[
1. R. R. Ramsay, M. R. Popovic-Nikolic, K. Nikolic, E. Uliassi and M. L. Bolognesi, A perspective on multi-target drug discovery and design for complex diseases, Clin. Transl. Med. 7(1) (2018) 3–16; https://doi.org/10.1186/s40169-017-0181-210.1186/s40169-017-0181-2577035329340951
]Search in Google Scholar
[
2. R. B. Mokhtari, T. S. Homayouni, N. Baluch, E. Morgatskaya, S. Kumar, B. Das and H. Yeger, Combination therapy in combating cancer, Oncotarget 8(23) (2017) 38022–38043; https://doi.org/10.18632/oncotarget.1672310.18632/oncotarget.16723551496928410237
]Search in Google Scholar
[
3. Y. Yamashita-Kashima, S. Iijima, K. Yorozu, K. Furugaki, M. Kurasawa, M. Ohta and K. Fujimoto-Ouchi, Pertuzumab in combination with trastuzumab shows significantly enhanced antitumor activity in HER2-positive human gastric cancer xenograft models, Clin. Cancer Res. 17(15) (2011) 5060–5070; https://doi.org/10.1158/1078-0432.CCR-10-292710.1158/1078-0432.CCR-10-292721700765
]Search in Google Scholar
[
4. S. C. Gupta, S. Patchva, W. Koh and B. B. Aggarwal, Discovery of curcumin, a component of golden spice, and its miraculous biological activities, Clin. Exp. Pharmacol. Physiol. 39(3) (2012) 283–299; https://doi.org/10.1111/j.1440-1681.2011.05648.x10.1111/j.1440-1681.2011.05648.x328865122118895
]Search in Google Scholar
[
5. A. Giordano and G. Tommonaro, Curcumin and cancer, Nutrients 11(10) (2019) Article ID 2376 (20 pages); https://doi.org/10.3390/nu1110237610.3390/nu11102376683570731590362
]Search in Google Scholar
[
6. A. Hosseini and A. Ghorbani, Cancer therapy with phytochemicals: evidence from clinical studies, Avicenna J. Phytomed. 5(2) (2015) 84–97.
]Search in Google Scholar
[
7. A. Banerjee, A. Kunwar, B. Mishra and K. I. Priyadarsini, Concentration dependent antioxidant/pro-oxidant activity of curcumin studies from AAPH induced hemolysis of RBCs, Chemico-biol. Interact. 174(2) (2008) 134–139; https://doi.org/10.1016/j.cbi.2008.05.00910.1016/j.cbi.2008.05.00918571152
]Search in Google Scholar
[
8. A. G. Miranda-Diaz, A. Garcia-Sanchez and E. G. Cardona-Munoz, Foods with potential prooxidant and antioxidant effects involved in Parkinson’s disease, Oxid. Med. Cell. Long. (2020) Article ID 6281454 (17 pages); https://doi.org/10.1155/2020/628145410.1155/2020/6281454742437432832004
]Search in Google Scholar
[
9. H. Zhou, C. S. Beevers and S. Huang, The targets of curcumin, Curr. Drug Targ. 12(3) (2011) 332–347; https://doi.org/10.2174/13894501179481535610.2174/138945011794815356302506720955148
]Search in Google Scholar
[
10. S. M. Johnson, P. Gulhati, I. Arrieta, X. Wang, T. Uchida, T. Gao and B. M. Evers, Curcumin inhibits proliferation of colorectal carcinoma by modulating Akt/mTOR signaling, Anticanc. Res. 29(8) (2009) 3185–3190.
]Search in Google Scholar
[
11. J. A. Bush, K. J. Cheung Jr. and G. Li, Curcumin induces apoptosis in human melanoma cells through a Fas receptor/caspase-8 pathway independent of p53, Exp. Cell Res. 271(2) (2001) 305–314; https://doi.org/10.1006/excr.2001.538110.1006/excr.2001.538111716543
]Search in Google Scholar
[
12. M. Rivera, Y. Ramos, M. Rodriguez-Valentin, S. Lopez-Acevedo, L. A. Cubano, J. Zou, Q. Zhang, G. Wang and N. M. Boukli, Targeting multiple pro-apoptotic signaling pathways with curcumin in prostate cancer cells, PloS One 12(6) (2017) e0179587 (25 pages); https://doi.org/10.1371/journal.pone.017958710.1371/journal.pone.0179587547631528628644
]Search in Google Scholar
[
13. Y. C. Chen, T. C. Kuo, S. Y. Lin-Shiau and J. K. Lin, Induction of HSP70 gene expression by modulation of Ca+2 ion and cellular p53 protein by curcumin in colorectal carcinoma cells, Mol. Carcinogen. 17(4) (1996) 224–234; https://doi.org/10.1002/(SICI)1098-2744(199612)17:4<224::AID-MC6>3.0.CO;2-D10.1002/(SICI)1098-2744(199612)17:4<224::AID-MC6>3.0.CO;2-D
]Search in Google Scholar
[
14. L. S. Angelo, J. Y. Wu, F. Meng, M. Sun, S. Kopetz, I. E. McCutcheon, J. M. Slopis and R. Kurzrock, Combining curcumin (diferuloylmethane) and heat shock protein inhibition for neurofibromatosis 2 treatment: analysis of response and resistance pathways, Mol. Cancer Therap. 10(11) (2011) 2094–2103; https://doi.org/10.1158/1535-7163.MCT-11-024310.1158/1535-7163.MCT-11-0243
]Search in Google Scholar
[
15. S. Nam, A. Williams, A. Vultur, A. List, K. Bhalla, D. Smith, F. Y. Lee and R. Jove, Dasatinib (BMS-354825) inhibits Stat5 signaling associated with apoptosis in chronic myelogenous leukemia cells, Mol. Cancer Therap. 6(4) (2007) 1400–1405; https://doi.org/10.1158/1535-7163.MCT-06-044610.1158/1535-7163.MCT-06-0446
]Search in Google Scholar
[
16. C. Zeng, L. Zhu, X. Jia, Y. Pang, Z. Li, X. Lu, F. Xie, L. Duan and Y. Wang, Spectrum of activity of dasatinib against mutant KIT kinases associated with drug-sensitive and drug-resistant gastrointestinal stromal tumors, Gastric Cancer 23(5) (2020) 837–847; https://doi.org/10.1007/s10120-020-01069-110.1007/s10120-020-01069-1
]Search in Google Scholar
[
17. G. E. Konecny, R. Glas, J. Dering, K. Manivong, J. Qi, R. S. Finn, G. R. Yang, K. L. Hong, C. Ginther, B. Winterhoff, G. Gao, J. Brugge and D. J. Slamon, Activity of the multikinase inhibitor dasatinib against ovarian cancer cells, Brit. J. Cancer 101(10) (2009) 1699–1708; https://doi.org/10.1038/sj.bjc.660538110.1038/sj.bjc.6605381
]Search in Google Scholar
[
18. Y. C. Lee, C. F. Huang, M. Murshed, K. Chu, J. C. Araujo, X. Ye, B. deCrombrugghe, L. Y. Yu-Lee, G. E. Gallick and S. H. Lin, Src family kinase/abl inhibitor dasatinib suppresses proliferation and enhances differentiation of osteoblasts, Oncogene 29(22) (2010) 3196–3207; https://doi.org/10.1038/onc.2010.7310.1038/onc.2010.73
]Search in Google Scholar
[
19. I. Dikic, T. Johansen and V. Kirkin, Selective autophagy in cancer development and therapy, Cancer Res. 70(9) (2010) 3431–3434; https://doi.org/10.1158/0008-5472.CAN-09-402710.1158/0008-5472.CAN-09-4027
]Search in Google Scholar
[
20. J. M. Zarzynska, The importance of autophagy regulation in breast cancer development and treatment, BioMed. Res. Int. 2014 (2014) Article ID 710345 (9 pages) https://doi.org/10.1155/2014/71034510.1155/2014/710345
]Search in Google Scholar
[
21. L. Galluzzi, F. Pietrocola, J. M. Bravo-San Pedro, R. K. Amaravadi, E. H. Baehrecke, F. Cecconi, P. Codogno, J. Debnath, D. A. Gewirtz, V. Karantza, A. Kimmelman, S. Kumar, B. Levine, M. C. Maiuri, S. J. Martin, J. Penninger, M. Piacentini, D. C. Rubinsztein, H. U. Simon, A. Simonsen, A. M. Thorburn, G. Velasco, K. M. Ryan and G. Kroemer, Autophagy in malignant transformation and cancer progression, EMBO J. 34(7) (2015) 856–858; https://doi.org/10.15252/embj.20149078410.15252/embj.201490784
]Search in Google Scholar
[
22. K. Wang, R. Liu, J. Li, J. Mao, Y. Lei, J. Wu, J. Zeng, J. T. Zhang, H. Wu, L. Chen, C. Huang and Y. Wei, Quercetin induces protective autophagy in gastric cancer cells: involvement of Akt-mTOR-and hypoxia-induced factor 1alpha-mediated signaling, Autophagy 7(9) (2011) 966–978; https://doi.org/10.4161/auto.7.9.1586310.4161/auto.7.9.15863
]Search in Google Scholar
[
23. Y. Lin, K. Wang, C. Hu, L. Lin, S. Qin and X. Cai, Elemene injection induced autophagy protects human hepatoma cancer cells from starvation and undergoing apoptosis, Evid. Based Compl. Alternat. Med. 2014 (2014) Article ID 637528 (9 pages); https://doi.org/10.1155/2014/63752810.1155/2014/637528
]Search in Google Scholar
[
24. S. F. Zhang, X. L. Wang, X. Q. Yang and N. Chen, Autophagy-associated targeting pathways of natural products during cancer treatment, Asian Pacific J. Cancer Prev. 15(24) (2014) 10557–10563; https://doi.org/10.7314/apjcp.2014.15.24.1055710.7314/APJCP.2014.15.24.10557
]Search in Google Scholar
[
25. J. S. O’Donnell, D. Massi, M. W. L. Teng and M. Mandala, PI3K-AKT-mTOR inhibition in cancer immunotherapy, redux, Sem. Cancer Biol. 48 (2018) 91–103; https://doi.org/10.1016/j.semcancer.2017.04.01510.1016/j.semcancer.2017.04.015
]Search in Google Scholar
[
26. G. M. Nitulescu, M. Van De Venter, G. Nitulescu, A. Ungurianu, P. Juzenas, Q. Peng, O. T. Olaru, D. Gradinaru, A. Tsatsakis, D. Tsoukalas, D. A. Spandidos and D. Margina, The Akt pathway in oncology therapy and beyond, Int. J. Oncol. 53(6) (2018) 2319–2331; https://doi.org/10.3892/ijo.2018.459710.3892/ijo.2018.4597
]Search in Google Scholar
[
27. K. A. West, S. S. Castillo and P. A. Dennis, Activation of the PI3K/Akt pathway and chemotherape utic resistance, Drug Resist. Updat. 5(6) (2002) 234–248; https://doi.org/10.1016/s1368-7646(02)00120-610.1016/S1368-7646(02)00120-6
]Search in Google Scholar
[
28. C. H. Chang, C. Y. Lee, C. C. Lu, F. J. Tsai, Y. M. Hsu, J. W. Tsao, Y. N. Juan, H. Y. Chiu, J. S. Yang and C. C. Wang, Resveratrol-induced autophagy and apoptosis in cisplatin-resistant human oral cancer CAR cells: A key role of AMPK and Akt/mTOR signaling, Int. J. Oncol. 50(3) (2017) 873–882; https://doi.org/10.3892/ijo.2017.386610.3892/ijo.2017.386628197628
]Search in Google Scholar
[
29. J. Xu, S. Zhang, R. Wang, X. Wu, L. Zeng and Z. Fu, Knockdown of PRDX2 sensitizes colon cancer cells to 5-FU by suppressing the PI3K/AKT signaling pathway, Biosci. Rep. 37(3) (2017) Article ID BSR20160447 (10 pages); https://doi.org/10.1042/BSR2016044710.1042/BSR20160447542628628432271
]Search in Google Scholar
[
30. M. J. Hour, S. C. Tsai, H. C. Wu, M. W. Lin, J. G. Chung, J. B. Wu, J. H. Chiang, M. Tsuzuki and J. S. Yang, Antitumor effects of the novel quinazolinone MJ-33: inhibition of metastasis through the MAPK, AKT, NF-kappaB and AP-1 signaling pathways in DU145 human prostate cancer cells, Int. J. Oncol. 41(4) (2012) 1513–1519; https://doi.org/10.3892/ijo.2012.156010.3892/ijo.2012.156022825655
]Search in Google Scholar
[
31. P. Lepont, J. T. Stickney, L. A. Foster, J. J. Meng, R. F. Hennigan and W. Ip, Point mutation in the NF2 gene of HEI-193 human schwannoma cells results in the expression of a merlin isoform with attenuated growth suppressive activity, Mutation Res. 637(1-2) (2008) 142–151; https://doi.org/10.1016/j.mrfmmm.2007.07.01510.1016/j.mrfmmm.2007.07.015223394017868749
]Search in Google Scholar
[
32. A. A. Waza, K. Andrabi and M. U. Hussain, Protein kinase C (PKC) mediated interaction between conexin43 (Cx43) and K(+)(ATP) channel subunit (Kir6.1) in cardiomyocyte mitochondria: Implications in cytoprotection against hypoxia induced cell apoptosis, Cell. Signalling 26(9) (2014) 1909–1917; https://doi.org/10.1016/j.cellsig.2014.05.00210.1016/j.cellsig.2014.05.00224815185
]Search in Google Scholar
[
33. R. M. Webster, Combination therapies in oncology, Nat. Rev. Drug Discov. 15(2) (2016) 81–82; https://doi.org/10.1038/nrd.2016.310.1038/nrd.2016.326837588
]Search in Google Scholar
[
34. A. M. Alizadeh, M. Sadeghizadeh, F. Najafi, S. K. Ardestani, V. Erfani-Moghadam, M. Khaniki, A. Rezaei, M. Zamani, S. Khodayari, H. Khodayari and M. A. Mohagheghi, Encapsulation of curcumin in diblock copolymer micelles for cancer therapy, BioMed. Res. Int. 2015 (2015) Article ID 824746 (15 pages); https://doi.org/10.1155/2015/82474610.1155/2015/824746435245325793208
]Search in Google Scholar
[
35. R. Chang, L. Sun and T. J. Webster, Short communication: selective cytotoxicity of curcumin on osteosarcoma cells compared to healthy osteoblasts, Int. J. Nanomed. 9 (2014) 461–465; https://doi.org/10.2147/IJN.S5550510.2147/IJN.S55505389413624453488
]Search in Google Scholar
[
36. G. Wei, S. Rafiyath and D. Liu, First-line treatment for chronic myeloid leukemia: dasatinib, nilotinib, or imatinib, J. Hematol. Oncol. 3 (2010) Article ID 47 (10 pages); https://doi.org/10.1186/1756-8722-3-4710.1186/1756-8722-3-47300036921108851
]Search in Google Scholar
[
37. H. Kantarjian, R. Pasquini, V. Levy, S. Jootar, J. Holowiecki, N. Hamerschlak, T. Hughes, E. Bleickardt, D. Dejardin, J. Cortes and N. P. Shah, Dasatinib or high-dose imatinib for chronic-phase chronic myeloid leukemia resistant to imatinib at a dose of 400 to 600 milligrams daily: two-year follow-up of a randomized phase 2 study (START-R), Cancer 115(18) (2009) 4136–4147; https://doi.org/10.1002/cncr.2450410.1002/cncr.24504534539119536906
]Search in Google Scholar
[
38. T. Bartke, D. Siegmund, N. Peters, M. Reichwein, F. Henkler, P. Scheurich and H. Wajant, p53 upregulates cFLIP, inhibits transcription of NF-kappaB-regulated genes and induces caspase-8-independent cell death in DLD-1 cells, Oncogene 20(5) (2001) 571–580; https://doi.org/10.1038/sj.onc.120412410.1038/sj.onc.120412411313989
]Search in Google Scholar
[
39. R. S. Wong, Apoptosis in cancer: from pathogenesis to treatment, J. Exp. Clin. Cancer Res. 30(1) (2011) Article ID 87 (14 pages); https://doi.org/10.1186/1756-9966-30-8710.1186/1756-9966-30-87319754121943236
]Search in Google Scholar
[
40. L. Ouyang, Z. Shi, S. Zhao, F. T. Wang, T. T. Zhou, B. Liu and J. K. Bao, Programmed cell death pathways in cancer: A review of apoptosis, autophagy and programmed necrosis, Cell Prolif. 45(6) (2012) 487–498; https://doi.org/10.1111/j.1365-2184.2012.00845.x10.1111/j.1365-2184.2012.00845.x649666923030059
]Search in Google Scholar
[
41. M. B. Schaaf, T. G. Keulers, M. A. Vooijs and K. M. Rouschop, LC3/GABARAP family proteins: Autophagy(un)related functions, FASEB J. 30(12) (2016) 3961–3978; https://doi.org/10.1096/fj.201600698R10.1096/fj.201600698R27601442
]Search in Google Scholar
[
42. M. S. Dong, S. H. Jung, H. J. Kim, J. R. Kim, L. X. Zhao, E. S. Lee, E. J. Lee, J. B. Yi, N. Lee, Y. B. Cho, W. J. Kwak and Y. I. Park, Structure-related cytotoxicity and anti-hepatofibric effect of asiatic acid derivatives in rat hepatic stellate cell-line, HSC-T6, Arch. Pharm. Res. 27(5) (2004) 512–517; https://doi.org/10.1007/BF0298012410.1007/BF0298012415202556
]Search in Google Scholar
[
43. J. Han, X. Y. Pan, Y. Xu, Y. Xiao, Y. An, L. Tie, Y. Pan and X. Li, Curcumin induces autophagy to protect vascular endothelial cell survival from oxidative stress damage, Autophagy 8(5) (2012) 812–825; https://doi.org/10.4161/auto.1947110.4161/auto.1947122622204
]Search in Google Scholar
[
44. F. Guan, Y. Ding, Y. Zhang, Y. Zhou, M. Li and C. Wang, Curcumin suppresses proliferation and migration of MDA-MB-231 breast cancer cells through autophagy-dependent Akt degradation, PLoS ONE 11(1) (2016) e0146553; https://doi.org/10.1371/journal.pone.014655310.1371/journal.pone.0146553470899026752181
]Search in Google Scholar
[
45. X. F. Le, W. Mao, Z. Lu, B. Z. Carter and R. C. Bast, Dasatinib induces autophagic cell death in human ovarian cancer, Cancer 116(21) (2010) 4980–4990; https://doi.org/10.1002/cncr.2542610.1002/cncr.25426297555520629079
]Search in Google Scholar
[
46. H. J. Lee, V. G. V. Saralamma, S. M. Kim, S. E. Ha, S. Raha, W. S. Lee, E. H. Kim, S. J. Lee, J. D. Heo and G. S. Kim, Pectolinarigenin induced cell cycle arrest, autophagy, and apoptosis in gastric cancer cell via PI3K/AKT/mTOR signaling pathway, Nutrients 10(8) (2018) Article ID 1043 (15 pages); https://doi.org/10.3390/nu1008104310.3390/nu10081043611585530096805
]Search in Google Scholar
[
47. K. Y. Kim, K. I. Park, S. H. Kim, S. N. Yu, S. G. Park, Y. W. Kim, Y. K. Seo, J. Y. Ma and S. C. Ahn, Inhibition of autophagy promotes salinomycin-induced apoptosis via reactive oxygen species-mediated PI3K/AKT/mTOR and ERK/p38 MAPK-dependent signaling in human prostate cancer cells, Int. J. Mol. Sci. 18(5) (2017) Article ID 1088 (15 pages); https://doi.org/10.3390/nu1008104310.3390/nu10081043
]Search in Google Scholar
[
48. C. Rozzo, M. Fanciulli, C. Fraumene, A. Corrias, T. Cubeddu, I. Sassu, S. Cossu, V. Nieddu, G. Galleri, E. Azara, M. A. Dettori, D. Fabbri, G. Palmieri and M. Pisano, Molecular changes induced by the curcumin analogue D6 in human melanoma cells, Mol. Cancer 12 (2013) Article ID 37 (16 pages); https://doi.org/10.1186/1476-4598-12-3710.1186/1476-4598-12-37365172023642048
]Search in Google Scholar
[
49. C. Porta, C. Paglino and A. Mosca, Targeting PI3K/Akt/mTOR signaling in cancer, Front. Oncol. 4 (2014) (11 pages); https://doi.org/10.3389/fonc.2014.0006410.3389/fonc.2014.00064399505024782981
]Search in Google Scholar
[
50. B. Chen, X. Xu, J. Luo, H. Wang and S. Zhou, Rapamycin enhances the anti-cancer effect of dasatinib by suppressing Src/PI3K/mTOR pathway in NSCLC cells, PLoS ONE 10(6) (2015); https://doi.org/10.1371/journal.pone.012966310.1371/journal.pone.0129663446569426061184
]Search in Google Scholar