{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T04:40:25Z","timestamp":1790311225387,"version":"4.1.0"},"reference-count":348,"publisher":"MDPI AG","issue":"10","license":[{"start":{"date-parts":[[2026,5,12]],"date-time":"2026-05-12T00:00:00Z","timestamp":1778544000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Ramanujan Fellowship","award":["RJF\/2023\/000034"],"award-info":[{"award-number":["RJF\/2023\/000034"]}]},{"name":"TERI School of Advanced Studies Internal grant","award":["25IGC001"],"award-info":[{"award-number":["25IGC001"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cancers"],"abstract":"<jats:p>Autophagy and apoptosis are two evolutionarily conserved catabolic processes that play important roles in maintaining cellular homeostasis and in determining cell fate when cells are exposed to various stresses in vivo. The interaction between autophagy and apoptosis has been studied extensively in cancer research, and it has been shown to affect cancer initiation and tumor formation, disease progression, therapeutic resistance, and overall survival. Autophagy typically functions as a cytoprotective mechanism in cancer cells subjected to metabolic, hypoxic, or therapeutic stress, whereas apoptosis primarily functions as an intrinsic programmed cell death pathway. While apoptosis and autophagy function as distinct pathways, there is significant molecular crosstalk, allowing cells to modulate their behavior from survival to death depending on the severity and duration of exposure to a given stressor and the cellular environment. This review examines the molecular landscape of the autophagy\u2013apoptosis interplay in cancers, with special attention paid to the major signaling pathways involved and their biological outcomes in oncology. We examine the molecular mechanisms and signal transduction pathways involved in the crosstalk between autophagy and apoptosis in cancer. In particular, we focus on several key proteins that regulate this crosstalk, including kinases, caspases, heat shock proteins and transcription factors. Furthermore, we describe the major signal transduction pathways that regulate this crosstalk, including the PI3K\/Akt\/mTOR, MAPK, unfolded protein response, oxidative stress, and calcium signaling pathways. Additionally, we discussed how dysregulation of these pathways contributes to cancer progression and treatment resistance. Finally, we summarized the use of currently available therapeutic agents targeting the crosstalk between autophagy and apoptosis, including FDA-approved drugs and natural products, with the potential to enhance the effectiveness of anticancer treatments. A better understanding of this complex process will allow the development of new, precision-based, combination cancer therapies.<\/jats:p>","DOI":"10.3390\/cancers18101564","type":"journal-article","created":{"date-parts":[[2026,5,12]],"date-time":"2026-05-12T12:33:37Z","timestamp":1778589217000},"page":"1564","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Autophagy\u2013Apoptosis Crosstalk in Cancer: Mechanisms, Signaling Pathways, and Therapeutic Targeting"],"prefix":"10.3390","volume":"18","author":[{"given":"Dia","family":"Kakkar","sequence":"first","affiliation":[{"name":"Cell and Molecular Biology Lab, TERI School of Advanced Studies, Plot No. 10, Sankar Rd, Vasant Kunj Institutional Area, New Delhi 110070, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Saloni","family":"Saxena","sequence":"additional","affiliation":[{"name":"Cell and Molecular Biology Lab, TERI School of Advanced Studies, Plot No. 10, Sankar Rd, Vasant Kunj Institutional Area, New Delhi 110070, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Utkarshita","family":"Dhawan","sequence":"additional","affiliation":[{"name":"Cell and Molecular Biology Lab, TERI School of Advanced Studies, Plot No. 10, Sankar Rd, Vasant Kunj Institutional Area, New Delhi 110070, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Naman","family":"Dosi","sequence":"additional","affiliation":[{"name":"Cell and Molecular Biology Lab, TERI School of Advanced Studies, Plot No. 10, Sankar Rd, Vasant Kunj Institutional Area, New Delhi 110070, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0006-5936-4994","authenticated-orcid":false,"given":"Charvi","family":"Khanna","sequence":"additional","affiliation":[{"name":"Cell and Molecular Biology Lab, TERI School of Advanced Studies, Plot No. 10, Sankar Rd, Vasant Kunj Institutional Area, New Delhi 110070, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8615-629X","authenticated-orcid":false,"given":"Souren","family":"Paul","sequence":"additional","affiliation":[{"name":"Cell and Molecular Biology Lab, TERI School of Advanced Studies, Plot No. 10, Sankar Rd, Vasant Kunj Institutional Area, New Delhi 110070, India"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,5,12]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Liu, S., Yao, S., Yang, H., Liu, S., and Wang, Y. (2023). Autophagy: Regulator of cell death. Cell Death Dis., 14.","DOI":"10.1038\/s41419-023-06154-8"},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Chai, H., Qian, H., Yao, S., Ma, S., and Su, W. (2025). Endoplasmic reticulum stress-mediated programmed cell death in the tumor microenvironment. Cell Death Discov., 11.","DOI":"10.1038\/s41420-025-02862-6"},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Eskander, G., AbdelHamid, S.G., Wahdan, S.A., and Radwan, S.M. (2025). Insights on the crosstalk among different cell death mechanisms. Cell Death Discov., 11.","DOI":"10.1038\/s41420-025-02328-9"},{"key":"ref_4","doi-asserted-by":"crossref","unstructured":"Rahal, Z., Darzi, R.E., Moghaddam, S.J., Cascone, T., and Kadara, H. (2025). Tumour and microenvironment crosstalk in NSCLC progression and response to therapy. Nat. Rev. Clin. Oncol., 22.","DOI":"10.1038\/s41571-025-01021-1"},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Das, S., Shukla, N., Singh, S.S., Kushwaha, S., and Shrivastava, R. (2021). Mechanism of interaction between autophagy and apoptosis in cancer. Apoptosis, 26.","DOI":"10.1007\/s10495-021-01687-9"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"3807","DOI":"10.21873\/anticanres.15871","article-title":"STAT3 Inactivation and Induction of Apoptosis Associate with Fluoxetine-Inhibited Epithelial\u2013Mesenchymal Transition and Growth of Triple-Negative Breast Cancer In Vivo","volume":"42","author":"Liao","year":"2022","journal-title":"Anticancer Res."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1111\/bjh.19218","article-title":"The ATR Inhibitor Elimusertib Exhibits Anti-Lymphoma Activity and Synergizes with the PI3K Inhibitor Copanlisib","volume":"204","author":"Sartori","year":"2024","journal-title":"Br. J. Haematol."},{"key":"ref_8","doi-asserted-by":"crossref","unstructured":"Li, M., Gao, P., and Zhang, J. (2016). Crosstalk between Autophagy and Apoptosis: Potential and Emerging Therapeutic Targets for Cardiac Diseases. Int. J. Mol. Sci., 17.","DOI":"10.3390\/ijms17030332"},{"key":"ref_9","doi-asserted-by":"crossref","unstructured":"Chen, Q., Kang, J., and Fu, C. (2018). The independence of and associations among apoptosis, autophagy, and necrosis. Signal Transduct. Target. Ther., 3.","DOI":"10.1038\/s41392-018-0018-5"},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Ojha, R., Ishaq, M., and Kumar, M. (2015). Caspase-mediated crosstalk between autophagy and apoptosis. J. Cancer Res. Ther., 11.","DOI":"10.4103\/0973-1482.163695"},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Tam, S.Y., Wu, V., and Law, H. (2017). Influence of autophagy on the efficacy of radiotherapy. Radiat. Oncol., 12.","DOI":"10.1186\/s13014-017-0795-y"},{"key":"ref_12","doi-asserted-by":"crossref","unstructured":"Gremke, N., Polo, P., Dort, A., Schneikert, J., Elmsh\u00e4user, S., Brehm, C.U., Klingm\u00fcller, U., Schmitt, A., Reinhardt, H.C., and Timofeev, O. (2020). mTOR-mediated cancer drug resistance suppresses autophagy and generates a druggable metabolic vulnerability. Nat. Commun., 11.","DOI":"10.1038\/s41467-020-18504-7"},{"key":"ref_13","doi-asserted-by":"crossref","unstructured":"Zhang, J., Xiang, Q., Wu, M., Lao, Y.-Z., Xian, Y.-F., Xu, H.-X., and Lin, Z.-X. (2023). Autophagy Regulators in Cancer. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms241310944"},{"key":"ref_14","doi-asserted-by":"crossref","unstructured":"Guo, T., Wu, C., Zhang, J., Yu, J., Li, G., Jiang, H., Zhang, X., Yu, R., and Liu, X. (2023). Dual blockade of EGFR and PI3K signaling pathways offers a therapeutic strategy for glioblastoma. Cell Commun. Signal., 21.","DOI":"10.1186\/s12964-023-01400-0"},{"key":"ref_15","doi-asserted-by":"crossref","unstructured":"Kitai, H., Choi, P.H., Yang, Y.C., Boyer, J.A., Whaley, A., Pancholi, P., Thant, C., Reiter, J., Chen, K., and Markov, V. (2024). Combined inhibition of KRASG12C and mTORC1 kinase is synergistic in non-small cell lung cancer. Nat. Commun., 15.","DOI":"10.1038\/s41467-024-50063-z"},{"key":"ref_16","doi-asserted-by":"crossref","unstructured":"Li, X., He, S., and Ma, B. (2020). Autophagy and autophagy-related proteins in cancer. Mol. Cancer, 19.","DOI":"10.1186\/s12943-020-1138-4"},{"key":"ref_17","doi-asserted-by":"crossref","unstructured":"Debnath, J., Gammoh, N., and Ryan, K.M. (2023). Autophagy and autophagy-related pathways in cancer. Nat. Rev. Mol. Cell Biol., 24.","DOI":"10.1038\/s41580-023-00585-z"},{"key":"ref_18","doi-asserted-by":"crossref","unstructured":"Singh, P., Ravanan, P., and Talwar, P. (2016). Death Associated Protein Kinase 1 (DAPK1): A Regulator of Apoptosis and Autophagy. Front. Mol. Neurosci., 9.","DOI":"10.3389\/fnmol.2016.00046"},{"key":"ref_19","doi-asserted-by":"crossref","unstructured":"Wu, Y., Chou, T.F., Young, L., Hsieh, F., Pan, H.Y., Mo, S.T., Brown, S.B., Chen, R.Y., Kimchi, A., and Lai, M.Z. (2020). Tumor suppressor death-associated protein kinase 1 inhibits necroptosis by p38 MAPK activation. Cell Death Dis., 11.","DOI":"10.1038\/s41419-020-2534-9"},{"key":"ref_20","doi-asserted-by":"crossref","unstructured":"Hill, S.M., Wr\u00f3bel, L., and Rubinsztein, D.C. (2018). Post-translational modifications of Beclin 1 provide multiple strategies for autophagy regulation. Cell Death Differ., 26.","DOI":"10.1038\/s41418-018-0254-9"},{"key":"ref_21","doi-asserted-by":"crossref","unstructured":"Zhang, X., Assaraf, Y.G., and Lin, Y. (2025). Death-associated protein kinase 1: A double-edged sword in health and disease. Front. Immunol., 16.","DOI":"10.3389\/fimmu.2025.1593394"},{"key":"ref_22","doi-asserted-by":"crossref","unstructured":"Wang, Y., Lin, K., Xu, T., Wang, L., Fu, L., Zhang, G., Jing, A., Jiao, Y., Zhu, R., and Han, X. (2021). Development and validation of prognostic model based on the analysis of autophagy-related genes in colon cancer. Aging, 13.","DOI":"10.18632\/aging.203352"},{"key":"ref_23","doi-asserted-by":"crossref","unstructured":"Shiloh, R., Gilad, Y., Ber, Y., Eisenstein, M., Aweida, D., Bialik, S., Cohen, S., and Kimchi, A. (2018). Non-canonical activation of DAPK2 by AMPK constitutes a new pathway linking metabolic stress to autophagy. Nat. Commun., 9.","DOI":"10.1038\/s41467-018-03907-4"},{"key":"ref_24","doi-asserted-by":"crossref","unstructured":"Makgoo, L., Mosebi, S., and Mbita, Z. (2023). The Role of Death-Associated Protein Kinase-1 in Cell Homeostasis-Related Processes. Genes, 14.","DOI":"10.3390\/genes14061274"},{"key":"ref_25","doi-asserted-by":"crossref","unstructured":"Chen, H., and MacDonald, J.A. (2021). Network analysis identifies DAPK3 as a potential biomarker for lymphovascular invasion and prognosis of colon adenocarcinoma. medRxiv.","DOI":"10.1101\/2021.02.03.21251102"},{"key":"ref_26","doi-asserted-by":"crossref","unstructured":"Xie, Y., Zhao, G., Lei, X., Cui, N., and Wang, H. (2023). Advances in the regulatory mechanisms of mTOR in necroptosis. Front. Immunol., 14.","DOI":"10.3389\/fimmu.2023.1297408"},{"key":"ref_27","first-page":"001","article-title":"Deciphering the intricate role of mTOR signaling and autophagy in Parkinson\u2019s disease and therapeutic prospects","volume":"14","author":"Narayanan","year":"2024","journal-title":"J. Appl. Pharm. Sci."},{"key":"ref_28","doi-asserted-by":"crossref","unstructured":"Marafie, S.K., Al-Mulla, F., and Abubaker, J. (2024). MTOR: Its critical role in metabolic diseases, cancer, and the aging process. Int. J. Mol. Sci., 25.","DOI":"10.3390\/ijms25116141"},{"key":"ref_29","doi-asserted-by":"crossref","unstructured":"Div\u00e9, I., Klann, K., Michaelis, J.B., Heinzen, D., Steinbach, J.P., M\u00fcnch, C., and Ronellenfitsch, M. (2022). Inhibition of mTOR signaling protects human glioma cells from hypoxia-induced cell death in an autophagy-independent manner. Cell Death Discov., 8.","DOI":"10.1038\/s41420-022-01195-y"},{"key":"ref_30","doi-asserted-by":"crossref","unstructured":"An, P., Xu, W., Luo, J., and Luo, Y. (2021). Expanding TOR Complex 2 Signaling: Emerging Regulators and New Connections. Front. Cell Dev. Biol., 9.","DOI":"10.3389\/fcell.2021.713806"},{"key":"ref_31","doi-asserted-by":"crossref","unstructured":"Sun, Y., Wang, H., Qu, T., Luo, J., An, P., Ren, F., Luo, Y., and Li, Y. (2023). mTORC2: A multifaceted regulator of autophagy. Cell Commun. Signal., 21.","DOI":"10.1186\/s12964-022-00859-7"},{"key":"ref_32","doi-asserted-by":"crossref","unstructured":"Deleyto-Seldas, N., and Efeyan, A. (2021). The MTOR\u2013autophagy axis and the control of metabolism. Front. Cell Dev. Biol., 9.","DOI":"10.3389\/fcell.2021.655731"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1089\/ars.2017.7234","article-title":"Autophagy in human health and disease: Novel therapeutic opportunities","volume":"30","author":"Giampieri","year":"2018","journal-title":"Antioxid. Redox Signal."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1389","DOI":"10.32604\/biocell.2024.049562","article-title":"DAPK2 promotes autophagy to accelerate the progression of ossification of the posterior longitudinal ligament through the mTORC1 complex","volume":"48","author":"Shi","year":"2024","journal-title":"Biocell"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"4959","DOI":"10.1007\/s11033-022-07154-1","article-title":"The impact of DAPK1 and mTORC1 signaling association on autophagy in cancer","volume":"49","author":"Movahhed","year":"2022","journal-title":"Mol. Biol. Rep."},{"key":"ref_36","doi-asserted-by":"crossref","unstructured":"Dite, T.A., Ling, N.X.Y., Scott, J.W., Hoque, A., Gali\u0107, S., Parker, B.L., Ngoei, K.R.W., Langendorf, C.G., O\u2019Brien, M.T., and Kundu, M. (2017). The autophagy initiator ULK1 sensitizes AMPK to allosteric drugs. Nat. Commun., 8.","DOI":"10.1038\/s41467-017-00628-y"},{"key":"ref_37","doi-asserted-by":"crossref","unstructured":"Saikia, R., and Joseph, J. (2021). AMPK: A key regulator of energy stress and calcium-induced autophagy. J. Mol. Med., 99.","DOI":"10.1007\/s00109-021-02125-8"},{"key":"ref_38","doi-asserted-by":"crossref","unstructured":"Grasso, D., Renna, F.J., and Vaccaro, M.I. (2018). Initial Steps in Mammalian Autophagosome Biogenesis. Front. Cell Dev. Biol., 6.","DOI":"10.3389\/fcell.2018.00146"},{"key":"ref_39","doi-asserted-by":"crossref","unstructured":"Zachari, M., and Ganley, I.G. (2017). The mammalian ULK1 complex and autophagy initiation. Essays Biochem., 61.","DOI":"10.1042\/EBC20170021"},{"key":"ref_40","doi-asserted-by":"crossref","unstructured":"Lee, Y., Jang, S., Song, H.S., Kwon, J.E., Ko, M., Hong, W., Gwon, A., Park, S., Jeong, Y., and Kim, H. (2025). Bakuchiol from Cullen corylifolium and its efficacy on apoptosis and autophagy in HepG2 cells. Heliyon, 10.","DOI":"10.1016\/j.heliyon.2024.e40758"},{"key":"ref_41","doi-asserted-by":"crossref","unstructured":"Zheng, Y., Feng, N., Li, C., and Li, Z. (2025). Natural products target programmed cell death signaling mechanisms to treat colorectal cancer. Front. Pharmacol., 16.","DOI":"10.3389\/fphar.2025.1565332"},{"key":"ref_42","doi-asserted-by":"crossref","unstructured":"Dibble, C.C., and Cantley, L.C. (2015). Regulation of mTORC1 by PI3K signaling. Trends Cell Biol., 25.","DOI":"10.1016\/j.tcb.2015.06.002"},{"key":"ref_43","doi-asserted-by":"crossref","unstructured":"Hoxhaj, G., and Manning, B.D. (2019). The PI3K\u2013AKT network at the interface of oncogenic signalling and cancer metabolism. Nat. Rev. Cancer, 20.","DOI":"10.1038\/s41568-019-0216-7"},{"key":"ref_44","doi-asserted-by":"crossref","unstructured":"Endicott, S.J., Ziemba, Z., Beckmann, L.J., Boynton, D.N., and Miller, R.A. (2020). Inhibition of class I PI3K enhances chaperone-mediated autophagy. J. Cell Biol., 219.","DOI":"10.1083\/jcb.202001031"},{"key":"ref_45","doi-asserted-by":"crossref","unstructured":"Kim, Y.C., and Guan, K. (2015). mTOR: A pharmacologic target for autophagy regulation. J. Clin. Investig., 125.","DOI":"10.1172\/JCI73939"},{"key":"ref_46","doi-asserted-by":"crossref","unstructured":"Popova, N.V., and J\u00fccker, M. (2021). The Role of mTOR Signaling as a Therapeutic Target in Cancer. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22041743"},{"key":"ref_47","doi-asserted-by":"crossref","unstructured":"Glaviano, A., Foo, A.S.C., Lam, H.Y., Yap, K.C.-Y., Jacot, W., Jones, R.H., Eng, H., Nair, M.G., Makvandi, P., and Geoerger, B. (2023). PI3K\/AKT\/mTOR signaling transduction pathway and targeted therapies in cancer. Mol. Cancer, 22.","DOI":"10.1186\/s12943-023-01827-6"},{"key":"ref_48","doi-asserted-by":"crossref","unstructured":"Zhou, L., Wang, J., Hou, H., Li, J., Li, J., Liang, J., Li, J., Niu, X., Hou, R., and Zhang, K.-M. (2022). Autophagy inhibits inflammation via down-regulation of p38 MAPK\/mTOR signaling cascade in endothelial cells. Res. Sq.","DOI":"10.21203\/rs.3.rs-2064260\/v1"},{"key":"ref_49","doi-asserted-by":"crossref","unstructured":"Shang, Y.-Y., Yao, M., Zhou, Z.-W., Cui, J., Xia, L., Hu, R.-Y., Yu, Y.-Y., Gao, Q., Yang, B., and Liu, Y.-X. (2017). Alisertib promotes apoptosis and autophagy in melanoma through p38 MAPK-mediated aurora a signaling. Oncotarget, 8.","DOI":"10.18632\/oncotarget.22328"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"659","DOI":"10.2147\/CCID.S405068","article-title":"Autophagy Inhibits Inflammation via Down-Regulation of p38 MAPK\/mTOR Signaling Cascade in Endothelial Cells","volume":"16","author":"Zhou","year":"2023","journal-title":"Clin. Cosmet. Investig. Dermatol."},{"key":"ref_51","doi-asserted-by":"crossref","unstructured":"Mustafa, M., Ahmad, R., Tantry, I.Q., Ahmad, W., Siddiqui, S., Alam, M., Abbas, K., Hassan, M.I., and Habib, S. (2024). Apoptosis: A comprehensive overview of signaling pathways, morphological changes, and physiological significance and therapeutic implications. Cells, 13.","DOI":"10.3390\/cells13221838"},{"key":"ref_52","doi-asserted-by":"crossref","unstructured":"Song, Y., Du, Y., Li, W., Fan, Y., Zhang, Y., Shen, H., Cheng, L., Wang, J., Deng, F., and Tang, B. (2025). Targeting the p38\/MAPK pathway to induce apoptosis: A multidimensional mechanistic exploration of Mentha and its active compound diosmetin against liver cancer. Sci. Rep., 15.","DOI":"10.1038\/s41598-025-23009-8"},{"key":"ref_53","doi-asserted-by":"crossref","unstructured":"Wei, Y., An, Z., Zou, Z., Sumpter, R., Su, M., Zang, X., Sinha, S., Gaestel, M., and Levine, B. (2015). The stress-responsive kinases MAPKAPK2\/MAPKAPK3 activate starvation-induced autophagy through Beclin 1 phosphorylation. eLife, 4.","DOI":"10.7554\/eLife.05289"},{"key":"ref_54","doi-asserted-by":"crossref","unstructured":"Kinsey, C.G., Camolotto, S.A., Boespflug, A., Guillen, K.P., Foth, M., Truong, A., Schuman, S.S., Shea, J.E., Seipp, M.T., and Yap, J.T. (2019). Protective autophagy elicited by RAF\u2192MEK\u2192ERK inhibition suggests a treatment strategy for RAS-driven cancers. Nat. Med., 25.","DOI":"10.1038\/s41591-019-0367-9"},{"key":"ref_55","doi-asserted-by":"crossref","unstructured":"Marchand, B., Poulin, M.-A., Lawson, C., Tai, L., Jean, S., and Boucher, M. (2023). Gemcitabine promotes autophagy and lysosomal function through ERK- and TFEB-dependent mechanisms. Cell Death Discov., 9.","DOI":"10.1038\/s41420-023-01342-z"},{"key":"ref_56","doi-asserted-by":"crossref","unstructured":"Bryant, K.L., Stalnecker, C.A., Zeitouni, D., Klomp, J.E., Peng, S., Tikunov, A.P., Gunda, V., Pierobon, M., Waters, A.M., and George, S.D. (2019). Combination of ERK and autophagy inhibition as a treatment approach for pancreatic cancer. Nat. Med., 25.","DOI":"10.1038\/s41591-019-0368-8"},{"key":"ref_57","doi-asserted-by":"crossref","unstructured":"Abdelrahman, K.S., Hassan, H.A., Abdel-Aziz, S.A., Marzouk, A.A., Narumi, A., Konno, H., and Abdel-Aziz, M. (2021). JNK signaling as a target for anticancer therapy. Pharmacol. Rep., 73.","DOI":"10.1007\/s43440-021-00238-y"},{"key":"ref_58","doi-asserted-by":"crossref","unstructured":"Zhou, Y., Li, Y., Jiang, W., and Zhou, L. (2015). MAPK\/JNK signalling: A potential autophagy regulation pathway. Biosci. Rep., 35.","DOI":"10.1042\/BSR20140141"},{"key":"ref_59","doi-asserted-by":"crossref","unstructured":"Bhardwaj, M., Leli, N.M., Koumenis, C., and Amaravadi, R.K. (2019). Regulation of autophagy by canonical and non-canonical ER stress responses. Semin. Cancer Biol., 66.","DOI":"10.1016\/j.semcancer.2019.11.007"},{"key":"ref_60","doi-asserted-by":"crossref","unstructured":"Schl\u00fctermann, D., Berleth, N., Deitersen, J., Hieke, N., Friesen, O., Wu, W., Stuhldreier, F., Sun, Y., Berning, L., and Friedrich, A. (2021). FIP200 controls the TBK1 activation threshold at SQSTM1\/p62-positive condensates. Sci. Rep., 11.","DOI":"10.1038\/s41598-021-92408-4"},{"key":"ref_61","doi-asserted-by":"crossref","unstructured":"Jiang, X., Bao, Y., Liu, H., Kou, X., Zhang, Z., Sun, F., Qian, Z., Lin, Z., Li, X., and Liu, X. (2017). VPS34 stimulation of p62 phosphorylation for cancer progression. Oncogene, 36.","DOI":"10.1038\/onc.2017.295"},{"key":"ref_62","doi-asserted-by":"crossref","unstructured":"Li, H.-Y., Zhang, J., Sun, L.-L., Li, B.-H., Gao, H.-L., Xie, T., Zhang, N., and Ye, Z.M. (2015). Celastrol induces apoptosis and autophagy via the ROS\/JNK signaling pathway in human osteosarcoma cells: An in vitro and in vivo study. Cell Death Dis., 6.","DOI":"10.1038\/cddis.2014.543"},{"key":"ref_63","doi-asserted-by":"crossref","unstructured":"Booth, L., Roberts, J.L., and Dent, P. (2019). The role of cell signaling in the crosstalk between autophagy and apoptosis in the regulation of tumor cell survival in response to sorafenib and neratinib. Semin. Cancer Biol., 66.","DOI":"10.1016\/j.semcancer.2019.10.013"},{"key":"ref_64","doi-asserted-by":"crossref","unstructured":"Siddiqui, M.A., Mukherjee, S., Manivannan, P., and Malathi, K. (2015). RNase L Cleavage Products Promote Switch from Autophagy to Apoptosis by Caspase-Mediated Cleavage of Beclin-1. Int. J. Mol. Sci., 16.","DOI":"10.3390\/ijms160817611"},{"key":"ref_65","doi-asserted-by":"crossref","unstructured":"Vega-Rub\u00edn-de-Celis, S. (2019). The Role of Beclin 1-Dependent Autophagy in Cancer. Biology, 9.","DOI":"10.3390\/biology9010004"},{"key":"ref_66","doi-asserted-by":"crossref","unstructured":"Mnich, K., Koryga, I., Pakos-Zebrucka, K., Thomas, M., Logue, S.E., Eriksson, L.A., Gorman, A.M., and Samali, A. (2021). The stressosome, a caspase-8-activating signalling complex assembled in response to cell stress in an ATG5-mediated manner. J. Cell. Mol. Med., 25.","DOI":"10.1111\/jcmm.16840"},{"key":"ref_67","doi-asserted-by":"crossref","unstructured":"Tsapras, P., and Nezis, I.P. (2017). Caspase involvement in autophagy. Cell Death Differ., 24.","DOI":"10.1038\/cdd.2017.43"},{"key":"ref_68","doi-asserted-by":"crossref","unstructured":"Frudd, K., Burgoyne, T., and Burgoyne, J.R. (2018). Oxidation of Atg3 and Atg7 mediates inhibition of autophagy. Nat. Commun., 9.","DOI":"10.1038\/s41467-017-02352-z"},{"key":"ref_69","doi-asserted-by":"crossref","unstructured":"Qin, P., Li, Q., Zu, Q., Dong, R., and Qi, Y. (2024). Natural products targeting autophagy and apoptosis in NSCLC: A novel therapeutic strategy. Front. Oncol., 14.","DOI":"10.3389\/fonc.2024.1379698"},{"key":"ref_70","doi-asserted-by":"crossref","unstructured":"Zhang, L., Li, J., Ouyang, L., Liu, B., and Cheng, Y. (2016). Unraveling the roles of Atg4 proteases from autophagy modulation to targeted cancer therapy. Cancer Lett., 373.","DOI":"10.1016\/j.canlet.2016.01.022"},{"key":"ref_71","doi-asserted-by":"crossref","unstructured":"Fritsch, M., G\u00fcnther, S.D., Schwarzer, R., Albert, M., Schorn, F., Werthenbach, J.P., Schiffmann, L.M., Stair, N., Stocks, H., and Seeger, J.M. (2019). Caspase-8 is the molecular switch for apoptosis, necroptosis and pyroptosis. Nature, 575.","DOI":"10.1038\/s41586-019-1770-6"},{"key":"ref_72","doi-asserted-by":"crossref","unstructured":"Beltr\u00e1n-Visiedo, M., Soler-Agesta, R., Sarosiek, K.A., Green, D.R., and Galluzzi, L. (2025). Regulation of inflammatory processes by caspases. Nat. Rev. Mol. Cell Biol., 26.","DOI":"10.1038\/s41580-025-00869-6"},{"key":"ref_73","doi-asserted-by":"crossref","unstructured":"Dho, S.H., Cho, M., Woo, W., Jeong, S., and Kim, L.K. (2025). Caspases as master regulators of programmed cell death: Apoptosis, pyroptosis and beyond. Exp. Mol. Med., 57.","DOI":"10.1038\/s12276-025-01470-9"},{"key":"ref_74","doi-asserted-by":"crossref","unstructured":"Lim, Y., Dorstyn, L., and Kumar, S. (2021). The p53-caspase-2 axis in the cell cycle and DNA damage response. Exp. Mol. Med., 53.","DOI":"10.1038\/s12276-021-00590-2"},{"key":"ref_75","doi-asserted-by":"crossref","unstructured":"Shalini, S., and Kumar, S. (2015). Caspase-2 and the oxidative stress response. Mol. Cell. Oncol., 2.","DOI":"10.1080\/23723556.2015.1004956"},{"key":"ref_76","doi-asserted-by":"crossref","unstructured":"Wible, D.J., and Bratton, S.B. (2017). Reciprocity in ROS and autophagic signaling. Curr. Opin. Toxicol., 7.","DOI":"10.1016\/j.cotox.2017.10.006"},{"key":"ref_77","doi-asserted-by":"crossref","unstructured":"Guo, W., Dong, A., Pan, X.-H., Lin, X., Lin, Y.N., He, M., Zhu, B., Jin, L., and Yao, R. (2016). Role of caspase-10 in the death of acute leukemia cells. Oncol. Lett., 12.","DOI":"10.3892\/ol.2016.4785"},{"key":"ref_78","doi-asserted-by":"crossref","unstructured":"Ikwegbue, P.C., Masamba, P., Oyinloye, B.E., and Kappo, A.P. (2017). Roles of Heat Shock Proteins in Apoptosis, Oxidative Stress, Human Inflammatory Diseases, and Cancer. Pharmaceuticals, 11.","DOI":"10.3390\/ph11010002"},{"key":"ref_79","doi-asserted-by":"crossref","unstructured":"Zuo, W., Pang, Q., Zhu, X., Yang, Q., Zhao, Q., He, G., Han, B., and Huang, W. (2024). Heat shock proteins as hallmarks of cancer: Insights from molecular mechanisms to therapeutic strategies. J. Hematol. Oncol., 17.","DOI":"10.1186\/s13045-024-01601-1"},{"key":"ref_80","doi-asserted-by":"crossref","unstructured":"Du, S., Liu, Y., Yuan, Y., Wang, Y., Chen, Y., Wang, S., and Chi, Y. (2022). Advances in the study of HSP70 inhibitors to enhance the sensitivity of tumor cells to radiotherapy. Front. Cell Dev. Biol., 10.","DOI":"10.3389\/fcell.2022.942828"},{"key":"ref_81","doi-asserted-by":"crossref","unstructured":"Kunachowicz, D., Kr\u00f3l-Kulikowska, M., Raczycka, W., Sleziak, J., B\u0142a\u017cejewska, M., and Kulbacka, J. (2024). Heat Shock Proteins, a Double-Edged Sword: Significance in Cancer Progression, Chemotherapy Resistance and Novel Therapeutic Perspectives. Cancers, 16.","DOI":"10.3390\/cancers16081500"},{"key":"ref_82","doi-asserted-by":"crossref","unstructured":"Albakova, Z., Mangasarova, Y., Albakov, A., and Gorenkova, L. (2022). HSP70 and HSP90 in Cancer: Cytosolic, Endoplasmic Reticulum and Mitochondrial Chaperones of Tumorigenesis. Front. Oncol., 12.","DOI":"10.3389\/fonc.2022.829520"},{"key":"ref_83","doi-asserted-by":"crossref","unstructured":"Hino, C., Chan, G., Jordaan, G., Chang, S.S., Saunders, J.T., Bashir, M.T., Hansen, J.E., Gera, J., Weisbart, R.H., and Nishimura, R.N. (2023). Cellular protection from H2O2 toxicity by Fv-Hsp70: Protection via catalase and gamma-glutamyl-cysteine synthase. Cell Stress Chaperones, 28.","DOI":"10.1007\/s12192-023-01349-6"},{"key":"ref_84","doi-asserted-by":"crossref","unstructured":"Sha, G., Jiang, Z., Zhang, W., Jiang, C., Wang, D., and Tang, D. (2023). The multifunction of HSP70 in cancer: Guardian or traitor to the survival of tumor cells and the next potential therapeutic target. Int. Immunopharmacol., 122.","DOI":"10.1016\/j.intimp.2023.110492"},{"key":"ref_85","doi-asserted-by":"crossref","unstructured":"Alhasan, B.A., Gladova, Y.A., Sverchinsky, D.V., Aksenov, N.D., Margulis, B.A., and Guzhova, I.V. (2024). Hsp70 Negatively Regulates Autophagy via Governing AMPK Activation, and Dual Hsp70-Autophagy Inhibition Induces Synergetic Cell Death in NSCLC Cells. Int. J. Mol. Sci., 25.","DOI":"10.3390\/ijms25169090"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s13277-015-4142-3","article-title":"Hsp90 regulates autophagy and plays a role in cancer therapy","volume":"37","author":"Wang","year":"2015","journal-title":"Tumor Biol."},{"key":"ref_87","doi-asserted-by":"crossref","unstructured":"Schopf, F.H., Biebl, M.M., and B\u00fcchner, J. (2017). The HSP90 chaperone machinery. Nat. Rev. Mol. Cell Biol., 18.","DOI":"10.1038\/nrm.2017.20"},{"key":"ref_88","doi-asserted-by":"crossref","unstructured":"Schaefer, S., Svenstrup, T.H., and Guerra, B. (2017). The small-molecule kinase inhibitor D11 counteracts 17-AAG-mediated up-regulation of HSP70 in brain cancer cells. PLoS ONE, 12.","DOI":"10.1371\/journal.pone.0177706"},{"key":"ref_89","doi-asserted-by":"crossref","unstructured":"Fuhrmann-Stroissnigg, H., Ling, Y.Y., Zhao, J., McGowan, S.J., Zhu, Y., Brooks, R.W., Grassi, D., Gregg, S.Q., Stripay, J.L., and Dorronsoro, A. (2017). Identification of HSP90 inhibitors as a novel class of senolytics. Nat. Commun., 8.","DOI":"10.1038\/s41467-017-00314-z"},{"key":"ref_90","doi-asserted-by":"crossref","unstructured":"Ahn, C., Park, J.E., Sim, D.Y., Park, S., Cha, H., Shim, B., Kim, B., and Kim, S. (2025). H STK32C as a Therapeutic Target in Colorectal Cancer via HSP90-PI3K\/AKT\/mTOR Signaling. Int. J. Biol. Sci., 21.","DOI":"10.7150\/ijbs.121647"},{"key":"ref_91","doi-asserted-by":"crossref","unstructured":"Bekki, H., Kohashi, K., Maekawa, A., Yamada, Y., Yamamoto, H., Harimaya, K., Hakozaki, M., Nabeshima, K., Iwamoto, Y., and Oda, Y. (2015). Elevated expression of HSP90 and the antitumor effect of an HSP90 inhibitor via inactivation of the Akt\/mTOR pathway in undifferentiated pleomorphic sarcoma. BMC Cancer, 15.","DOI":"10.1186\/s12885-015-1830-8"},{"key":"ref_92","doi-asserted-by":"crossref","unstructured":"Peng, C., Zhao, F., Li, H., Li, L., Yang, Y., and Liu, F. (2022). HSP90 mediates the connection of multiple programmed cell death in diseases. Cell Death Dis., 13.","DOI":"10.1038\/s41419-022-05373-9"},{"key":"ref_93","doi-asserted-by":"crossref","unstructured":"Jiang, M., Zhang, K., Zhang, Z., Zeng, X., Huang, Z., Qin, P., Xie, Z., Cai, X., Ashrafizadeh, M., and Tian, Y. (2025). PI3K\/AKT\/MTOR axis in cancer: From pathogenesis to treatment. MedComm, 6.","DOI":"10.1002\/mco2.70295"},{"key":"ref_94","doi-asserted-by":"crossref","unstructured":"Panwar, V., Singh, A., Bhatt, M., Tonk, R.K., Azizov, S., Raza, A.S., Sengupta, S., Kumar, D., and Garg, M. (2023). Multifaceted role of mTOR (mammalian target of rapamycin) signaling pathway in human health and disease. Signal Transduct. Target. Ther., 8.","DOI":"10.1038\/s41392-023-01608-z"},{"key":"ref_95","doi-asserted-by":"crossref","unstructured":"Matsuda-Lennikov, M., Suizu, F., Hirata, N., Hashimoto, M., Kimura, K., Nagamine, T., Fujioka, Y., Ohba, Y., Iwanaga, T., and Noguchi, M. (2014). Lysosomal interaction of Akt with Phafin2: A critical step in the induction of autophagy. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0079795"},{"key":"ref_96","doi-asserted-by":"crossref","unstructured":"Fang, Y., Bai, J., Bo, S., Cui, X., Song, H., Guo, L., Luan, Z., Sui, Q., Zheng, Y., and Sun, L. (2026). Targeting the AKT\/mTOR axis: Pectolinarigenin induces autophagy and apoptosis in human cervical cancer cells. Front. Pharmacol., 17.","DOI":"10.3389\/fphar.2026.1544170"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1021\/jm9004708","article-title":"Heat shock protein 90: Inhibitors in clinical trials","volume":"53","author":"Biamonte","year":"2009","journal-title":"J. Med. Chem."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"1045","DOI":"10.1124\/mol.115.101451","article-title":"A novel HSP90 inhibitor activates compensatory heat shock protein responses and autophagy and alleviates mutant A53T \u03b1-synuclein toxicity","volume":"88","author":"Xiong","year":"2015","journal-title":"Mol. Pharmacol."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"15968","DOI":"10.1021\/acs.jmedchem.4c00966","article-title":"Targeting HSP90 for cancer therapy: Current progress and emerging prospects","volume":"67","author":"Liang","year":"2024","journal-title":"J. Med. Chem."},{"key":"ref_100","doi-asserted-by":"crossref","unstructured":"Sun, C., Bai, M., Ke, W., Wang, X., Zhao, X., and Lu, Z. (2021). The HSP90 Inhibitor, XL888, Enhanced Cell Apoptosis via Downregulating STAT3 after Insufficient Radiofrequency Ablation in Hepatocellular Carcinoma. Life Sci., 282.","DOI":"10.1016\/j.lfs.2021.119762"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"507","DOI":"10.2217\/fon-2022-1172","article-title":"Pimitespib for the treatment of advanced gastrointestinal stromal tumors and other tumors","volume":"20","author":"Doi","year":"2023","journal-title":"Future Oncol."},{"key":"ref_102","doi-asserted-by":"crossref","unstructured":"Goel, B., Jaiswal, S., and Tripathi, N. (2025). Recent advances in HSP90 inhibitors as targeted cancer therapy: Chemical scaffolds, isoform selectivity, and clinical progress. Bioorg. Chem., 163.","DOI":"10.1016\/j.bioorg.2025.108782"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"959","DOI":"10.1016\/j.annonc.2022.05.518","article-title":"Pimitespib in patients with advanced gastrointestinal stromal tumor (CHAPTER-GIST-301): A randomized, double-blind, placebo-controlled phase III trial","volume":"33","author":"Kurokawa","year":"2022","journal-title":"Ann. Oncol."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"935","DOI":"10.1007\/s10147-025-02726-0","article-title":"Pimitespib in patients with advanced gastrointestinal stromal tumors in Japan: An expanded access program","volume":"30","author":"Naito","year":"2025","journal-title":"Int. J. Clin. Oncol."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1016\/j.cstres.2024.05.005","article-title":"An update on the status of HSP90 inhibitors in cancer clinical trials","volume":"29","author":"Rastogi","year":"2024","journal-title":"Cell Stress Chaperones"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"1798","DOI":"10.1021\/acs.jmedchem.9b00940","article-title":"Heat shock protein 90 inhibitors: An update on achievements, challenges, and future directions","volume":"63","author":"Li","year":"2019","journal-title":"J. Med. Chem."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1200\/JCO.19.00816","article-title":"Randomized phase III study of ganetespib, a heat shock protein 90 inhibitor, with docetaxel versus docetaxel in advanced non\u2013small-cell lung cancer (GALAXY-2)","volume":"38","author":"Pillai","year":"2019","journal-title":"J. Clin. Oncol."},{"key":"ref_108","doi-asserted-by":"crossref","unstructured":"Tufano, M., Marrone, L., D\u2019Ambrosio, C., Giacomo, V.D., Urzini, S., Xiao, Y., Matuozzo, M., Scaloni, A., Romano, M.F., and Romano, S. (2023). FKBP51 plays an essential role in Akt ubiquitination that requires Hsp90 and PHLPP. Cell Death Dis., 14.","DOI":"10.1038\/s41419-023-05629-y"},{"key":"ref_109","doi-asserted-by":"crossref","unstructured":"Li, W., Zhu, J., Dou, J., She, H., Tao, K., Xu, H., Yang, Q., and Mao, Z. (2017). Phosphorylation of LAMP2A by p38 MAPK couples ER stress to chaperone-mediated autophagy. Nat. Commun., 8.","DOI":"10.1038\/s41467-017-01609-x"},{"key":"ref_110","doi-asserted-by":"crossref","unstructured":"Xiao, X., Wang, W., Li, Y., Yang, D., Li, X., Shen, C., Liu, Y., Ke, X., Guo, S., and Guo, Z. (2018). HSP90AA1-mediated autophagy promotes drug resistance in osteosarcoma. J. Exp. Clin. Cancer Res., 37.","DOI":"10.1186\/s13046-018-0880-6"},{"key":"ref_111","doi-asserted-by":"crossref","unstructured":"Giulino-Roth, L., van Besien, H.J., Dalton, T.C., Totonchy, J., Rodina, A., Taldone, T., Bolaender, A., Erdjument-Bromage, H., Sadek, J., and Chadburn, A. (2017). Inhibition of Hsp90 Suppresses PI3K\/AKT\/mTOR Signaling and Has Antitumor Activity in Burkitt Lymphoma. Mol. Cancer Ther., 16.","DOI":"10.1158\/1535-7163.MCT-16-0848"},{"key":"ref_112","doi-asserted-by":"crossref","unstructured":"Albakova, Z. (2024). HSP90 multi-functionality in cancer. Front. Immunol., 15.","DOI":"10.3389\/fimmu.2024.1436973"},{"key":"ref_113","doi-asserted-by":"crossref","unstructured":"Joshi, A., Itoh, T., Picard, D., and Neckers, L. (2022). The Mitochondrial HSP90 Paralog TRAP1: Structural Dynamics, Interactome, Role in Metabolic Regulation, and Inhibitors. Biomolecules, 12.","DOI":"10.3390\/biom12070880"},{"key":"ref_114","doi-asserted-by":"crossref","unstructured":"Wengert, L.A., Backe, S.J., Bourboulia, D., Mollapour, M., and Woodford, M.R. (2022). TRAP1 Chaperones the Metabolic Switch in Cancer. Biomolecules, 12.","DOI":"10.3390\/biom12060786"},{"key":"ref_115","doi-asserted-by":"crossref","unstructured":"Zada, S., Hwang, J.S., Ahmed, M., Lai, T.H., Pham, T.M., Elashkar, O., and Kim, D.R. (2021). Cross talk between autophagy and oncogenic signaling pathways and implications for cancer therapy. Biochim. Biophys. Acta (BBA) Rev. Cancer, 1876.","DOI":"10.1016\/j.bbcan.2021.188565"},{"key":"ref_116","doi-asserted-by":"crossref","unstructured":"Li, S., Song, Y., Quach, C., Guo, H., Jang, G.-B., Maazi, H., Zhao, S., Sands, N.A., Liu, Q., and In, G.K. (2019). Transcriptional regulation of autophagy-lysosomal function in BRAF-driven melanoma progression and chemoresistance. Nat. Commun., 10.","DOI":"10.1038\/s41467-019-09634-8"},{"key":"ref_117","doi-asserted-by":"crossref","unstructured":"Malta, C.D., Cinque, L., and Settembre, C. (2019). Transcriptional Regulation of Autophagy: Mechanisms and Diseases. Front. Cell Dev. Biol., 7.","DOI":"10.3389\/fcell.2019.00114"},{"key":"ref_118","doi-asserted-by":"crossref","unstructured":"Rozp\u0119dek-Kami\u0144ska, W., Pytel, D., Mucha, B., Leszczynska, H., Diehl, J.A., and Majsterek, I. (2016). The Role of the PERK\/eIF2\u03b1\/ATF4\/CHOP Signaling Pathway in Tumor Progression During Endoplasmic Reticulum Stress. Curr. Mol. Med., 16.","DOI":"10.2174\/1566524016666160523143937"},{"key":"ref_119","doi-asserted-by":"crossref","unstructured":"Madhoun, A.A., Haddad, D., Tarrah, M.A., Jacob, S., Al-Ali, W., Nizam, R., Miranda, L., Al-Rashed, F., Sindhu, S., and Ahmad, R. (2021). Microarray analysis reveals ONC201 mediated differential mechanisms of CHOP gene regulation in metastatic and nonmetastatic colorectal cancer cells. Sci. Rep., 11.","DOI":"10.1038\/s41598-021-91092-8"},{"key":"ref_120","doi-asserted-by":"crossref","unstructured":"Fusakio, M.E., Willy, J.A., Wang, Y., Mirek, E.T., Al-Baghdadi, R.J.T., Adams, C.M., Anthony, T.G., and Wek, R.C. (2016). Transcription factor ATF4 directs basal and stress-induced gene expression in the unfolded protein response and cholesterol metabolism in the liver. Mol. Biol. Cell, 27.","DOI":"10.1091\/mbc.E16-01-0039"},{"key":"ref_121","doi-asserted-by":"crossref","unstructured":"Ong, G., and Logue, S.E. (2023). Unfolding the Interactions between Endoplasmic Reticulum Stress and Oxidative Stress. Antioxidants, 12.","DOI":"10.3390\/antiox12050981"},{"key":"ref_122","doi-asserted-by":"crossref","unstructured":"Gonuguntla, S., Humphrey, R.K., Gorantla, A., Hao, E., and Jhala, U.S. (2023). Stress-induced pseudokinase TRB3 augments IL1\u03b2 signaling by interacting with Flightless homolog 1. J. Biol. Chem., 299.","DOI":"10.1016\/j.jbc.2023.104803"},{"key":"ref_123","doi-asserted-by":"crossref","unstructured":"Hu, H., Tian, M., Ding, C., and Yu, S. (2019). The C\/EBP homologous protein (CHOP) transcription factor functions in endoplasmic reticulum stress-induced apoptosis and microbial infection. Front. Immunol., 9.","DOI":"10.3389\/fimmu.2018.03083"},{"key":"ref_124","doi-asserted-by":"crossref","unstructured":"Yan, M., Ni, J., Song, D., Ding, M., and Huang, J. (2015). Interplay between unfolded protein response and autophagy promotes tumor drug resistance. Oncol. Lett., 10.","DOI":"10.3892\/ol.2015.3508"},{"key":"ref_125","doi-asserted-by":"crossref","unstructured":"Hetz, C., Zhang, K., and Kaufman, R.J. (2020). Mechanisms, regulation and functions of the unfolded protein response. Nat. Rev. Mol. Cell Biol., 21.","DOI":"10.1038\/s41580-020-0250-z"},{"key":"ref_126","doi-asserted-by":"crossref","unstructured":"Han, J., and Kaufman, R.J. (2017). Physiological\/pathological ramifications of transcription factors in the unfolded protein response. Genes Dev., 31.","DOI":"10.1101\/gad.297374.117"},{"key":"ref_127","doi-asserted-by":"crossref","unstructured":"Rashid, H.-O., Yadav, R.K., Kim, H., and Chae, H. (2015). ER stress: Autophagy induction, inhibition and selection. Autophagy, 11.","DOI":"10.1080\/15548627.2015.1091141"},{"key":"ref_128","doi-asserted-by":"crossref","unstructured":"Kolluru, V., Tyagi, A., Chandrasekaran, B., Ankem, M.K., and Damodaran, C. (2019). Induction of endoplasmic reticulum stress might be responsible for defective autophagy in cadmium-induced prostate carcinogenesis. Toxicol. Appl. Pharmacol., 373.","DOI":"10.1016\/j.taap.2019.04.012"},{"key":"ref_129","doi-asserted-by":"crossref","unstructured":"Alasiri, G., Jiramongkol, Y., Zona, S., Fan, L.Y.-N., Mahmud, Z., Gong, G., Lee, H.J., and Lam, E.W. (2019). Regulation of PERK expression by FOXO3: A vulnerability of drug-resistant cancer cells. Oncogene, 38.","DOI":"10.1038\/s41388-019-0890-7"},{"key":"ref_130","doi-asserted-by":"crossref","unstructured":"Calissi, G., Lam, E.W.-F., and Link, W. (2020). Therapeutic strategies targeting FOXO transcription factors. Nat. Rev. Drug Discov., 20.","DOI":"10.1038\/s41573-020-0088-2"},{"key":"ref_131","doi-asserted-by":"crossref","unstructured":"Urushihara, Y., Hashimoto, T., Fujishima, Y., and Hosoi, Y. (2023). AMPK\/FOXO3a Pathway Increases Activity and\/or Expression of ATM, DNA-PKcs, Src, EGFR, PDK1, and SOD2 and Induces Radioresistance under Nutrient Starvation. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms241612828"},{"key":"ref_132","doi-asserted-by":"crossref","unstructured":"Xing, Y., Li, A., Yang, Y., Li, X., Zhang, L., and Guo, H. (2017). The regulation of FOXO1 and its role in disease progression. Life Sci., 193.","DOI":"10.1016\/j.lfs.2017.11.030"},{"key":"ref_133","doi-asserted-by":"crossref","unstructured":"Fitzwalter, B.E., and Thorburn, A. (2015). Recent insights into cell death and autophagy. FEBS J., 282.","DOI":"10.1111\/febs.13515"},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.molcel.2013.01.024","article-title":"ZKSCAN3 is a master transcriptional repressor of autophagy","volume":"50","author":"Chauhan","year":"2013","journal-title":"Mol. Cell"},{"key":"ref_135","doi-asserted-by":"crossref","unstructured":"Metur, S.P., Lei, Y., Zhang, Z., and Klionsky, D.J. (2023). Regulation of autophagy gene expression and its implications in cancer. J. Cell Sci., 136.","DOI":"10.1242\/jcs.260631"},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"305","DOI":"10.3109\/07853890.2015.1040831","article-title":"The critical molecular interconnections in regulating apoptosis and autophagy","volume":"47","author":"Zhao","year":"2015","journal-title":"Ann. Med."},{"key":"ref_137","doi-asserted-by":"crossref","unstructured":"Singh, A., Wilson, J.W., Schofield, C.J., and Chen, R. (2020). Hypoxia-inducible factor (HIF) prolyl hydroxylase inhibitors induce autophagy and have a protective effect in an in-vitro ischaemia model. Sci. Rep., 10.","DOI":"10.1038\/s41598-020-58482-w"},{"key":"ref_138","doi-asserted-by":"crossref","unstructured":"Zaarour, R.F., Azakir, B., Hajam, E.Y., Nawafleh, H., Zeinelabdin, N.A., Engelsen, A.S.T., Thiery, J., Jamora, C., and Chouaib, S. (2021). Role of Hypoxia-Mediated Autophagy in Tumor Cell Death and Survival. Cancers, 13.","DOI":"10.3390\/cancers13030533"},{"key":"ref_139","doi-asserted-by":"crossref","unstructured":"Yang, G., Shi, R., and Zhang, Q. (2020). Hypoxia and Oxygen-Sensing Signaling in Gene Regulation and Cancer Progression. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21218162"},{"key":"ref_140","doi-asserted-by":"crossref","unstructured":"Yang, X., Yu, D., Yan, F., Jing, Y., Han, Z., Sun, K., Liang, L., Hou, J., and Wei, L.X. (2015). The role of autophagy induced by tumor microenvironment in different cells and stages of cancer. Cell Biosci., 5.","DOI":"10.1186\/s13578-015-0005-2"},{"key":"ref_141","first-page":"155","article-title":"Autophagy\/Apoptosis Induced by Geraniol through HIF-1\u03b1\/BNIP3\/Beclin-1 Signaling Pathway in A549 CoCl2 Treated Cells","volume":"12","year":"2020","journal-title":"Adv. Pharm. Bull."},{"key":"ref_142","doi-asserted-by":"crossref","unstructured":"Thomas, L.W., and Ashcroft, M. (2019). Exploring the molecular interface between hypoxia-inducible factor signalling and mitochondria. Cell. Mol. Life Sci., 76.","DOI":"10.1007\/s00018-019-03039-y"},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"1690","DOI":"10.1021\/acs.chemrestox.2c00131","article-title":"HIF1, HSF1, and NRF2: Oxidant-responsive trio raising cellular defenses and engaging immune system","volume":"35","author":"Cyran","year":"2022","journal-title":"Chem. Res. Toxicol."},{"key":"ref_144","doi-asserted-by":"crossref","unstructured":"Xiong, S., Chng, W.J., and Zhou, J. (2021). Crosstalk between endoplasmic reticulum stress and oxidative stress: A dynamic duo in multiple myeloma. Cell. Mol. Life Sci., 78.","DOI":"10.1007\/s00018-021-03756-3"},{"key":"ref_145","doi-asserted-by":"crossref","unstructured":"Naidu, S.D., Dikovskaya, D., Gaurilcikaite, E., Knatko, E.V., Healy, Z.R., Mohan, H., Koh, G., Laurell, A., Ball, G., and Olagnier, D. (2017). Transcription factors NRF2 and HSF1 have opposing functions in autophagy. Sci. Rep., 7.","DOI":"10.1038\/s41598-017-11262-5"},{"key":"ref_146","doi-asserted-by":"crossref","unstructured":"Dodson, M., Redmann, M., Rajasekaran, N.S., Darley-Usmar, V., and Zhang, J. (2015). KEAP1\u2013NRF2 signalling and autophagy in protection against oxidative and reductive proteotoxicity. Biochem. J., 469.","DOI":"10.1042\/BJ20150568"},{"key":"ref_147","doi-asserted-by":"crossref","unstructured":"He, F., Ru, X., and Wen, T. (2020). NRF2, a Transcription Factor for Stress Response and Beyond. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21134777"},{"key":"ref_148","doi-asserted-by":"crossref","unstructured":"K\u00fcper, A., Baumann, J., G\u00f6pelt, K., Baumann, M., S\u00e4nger, C., Metzen, E., Kranz, P., and Brockmeier, U. (2021). Overcoming hypoxia-induced resistance of pancreatic and lung tumor cells by disrupting the PERK-NRF2-HIF-axis. Cell Death Dis., 12.","DOI":"10.1038\/s41419-020-03319-7"},{"key":"ref_149","doi-asserted-by":"crossref","unstructured":"Zhang, C., Ma, S., Zhao, X., Wen, B., Sun, P., and Fu, Z. (2021). Upregulation of antioxidant and autophagy pathways via NRF2 activation protects spinal cord neurons from ozone damage. Mol. Med. Rep., 23.","DOI":"10.3892\/mmr.2021.12067"},{"key":"ref_150","doi-asserted-by":"crossref","unstructured":"Kageyama, S., Gu\u00f0mundsson, S., Sou, Y., Ichimura, Y., Tamura, N., Kazuno, S., Ueno, T., Miura, Y., Noshiro, D., and Abe, M. (2021). p62\/SQSTM1-droplet serves as a platform for autophagosome formation and anti-oxidative stress response. Nat. Commun., 12.","DOI":"10.1038\/s41467-020-20185-1"},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1016\/j.freeradbiomed.2015.06.014","article-title":"p62 links autophagy and Nrf2 signaling","volume":"88","author":"Jiang","year":"2015","journal-title":"Free Radic. Biol. Med."},{"key":"ref_152","doi-asserted-by":"crossref","unstructured":"Ichimura, Y., and Komatsu, M. (2018). Activation of p62\/SQSTM1\u2013Keap1\u2013nuclear factor erythroid 2-related factor 2 pathway in cancer. Front. Oncol., 8.","DOI":"10.3389\/fonc.2018.00210"},{"key":"ref_153","first-page":"1412","article-title":"Curcumin Modulates p62\u2013Keap1\u2013Nrf2-Mediated Autophagy in Rotenone-Induced Parkinson\u2019s Disease Mouse Models","volume":"14","author":"Rathore","year":"2023","journal-title":"ACS Chem. Neurosci."},{"key":"ref_154","doi-asserted-by":"crossref","unstructured":"Xia, Q., Xie, J., Zhang, J., Zhang, L., Zhou, Y., Zhu, B., Wu, Y., Yang, Z., and Li, J. (2023). Ovatodiolide induces autophagy-mediated cell death through the p62-Keap1-Nrf2 signaling pathway in chronic myeloid leukemia cells. Chem.-Biol. Interact., 387.","DOI":"10.1016\/j.cbi.2023.110819"},{"key":"ref_155","doi-asserted-by":"crossref","unstructured":"Hennig, P., Fenini, G., Filippo, M.D., Karakaya, T., and Beer, H. (2021). The Pathways Underlying the Multiple Roles of p62 in Inflammation and Cancer. Biomedicines, 9.","DOI":"10.3390\/biomedicines9070707"},{"key":"ref_156","doi-asserted-by":"crossref","unstructured":"Glorieux, C., Enr\u00edquez, C., Gonz\u00e1lez, C.D., Aguirre-Mart\u00ednez, G.V., and Calder\u00f3n, P.B. (2024). The Multifaceted Roles of NRF2 in Cancer: Friend or Foe?. Antioxidants, 13.","DOI":"10.3390\/antiox13010070"},{"key":"ref_157","doi-asserted-by":"crossref","unstructured":"Li, W., Cao, J., Zhang, Y., Ling, G., Tan, N., Wei, Y., Zhang, Y., Wang, X., Qian, W., and Jiang, J. (2024). Aucubin alleviates doxorubicin-induced cardiotoxicity through crosstalk between NRF2 and HIPK2 mediating autophagy and apoptosis. Phytomedicine, 127.","DOI":"10.1016\/j.phymed.2024.155473"},{"key":"ref_158","doi-asserted-by":"crossref","unstructured":"Wang, Y., Mandal, A., Son, Y., Pratheeshkumar, P., Wise, J., Wang, L., Zhang, Z., Shi, X., and Chen, Z. (2018). Roles of ROS, Nrf2, and autophagy in cadmium-carcinogenesis and its prevention by sulforaphane. Toxicol. Appl. Pharmacol., 353.","DOI":"10.1016\/j.taap.2018.06.003"},{"key":"ref_159","doi-asserted-by":"crossref","unstructured":"Guo, Y., Yu, S., Zhang, C., and Kong, A.T. (2015). Epigenetic regulation of Keap1-Nrf2 signaling. Free Radic. Biol. Med., 88.","DOI":"10.1016\/j.freeradbiomed.2015.06.013"},{"key":"ref_160","doi-asserted-by":"crossref","unstructured":"Kim, Y.-J., Lee, H.-H., Jung, Y.-H., Han, K.-H., and Han, J.-M. (2026). The Roles of SQSTM1\/p62 in Selective Autophagy and Oncogenic Signaling. Int. J. Mol. Sci., 27.","DOI":"10.3390\/ijms27052342"},{"key":"ref_161","doi-asserted-by":"crossref","unstructured":"Shi, Y., Norberg, E., and Vakifahmetoglu-Norberg, H. (2021). Mutant p53 as a Regulator and Target of Autophagy. Front. Oncol., 10.","DOI":"10.3389\/fonc.2020.607149"},{"key":"ref_162","doi-asserted-by":"crossref","unstructured":"Yang, Y., Karsli-Uzunbas, G., Poillet-Perez, L., Sawant, A., Hu, Z., Zhao, Y., Moore, D., Hu, W., and White, E. (2020). Autophagy promotes mammalian survival by suppressing oxidative stress and p53. Genes Dev., 34.","DOI":"10.1101\/gad.335570.119"},{"key":"ref_163","first-page":"85","article-title":"P53-regulated autophagy and its impact on drug resistance and cell fate","volume":"4","author":"Shim","year":"2021","journal-title":"Cancer Drug Resist."},{"key":"ref_164","doi-asserted-by":"crossref","unstructured":"Mrakovcic, M., and Fr\u00f6hlich, L.F. (2018). p53-Mediated Molecular Control of Autophagy in Tumor Cells. Biomolecules, 8.","DOI":"10.3390\/biom8020014"},{"key":"ref_165","doi-asserted-by":"crossref","unstructured":"Xia, Z., Kon, N., Gu, A.P., Tavana, O., and Gu, W. (2022). Deciphering the acetylation code of p53 in transcription regulation and tumor suppression. Oncogene, 41.","DOI":"10.1038\/s41388-022-02331-9"},{"key":"ref_166","doi-asserted-by":"crossref","unstructured":"Ghate, N.B., Kim, S., Mehmood, R., Shin, Y., Kim, K., and An, W. (2023). VprBP\/DCAF1 regulates p53 function and stability through site-specific phosphorylation. Oncogene, 42.","DOI":"10.1038\/s41388-023-02685-8"},{"key":"ref_167","doi-asserted-by":"crossref","unstructured":"Marei, H.E., Althani, A., Afifi, N., Hasan, A., Caceci, T., Pozzoli, G., Morrione, A., Giordano, A., and Cenciarelli, C. (2021). p53 signaling in cancer progression and therapy. Cancer Cell Int., 21.","DOI":"10.1186\/s12935-021-02396-8"},{"key":"ref_168","doi-asserted-by":"crossref","unstructured":"Kruiswijk, F., Labuschagne, C.F., and Vousden, K.H. (2015). p53 in survival, death and metabolic health: A lifeguard with a licence to kill. Nat. Rev. Mol. Cell Biol., 16.","DOI":"10.1038\/nrm4007"},{"key":"ref_169","doi-asserted-by":"crossref","unstructured":"Eriksson, S., Ceder, S., Bykov, V.J.N., and Wiman, K.G. (2019). p53 as a hub in cellular redox regulation and therapeutic target in cancer. J. Mol. Cell Biol., 11.","DOI":"10.1093\/jmcb\/mjz005"},{"key":"ref_170","doi-asserted-by":"crossref","unstructured":"Zhong, Y., Le, F., Cheng, J., Luo, C., Zhang, X., Wu, X., Xu, F., Zuo, Q., and Tan, B. (2021). Triptolide inhibits JAK2\/STAT3 signaling and induces lethal autophagy through ROS generation in cisplatin-resistant SKOV3\/DDP ovarian cancer cells. Oncol. Rep., 45.","DOI":"10.3892\/or.2021.8020"},{"key":"ref_171","doi-asserted-by":"crossref","unstructured":"Liang, F., Ren, C., Wang, J., Wang, S., Yang, L., Han, X., Chen, Y., Tong, G., and Yang, G. (2019). The crosstalk between STAT3 and p53\/RAS signaling controls cancer cell metastasis and cisplatin resistance via the Slug\/MAPK\/PI3K\/AKT-mediated regulation of EMT and autophagy. Oncogenesis, 8.","DOI":"10.1038\/s41389-019-0165-8"},{"key":"ref_172","doi-asserted-by":"crossref","unstructured":"Sarapultsev, A., Gusev, E., Komelkova, M., Utepova, I.A., Luo, S., and Hu, D. (2023). JAK-STAT signaling in inflammation and stress-related diseases: Implications for therapeutic interventions. Mol. Biomed., 4.","DOI":"10.1186\/s43556-023-00151-1"},{"key":"ref_173","doi-asserted-by":"crossref","unstructured":"Tolomeo, M., and Cascio, A. (2021). The Multifaced Role of STAT3 in Cancer and Its Implication for Anticancer Therapy. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22020603"},{"key":"ref_174","doi-asserted-by":"crossref","unstructured":"Remy, J., Linder, B., Weirauch, U., Day, B.W., Stringer, B.W., Herold-Mende, C., Aigner, A., Krohn, K., and K\u00f6gel, D. (2022). STAT3 enhances sensitivity of glioblastoma to drug-induced autophagy-dependent cell death. Cancers, 14.","DOI":"10.3390\/cancers14020339"},{"key":"ref_175","first-page":"415","article-title":"Direct interaction between STAT3 and EIF2AK2 controls fatty acid-induced autophagy","volume":"9","author":"Shen","year":"2012","journal-title":"Autophagy"},{"key":"ref_176","doi-asserted-by":"crossref","unstructured":"Kim, S., Saeidi, S., Cho, N.-C., Kim, S.H., Lee, H., Han, W., Noh, D.Y., and Surh, Y.J. (2020). Interaction of Nrf2 with dimeric STAT3 induces IL-23 expression: Implications for breast cancer progression. Cancer Lett., 500.","DOI":"10.1016\/j.canlet.2020.11.047"},{"key":"ref_177","doi-asserted-by":"crossref","unstructured":"Iqbal, M.J., Kabeer, A., Abbas, Z., Siddiqui, H.A., C\u0103lina, D., Sharifi-Rad, J., and Cho, W.C. (2024). Interplay of oxidative stress, cellular communication and signaling pathways in cancer. Cell Commun. Signal., 22.","DOI":"10.1186\/s12964-023-01398-5"},{"key":"ref_178","doi-asserted-by":"crossref","unstructured":"Avalle, L., Camporeale, A., Camperi, A., and Poli, V. (2017). STAT3 in cancer: A double edged sword. Cytokine, 98.","DOI":"10.1016\/j.cyto.2017.03.018"},{"key":"ref_179","doi-asserted-by":"crossref","unstructured":"Laribee, R.N., Boucher, A., Madireddy, S., and Pfeffer, L.M. (2023). The STAT3-Regulated Autophagy Pathway in Glioblastoma. Pharmaceuticals, 16.","DOI":"10.3390\/ph16050671"},{"key":"ref_180","doi-asserted-by":"crossref","unstructured":"You, L., Wang, Z., Li, H., Shou, J., Zhao, J., Xie, J.-J., Sui, X., Pan, H., and Han, W. (2015). The role of STAT3 in autophagy. Autophagy, 11.","DOI":"10.1080\/15548627.2015.1017192"},{"key":"ref_181","unstructured":"Sorrentino, D. (2020). Role and Regulation of Autophagy in ALK Positive Cancers. [Ph.D. Thesis, HAL (Le Centre pour la Communication Scientifique Directe)]."},{"key":"ref_182","doi-asserted-by":"crossref","unstructured":"Xu, J., Zhang, J., Mao, Q., Wu, J., and Wang, Y. (2022). The Interaction Between Autophagy and JAK\/STAT3 Signaling Pathway in Tumors. Front. Genet., 13.","DOI":"10.3389\/fgene.2022.880359"},{"key":"ref_183","doi-asserted-by":"crossref","unstructured":"To\u0161i\u0107, I., and Frank, D.A. (2021). STAT3 as a mediator of oncogenic cellular metabolism: Pathogenic and therapeutic implications. Neoplasia, 23.","DOI":"10.1016\/j.neo.2021.10.003"},{"key":"ref_184","doi-asserted-by":"crossref","unstructured":"Guo, X., Hong, S., He, H., Zeng, Y., Chen, Y., Mo, X., Li, J., Li, L., Steinmetz, R., and Liu, Q. (2020). NF\u03baB promotes oxidative stress-induced necrosis and ischemia\/reperfusion injury by inhibiting Nrf2-ARE pathway. Free Radic. Biol. Med., 159.","DOI":"10.1016\/j.freeradbiomed.2020.07.031"},{"key":"ref_185","doi-asserted-by":"crossref","unstructured":"Kanamoto, M., Tsuchiya, Y., Nakao, Y., Suzuki, T., Motohashi, H., Yamamoto, M., and Kamata, H. (2018). Structural instability of I\u03baB kinase \u03b2 promotes autophagic degradation through enhancement of Keap1 binding. PLoS ONE, 13.","DOI":"10.1101\/407429"},{"key":"ref_186","doi-asserted-by":"crossref","unstructured":"Lee, E., Kim, H., Choi, M.S., and Chang, J. (2021). Crosstalk between Autophagy and Inflammatory Processes in Cancer. Life, 11.","DOI":"10.3390\/life11090903"},{"key":"ref_187","doi-asserted-by":"crossref","unstructured":"Mao, H., Zhao, X., and Sun, S. (2025). NF-\u03baB in inflammation and cancer. Cell. Mol. Immunol., 22.","DOI":"10.1038\/s41423-025-01310-w"},{"key":"ref_188","doi-asserted-by":"crossref","unstructured":"Verzella, D., Pescatore, A., Capece, D., Vecchiotti, D., Ursini, M.V., Franzoso, G., Alesse, E., and Zazzeroni, F. (2020). Life, death, and autophagy in cancer: NF-\u03baB turns up everywhere. Cell Death Dis., 11.","DOI":"10.1038\/s41419-020-2399-y"},{"key":"ref_189","doi-asserted-by":"crossref","unstructured":"Vega-Rub\u00edn-de-Celis, S., Kinch, L.N., and Pe\u00f1a-Llopis, S. (2020). Regulation of Beclin 1-Mediated Autophagy by Oncogenic Tyrosine Kinases. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21239210"},{"key":"ref_190","doi-asserted-by":"crossref","unstructured":"Peng, X., Wang, Y., Li, H., Fan, J., Shen, J., Yu, X., Zhou, Y., and Mao, H. (2019). ATG5-mediated autophagy suppresses NF-\u03baB signaling to limit epithelial inflammatory response to kidney injury. Cell Death Dis., 10.","DOI":"10.1038\/s41419-019-1483-7"},{"key":"ref_191","doi-asserted-by":"crossref","unstructured":"Nandy, A., Lin, L., Velentzas, P.D., Wu, L.P., Baehrecke, E.H., and Silverman, N. (2018). The NF-\u03baB Factor Relish Regulates Atg1 Expression and Controls Autophagy. Cell Rep., 25.","DOI":"10.1016\/j.celrep.2018.10.076"},{"key":"ref_192","doi-asserted-by":"crossref","unstructured":"Zhang, Y., Guo, X., Yan, W., Chen, Y., Ke, M., Cheng, C., Zhu, X., Xue, W., Zhou, Q., and Zheng, L. (2017). ANGPTL8 negatively regulates NF-\u03baB activation by facilitating selective autophagic degradation of IKK\u03b3. Nat. Commun., 8.","DOI":"10.1038\/s41467-017-02355-w"},{"key":"ref_193","doi-asserted-by":"crossref","unstructured":"Hennig, P., Garstkiewicz, M., Grossi, S., Filippo, M.D., French, L.E., and Beer, H. (2018). The Crosstalk between Nrf2 and Inflammasomes. Int. J. Mol. Sci., 19.","DOI":"10.3390\/ijms19020562"},{"key":"ref_194","doi-asserted-by":"crossref","unstructured":"Pajares, M., Rojo, A.I., and Cuadrado, A. (2017). NRF2 controls proteostasis through the transcriptional regulation of autophagy. Free Radic. Biol. Med., 108.","DOI":"10.1016\/j.freeradbiomed.2017.04.172"},{"key":"ref_195","doi-asserted-by":"crossref","unstructured":"Yuan, S.C., She, D., Jiang, S., Deng, N., Peng, J., and Ma, L. (2024). Endoplasmic reticulum stress and therapeutic strategies in metabolic, neurodegenerative diseases and cancer. Mol. Med., 30.","DOI":"10.1186\/s10020-024-00808-9"},{"key":"ref_196","doi-asserted-by":"crossref","unstructured":"Hetz, C., Chevet, \u00c9., and Oakes, S.A. (2015). Proteostasis control by the unfolded protein response. Nat. Cell Biol., 17.","DOI":"10.1038\/ncb3184"},{"key":"ref_197","doi-asserted-by":"crossref","unstructured":"Bhattarai, K.R., Riaz, T.A., Kim, H., and Chae, H. (2021). The aftermath of the interplay between the endoplasmic reticulum stress response and redox signaling. Exp. Mol. Med., 53.","DOI":"10.1038\/s12276-021-00560-8"},{"key":"ref_198","doi-asserted-by":"crossref","unstructured":"Corazzari, M., Gagliardi, M., Fimia, G.M., and Piacentini, M. (2017). Endoplasmic Reticulum Stress, Unfolded Protein Response, and Cancer Cell Fate. Front. Oncol., 7.","DOI":"10.3389\/fonc.2017.00078"},{"key":"ref_199","first-page":"774","article-title":"Spatiotemporal activation of unfolded protein response by combined sonodynamic therapy and proteasome inhibition with bortezomib-conjugated TiN nanoparticles","volume":"61","author":"Yin","year":"2026","journal-title":"Bioact. Mater."},{"key":"ref_200","doi-asserted-by":"crossref","unstructured":"Wei, S., Zhang, N., Zhang, H., Chen, Z., Li, S., Wu, W., Liu, Z., Xia, Z., Luo, P., and Cheng, Q. (2026). Endoplasmic reticulum stress in disease pathogenesis: Its implications for therapy. Signal Transduct. Target. Ther., 11.","DOI":"10.1038\/s41392-026-02600-z"},{"key":"ref_201","doi-asserted-by":"crossref","unstructured":"Ong, G., Ragetli, R., Mnich, K., Doble, B.W., Kammouni, W., and Logue, S.E. (2024). IRE1 signaling increases PERK expression during chronic ER stress. Cell Death Dis., 15.","DOI":"10.1038\/s41419-024-06663-0"},{"key":"ref_202","doi-asserted-by":"crossref","unstructured":"Kopp, M.C., Larburu, N., Durairaj, V., Adams, C.J., and Ali, M.M.U. (2019). UPR proteins IRE1 and PERK switch BiP from chaperone to ER stress sensor. Nat. Struct. Mol. Biol., 26.","DOI":"10.1038\/s41594-019-0324-9"},{"key":"ref_203","doi-asserted-by":"crossref","unstructured":"Adams, C.J., Kopp, M.C., Larburu, N., Nowak, P.R., and Ali, M.M.U. (2019). Structure and Molecular Mechanism of ER Stress Signaling by the Unfolded Protein Response Signal Activator IRE1. Front. Mol. Biosci., 6.","DOI":"10.3389\/fmolb.2019.00011"},{"key":"ref_204","doi-asserted-by":"crossref","unstructured":"Daverkausen-Fischer, L., Draga, M., and Pr\u00f6ls, F. (2022). Regulation of Translation, Translocation, and Degradation of Proteins at the Membrane of the Endoplasmic Reticulum. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23105576"},{"key":"ref_205","doi-asserted-by":"crossref","unstructured":"Gonen, N., Sabath, N., Burge, C.B., and Shalgi, R. (2019). Widespread PERK-dependent repression of ER targets in response to ER stress. Sci. Rep., 9.","DOI":"10.1038\/s41598-019-38705-5"},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"4561","DOI":"10.7150\/ijms.120874","article-title":"Endoplasmic reticulum stress in cancer progression: A comprehensive review of its role and mechanisms","volume":"22","author":"Yu","year":"2025","journal-title":"Int. J. Med. Sci."},{"key":"ref_207","doi-asserted-by":"crossref","unstructured":"Luo, Q., Gao, X., Meng, P., Qi, X., Wang, W., Li, S., and Duan, L. (2025). Endoplasmic reticulum stress in non-small cell lung cancer: A review of therapeutic agents, mechanistic insights, and implications for therapy. Front. Cell Dev. Biol., 13.","DOI":"10.3389\/fcell.2025.1693023"},{"key":"ref_208","doi-asserted-by":"crossref","unstructured":"Bhat, T.A., Chaudhary, A.K., Kumar, S., O\u2019Malley, J., Inigo, J.R., Kumar, R., Yadav, N., and Chandra, D. (2016). Endoplasmic reticulum-mediated unfolded protein response and mitochondrial apoptosis in cancer. Biochim. Biophys. Acta (BBA) Rev. Cancer, 1867.","DOI":"10.1016\/j.bbcan.2016.12.002"},{"key":"ref_209","doi-asserted-by":"crossref","unstructured":"Xu, Y., Wang, C., Su, J., Xie, Q., Ma, L., Zeng, L., Yu, Y., Liu, S., Li, S., and Li, Z. (2015). Tolerance to endoplasmic reticulum stress mediates cisplatin resistance in human ovarian cancer cells by maintaining endoplasmic reticulum and mitochondrial homeostasis. Oncol. Rep., 34.","DOI":"10.3892\/or.2015.4283"},{"key":"ref_210","doi-asserted-by":"crossref","unstructured":"Hong, Y.H., Uddin, M.H., Jo, U., Kim, B., Song, J., Suh, D.H., Kim, H.S., and Song, Y.S. (2015). ROS accumulation by PEITC selectively kills ovarian cancer cells via UPR-mediated apoptosis. Front. Oncol., 5.","DOI":"10.3389\/fonc.2015.00167"},{"key":"ref_211","doi-asserted-by":"crossref","unstructured":"Zong, Y., Feng, S., Cheng, J.-W., Yu, C., and GuoCai, L. (2017). Up-Regulated ATF4 Expression Increases Cell Sensitivity to Apoptosis in Response to Radiation. Cell. Physiol. Biochem., 41.","DOI":"10.1159\/000458742"},{"key":"ref_212","doi-asserted-by":"crossref","unstructured":"Unal, B., and Saatcioglu, F. (2025). Targeting the unfolded protein response for cancer therapy: Mitigating tumor adaptation and immune suppression. Biomark. Res., 13.","DOI":"10.1186\/s40364-025-00813-y"},{"key":"ref_213","doi-asserted-by":"crossref","unstructured":"Flindris, S., Flindris, K., Foutadakis, S., Kalinderis, M., Traianos, A., Kigka, V.I., Nteka, F., Mpourazanis, G., Styliara, I., and Styliara, E. (2025). The role of endoplasmic reticulum stress and unfolded protein response in gynecological cancers: A narrative review. Cureus, 17.","DOI":"10.7759\/cureus.94434"},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"363","DOI":"10.21873\/cgp.20507","article-title":"The role of ER stress and the unfolded protein response in cancer","volume":"22","author":"Ghemrawi","year":"2025","journal-title":"Cancer Genom. Proteom."},{"key":"ref_215","doi-asserted-by":"crossref","unstructured":"Wiese, W., Siwecka, N., Wawrzynkiewicz, A., Rozp\u0119dek-Kami\u0144ska, W., Kucharska, E., and Majsterek, I. (2022). IRE1\u03b1 inhibitors as a promising therapeutic strategy in blood malignancies. Cancers, 14.","DOI":"10.3390\/cancers14102526"},{"key":"ref_216","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1182\/blood.V118.21.133.133","article-title":"Blockade of XBP1 splicing by inhibition of IRE1\u03b1 is a promising therapeutic option in multiple myeloma","volume":"118","author":"Mimura","year":"2011","journal-title":"Blood"},{"key":"ref_217","doi-asserted-by":"crossref","unstructured":"Mai, P.M.Q., Truong, T., Samala, S.K., Lakshmisha, B.M., Biswal, P., Koushki, K., Mallepaddi, P.C., Vijay, G., and Krishnan, S. (2025). The unfolded protein response\u2014Novel mechanisms, challenges, and key considerations for therapeutic intervention. Cancers, 17.","DOI":"10.3390\/cancers17223639"},{"key":"ref_218","doi-asserted-by":"crossref","unstructured":"Marfatiya, S., Mubariz, F., Pal, A., RoyChoudhuri, D., Mukherjee, S., Maharajan, N., Zalzman, M., and Banerjee, A. (2025). Targeting the unfolded protein response in cancer: Exploiting endoplasmic reticulum stress for therapeutic intervention. Biochem. Pharmacol., 242.","DOI":"10.1016\/j.bcp.2025.117221"},{"key":"ref_219","doi-asserted-by":"crossref","unstructured":"Taucher, E., Mykoliuk, I., Fediuk, M., and Smolle-J\u00fcttner, F. (2022). Autophagy, Oxidative Stress and Cancer Development. Cancers, 14.","DOI":"10.3390\/cancers14071637"},{"key":"ref_220","doi-asserted-by":"crossref","unstructured":"Catalani, E., Giovarelli, M., Zecchini, S., Perrotta, C., and Cervia, D. (2021). Oxidative Stress and Autophagy as Key Targets in Melanoma Cell Fate. Cancers, 13.","DOI":"10.3390\/cancers13225791"},{"key":"ref_221","doi-asserted-by":"crossref","unstructured":"Deng, J., Pan, T., Liu, Z., McCarthy, C., Vicencio, J.M., Cao, L., Alfano, G., Suwaidan, A.A., Yin, M., and Beatson, R. (2023). The role of TXNIP in cancer: A fine balance between redox, metabolic, and immunological tumor control. Br. J. Cancer, 129.","DOI":"10.1038\/s41416-023-02442-4"},{"key":"ref_222","doi-asserted-by":"crossref","unstructured":"Endale, H.T., Tesfaye, W., and Mengstie, T.A. (2023). ROS induced lipid peroxidation and their role in ferroptosis. Front. Cell Dev. Biol., 11.","DOI":"10.3389\/fcell.2023.1226044"},{"key":"ref_223","doi-asserted-by":"crossref","unstructured":"Wang, B., Wang, Y., Zhang, J., Hu, C., Jiang, J., Li, Y., and Peng, Z. (2023). ROS-induced lipid peroxidation modulates cell death outcome: Mechanisms behind apoptosis, autophagy, and ferroptosis. Arch. Toxicol., 97.","DOI":"10.1007\/s00204-023-03476-6"},{"key":"ref_224","doi-asserted-by":"crossref","unstructured":"Arfin, S., Jha, N.K., Jha, S.K., Kesari, K.K., Ruokolainen, J., Roychoudhury, S., Rathi, B., and Kumar, D. (2021). Oxidative Stress in Cancer Cell Metabolism. Antioxidants, 10.","DOI":"10.3390\/antiox10050642"},{"key":"ref_225","doi-asserted-by":"crossref","unstructured":"George, S.D., and Abrahamse, H. (2020). Redox Potential of Antioxidants in Cancer Progression and Prevention. Antioxidants, 9.","DOI":"10.3390\/antiox9111156"},{"key":"ref_226","doi-asserted-by":"crossref","unstructured":"Ren, Y., Wang, R., Weng, S., Xu, H., Zhang, Y., Chen, S., Liu, S., Ba, Y., Zhou, Z., and Luo, P. (2023). Multifaceted role of redox pattern in the tumor immune microenvironment regarding autophagy and apoptosis. Mol. Cancer, 22.","DOI":"10.1186\/s12943-023-01831-w"},{"key":"ref_227","doi-asserted-by":"crossref","unstructured":"Sies, H., and Jones, D.P. (2020). Reactive oxygen species (ROS) as pleiotropic physiological signalling agents. Nat. Rev. Mol. Cell Biol., 21.","DOI":"10.1038\/s41580-020-0230-3"},{"key":"ref_228","doi-asserted-by":"crossref","unstructured":"Sahu, M., and Jain, U. (2026). ROS-mediated therapeutic approach through oxidative stress and cell signalling modulation. Crit. Rev. Oncol. Hematol., 220.","DOI":"10.1016\/j.critrevonc.2026.105168"},{"key":"ref_229","doi-asserted-by":"crossref","unstructured":"Li, L., Tan, J., Miao, Y., Lei, P., and Zhang, Q. (2015). ROS and Autophagy: Interactions and Molecular Regulatory Mechanisms. Cell. Mol. Neurobiol., 35.","DOI":"10.1007\/s10571-015-0166-x"},{"key":"ref_230","doi-asserted-by":"crossref","unstructured":"He, J., Dong, L., Luo, L., and Wang, K. (2022). Redox Regulation of Autophagy in Cancer: Mechanism, Prevention and Therapy. Life, 13.","DOI":"10.3390\/life13010098"},{"key":"ref_231","doi-asserted-by":"crossref","unstructured":"Koundouros, N., and Poulogiannis, G. (2018). Phosphoinositide 3-Kinase\/Akt Signaling and Redox Metabolism in Cancer. Front. Oncol., 8.","DOI":"10.3389\/fonc.2018.00160"},{"key":"ref_232","doi-asserted-by":"crossref","unstructured":"Bae, T., Hallis, S.P., and Kwak, M. (2024). Hypoxia, oxidative stress, and the interplay of HIFs and NRF2 signaling in cancer. Exp. Mol. Med., 56.","DOI":"10.1038\/s12276-024-01180-8"},{"key":"ref_233","doi-asserted-by":"crossref","unstructured":"Kirtonia, A., Sethi, G., and Garg, M. (2020). The multifaceted role of reactive oxygen species in tumorigenesis. Cell. Mol. Life Sci., 77.","DOI":"10.1007\/s00018-020-03536-5"},{"key":"ref_234","doi-asserted-by":"crossref","unstructured":"Seebacher, N.A., Krchniakov\u00e1, M., Stacy, A.E., \u0160koda, J., and Jansson, P.J. (2021). Tumour Microenvironment Stress Promotes the Development of Drug Resistance. Antioxidants, 10.","DOI":"10.3390\/antiox10111801"},{"key":"ref_235","doi-asserted-by":"crossref","unstructured":"Wu, L., Zheng, H., Guo, X., Li, N., Qin, L., Li, X., and Lou, G. (2024). Integrative analyses of genes associated with oxidative stress and cellular senescence in triple-negative breast cancer. Heliyon, 10.","DOI":"10.1016\/j.heliyon.2024.e34524"},{"key":"ref_236","doi-asserted-by":"crossref","unstructured":"Aggarwal, V., Tuli, H.S., Varol, A., Thakral, F., Yerer, M.B., Sak, K., Varol, M., Jain, A., Khan, M.A., and Sethi, G. (2019). Role of Reactive Oxygen Species in Cancer Progression: Molecular Mechanisms and Recent Advancements. Biomolecules, 9.","DOI":"10.3390\/biom9110735"},{"key":"ref_237","doi-asserted-by":"crossref","unstructured":"Sun, C., Cao, D., Ren, Q., Zhang, S., Zhou, N., Mai, S., Feng, B., and Wang, H.Y. (2021). Combination Treatment With Inhibitors of ERK and Autophagy Enhances Antitumor Activity of Betulinic Acid in Non\u2013small-Cell Lung Cancer In Vivo and In Vitro. Front. Pharmacol., 12.","DOI":"10.3389\/fphar.2021.684243"},{"key":"ref_238","doi-asserted-by":"crossref","unstructured":"Hu, M., Yu, Z., Mei, P., Li, J., Luo, D., Zhang, H., Zhou, M., Liang, F., and Chen, R. (2020). Lycorine induces autophagy-associated apoptosis by targeting MEK2 and enhances vemurafenib activity in colorectal cancer. Aging, 12.","DOI":"10.2139\/ssrn.3403340"},{"key":"ref_239","doi-asserted-by":"crossref","unstructured":"Deng, L., Gao, X., Liu, B., He, X., Xu, J., Qiang, J., Wu, Q., and Liu, S. (2018). NMT1 inhibition modulates breast cancer progression through stress-triggered JNK pathway. Cell Death Dis., 9.","DOI":"10.1038\/s41419-018-1201-x"},{"key":"ref_240","doi-asserted-by":"crossref","unstructured":"Slobodnyuk, K., Radic, N., Ivanova, S., Llad\u00f3, A., Trempolec, N., Zorzano, A., and Nebreda, A.R. (2019). Autophagy-induced senescence is regulated by p38\u03b1 signaling. Cell Death Dis., 10.","DOI":"10.1038\/s41419-019-1607-0"},{"key":"ref_241","doi-asserted-by":"crossref","unstructured":"Menon, M., and Dhamija, S. (2018). Beclin 1 Phosphorylation\u2014At the Center of Autophagy Regulation. Front. Cell Dev. Biol., 6.","DOI":"10.3389\/fcell.2018.00137"},{"key":"ref_242","doi-asserted-by":"crossref","unstructured":"Ge, D., Tao, H., Fang, L., Kong, X., Han, L., Li, N., Xu, Y.X., Li, L.Y., Yu, M., and Zhang, H. (2020). 11-Methoxytabersonine Induces Necroptosis with Autophagy through AMPK\/mTOR and JNK Pathways in Human Lung Cancer Cells. Chem. Pharm. Bull., 68.","DOI":"10.1248\/cpb.c19-00851"},{"key":"ref_243","doi-asserted-by":"crossref","unstructured":"Ma, Q., Long, S., Gan, Z., Tettamanti, G., Li, K., and Tian, L. (2022). Transcriptional and Post-Transcriptional Regulation of Autophagy. Cells, 11.","DOI":"10.3390\/cells11030441"},{"key":"ref_244","doi-asserted-by":"crossref","unstructured":"Sansa, A., Miralles, M.P., Beltran, M., Nos, F.C., Calder\u00f3, J., Garcer\u00e1, A., and Soler, R.M. (2023). ERK MAPK signaling pathway inhibition as a potential target to prevent autophagy alterations in Spinal Muscular Atrophy motoneurons. Cell Death Discov., 9.","DOI":"10.1038\/s41420-023-01409-x"},{"key":"ref_245","doi-asserted-by":"crossref","unstructured":"C\u00e1novas, B., and Nebreda, \u00c1.R. (2021). Diversity and versatility of p38 kinase signalling in health and disease. Nat. Rev. Mol. Cell Biol., 22.","DOI":"10.1038\/s41580-020-00322-w"},{"key":"ref_246","doi-asserted-by":"crossref","unstructured":"Pua, L.J.W., Mai, C., Chung, F.F., Khoo, A.S.B., Leong, C., Lim, W.M., and Hii, L.W. (2022). Functional Roles of JNK and p38 MAPK Signaling in Nasopharyngeal Carcinoma. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23031108"},{"key":"ref_247","doi-asserted-by":"crossref","unstructured":"Nishimura, T., and Tooze, S.A. (2020). Emerging roles of ATG proteins and membrane lipids in autophagosome formation. Cell Discov., 6.","DOI":"10.1038\/s41421-020-0161-3"},{"key":"ref_248","doi-asserted-by":"crossref","unstructured":"She, H., He, Y., Zhao, S., and Mao, Z. (2018). Autophagy in Inflammation: The p38\u03b1 MAPK-ULK1 Axis. Macrophage, 4.","DOI":"10.14800\/macrophage.1629"},{"key":"ref_249","doi-asserted-by":"crossref","unstructured":"Patergnani, S., Danese, A., Bouhamida, E., Aguiari, G., Previati, M., Pinton, P., and Giorgi, C. (2020). Various Aspects of Calcium Signaling in the Regulation of Apoptosis, Autophagy, Cell Proliferation, and Cancer. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21218323"},{"key":"ref_250","doi-asserted-by":"crossref","unstructured":"Kania, E., Roest, G., Vervliet, T., Parys, J.B., and Bultynck, G. (2017). IP3 Receptor-Mediated Calcium Signaling and Its Role in Autophagy in Cancer. Front. Oncol., 7.","DOI":"10.3389\/fonc.2017.00140"},{"key":"ref_251","doi-asserted-by":"crossref","unstructured":"Sun, F., Xu, X., Wang, X., and Zhang, B. (2016). Regulation of autophagy by Ca2+. Tumor Biol., 37.","DOI":"10.1007\/s13277-016-5353-y"},{"key":"ref_252","doi-asserted-by":"crossref","unstructured":"Chiu, W., Chang, H.-A., Lin, Y.-H., Lin, Y.-S., Chang, H.-T., Lin, H.H., Huang, S.C., Tang, M.J., and Shen, M.R. (2018). Bcl-2 regulates store-operated Ca2+ entry to modulate ER stress-induced apoptosis. Cell Death Discov., 4.","DOI":"10.1038\/s41420-018-0039-4"},{"key":"ref_253","doi-asserted-by":"crossref","unstructured":"Marchi, S., Patergnani, S., Missiroli, S., Morciano, G., Rimessi, A., Wi\u0119ckowski, M.R., Giorgi, C., and Pinton, P. (2017). Mitochondrial and endoplasmic reticulum calcium homeostasis and cell death. Cell Calcium, 69.","DOI":"10.1016\/j.ceca.2017.05.003"},{"key":"ref_254","doi-asserted-by":"crossref","unstructured":"Genovese, I., Vezzani, B., Danese, A., Modesti, L., Vitto, V.A.M., Corazzi, V., Pelucchi, S., Pinton, P., and Giorgi, C. (2020). Mitochondria as the decision makers for cancer cell fate: From signaling pathways to therapeutic strategies. Cell Calcium, 92.","DOI":"10.1016\/j.ceca.2020.102308"},{"key":"ref_255","doi-asserted-by":"crossref","unstructured":"Dejos, C., Gkika, D., and Cantelmo, A.R. (2020). The Two-Way Relationship Between Calcium and Metabolism in Cancer. Front. Cell Dev. Biol., 8.","DOI":"10.3389\/fcell.2020.573747"},{"key":"ref_256","doi-asserted-by":"crossref","unstructured":"Kuchay, S., Giorgi, C., Simoneschi, D., Pagan, J.K., Missiroli, S., Saraf, A., Florens, L., Washburn, M.P., Collazo-Lorduy, A., and Castillo-Martin, M. (2017). PTEN counteracts FBXL2 to promote IP3R3- and Ca2+-mediated apoptosis limiting tumour growth. Nature, 546.","DOI":"10.1038\/nature22965"},{"key":"ref_257","doi-asserted-by":"crossref","unstructured":"Mangla, A., Guerra, M.T., and Nathanson, M.H. (2019). Type 3 inositol 1,4,5-trisphosphate receptor: A calcium channel for all seasons. Cell Calcium, 85.","DOI":"10.1016\/j.ceca.2019.102132"},{"key":"ref_258","doi-asserted-by":"crossref","unstructured":"Sassano, M.L., van Vliet, A.R., and Agostinis, P. (2017). Mitochondria-Associated Membranes As Networking Platforms and Regulators of Cancer Cell Fate. Front. Oncol., 7.","DOI":"10.3389\/fonc.2017.00174"},{"key":"ref_259","doi-asserted-by":"crossref","unstructured":"C\u00e1rdenas, C., Lovy, A., Silva-Pavez, E., Urra, F.A., Mizzoni, C., Ahumada-Castro, U., Bustos, G., Ja\u0148a, F., Cruz, P., and Farias, P. (2020). Cancer cells with defective oxidative phosphorylation require endoplasmic reticulum\u2013to\u2013mitochondria Ca 2+ transfer for survival. Sci. Signal., 13.","DOI":"10.1126\/scisignal.aay1212"},{"key":"ref_260","doi-asserted-by":"crossref","unstructured":"Madreiter-Sokolowski, C.T., Gottschalk, B., Sokolowski, A., Malli, R., and Graier, W.F. (2021). Dynamic Control of Mitochondrial Ca2+ Levels as a Survival Strategy of Cancer Cells. Front. Cell Dev. Biol., 9.","DOI":"10.3389\/fcell.2021.614668"},{"key":"ref_261","doi-asserted-by":"crossref","unstructured":"Chen, Q., Lei, J.H., Bao, J., Wang, H., Hao, W., Li, L., Peng, C., Masuda, T., Miao, K., and Xu, J. (2020). BRCA1 Deficiency Impairs Mitophagy and Promotes Inflammasome Activation and Mammary Tumor Metastasis. Adv. Sci., 7.","DOI":"10.1002\/advs.201903616"},{"key":"ref_262","doi-asserted-by":"crossref","unstructured":"Yu, H., Sun, C., Gong, Q., and Feng, D. (2021). Mitochondria-Associated Endoplasmic Reticulum Membranes in Breast Cancer. Front. Cell Dev. Biol., 9.","DOI":"10.3389\/fcell.2021.629669"},{"key":"ref_263","doi-asserted-by":"crossref","unstructured":"Chaikovsky, A.C., Li, C., Jeng, E.E., Loebell, S., Lee, M.C., Murray, C.W., Cheng, R., Demeter, J., Swaney, D.L., and Chen, S.H. (2021). The AMBRA1 E3 ligase adaptor regulates the stability of cyclin D. Nature, 592.","DOI":"10.1038\/s41586-021-03474-7"},{"key":"ref_264","doi-asserted-by":"crossref","unstructured":"Peruzzo, R., Costa, R., Bachmann, M., Leanza, L., and Szab\u00f3, I. (2020). Mitochondrial Metabolism, Contact Sites and Cellular Calcium Signaling: Implications for Tumorigenesis. Cancers, 12.","DOI":"10.3390\/cancers12092574"},{"key":"ref_265","doi-asserted-by":"crossref","unstructured":"Yan, S., Zhou, N., Zhang, D., Zhang, K., Zheng, W., Bao, Y., and Yang, W. (2019). PFKFB3 Inhibition Attenuates Oxaliplatin-Induced Autophagy and Enhances Its Cytotoxicity in Colon Cancer Cells. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20215415"},{"key":"ref_266","doi-asserted-by":"crossref","unstructured":"Missiroli, S., Bonora, M., Patergnani, S., and Giorgi, C. (2017). Novel function of the tumor suppressor PML at ER-mitochondria sites in the control of autophagy. Oncotarget, 8.","DOI":"10.18632\/oncotarget.18974"},{"key":"ref_267","doi-asserted-by":"crossref","unstructured":"Wu, Y., Huang, P., and Dong, X. (2021). Lysosomal Calcium Channels in Autophagy and Cancer. Cancers, 13.","DOI":"10.3390\/cancers13061299"},{"key":"ref_268","doi-asserted-by":"crossref","unstructured":"Santoni, G., Santoni, M., Maggi, F., Marinelli, O., and Morelli, M.B. (2020). Emerging Role of Mucolipins TRPML Channels in Cancer. Front. Oncol., 10.","DOI":"10.3389\/fonc.2020.00659"},{"key":"ref_269","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.bcp.2014.12.018","article-title":"Cancer-type-specific crosstalk between autophagy, necroptosis and apoptosis as a pharmacological target","volume":"94","author":"Radogna","year":"2015","journal-title":"Biochem. Pharmacol."},{"key":"ref_270","doi-asserted-by":"crossref","unstructured":"Guam\u00e1n-Ortiz, L.M., Orellana, M., and Ratovitski, E.A. (2017). Natural Compounds As Modulators of Non-apoptotic Cell Death in Cancer Cells. Curr. Genom., 18.","DOI":"10.2174\/1389202917666160803150639"},{"key":"ref_271","doi-asserted-by":"crossref","unstructured":"Xiao, M., Benoit, A., Hasmim, M., Duhem, C., Vogin, G., Berchem, G., Noman, M.Z., and Janji, B. (2021). Targeting Cytoprotective Autophagy to Enhance Anticancer Therapies. Front. Oncol., 11.","DOI":"10.3389\/fonc.2021.626309"},{"key":"ref_272","doi-asserted-by":"crossref","unstructured":"Harrath, A.H., Jalouli, M., Al-Zharani, M., and Rahman, A. (2026). Recent Update Targeting Autophagy-Apoptosis Crosstalk Using Bioactive Natural Products for Ovarian Cancer Treatment. Biomedicines, 14.","DOI":"10.3390\/biomedicines14010212"},{"key":"ref_273","doi-asserted-by":"crossref","unstructured":"Rahman, A., Hannan, A., Dash, R., Rahman, H., Islam, R., Uddin, J., Sohag, A.A.M., Rahman, H., and Rhim, H. (2021). Phytochemicals as a Complement to Cancer Chemotherapy: Pharmacological Modulation of the Autophagy-Apoptosis Pathway. Front. Pharmacol., 12.","DOI":"10.3389\/fphar.2021.639628"},{"key":"ref_274","unstructured":"Mosoh, D.A. (2024). Recent Advances in Phytochemical Research for Cancer Treatment. Biochemistry, IntechOpen."},{"key":"ref_275","doi-asserted-by":"crossref","unstructured":"Patra, S., Pradhan, B., Nayak, R., Behera, C., Panda, K.C., Das, S., Jena, M., and Bhutia, S.K. (2021). Apoptosis and autophagy modulating dietary phytochemicals in cancer therapeutics: Current evidences and future perspectives. Phytother. Res., 35.","DOI":"10.1002\/ptr.7082"},{"key":"ref_276","doi-asserted-by":"crossref","unstructured":"Achi, I.T., Sarbadhikary, P., George, B.P., and Abrahamse, H. (2022). Multi-Target Potential of Berberine as an Antineoplastic and Antimetastatic Agent: A Special Focus on Lung Cancer Treatment. Cells, 11.","DOI":"10.3390\/cells11213433"},{"key":"ref_277","doi-asserted-by":"crossref","unstructured":"Haasler, L., Kondadi, A.K., Tsigaras, T., von Montfort, C., Graf, P., Stahl, W., and Brenneisen, P. (2021). The BH3 mimetic (\u00b1) gossypol induces ROS-independent apoptosis and mitochondrial dysfunction in human A375 melanoma cells in vitro. Arch. Toxicol., 95.","DOI":"10.1007\/s00204-021-02987-4"},{"key":"ref_278","doi-asserted-by":"crossref","unstructured":"Lu, J., He, R., Liu, Y., Zhang, J., Xu, H., Zhang, T., Chen, L., Yang, G., Zhang, J., and Liu, J. (2024). Exploiting cell death and tumor immunity in cancer therapy: Challenges and future directions. Front. Cell Dev. Biol., 12.","DOI":"10.3389\/fcell.2024.1416115"},{"key":"ref_279","doi-asserted-by":"crossref","unstructured":"Jin, X., Tang, J., Qiu, X., Nie, X., Ou, S.-H.I., Wu, G., Zhang, R., and Zhu, J. (2024). Ferroptosis: Emerging mechanisms, biological function, and therapeutic potential in cancer and inflammation. Cell Death Discov., 10.","DOI":"10.1038\/s41420-024-01825-7"},{"key":"ref_280","doi-asserted-by":"crossref","unstructured":"Hajj, S.E., Canabady-Rochelle, L., and Gaucher, C. (2023). Nature-Inspired Bioactive Compounds: A Promising Approach for Ferroptosis-Linked Human Diseases?. Molecules, 28.","DOI":"10.3390\/molecules28062636"},{"key":"ref_281","doi-asserted-by":"crossref","unstructured":"Zhang, Y., and Xie, J. (2024). Targeting ferroptosis regulators by natural products in colorectal cancer. Front. Pharmacol., 15.","DOI":"10.3389\/fphar.2024.1374722"},{"key":"ref_282","doi-asserted-by":"crossref","unstructured":"Talebi, M., Shahbazi, K., Dakkali, M.S., Akbari, M., Ghale, R.A., Hashemi, S., Sashourpour, M., Mojab, F., and Aminzadeh, S. (2025). Phytosomes: A promising nanocarrier system for enhanced bioavailability and therapeutic efficacy of herbal products. Phytomed. Plus, 5.","DOI":"10.1016\/j.phyplu.2025.100779"},{"key":"ref_283","doi-asserted-by":"crossref","unstructured":"Li, L., Jin, P., Guan, Y., Luo, M., Wang, Y., He, B., Li, B., He, K., Cao, J., and Huang, C. (2022). Exploiting Polyphenol-Mediated Redox Reorientation in Cancer Therapy. Pharmaceuticals, 15.","DOI":"10.3390\/ph15121540"},{"key":"ref_284","doi-asserted-by":"crossref","unstructured":"Petsri, K., Thongsom, S., Racha, S., Chamni, S., Jindapol, S., Kaekratoke, N., Zou, H., and Chanvorachote, P. (2022). Novel mechanism of napabucasin, a naturally derived furanonaphthoquinone: Apoptosis and autophagy induction in lung cancer cells through direct targeting on Akt\/mTOR proteins. BMC Complement. Med. Ther., 22.","DOI":"10.1186\/s12906-022-03727-6"},{"key":"ref_285","first-page":"5964","article-title":"Tetrahydrocurcumin-induced autophagy via suppression of PI3K\/Akt\/mTOR in non-small cell lung carcinoma cells","volume":"17","author":"Song","year":"2018","journal-title":"Mol. Med. Rep."},{"key":"ref_286","doi-asserted-by":"crossref","unstructured":"Yang, W., Liu, J., Hou, L., Chen, Q., and Liu, Y. (2020). Shikonin differentially regulates glucose metabolism via PKM2 and HIF1\u03b1 to overcome apoptosis in a refractory HCC cell line. Life Sci., 265.","DOI":"10.1016\/j.lfs.2020.118796"},{"key":"ref_287","doi-asserted-by":"crossref","unstructured":"Shuvalov, O., Kirdeeva, Y., Daks, A., Fedorova, O., Parfenyev, S., Simon, H., and Barlev, N.A. (2023). Phytochemicals Target Multiple Metabolic Pathways in Cancer. Antioxidants, 12.","DOI":"10.3390\/antiox12112012"},{"key":"ref_288","doi-asserted-by":"crossref","unstructured":"Li, X., Cheng, X., Wu, J., Wu, K., and Liu, T. (2024). Targeted inhibition of the PI3K\/AKT\/mTOR pathway by (+)-anthrabenzoxocinone induces cell cycle arrest, apoptosis, and autophagy in non-small cell lung cancer. Cell. Mol. Biol. Lett., 29.","DOI":"10.1186\/s11658-024-00578-6"},{"key":"ref_289","doi-asserted-by":"crossref","unstructured":"Ivanova, H., Kerkhofs, M., Rovere, R.M.L., and Bultynck, G. (2017). Endoplasmic Reticulum\u2013Mitochondrial Ca2+ Fluxes Underlying Cancer Cell Survival. Front. Oncol., 7.","DOI":"10.3389\/fonc.2017.00070"},{"key":"ref_290","doi-asserted-by":"crossref","unstructured":"Chen, P., Wu, Q., Feng, J., Yan, L., Sun, Y., Liu, S., Xiang, Y., Zhang, M., Pan, T., and Chen, X. (2020). Erianin, a novel dibenzyl compound in Dendrobium extract, inhibits lung cancer cell growth and migration via calcium\/calmodulin-dependent ferroptosis. Signal Transduct. Target. Ther., 5.","DOI":"10.1038\/s41392-020-0149-3"},{"key":"ref_291","doi-asserted-by":"crossref","unstructured":"Xie, Q., Chen, Y., Tan, H., Liu, B., Zheng, L., and Mu, Y. (2021). Targeting Autophagy with Natural Compounds in Cancer: A Renewed Perspective from Molecular Mechanisms to Targeted Therapy. Front. Pharmacol., 12.","DOI":"10.3389\/fphar.2021.748149"},{"key":"ref_292","doi-asserted-by":"crossref","unstructured":"El-Baba, C., Baassiri, A., Kiriako, G., Dia, B., Fadlallah, S., Moodad, S., and Darwiche, N. (2021). Terpenoids\u2019 anti-cancer effects: Focus on autophagy. Apoptosis, 26.","DOI":"10.1007\/s10495-021-01684-y"},{"key":"ref_293","doi-asserted-by":"crossref","unstructured":"Ye, F., Dewanjee, S., Li, Y., Jha, N.K., Chen, Z., Kumar, A., Behl, T., Jha, S.K., and Tang, H. (2023). Advancements in clinical aspects of targeted therapy and immunotherapy in breast cancer. Mol. Cancer, 22.","DOI":"10.1186\/s12943-023-01805-y"},{"key":"ref_294","doi-asserted-by":"crossref","unstructured":"Fu, L., Han, B., Zhou, Y., Ren, J., Cao, W., Patel, G., Kai, G., and Zhang, J. (2020). The Anticancer Properties of Tanshinones and the Pharmacological Effects of Their Active Ingredients. Front. Pharmacol., 11.","DOI":"10.3389\/fphar.2020.00193"},{"key":"ref_295","doi-asserted-by":"crossref","unstructured":"Yoo, H., Kim, J.M., Jo, E., Cho, C.-K., Lee, S.-Y., Kang, H.S., Lee, M.G., Yang, P.Y., and Jang, I.S. (2017). Modified Panax ginseng extract regulates autophagy by AMPK signaling in A549 human lung cancer cells. Oncol. Rep., 37.","DOI":"10.3892\/or.2017.5590"},{"key":"ref_296","doi-asserted-by":"crossref","unstructured":"Chen, L., Meng, Y., Sun, Q., Zhang, Z., Guo, X., Sheng, X., Tai, G., Cheng, H., and Zhou, Y. (2016). Ginsenoside compound K sensitizes human colon cancer cells to TRAIL-induced apoptosis via autophagy-dependent and -independent DR5 upregulation. Cell Death Dis., 7.","DOI":"10.1038\/cddis.2016.234"},{"key":"ref_297","doi-asserted-by":"crossref","unstructured":"Giansanti, L., Condello, M., Altieri, B., Galantini, L., Meschini, S., and Mancini, G. (2019). Influence of lipid composition on the ability of liposome loaded voacamine to improve the reversion of doxorubicin resistant osteosarcoma cells. Chem. Phys. Lipids, 223.","DOI":"10.1016\/j.chemphyslip.2019.05.006"},{"key":"ref_298","doi-asserted-by":"crossref","unstructured":"Liou, J., Lin, C., Liao, Y.-C., Ho, L., Yang, S.-P., and Lai, J.-H. (2017). JNK\/AP-1 activation contributes to tetrandrine resistance in T-cell acute lymphoblastic leukaemia. Acta Pharmacol. Sin., 38.","DOI":"10.1038\/aps.2017.26"},{"key":"ref_299","doi-asserted-by":"crossref","unstructured":"Liu, T., Liu, X., and Li, W. (2016). Tetrandrine, a Chinese plant-derived alkaloid, is a potential candidate for cancer chemotherapy. Oncotarget, 7.","DOI":"10.18632\/oncotarget.8315"},{"key":"ref_300","doi-asserted-by":"crossref","unstructured":"Li, C., Wang, Y., Wang, C., Yi, X., Ming-ya, L., and He, X. (2017). Anticancer activities of harmine by inducing a pro-death autophagy and apoptosis in human gastric cancer cells. Phytomedicine, 28.","DOI":"10.1016\/j.phymed.2017.02.008"},{"key":"ref_301","doi-asserted-by":"crossref","unstructured":"Mielcke, T.R., Murad\u00e1s, T.C., Filippi\u2013Chiela, E.C., Amaral, M.E.A., Kist, L.W., Bogo, M.R., Mascarello, A., Neuenfeldt, P.D., Nunes, R.J., and Campos, M.M. (2017). Mechanisms underlying the antiproliferative effects of a series of quinoxaline-derived chalcones. Sci. Rep., 7.","DOI":"10.1038\/s41598-017-16199-3"},{"key":"ref_302","doi-asserted-by":"crossref","unstructured":"Qin, R., You, F., Zhao, Q., Xie, X., Peng, C., Zhan, G., and Han, B. (2022). Naturally derived indole alkaloids targeting regulated cell death (RCD) for cancer therapy: From molecular mechanisms to potential therapeutic targets. J. Hematol. Oncol., 15.","DOI":"10.1186\/s13045-022-01371-8"},{"key":"ref_303","doi-asserted-by":"crossref","unstructured":"An, G., Park, J., Song, J., Hong, T., Song, G., and Lim, W. (2024). Relevance of the endoplasmic reticulum-mitochondria axis in cancer diagnosis and therapy. Exp. Mol. Med., 56.","DOI":"10.1038\/s12276-023-01137-3"},{"key":"ref_304","doi-asserted-by":"crossref","unstructured":"Sui, X., Han, X., Chen, P., Wu, Q., Feng, J., Duan, T., Chen, X., Pan, T., Yan, L., and Jin, T. (2021). Baicalin Induces Apoptosis and Suppresses the Cell Cycle Progression of Lung Cancer Cells Through Downregulating Akt\/mTOR Signaling Pathway. Front. Mol. Biosci., 7.","DOI":"10.3389\/fmolb.2020.602282"},{"key":"ref_305","doi-asserted-by":"crossref","unstructured":"Wang, F., Mao, Y., You, Q., Hua, D., and Cai, D. (2015). Piperlongumine induces apoptosis and autophagy in human lung cancer cells through inhibition of PI3K\/Akt\/mTOR pathway. Int. J. Immunopathol. Pharmacol., 28.","DOI":"10.1177\/0394632015598849"},{"key":"ref_306","doi-asserted-by":"crossref","unstructured":"Zhao, L., Liu, S., Xu, J., Li, W., Duan, G., Wang, H., Yang, H., Yang, Z., and Zhou, R. (2017). A new molecular mechanism underlying the EGCG-mediated autophagic modulation of AFP in HepG2 cells. Cell Death Dis., 8.","DOI":"10.1038\/cddis.2017.563"},{"key":"ref_307","doi-asserted-by":"crossref","unstructured":"Huang, K., Chen, Y., Zhang, R., Wu, Y., Ma, Y., Fang, X., and Shen, S. (2018). Honokiol induces apoptosis and autophagy via the ROS\/ERK1\/2 signaling pathway in human osteosarcoma cells in vitro and in vivo. Cell Death Dis., 9.","DOI":"10.1038\/s41419-017-0166-5"},{"key":"ref_308","doi-asserted-by":"crossref","unstructured":"Lee, H., Park, B.-S., Kang, H., Kim, J., Shin, S., and Kim, I. (2021). Role of Luteolin-Induced Apoptosis and Autophagy in Human Glioblastoma Cell Lines. Medicina, 57.","DOI":"10.3390\/medicina57090879"},{"key":"ref_309","doi-asserted-by":"crossref","unstructured":"Bai, L., Wu, Q., Zhang, X., and Zhao, Y. (2023). Autosis as a selective type of cell death. Front. Cell Dev. Biol., 11.","DOI":"10.3389\/fcell.2023.1164681"},{"key":"ref_310","doi-asserted-by":"crossref","unstructured":"Deng, S., Shanmugam, M.K., Kumar, A.P., Yap, C.T., Sethi, G., and Bishayee, A. (2019). Targeting autophagy using natural compounds for cancer prevention and therapy. Cancer, 125.","DOI":"10.1002\/cncr.31978"},{"key":"ref_311","doi-asserted-by":"crossref","unstructured":"Wang, J., Qi, Q., Feng, Z., Zhang, X., Huang, B., Chen, A., Prestegarden, L., Li, X., and Wang, J. (2016). Berberine induces autophagy in glioblastoma by targeting the AMPK\/mTOR\/ULK1-pathway. Oncotarget, 7.","DOI":"10.18632\/oncotarget.11396"},{"key":"ref_312","doi-asserted-by":"crossref","unstructured":"Holczer, M., Hajd\u00fa, B., L\u0151rincz, T., Szarka, A., B\u00e1nhegyi, G., and Kapuy, O. (2020). Fine-tuning of AMPK\u2013ULK1\u2013mTORC1 regulatory triangle is crucial for autophagy oscillation. Sci. Rep., 10.","DOI":"10.1038\/s41598-020-75030-8"},{"key":"ref_313","doi-asserted-by":"crossref","unstructured":"Musia\u0142, C., Siedlecka-Kroplewska, K., Kmie\u0107, Z., and G\u00f3rska-Ponikowska, M. (2021). Modulation of Autophagy in Cancer Cells by Dietary Polyphenols. Antioxidants, 10.","DOI":"10.3390\/antiox10010123"},{"key":"ref_314","doi-asserted-by":"crossref","unstructured":"Zheng, W., Xie, W., Yin, D., Luo, R., Liu, M., and Guo, F. (2019). ATG5 and ATG7 induced autophagy interplays with UPR via PERK signaling. Cell Commun. Signal., 17.","DOI":"10.1186\/s12964-019-0353-3"},{"key":"ref_315","doi-asserted-by":"crossref","unstructured":"Lin, Y., Jiang, M., Chen, W., Zhao, T., and Wei, Y. (2019). Cancer and ER stress: Mutual crosstalk between autophagy, oxidative stress and inflammatory response. Biomed. Pharmacother., 118.","DOI":"10.1016\/j.biopha.2019.109249"},{"key":"ref_316","doi-asserted-by":"crossref","unstructured":"Rong, L., Wang, R., Zheng, X., Feng, X., Zhang, L., Zhang, L., Zhang, L., Lin, Y., Li, Z.P., and Wang, X. (2017). Combination of wogonin and sorafenib effectively kills human hepatocellular carcinoma cells through apoptosis potentiation and autophagy inhibition. Oncol. Lett., 13.","DOI":"10.3892\/ol.2017.6059"},{"key":"ref_317","doi-asserted-by":"crossref","unstructured":"Wang, H., Li, J., Kan, W., Xu, G., Luo, G., Song, N., Wu, W.B., Feng, B., Fu, J.F., and Tu, Y.T. (2023). Chloroquine enhances the efficacy of chemotherapy drugs against acute myeloid leukemia by inactivating the autophagy pathway. Acta Pharmacol. Sin., 44.","DOI":"10.1038\/s41401-023-01112-8"},{"key":"ref_318","doi-asserted-by":"crossref","unstructured":"Zhang, Z., Zhou, L., Xie, N., Nice, E.C., Zhang, T., Cui, Y., and Huang, C. (2020). Overcoming cancer therapeutic bottleneck by drug repurposing. Signal Transduct. Target. Ther., 5.","DOI":"10.1038\/s41392-020-00213-8"},{"key":"ref_319","doi-asserted-by":"crossref","unstructured":"Liu, X., Sun, K., Wang, H., and Dai, Y. (2016). Inhibition of Autophagy by Chloroquine Enhances the Antitumor Efficacy of Sorafenib in Glioblastoma. Cell. Mol. Neurobiol., 36.","DOI":"10.1007\/s10571-015-0318-z"},{"key":"ref_320","doi-asserted-by":"crossref","unstructured":"Kriel, J., M\u00fcller-Nedebock, K.K., Maarman, G.J., Mbizana, S., Ojuka, E.O., Klumperman, B., and Loos, B. (2018). Coordinated autophagy modulation overcomes glioblastoma chemoresistance through disruption of mitochondrial bioenergetics. Sci. Rep., 8.","DOI":"10.1038\/s41598-018-28590-9"},{"key":"ref_321","doi-asserted-by":"crossref","unstructured":"Lernia, G.D., Leone, P., Solimando, A.G., Buonavoglia, A., Saltarella, I., Ria, R., Ditonno, P., Silvestris, N., Crudele, L., and Vacca, A. (2020). Bortezomib Treatment Modulates Autophagy in Multiple Myeloma. J. Clin. Med., 9.","DOI":"10.3390\/jcm9020552"},{"key":"ref_322","doi-asserted-by":"crossref","unstructured":"Yamamoto, K., Iwadate, D., Kato, H., Nakai, Y., Tateishi, K., and Fujishiro, M. (2022). Targeting autophagy as a therapeutic strategy against pancreatic cancer. J. Gastroenterol., 57.","DOI":"10.1007\/s00535-022-01889-1"},{"key":"ref_323","doi-asserted-by":"crossref","unstructured":"He, K., Chen, M., Liu, J., Du, S., Ren, C., and Zhang, J. (2024). Nanomedicine for cancer targeted therapy with autophagy regulation. Front. Immunol., 14.","DOI":"10.3389\/fimmu.2023.1238827"},{"key":"ref_324","doi-asserted-by":"crossref","unstructured":"Yang, Q., Gao, L., Huang, X., Weng, J., Chen, Y., Lin, S., and Yin, Q. (2021). Sorafenib prevents the proliferation and induces the apoptosis of liver cancer cells by regulating autophagy and hypoxia-inducible factor-1. Exp. Ther. Med., 22.","DOI":"10.3892\/etm.2021.10412"},{"key":"ref_325","doi-asserted-by":"crossref","unstructured":"Salama, B.M., Helmy, M.W., Fouad, H., Shamaa, M.M., and Houssen, M.E. (2023). The Synergistic Antitumor Effect of Decitabine and Vorinostat Combination on HepG2 Human Hepatocellular Carcinoma Cell Line via Epigenetic Modulation of Autophagy\u2013Apoptosis Molecular Crosstalk. Curr. Issues Mol. Biol., 45.","DOI":"10.3390\/cimb45070375"},{"key":"ref_326","doi-asserted-by":"crossref","unstructured":"Sun, T., Liu, H., and Ming, L. (2017). Multiple Roles of Autophagy in the Sorafenib Resistance of Hepatocellular Carcinoma. Cell. Physiol. Biochem., 44.","DOI":"10.1159\/000485285"},{"key":"ref_327","doi-asserted-by":"crossref","unstructured":"Qian, H., Shi, Z., Zhu, H., Gu, L., Wang, X., and Yang, Y. (2017). Interplay between apoptosis and autophagy in colorectal cancer. Oncotarget, 8.","DOI":"10.18632\/oncotarget.18663"},{"key":"ref_328","doi-asserted-by":"crossref","unstructured":"Inamura, S., Ito, H., Taga, M., Tsuchiyama, K., Hoshino, H., Kobayashi, M., and Yokoyama, O. (2019). Low-dose Docetaxel Enhanced the Anticancer Effect of Temsirolimus by Overcoming Autophagy in Prostate Cancer Cells. Anticancer Res., 39.","DOI":"10.21873\/anticanres.13735"},{"key":"ref_329","doi-asserted-by":"crossref","unstructured":"Rahman, M.A., Engelsen, A.S.T., Sarowar, S., Bindesb\u00f8ll, C., Birkeland, E., Goplen, D., Lotsberg, M.L., Knappskog, S., Simonsen, A., and Chekenya, M. (2022). Bortezomib abrogates temozolomide-induced autophagic flux through an ATG5 dependent pathway. Front. Cell Dev. Biol., 10.","DOI":"10.3389\/fcell.2022.1022191"},{"key":"ref_330","doi-asserted-by":"crossref","unstructured":"Zhuang, L., Ma, Y., Wang, Q., Zhang, J., Zhu, C., Zhang, L., and Xu, X. (2016). Atg3 Overexpression Enhances Bortezomib-Induced Cell Death in SKM-1 Cell. PLoS ONE, 11.","DOI":"10.1371\/journal.pone.0158761"},{"key":"ref_331","first-page":"1883","article-title":"Momelotinib sensitizes glioblastoma cells to temozolomide by enhancement of autophagy via JAK2\/STAT3 inhibition","volume":"41","author":"Liu","year":"2019","journal-title":"Oncol. Rep."},{"key":"ref_332","doi-asserted-by":"crossref","unstructured":"Pandey, V., Ranjan, N., Narne, P., and Babu, P.P. (2019). Roscovitine effectively enhances antitumor activity of temozolomide in vitro and in vivo mediated by increased autophagy and Caspase-3 dependent apoptosis. Sci. Rep., 9.","DOI":"10.1038\/s41598-019-41380-1"},{"key":"ref_333","doi-asserted-by":"crossref","unstructured":"Rangwala, R., Chang, Y.C., Hu, J., Algazy, K.M., Evans, T.L., Fecher, L.A., Schuchter, L.M., Torigian, D.A., Panosian, J.T., and Troxel, A.B. (2014). Combined MTOR and autophagy inhibition. Autophagy, 10.","DOI":"10.4161\/auto.29119"},{"key":"ref_334","doi-asserted-by":"crossref","unstructured":"Cao, Y., Chen, M., Tang, D., Yan, H., Ding, X., Zhou, F., Zhang, M., Xu, G., Zhang, W., and Zhang, S. (2018). The proton pump inhibitor pantoprazole disrupts protein degradation systems and sensitizes cancer cells to death under various stresses. Cell Death Dis., 9.","DOI":"10.1038\/s41419-018-0642-6"},{"key":"ref_335","doi-asserted-by":"crossref","unstructured":"Rangwala, R., Leone, R.D., Chang, Y.C., Fecher, L.A., Schuchter, L.M., Kramer, A., Tan, K.S., Heitjan, D.F., Rodgers, G., and Gallagher, M. (2014). Phase I trial of hydroxychloroquine with dose-intense temozolomide in patients with advanced solid tumors and melanoma. Autophagy, 10.","DOI":"10.4161\/auto.29118"},{"key":"ref_336","doi-asserted-by":"crossref","unstructured":"Fan, Y., Chiu, J., Liu, J., Deng, Y., Xu, C., Zhang, J., and Li, G. (2018). Resveratrol induces autophagy-dependent apoptosis in HL-60 cells. BMC Cancer, 18.","DOI":"10.1186\/s12885-018-4504-5"},{"key":"ref_337","doi-asserted-by":"crossref","unstructured":"Liu, T., Zhang, J., Li, K., Deng, L., and Wang, H. (2020). Combination of an Autophagy Inducer and an Autophagy Inhibitor: A Smarter Strategy Emerging in Cancer Therapy. Front. Pharmacol., 11.","DOI":"10.3389\/fphar.2020.00408"},{"key":"ref_338","doi-asserted-by":"crossref","unstructured":"Kozalak, G., and Ko\u015far, A. (2023). Autophagy-related mechanisms for treatment of multiple myeloma. Cancer Drug Resist., 6.","DOI":"10.20517\/cdr.2023.108"},{"key":"ref_339","doi-asserted-by":"crossref","unstructured":"Salimi, A., Schroeder, K.M., Schemionek, M., Vieri, M., Maletzke, S., Gezer, D., Masouleh, B.K., and Appelmann, I. (2022). Targeting autophagy increases the efficacy of proteasome inhibitor treatment in multiple myeloma by induction of apoptosis and activation of JNK. BMC Cancer, 22.","DOI":"10.1186\/s12885-022-09775-y"},{"key":"ref_340","doi-asserted-by":"crossref","unstructured":"Wang, Y., Han, C., Lu, L., Magliato, S., and Wu, T. (2013). Hedgehog Signaling Pathway Regulates Autophagy in Human Hepatocellular Carcinoma Cells. Hepatology, 58.","DOI":"10.1002\/hep.26394"},{"key":"ref_341","doi-asserted-by":"crossref","unstructured":"Kolour, H.R., Bahrami, N., Mojarad, E.N., Sadeghi, A., Shamsara, M., and Fatemi, N. (2025). Metformin\u2019s multifaceted role in colorectal cancer: Mechanisms of action and synergy with standard treatments. Discov. Oncol., 16.","DOI":"10.1007\/s12672-025-03905-1"},{"key":"ref_342","doi-asserted-by":"crossref","unstructured":"Zhao, Z., Yu, Z.-Y., Li, J., and Ouyang, X. (2016). Gefitinib induces lung cancer cell autophagy and apoptosis via blockade of the PI3K\/AKT\/mTOR pathway. Oncol. Lett., 12.","DOI":"10.3892\/ol.2016.4606"},{"key":"ref_343","doi-asserted-by":"crossref","unstructured":"Dragowska, W.H., Weppler, S.A., Wang, J.C., Wong, L.Y., Kapanen, A.I., Rawji, J.S., Warburton, C., Qadir, M.A., Donohue, E., and Roberge, M. (2013). Induction of Autophagy Is an Early Response to Gefitinib and a Potential Therapeutic Target in Breast Cancer. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0076503"},{"key":"ref_344","doi-asserted-by":"crossref","unstructured":"Ho, J., Byun, S., Kim, D.H., Ryu, H., and Lee, S. (2024). Dasatinib induces apoptosis and autophagy by suppressing the PI3K\/Akt\/mTOR pathway in bladder cancer cells. Investig. Clin. Urol., 65.","DOI":"10.4111\/icu.20240250"},{"key":"ref_345","doi-asserted-by":"crossref","unstructured":"Lee, H., Mustafa, A., Hudes, G.R., and Kruger, W.D. (2015). Hydroxychloroquine Destabilizes Phospho-S6 in Human Renal Carcinoma Cells. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0131464"},{"key":"ref_346","doi-asserted-by":"crossref","unstructured":"Haas, N.B., Appleman, L.J., Stein, M.N., Redlinger, M., Wilks, M., Xu, X., Onorati, A., Kalavacharla, A., Kim, T., and Zhen, C.J. (2019). Autophagy Inhibition to Augment mTOR Inhibition: A Phase I\/II Trial of Everolimus and Hydroxychloroquine in Patients with Previously Treated Renal Cell Carcinoma. Clin. Cancer Res., 25.","DOI":"10.1158\/1078-0432.CCR-18-2204"},{"key":"ref_347","doi-asserted-by":"crossref","unstructured":"Cordani, M., and Somoza, \u00c1. (2018). Targeting autophagy using metallic nanoparticles: A promising strategy for cancer treatment. Cell. Mol. Life Sci., 76.","DOI":"10.1007\/s00018-018-2973-y"},{"key":"ref_348","doi-asserted-by":"crossref","unstructured":"Rachamala, H.K., Madamsetty, V.S., Angom, R.S., Nakka, N.M.R., Dutta, S.K., Wang, E., Mukhopadhyay, D., and Pal, K. (2024). Targeting mTOR and survivin concurrently potentiates radiation therapy in renal cell carcinoma by suppressing DNA damage repair and amplifying mitotic catastrophe. J. Exp. Clin. Cancer Res., 43.","DOI":"10.1186\/s13046-024-03079-8"}],"container-title":["Cancers"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2072-6694\/18\/10\/1564\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,5,12]],"date-time":"2026-05-12T13:01:45Z","timestamp":1778590905000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2072-6694\/18\/10\/1564"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,5,12]]},"references-count":348,"journal-issue":{"issue":"10","published-online":{"date-parts":[[2026,5]]}},"alternative-id":["cancers18101564"],"URL":"https:\/\/doi.org\/10.3390\/cancers18101564","relation":{},"ISSN":["2072-6694"],"issn-type":[{"value":"2072-6694","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,5,12]]}}}