takahashi, M. M., Komatsu, M., Sakane, I., Takahashi, H., Kawaguchi, H., Ohtani‐Kaneko, R., & Ohsawa, I. (2018) · Scientific Reports · doi:10.1038/s41598-018-35239-0 · Cited by 35
Ow, T. J., Fulcher, C. D., Thomas, C., Broin, P. Ó., López, A., Reyna, D. E., Smith, R. V., Sarta, C., Prystowsky, M. B., Schlecht, N. F., et al. (2019) · Oncotarget · doi:10.18632/oncotarget.26563 · Cited by 35
Joly, F., Fabbro, M., Follana, P., Lequesne, J., Médioni, J., Lesoin, A., Frenel, J., Abadie‐Lacourtoisie, S., Floquet, A., Gladieff, L., et al. (2022) · Gynecologic Oncology · doi:10.1016/j.ygyno.2022.01.021 · Cited by 35
Context‐dependent roles of cellular senescence in normal, aged, and disease states
Moiseeva, V., Cisneros, A., Cobos, A. C., Tarrega, A. B., Oñate, C. S., Perdiguero, E., Serrano, A. L., & Muñoz‐Cánoves, P. (2023) · The FEBS Journal · doi:10.1111/febs.16573 · Cited by 34
Mattoo, A. R., & FitzGerald, D. J. (2012) · International Journal of Cancer · doi:10.1002/ijc.27732 · Cited by 34
Ono, A., Naito, T., Ito, I., Watanabe, R., Shukuya, T., Kenmotsu, H., Tsuya, A., Nakamura, Y., Murakami, H., Kaira, K., et al. (2012) · Lung Cancer · doi:10.1016/j.lungcan.2011.12.012 · Cited by 34
Kamath, P. R., Sunil, D., Ajees, A. A., Pai, K. S. R., & Biswas, S. (2016) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2016.05.010 · Cited by 34
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
Tutumlu, G., Doğan, B., Avşar, T., Orhan, M. D., Calis, S., & Durdağı, S. (2020) · Frontiers in Chemistry · doi:10.3389/fchem.2020.00167 · Cited by 34
Olotu, F. A., Agoni, C., Adeniji, E. A., Abdullahi, M., & Soliman, M. E. S. (2018) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-018-2863-7 · Cited by 34
Ryu, W., Park, C.-W., Kim, J., Lee, H., & Chung, H. (2023) · Molecules and Cells · doi:10.14348/molcells.2023.2188 · Cited by 34
Samra, A. A., Robert, A., Gov, C., Favre, L., Eloy, L., Jacquet, E., Bignon, J. S., Wiels, J., Desrat, S., & Roussi, F. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.01.100 · Cited by 33
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
Self-citationTargeting Mitochondria with ClpP Agonists as a Novel Therapeutic Opportunity in Breast Cancer
Wedam, R., Greer, Y. E., Wisniewski, D. J., Weltz, S., Kundu, M., Voeller, D. M., & Lipkowitz, S. (2023) · Cancers · doi:10.3390/cancers15071936 · Cited by 36
Alkhatabi, H. A., Zohny, S. F., Mohammed, M. R. S., Choudhry, H., Rehan, M., Ahmad, A., Ahmed, F., & Khan, M. I. (2022) · Antioxidants · doi:10.3390/antiox11030461 · Cited by 32
Korell, F., Olson, M., Salas‐Benito, D., Leick, M. B., Larson, R. C., Bouffard, A. A., Silva, H. J., Gasparetto, A., Berger, T. R., Kann, M. C., et al. (2024) · Science Translational Medicine · doi:10.1126/scitranslmed.adk7640 · Cited by 32
Zhou, W., Xu, J., Gelston, E., Wu, X., Zou, Z., Wang, B., Zeng, Y., Wang, H., Liu, A., Xu, L., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.4306 · Cited by 33
Discovery of Small Molecule Bak Activator for Lung Cancer Therapy
Park, D., Anisuzzaman, A. S. M., Magis, A. T., Chen, G., Xie, M., Zhang, G., Behera, M., Sica, G., Ramalingam, S. S., Owonikoko, T. K., et al. (2021) · Theranostics · doi:10.7150/thno.60349 · Cited by 32
Glory, A., Bettaieb, A., & Averill‐Bates, D. A. (2014) · International Journal of Hyperthermia · doi:10.3109/02656736.2014.968641 · Cited by 32
Utilisation of Nanoparticle Technology in Cancer Chemoresistance
Ayers, D., & Nasti, A. (2012) · Journal of Drug Delivery · doi:10.1155/2012/265691 · Cited by 32
Rational combination of dual PI3K/mTOR blockade and Bcl-2/-xL inhibition in AML
Vachhani, P. J., Bose, P., Rahmani, M., & Grant, S. (2014) · Physiological Genomics · doi:10.1152/physiolgenomics.00173.2013 · Cited by 34
Zannetti, A., Iommelli, F., Speranza, A., Salvatore, M., & Vecchio, S. D. (2012) · Journal of Nuclear Medicine · doi:10.2967/jnumed.111.096503 · Cited by 31
Clinical candidates modulating protein-protein interactions: The fragment-based experience
Valenti, D., Hristeva, S., Tzalis, D., & Ottmann, C. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.01.084 · Cited by 32
pdCSM-PPI: Using Graph-Based Signatures to Identify Protein–Protein Interaction Inhibitors
Rodrigues, C. H. M., Pires, D. E. V., & Ascher, D. B. (2021) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.1c01135 · Cited by 31
Soderquist, R. S., Pletnev, A. A., Danilov, A. V., & Eastman, A. R. (2013) · APOPTOSIS · doi:10.1007/s10495-013-0910-y · Cited by 32
Lee, Y., Wang, L., Huang, C., Shi, Y., & Chang, L. (2018) · Cancer Letters · doi:10.1016/j.canlet.2018.06.019 · Cited by 31
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
Rational Combinations of Targeted Agents in AML
Bose, P., & Grant, S. (2015) · Journal of Clinical Medicine · doi:10.3390/jcm4040634 · Cited by 30
Daniëls, V. W., Zoeller, J. J., van Gastel, N., McQueeney, K. E., Parvin, S., Potter, D. S., Fell, G. G., Ferreira, V. G., Yilma, B., Gupta, R., et al. (2021) · Science Signaling · doi:10.1126/scisignal.abc7405 · Cited by 30
Metadata
- Authors
- Gandhi, L., Camidge, D. R., Ribeiro de Oliveira, M., Bonomi, P., Gandara, D., Khaira, D., Hann, C. L., McKeegan, E. M., Litvinovich, E., Hemken, P. M., Dive, C., Enschede, S. H., Nolan, C., Chiu, Y.-L., Busman, T., Xiong, H., Krivoshik, A. P., Humerickhouse, R., Shapiro, G. I., & Rudin, C. M.
- Affiliations
- Rush University Medical Center (US)
- From the Dana-Farber Cancer Institute, Boston, MA; University of Colorado Cancer Center, Aurora, CO; Northwest Medical Specialties, Tacoma, WA; Rush University Medical Center, Chicago; Abbott Laboratories, Abbott Park, IL; University of California Davis Cancer Center, Sacramento, CA; Sunterra Oncology Associates, Phoenix, AZ; Johns Hopkins University, Baltimore, MD; and Paterson Institute for Cancer Research, University of Manchester, United Kingdom.
- ORCID
- Venue
- Journal of Clinical Oncology
- Published
- 2011-03-01
- Volume
- 29
- Issue
- 7
- Pages
- 909-916
- ISSN
- 0732-183X (ISSN-L)
- 1527-7755
- PMC
- PMC4668282
- OpenAlex
- W2119316461
- Cited by
- 603
- References
- 39
- Citations by year
- 2026: 35 · 2025: 28 · 2024: 30 · 2023: 34 · 2022: 32 · 2021: 37 · 2020: 39 · 2019: 29 · 2018: 33 · 2017: 31 · 2016: 40 · 2015: 46 · 2014: 57 · 2013: 54 · 2012: 51
- FWCI
- 24.82
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Clinical Oncology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Research Explorer (The University of Manchester) (publishedVersion)
- Funders
- National Cancer Institute (P30CA006973)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Health Sciences › Medicine › Oncology › Lung Cancer Research Studies
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Keywords
- navitoclax, BCL-2 inhibitor, small cell lung cancer, bronchial carcinoid, thrombocytopenia, progastrin-releasing peptide, apoptosis resistance, pharmacokinetics, safety and tolerability, intermittent dosing, continuous dosing, surrogate markers
- MeSH terms
- Administration, Oral, Aged, Aged, 80 and over, Aniline Compounds, Dose-Response Relationship, Drug, Drug Administration Schedule, Female, Humans, Male, Middle Aged, Neoplasms, Prognosis, Sulfonamides, Survival Analysis, Treatment Outcome, Risk Assessment, Genes, bcl-2, Maximum Tolerated Dose, Small Cell Lung Carcinoma
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