Programmed Cell Death in Cancer

Abstract

Cancer remains the most lethal disease globally, despite the significant progress made in early screening, surgery, and therapeutic development in recent decades. Programmed cell death (PCD) is a genetically regulated process essential for eliminating aberrant cells, yet its dysregulation drives tumorigenesis and therapy resistance. In this review, we present a complete discovery timeline of them and comprehensively synthesize the roles and mechanisms of major PCD forms, such as apoptosis, necroptosis, autophagy, pyroptosis, ferroptosis, and cuproptosis, across diverse cancer types. We not only detail the molecular mechanisms, dual functions, and alterations of these PCD modalities in cancers, but also summarize their interconnections and intrinsic crosstalk. Furthermore, we comprehensively discuss how diverse therapies, including chemotherapy, radiotherapy, immunotherapy, targeted agents, and hormone therapy, engage and manipulate specific PCD pathways, revealing the involvement of PCD in cancer treatment mechanisms. This review integrates extensive preclinical and clinical evidence on PCD-targeted therapies with an in-depth focus on ferroptosis, including its regulatory networks and therapeutic relevance. Special emphasis is placed on prostate cancer, highlighting the PCD-based translational opportunities in this common malignancy. Taken together, we provide novel insights into the complex interplay between PCD and cancer biology and offer a framework for developing precision oncology therapies.

Keywords

anticancer therapy / cancer / ferroptosis / programmed cell death / prostate cancer

References

[1] G. S. Kopeina and B. Zhivotovsky, “Programmed Cell Death: Past, Present and Future,” Biochemical and Biophysical Research Communications 633 (2022): 55-58.

[2] L. Galluzzi, I. Vitale, S. A. Aaronson, et al., “Molecular Mechanisms of Cell Death: Recommendations of the Nomenclature Committee on Cell Death,” Cell Death and Differentiation 25, no. 3 (2018): 486-541.

[3] P. Tsvetkov, S. Coy, B. Petrova, et al., “Copper Induces Cell Death by Targeting Lipoylated TCA Cycle Proteins,” Science 375, no. 6586 (2022): 1254-1261.

[4] W. Fu, J. Wang, T. Li, et al., “Persistent Activation of TRPM4 Triggers Necrotic Cell Death Characterized by Sodium Overload,” Nature Chemical Biology 21, no. 8 (2025): 1238-1249.

[5] X. Liu, L. Nie, Y. Zhang, et al., “Actin Cytoskeleton Vulnerability to Disulfide Stress Mediates Disulfidptosis,” Nature Cell Biology 25, no. 3 (2023): 404-414.

[6] J. Yuan and D. Ofengeim, “A Guide to Cell Death Pathways,” Nature Reviews Molecular Cell Biology 25, no. 5 (2024): 379-395.

[7] S. K. Yu, J. Yang, Q. Zhang, T. Yu, and K. H. Lu, “A Novel Signature Based on Twelve Programmed Cell Death Patterns to Predict the Prognosis of Lung Adenocarcinoma,” American Journal of Translational Research 16, no. 5 (2024): 2082-2102.

[8] L. Zhang and M. Peng, “Integrated Bioinformatic Analysis Identified a Novel Prognostic Pan-programmed Cell Death Signature for Bladder Cancer,” Frontiers in Immunology 13 (2022): 1030097.

[9] S. Bedoui, M. J. Herold, and A. Strasser, “Emerging Connectivity of Programmed Cell Death Pathways and Its Physiological Implications,” Nature Reviews Molecular Cell Biology 21, no. 11 (2020): 678-695.

[10] M. Wang, F. Yu, Y. Zhang, and P. Li, “Programmed Cell Death in Tumor Immunity: Mechanistic Insights and Clinical Implications,” Frontiers in Immunology 14 (2023): 1309635.

[11] A. P. Mishra, B. Salehi, M. Sharifi-Rad, et al., “Programmed Cell Death, From a Cancer Perspective: An Overview,” Molecular Diagnosis & Therapy 22, no. 3 (2018): 281-295.

[12] K. Cao, J. Zhu, M. Lu, et al., “Analysis of Multiple Programmed Cell Death-related Prognostic Genes and Functional Validations of Necroptosis-associated Genes in Oesophageal Squamous Cell Carcinoma,” EBioMedicine 99 (2024): 104920.

[13] J. Gao, A. Xiong, J. Liu, et al., “PANoptosis: Bridging Apoptosis, Pyroptosis, and Necroptosis in Cancer Progression and Treatment,” Cancer Gene Therapy 31, no. 7 (2024): 970-983.

[14] S. Maitra, D. Bhattacharya, S. Paul, et al., “Programmed Cell Death Protein 1 (PD-1) in Relation to PANoptosis: Immune Pharmacological Targets for Management of Breast Adenocarcinoma,” Endocrine, Metabolic & Immune Disorders Drug Targets 23, no. 13 (2023): 1571-1585.

[15] H. Li, Y. Sun, Y. Yao, et al., “USP8-governed GPX4 Homeostasis Orchestrates Ferroptosis and Cancer Immunotherapy,” PNAS 121, no. 16 (2024): e2315541121.

[16] F. Yang, Y. Xiao, J. H. Ding, et al., “Ferroptosis Heterogeneity in Triple-negative Breast Cancer Reveals an Innovative Immunotherapy Combination Strategy,” Cell Metabolism 35, no. 1 (2023): 84-100.e108.

[17] L. Zhao, X. Zhou, F. Xie, et al., “Ferroptosis in Cancer and Cancer Immunotherapy,” Cancer communications (London) 42, no. 2 (2022): 88-116.

[18] M. Wu, Q. Huang, Y. Xie, et al., “Improvement of the Anticancer Efficacy of PD-1/PD-L1 Blockade via Combination Therapy and PD-L1 Regulation,” Journal of Hematology & Oncology 15, no. 1 (2022): 24.

[19] Y. Zhang and Z. Zhang, “The History and Advances in Cancer Immunotherapy: Understanding the Characteristics of Tumor-infiltrating Immune Cells and Their Therapeutic Implications,” Cellular & Molecular Immunology 17, no. 8 (2020): 807-821.

[20] K. Hänggi and B. Ruffell, “Cell Death, Therapeutics, and the Immune Response in Cancer,” Trends in Cancer 9, no. 5 (2023): 381-396.

[21] X. Chen, R. Kang, G. Kroemer, and D. Tang, “Broadening Horizons: The Role of Ferroptosis in Cancer,” Nature Reviews Clinical Oncology 18, no. 5 (2021): 280-296.

[22] Z. Su, Z. Yang, Y. Xu, Y. Chen, and Q. Yu, “Apoptosis, Autophagy, Necroptosis, and Cancer Metastasis,” Molecular Cancer 14 (2015): 48.

[23] P. R. Nepali and N. Kyprianou, “Anoikis in Phenotypic Reprogramming of the Prostate Tumor Microenvironment,” Frontiers in Endocrinology (Lausanne) 14 (2023): 1160267.

[24] J. Song, R. Xu, H. Zhang, et al., “Cell-in-Cell-Mediated Entosis Reveals a Progressive Mechanism in Pancreatic Cancer,” Gastroenterology 165, no. 6 (2023): 1505-1521.e1520.

[25] S. K. Hsu, C. Y. Li, I. L. Lin, et al., “Inflammation-related Pyroptosis, a Novel Programmed Cell Death Pathway, and Its Crosstalk With Immune Therapy in Cancer Treatment,” Theranostics 11, no. 18 (2021): 8813-8835.

[26] Y. Zhou, L. Liu, S. Tao, et al., “Parthanatos and Its Associated Components: Promising Therapeutic Targets for Cancer,” Pharmacological Research 163 (2021): 105299.

[27] P. Zheng, C. Zhou, Y. Ding, and S. Duan, “Disulfidptosis: A New Target for Metabolic Cancer Therapy,” Journal of Experimental & Clinical Cancer Research 42, no. 1 (2023): 103.

[28] D. Tang, G. Kroemer, and R. Kang, “Targeting Cuproplasia and Cuproptosis in Cancer,” Nature Reviews Clinical Oncology 21, no. 5 (2024): 370-388.

[29] J. F. Kerr, A. H. Wyllie, and A. R. Currie, “Apoptosis: A Basic Biological Phenomenon With Wide-ranging Implications in Tissue Kinetics,” British Journal of Cancer 26, no. 4 (1972): 239-257.

[30] X. Xu, Y. Lai, and Z. C. Hua, “Apoptosis and Apoptotic Body: Disease Message and Therapeutic Target Potentials,” Bioscience Reports 39, no. 1 (2019): BSR20180992.

[31] J. F. Kerr and J. Searle, “Deletion of Cells by Apoptosis During Castration-induced Involution of the Rat Prostate,” Virchows Archiv B: Cell Pathology 13, no. 2 (1973): 87-102.

[32] J. Searle, D. J. Collins, B. Harmon, and J. F. Kerr, “The Spontaneous Occurrence of Apoptosis in Squamous Carcinomas of the Uterine Cervix,” Pathology 5, no. 2 (1973): 163-169.

[33] A. Young, W. Bu, W. Jiang, et al., “Targeting the Pro-survival Protein BCL-2 to Prevent Breast Cancer,” Cancer Prevention Research (Philadelphia, Pa) 15, no. 1 (2022): 3-10.

[34] Y. G. Lee, P. Guruprasad, G. Ghilardi, et al., “Modulation of BCL-2 in both T Cells and Tumor Cells to Enhance Chimeric Antigen Receptor T-cell Immunotherapy Against Cancer,” Cancer Discovery 12, no. 10 (2022): 2372-2391.

[35] S. Chen, Y. Ren, and P. Duan, “Biomimetic Nanoparticle Loading Obatoclax Mesylate for the Treatment of Non-small-cell Lung Cancer (NSCLC) Through Suppressing Bcl-2 Signaling,” Biomedicine & Pharmacotherapy 129 (2020): 110371.

[36] J. Sun, J. Piao, N. Li, Y. Yang, K. Y. Kim, and Z. Lin, “Valproic Acid Targets HDAC1/2 and HDAC1/PTEN/Akt Signalling to Inhibit Cell Proliferation via the Induction of Autophagy in Gastric Cancer,” The FEBS Journal 287, no. 10 (2020): 2118-2133.

[37] A. M. Pesch, B. C. Chandler, A. R. Michmerhuizen, et al., “Bcl-xL Inhibition Radiosensitizes PIK3CA/PTEN Wild-type Triple Negative Breast Cancers With Low Mcl-1 Expression,” Cancer Research Communications 2, no. 7 (2022): 679-693.

[38] I. Guccini, A. Revandkar, M. D'Ambrosio, et al., “Senescence Reprogramming by TIMP1 Deficiency Promotes Prostate Cancer Metastasis,” Cancer Cell 39, no. 1 (2021): 68-82.e69.

[39] L. Trabzonlu, I. Kulac, Q. Zheng, et al., “Molecular Pathology of High-Grade Prostatic Intraepithelial Neoplasia: Challenges and Opportunities,” Cold Spring Harbor Perspectives in Medicine 9, no. 4 (2019): a030403.

[40] M. C. Haffner and C. E. Barbieri, “Shifting Paradigms for High-grade Prostatic Intraepithelial Neoplasia,” European Urology 69, no. 5 (2016): 831-833.

[41] M. I. Johnson, M. C. Robinson, C. Marsh, C. N. Robson, D. E. Neal, and F. C. Hamdy, “Expression of Bcl-2, Bax, and p53 in High-grade Prostatic Intraepithelial Neoplasia and Localized Prostate Cancer: Relationship With Apoptosis and Proliferation,” Prostate 37, no. 4 (1998): 223-229.

[42] S. Baspinar, S. Bircan, H. Orhan, N. Kapucuoglu, and K. K. Bozkurt, “The Relation of Beclin 1 and Bcl-2 Expressions in High Grade Prostatic Intraepithelial Neoplasia and Prostate Adenocarcinoma: A Tissue Microarray Study,” Pathology, Research and Practice 210, no. 7 (2014): 412-418.

[43] D. A. Bax, J. Haringsma, A. W. Einerhand, et al., “MUC4 is Increased in High Grade Intraepithelial Neoplasia in Barrett's Oesophagus and is Associated With a Proapoptotic Bax to Bcl-2 Ratio,” Journal of Clinical Pathology 57, no. 12 (2004): 1267-1272.

[44] V. R. Litle, J. D. Leavenworth, T. M. Darragh, et al., “Angiogenesis, Proliferation, and Apoptosis in Anal High-grade Squamous Intraepithelial Lesions,” Diseases of the Colon and Rectum 43, no. 3 (2000): 346-352.

[45] S. Heimer, G. Knoll, K. Schulze-Osthoff, and M. Ehrenschwender, “Raptinal Bypasses BAX, BAK, and BOK for Mitochondrial Outer Membrane Permeabilization and Intrinsic Apoptosis,” Cell Death & Disease 10, no. 8 (2019): 556.

[46] A. Safi, E. Heidarian, and R. Ahmadi, “Quercetin Synergistically Enhances the Anticancer Efficacy of Docetaxel Through Induction of Apoptosis and Modulation of PI3K/AKT, MAPK/ERK, and JAK/STAT3 Signaling Pathways in MDA-MB-231 Breast Cancer Cell Line,” International Journal of Molecular and Cellular Medicine 10, no. 1 (2021): 11-22.

[47] S. Shukla, P. Fu, and S. Gupta, “Apigenin Induces Apoptosis by Targeting Inhibitor of Apoptosis Proteins and Ku70-Bax Interaction in Prostate Cancer,” Apoptosis 19, no. 5 (2014): 883-894.

[48] J. Duo, G. G. Ying, G. W. Wang, and L. Zhang, “Quercetin Inhibits human Breast Cancer Cell Proliferation and Induces Apoptosis via Bcl-2 and Bax Regulation,” Molecular Medicine Reports 5, no. 6 (2012): 1453-1456.

[49] S. von Karstedt, A. Montinaro, and H. Walczak, “Exploring the TRAILs Less Travelled: TRAIL in Cancer Biology and Therapy,” Nature Reviews Cancer 17, no. 6 (2017): 352-366.

[50] H. Lai, D. Zeng, C. Liu, Q. Zhang, X. Wang, and T. Chen, “Selenium-containing Ruthenium Complex Synergizes With Natural Killer Cells to Enhance Immunotherapy Against Prostate Cancer via Activating TRAIL/FasL Signaling,” Biomaterials 219 (2019): 119377.

[51] S. Y. Tung, K. C. Lee, K. F. Lee, et al., “Apoptotic Mechanisms of Gastric Cancer Cells Induced by Isolated Erinacine S Through Epigenetic Histone H3 Methylation of FasL and TRAIL,” Food & Function 12, no. 8 (2021): 3455-3468.

[52] A. Rossin, G. Miloro, and A. O. Hueber, “TRAIL and FasL Functions in Cancer and Autoimmune Diseases: Towards an Increasing Complexity,” Cancers (Basel) 11, no. 5 (2019): 639.

[53] A. Degterev, Z. Huang, M. Boyce, et al., “Chemical Inhibitor of Nonapoptotic Cell Death With Therapeutic Potential for Ischemic Brain Injury,” Nature Chemical Biology 1, no. 2 (2005): 112-119.

[54] T. Vanden Berghe, A. Linkermann, S. Jouan-Lanhouet, H. Walczak, and P. Vandenabeele, “Regulated Necrosis: The Expanding Network of Non-apoptotic Cell Death Pathways,” Nature Reviews Molecular Cell Biology 15, no. 2 (2014): 135-147.

[55] D. Ma, X. Wang, J. Liu, Y. Cui, S. Luo, and F. Wang, “The Development of Necroptosis: What We Can Learn,” Cell Stress & Chaperones 28, no. 6 (2023): 969-987.

[56] K. Ye, Z. Chen, and Y. Xu, “The Double-edged Functions of Necroptosis,” Cell Death & Disease 14, no. 2 (2023): 163.

[57] P. Lin, C. Lin, R. He, et al., “TRAF6 regulates the Abundance of RIPK1 and Inhibits the RIPK1/RIPK3/MLKL Necroptosis Signaling Pathway and Affects the Progression of Colorectal Cancer,” Cell Death & Disease 14, no. 1 (2023): 6.

[58] C. C. Lin, N. W. Mabe, Y. T. Lin, et al., “RIPK3 upregulation Confers Robust Proliferation and Collateral Cystine-dependence on Breast Cancer Recurrence,” Cell Death and Differentiation 27, no. 7 (2020): 2234-2247.

[59] L. Jing, M. E. Zhai, J. Cui, et al., “CNOT3 contributes to Cisplatin Resistance in Lung Cancer Through Inhibiting RIPK3 Expression,” Apoptosis 24, no. 7-8 (2019): 673-685.

[60] R. Karlowitz and S. J. L. van Wijk, “Surviving Death: Emerging Concepts of RIPK3 and MLKL Ubiquitination in the Regulation of Necroptosis,” The FEBS Journal 290, no. 1 (2023): 37-54.

[61] Y. Tan, E. Sementino, M. Cheung, et al., “Somatic Epigenetic Silencing of RIPK3 Inactivates Necroptosis and Contributes to Chemoresistance in Malignant Mesothelioma,” Clinical Cancer Research 27, no. 4 (2021): 1200-1213.

[62] X. Guo, R. Li, J. Cui, et al., “Induction of RIPK3/MLKL-mediated Necroptosis by Erigeron Breviscapus Injection Exhibits Potent Antitumor Effect,” Frontiers in Pharmacology 14 (2023): 1219362.

[63] Y. Liu, H. Wei, and J. Li, “A Review on SIRT3 and Its Natural Small Molecule Activators as a Potential Preventive and Therapeutic Target,” European Journal of Pharmacology 963 (2024): 176155.

[64] N. D'Onofrio, E. Martino, A. Balestrieri, et al., “Diet-derived Ergothioneine Induces Necroptosis in Colorectal Cancer Cells by Activating the SIRT3/MLKL Pathway,” The FEBS Letters 596, no. 10 (2022): 1313-1329.

[65] W. Fu, H. Li, H. Fu, et al., “The SIRT3 and SIRT6 Promote Prostate Cancer Progression by Inhibiting Necroptosis-Mediated Innate Immune Response,” Journal of Immunology Research 2020 (2020): 8820355.

[66] X. Tang, Y. Li, L. Liu, et al., “Sirtuin 3 Induces Apoptosis and Necroptosis by Regulating Mutant p53 Expression in Small‑Cell Lung Cancer,” Oncology Reports 43, no. 2 (2020): 591-600.

[67] X. Liu, N. Zhang, D. Wang, et al., “Downregulation of Reticulocalbin-1 Differentially Facilitates Apoptosis and Necroptosis in human Prostate Cancer Cells,” Cancer Science 109, no. 4 (2018): 1147-1157.

[68] R. Karki, B. Sundaram, B. R. Sharma, et al., “ADAR1 restricts ZBP1-mediated Immune Response and PANoptosis to Promote Tumorigenesis,” Cell Reports 37, no. 3 (2021): 109858.

[69] M. Zheng and T. D. Kanneganti, “The Regulation of the ZBP1-NLRP3 Inflammasome and Its Implications in Pyroptosis, Apoptosis, and Necroptosis (PANoptosis),” Immunological Reviews 297, no. 1 (2020): 26-38.

[70] N. Mizushima and M. Komatsu, “Autophagy: Renovation of Cells and Tissues,” Cell 147, no. 4 (2011): 728-741.

[71] J. D. Mancias and A. C. Kimmelman, “Mechanisms of Selective Autophagy in Normal Physiology and Cancer,” Journal of Molecular Biology 428, no. 9 Pt A (2016): 1659-1680.

[72] S. S. Singh, S. Vats, A. Y. Chia, et al., “Dual Role of Autophagy in Hallmarks of Cancer,” Oncogene 37, no. 9 (2018): 1142-1158.

[73] S. Liu, S. Yao, H. Yang, S. Liu, and Y. Wang, “Autophagy: Regulator of Cell Death,” Cell Death & Disease 14, no. 10 (2023): 648.

[74] J. Liu, Y. Liu, Y. Wang, et al., “TMEM164 is a New Determinant of Autophagy-dependent Ferroptosis,” Autophagy 19, no. 3 (2023): 945-956.

[75] F. Chen, X. Cai, R. Kang, J. Liu, and D. Tang, “Autophagy-Dependent Ferroptosis in Cancer,” Antioxid Redox Signaling 39, no. 1-3 (2023): 79-101.

[76] B. Zhou, J. Liu, R. Kang, D. J. Klionsky, G. Kroemer, and D. Tang, “Ferroptosis Is a Type of Autophagy-dependent Cell Death,” Seminars in Cancer Biology 66 (2020): 89-100.

[77] J. Debnath, N. Gammoh, and K. M. Ryan, “Autophagy and Autophagy-related Pathways in Cancer,” Nature Reviews Molecular Cell Biology 24, no. 8 (2023): 560-575.

[78] L. Polletta, E. Vernucci, I. Carnevale, et al., “SIRT5 regulation of Ammonia-induced Autophagy and Mitophagy,” Autophagy 11, no. 2 (2015): 253-270.

[79] Z. Deng, M. Sun, J. Wu, et al., “SIRT1 attenuates sepsis-induced Acute Kidney Injury via Beclin1 Deacetylation-mediated Autophagy Activation,” Cell Death & Disease 12, no. 2 (2021): 217.

[80] J. Li, H. Zhan, Y. Ren, et al., “Sirtuin 4 Activates Autophagy and Inhibits Tumorigenesis by Upregulating the p53 Signaling Pathway,” Cell Death and Differentiation 30, no. 2 (2023): 313-326.

[81] X. Wei, X. Xiong, P. Wang, S. Zhang, and D. Peng, “SIRT1-mediated Deacetylation of FOXO3 Enhances Mitophagy and Drives Hormone Resistance in Endometrial Cancer,” Molecular Medicine 30, no. 1 (2024): 147.

[82] H. Guo, H. Ding, X. Tang, et al., “Quercetin Induces Pro-apoptotic Autophagy via SIRT1/AMPK Signaling Pathway in human Lung Cancer Cell Lines A549 and H1299 in Vitro,” Thoracic Cancer 12, no. 9 (2021): 1415-1422.

[83] M. J. Powell, M. C. Casimiro, C. Cordon-Cardo, et al., “Disruption of a Sirt1-dependent Autophagy Checkpoint in the Prostate Results in Prostatic Intraepithelial Neoplasia Lesion Formation,” Cancer Research 71, no. 3 (2011): 964-975.

[84] S. Yi, B. Zheng, Y. Zhu, Y. Cai, H. Sun, and J. Zhou, “Melatonin Ameliorates Excessive PINK1/Parkin-mediated Mitophagy by Enhancing SIRT1 Expression in Granulosa Cells of PCOS,” American Journal of Physiology. Endocrinology and Metabolism 319, no. 1 (2020): e91-e101.

[85] J. Yao, J. Wang, Y. Xu, et al., “CDK9 inhibition Blocks the Initiation of PINK1-PRKN-mediated Mitophagy by Regulating the SIRT1-FOXO3-BNIP3 Axis and Enhances the Therapeutic Effects Involving Mitochondrial Dysfunction in Hepatocellular Carcinoma,” Autophagy 18, no. 8 (2022): 1879-1897.

[86] X. Wang, F. Xu, H. Kou, et al., “Stromal Cell-derived Small Extracellular Vesicles Enhance Radioresistance of Prostate Cancer Cells via Interleukin-8-induced Autophagy,” Journal of Extracellular Vesicles 12, no. 7 (2023): e12342.

[87] L. Yin, Y. Ye, L. Zou, et al., “AR Antagonists Develop Drug Resistance Through TOMM20 Autophagic Degradation-promoted Transformation to Neuroendocrine Prostate Cancer,” Journal of Experimental & Clinical Cancer Research 42, no. 1 (2023): 204.

[88] Y. Wang, N. Wu, J. Li, et al., “YAP1 Regulates the YAP1/AR/PSA Axis Through Autophagy in Castration-Resistant Prostate Cancer and Mediates T-Cell Immune and Inflammatory Cytokine Infiltration,” Biomedicines 12, no. 3 (2024): 661.

[89] J. Chen, F. Wang, H. Xu, et al., “Long Non-Coding RNA SNHG1 Regulates the Wnt/β-Catenin and PI3K/AKT/mTOR Signaling Pathways via EZH2 to Affect the Proliferation, Apoptosis, and Autophagy of Prostate Cancer Cell,” Frontiers in Oncology 10 (2020): 552907.

[90] Y. Yu, Y. Song, L. Cheng, et al., “CircCEMIP Promotes Anoikis-resistance by Enhancing Protective Autophagy in Prostate Cancer Cells,” Journal of Experimental & Clinical Cancer Research 41, no. 1 (2022): 188.

[91] Y. Yu, B. Liu, X. Li, et al., “ATF4/CEMIP/PKCα Promotes Anoikis Resistance by Enhancing Protective Autophagy in Prostate Cancer Cells,” Cell Death & Disease 13, no. 1 (2022): 46.

[92] R. K. S. Malireddi, S. Kesavardhana, and T. D. Kanneganti, “ZBP1 and TAK1: Master Regulators of NLRP3 Inflammasome/Pyroptosis, Apoptosis, and Necroptosis (PAN-optosis),” Frontiers in Cellular and Infection Microbiology 9 (2019): 406.

[93] D. E. Place, S. Lee, and T. D. Kanneganti, “PANoptosis in Microbial Infection,” Current Opinion in Microbiology 59 (2021): 42-49.

[94] R. Karki, B. R. Sharma, E. Lee, et al., “Interferon Regulatory Factor 1 Regulates PANoptosis to Prevent Colorectal Cancer,” JCI Insight 5, no. 12 (2020): e136720.

[95] B. T. Cookson and M. A. Brennan, “Pro-inflammatory Programmed Cell Death,” Trends in Microbiology 9, no. 3 (2001): 113-114.

[96] K. Newton, V. M. Dixit, and N. Kayagaki, “Dying Cells Fan the Flames of Inflammation,” Science 374, no. 6571 (2021): 1076-1080.

[97] X. Lou, K. Li, B. Qian, Y. Li, D. Zhang, and W. Cui, “Pyroptosis Correlates With Tumor Immunity and Prognosis,” Communications Biology 5, no. 1 (2022): 917.

[98] J. B. Wang, Y. X. Gao, Y. H. Ye, et al., “Comprehensive Multi-omics Analysis of Pyroptosis for Optimizing Neoadjuvant Immunotherapy in Patients With Gastric Cancer,” Theranostics 14, no. 7 (2024): 2915-2933.

[99] X. Zhang, X. Wei, Y. Wang, et al., “Pyroptosis Regulators and Tumor Microenvironment Infiltration Characterization in Clear Cell Renal Cell Carcinoma,” Frontiers in Oncology 11 (2021): 774279.

[100] Z. Liu, S. Kuang, and Q. Chen, “A Review Focusing on the Role of Pyroptosis in Prostate Cancer,” Medicine 102, no. 50 (2023): e36605.

[101] Y. Ren, M. Feng, X. Hao, et al., “USP48 Stabilizes Gasdermin E to Promote Pyroptosis in Cancer,” Cancer Research 83, no. 7 (2023): 1074-1093.

[102] R. N. Zhang, Z. Q. Jing, L. Zhang, and Z. J. Sun, “Epigenetic Regulation of Pyroptosis in Cancer: Molecular Pathogenesis and Targeting Strategies,” Cancer Letters 575 (2023): 216413.

[103] Y. Zhang, J. Yang, Z. Wen, et al., “A Novel 3',5'-diprenylated Chalcone Induces Concurrent Apoptosis and GSDME-dependent Pyroptosis Through Activating PKCδ/JNK Signal in Prostate Cancer,” Aging (Albany NY) 12, no. 10 (2020): 9103-9124.

[104] A. Tian, T. Wu, Y. Zhang, J. Chen, J. Sha, and W. Xia, “Triggering Pyroptosis Enhances the Antitumor Efficacy of PARP Inhibitors in Prostate Cancer,” ellular Oncology (Dordr) 46, no. 6 (2023): 1855-1870.

[105] F. Wu, M. Wang, T. Zhong, et al., “Inhibition of CDC20 Potentiates Anti-tumor Immunity Through Facilitating GSDME-mediated Pyroptosis in Prostate Cancer,” Experimental Hematology & Oncology 12, no. 1 (2023): 67.

[106] A. El-Kenawi, A. Berglund, V. Estrella, et al., “Elevated Methionine Flux Drives Pyroptosis Evasion in Persister Cancer Cells,” Cancer Research 83, no. 5 (2023): 720-734.

[107] Y. Zeng, M. X. Li, S. Q. Wu, and C. Xu, “Carvedilol Induces Pyroptosis Through NLRP3-caspase1-ASC Inflammasome by Nuclear Migration of NF-κB in Prostate Cancer Models,” Molecular Biology Reports 51, no. 1 (2024): 201.

[108] X. W. Zhang, L. Li, M. Liao, et al., “Thermal Proteome Profiling Strategy Identifies CNPY3 as a Cellular Target of Gambogic Acid for Inducing Prostate Cancer Pyroptosis,” Journal of Medicinal Chemistry 67, no. 12 (2024): 10005-10011.

[109] M. Overholtzer, A. A. Mailleux, G. Mouneimne, et al., “A Nonapoptotic Cell Death Process, Entosis, That Occurs by Cell-in-cell Invasion,” Cell 131, no. 5 (2007): 966-979.

[110] M. Kianfar, A. Balcerak, M. Chmielarczyk, L. Tarnowski, and E. A. Grzybowska, “Cell Death by Entosis: Triggers, Molecular Mechanisms and Clinical Significance,” International Journal of Molecular Sciences 23, no. 9 (2022): 4985.

[111] C. Zeng, B. Zeng, C. Dong, J. Liu, and F. Xing, “Rho-ROCK Signaling Mediates Entotic Cell Death in Tumor,” Cell Death Discovery 6 (2020): 4.

[112] J. Durgan, Y. Y. Tseng, J. C. Hamann, et al., “Mitosis Can Drive Cell Cannibalism Through Entosis,” Elife 6 (2017): e27134.

[113] J. Durgan and O. Florey, “Cancer Cell Cannibalism: Multiple Triggers Emerge for Entosis,” Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1865, no. 6 (2018): 831-841.

[114] A. Hayashi, A. Yavas, C. A. McIntyre, et al., “Genetic and Clinical Correlates of Entosis in Pancreatic Ductal Adenocarcinoma,” Modern Pathology 33, no. 9 (2020): 1822-1831.

[115] S. Basbous, L. Dif, C. Dantzer, et al., “Loss of RND3/RHOE Controls Entosis Through LAMP1 Expression in Hepatocellular Carcinoma,” Cell Death & Disease 15, no. 1 (2024): 46.

[116] A. R. Lee and C. Y. Park, “Orai1 is an Entotic Ca(2+) Channel for Non-Apoptotic Cell Death, Entosis in Cancer Development,” Advanced Science (Weinh) 10, no. 14 (2023): e2205913.

[117] K. Gaptulbarova, I. A. Tsydenova, D. S. Dolgasheva, et al., “Mechanisms and Significance of Entosis for Tumour Growth and Progression,” Cell Death Discovery 10, no. 1 (2024): 109.

[118] E. Bozkurt, H. Düssmann, M. Salvucci, et al., “TRAIL Signaling Promotes Entosis in Colorectal Cancer,” Journal of Cell Biology 220, no. 11 (2021): e202010030.

[119] I. Dziuba, A. M. Gawel, P. Tyrna, et al., “Homotypic Entosis as a Potential Novel Diagnostic Marker in Breast Cancer,” International Journal of Molecular Sciences 24, no. 7 (2023): 6819.

[120] S. Wen, Z. Shang, S. Zhu, C. Chang, and Y. Niu, “Androgen Receptor Enhances Entosis, a Non-apoptotic Cell Death, Through Modulation of Rho/ROCK Pathway in Prostate Cancer Cells,” Prostate 73, no. 12 (2013): 1306-1315.

[121] J. Gilloteaux, C. Ruffo, J. M. Jamison, and J. L. Summers, “Modes of Internalizations of human Prostate Carcinoma (DU145) Cells in Vitro and in Murine Xenotransplants,” Ultrastructural Pathology 40, no. 5 (2016): 231-239.

[122] J. Balvan, J. Gumulec, M. Raudenska, et al., “Oxidative Stress Resistance in Metastatic Prostate Cancer: Renewal by Self-Eating,” PLoS ONE 10, no. 12 (2015): e0145016.

[123] J. Liu, L. Wang, Y. Zhang, et al., “Induction of Entosis in Prostate Cancer Cells by nintedanib and Its Therapeutic Implications,” Oncology Letters 17, no. 3 (2019): 3151-3162.

[124] J. C. Patterson, A. Varkaris, P. J. P. Croucher, et al., “Plk1 Inhibitors and Abiraterone Synergistically Disrupt Mitosis and Kill Cancer Cells of Disparate Origin Independently of Androgen Receptor Signaling,” Cancer Research 83, no. 2 (2023): 219-238.

[125] S. J. Dixon, K. M. Lemberg, M. R. Lamprecht, et al., “Ferroptosis: An Iron-dependent Form of Nonapoptotic Cell Death,” Cell 149, no. 5 (2012): 1060-1072.

[126] X. Jiang, B. R. Stockwell, and M. Conrad, “Ferroptosis: Mechanisms, Biology and Role in Disease,” Nature Reviews Molecular Cell Biology 22, no. 4 (2021): 266-282.

[127] K. Wu, M. Yan, T. Liu, et al., “Creatine Kinase B Suppresses Ferroptosis by Phosphorylating GPX4 Through a Moonlighting Function,” Nature Cell Biology 25, no. 5 (2023): 714-725.

[128] Y. He, W. Xu, Y. T. Xiao, H. Huang, D. Gu, and S. Ren, “Targeting Signaling Pathways in Prostate Cancer: Mechanisms and Clinical Trials,” Signal Transduction and Targeted Therapy 7, no. 1 (2022): 198.

[129] L. L. Sun, D. L. Linghu, and M. C. Hung, “Ferroptosis: A Promising Target for Cancer Immunotherapy,” American Journal of Cancer Research 11, no. 12 (2021): 5856-5863.

[130] Y. Liu, C. Duan, R. Dai, and Y. Zeng, “Ferroptosis-mediated Crosstalk in the Tumor Microenvironment Implicated in Cancer Progression and Therapy,” Frontiers in Cell and Developmental Biology 9 (2021): 739392.

[131] C. M. Bebber, F. Müller, L. Prieto Clemente, J. Weber, and S. von Karstedt, “Ferroptosis in Cancer Cell Biology,” Cancers (Basel) 12, no. 1 (2020): 164.

[132] M. J. Hangauer, V. S. Viswanathan, M. J. Ryan, et al., “Drug-tolerant Persister Cancer Cells Are Vulnerable to GPX4 Inhibition,” Nature 551, no. 7679 (2017): 247-250.

[133] V. S. Viswanathan, M. J. Ryan, H. D. Dhruv, et al., “Dependency of a Therapy-resistant state of Cancer Cells on a Lipid Peroxidase Pathway,” Nature 547, no. 7664 (2017): 453-457.

[134] L. Cheng, Q. He, B. Liu, et al., “SGK2 promotes Prostate Cancer Metastasis by Inhibiting Ferroptosis via Upregulating GPX4,” Cell Death & Disease 14, no. 1 (2023): 74.

[135] X. Zhao, T. Zhou, Y. Wang, et al., “Trigred Motif 36 Regulates Neuroendocrine Differentiation of Prostate Cancer via HK2 Ubiquitination and GPx4 Deficiency,” Cancer Science 114, no. 6 (2023): 2445-2459.

[136] J. Shi, C. Ma, Z. Zheng, et al., “Low-dose Antimony Exposure Promotes Prostate Cancer Proliferation by Inhibiting Ferroptosis via Activation of the Nrf2-SLC7A11-GPX4 Pathway,” Chemosphere 339 (2023): 139716.

[137] Z. Zhang, T. Xie, S. Zhang, et al., “Second Generation Androgen Receptor Antagonist, TQB3720 Abrogates Prostate Cancer Growth via AR/GPX4 Axis Activated Ferroptosis,” Frontiers in Pharmacology 14 (2023): 1110146.

[138] Y. Zhang, X. W. Song, N. Zhang, et al., “Ezetimibe Engineered L14-8 Suppresses Advanced Prostate Cancer by Activating PLK1/TP53-SAT1-Induced Ferroptosis,” Advanced Science (Weinheim, Baden-Wurttemberg, Germany) 12, no. 29 (2025): e04192.

[139] G. Li, Y. Yuan, X. Wu, and L. Wu, “Modulating NPC1L1 to Potentiate PARP Inhibitor-Induced Ferroptosis and Immune Response in Triple-Negative Breast Cancer,” Pharmaceutics 17, no. 5 (2025): 554.

[140] Q. Wang, S. Gao, Y. Shou, et al., “AIM2 promotes Renal Cell Carcinoma Progression and Sunitinib Resistance Through FOXO3a-ACSL4 Axis-regulated Ferroptosis,” International Journal of Biological Sciences 19, no. 4 (2023): 1266-1283.

[141] K. D. Tousignant, A. Rockstroh, B. L. J. Poad, et al., “Therapy-induced Lipid Uptake and Remodeling Underpin Ferroptosis Hypersensitivity in Prostate Cancer,” Cancer & Metabolism 8 (2020): 11.

[142] B. Feng, H. Y. Guo, Y. Ning, Y. Y. Zhao, X. Wang, and R. Cui, “LPCAT3 regulates the Immune Infiltration and Prognosis of ccRCC Patients by Mediating Ferroptosis and Endoplasmic Reticulum Stress,” Discover Oncology 16, no. 1 (2025): 574.

[143] Y. Qiu, X. Wang, Y. Sun, et al., “ACSL4-Mediated Membrane Phospholipid Remodeling Induces Integrin β1 Activation to Facilitate Triple-Negative Breast Cancer Metastasis,” Cancer Research 84, no. 11 (2024): 1856-1871.

[144] J. Chen, C. Ding, Y. Chen, et al., “ACSL4 reprograms Fatty Acid Metabolism in Hepatocellular Carcinoma via c-Myc/SREBP1 Pathway,” Cancer Letters 502 (2021): 154-165.

[145] A. F. Castillo, U. D. Orlando, P. M. Maloberti, et al., “New Inhibitor Targeting Acyl-CoA Synthetase 4 Reduces Breast and Prostate Tumor Growth, Therapeutic Resistance and Steroidogenesis,” Cellular and Molecular Life Sciences 78, no. 6 (2021): 2893-2910.

[146] J. Chen, Y. Jiang, H. Shi, Y. Peng, X. Fan, and C. Li, “The Molecular Mechanisms of Copper Metabolism and Its Roles in human Diseases,” Pflugers Archiv: European Journal of Physiology 472, no. 10 (2020): 1415-1429.

[147] A. Dancis, D. G. Roman, G. J. Anderson, A. G. Hinnebusch, and R. D. Klausner, “Ferric Reductase of Saccharomyces Cerevisiae: Molecular Characterization, Role in Iron Uptake, and Transcriptional Control by Iron,” PNAS 89, no. 9 (1992): 3869-3873.

[148] J. Xie, Y. Yang, Y. Gao, and J. He, “Cuproptosis: Mechanisms and Links With Cancers,” Molecular Cancer 22, no. 1 (2023): 46.

[149] Y. Feng, Z. Yang, J. Wang, and H. Zhao, “Cuproptosis: Unveiling a New Frontier in Cancer Biology and Therapeutics,” Cell Communication and Signaling 22, no. 1 (2024): 249.

[150] B. Halliwell and J. M. Gutteridge, “Oxygen Toxicity, Oxygen Radicals, Transition Metals and Disease,” Biochemical Journal 219, no. 1 (1984): 1-14.

[151] D. Cen, D. Brayton, B. Shahandeh, and F. L. Meyskens, “Farmer PJ: Disulfiram Facilitates Intracellular Cu Uptake and Induces Apoptosis in human Melanoma Cells,” Journal of Medicinal Chemistry 47, no. 27 (2004): 6914-6920.

[152] M. Yang, X. Wu, J. Hu, et al., “COMMD10 inhibits HIF1α/CP Loop to Enhance Ferroptosis and Radiosensitivity by Disrupting Cu-Fe Balance in Hepatocellular Carcinoma,” Journal of Hepatology 76, no. 5 (2022): 1138-1150.

[153] H. Wen, C. Qu, Z. Wang, et al., “Cuproptosis Enhances Docetaxel Chemosensitivity by Inhibiting Autophagy via the DLAT/mTOR Pathway in Prostate Cancer,” The FASEB Journal 37, no. 9 (2023): e23145.

[154] K. Li, L. Tan, Y. Li, et al., “Cuproptosis Identifies respiratory Subtype of Renal Cancer That Confers Favorable Prognosis,” Apoptosis 27, no. 11-12 (2022): 1004-1014.

[155] B. Cheng, C. Tang, J. Xie, et al., “Cuproptosis Illustrates Tumor Micro-environment Features and Predicts Prostate Cancer Therapeutic Sensitivity and Prognosis,” Life Sciences 325 (2023): 121659.

[156] C. Xiao, X. Wang, S. Li, et al., “A Cuproptosis-based Nanomedicine Suppresses Triple Negative Breast Cancers by Regulating Tumor Microenvironment and Eliminating Cancer Stem Cells,” Biomaterials 313 (2025): 122763.

[157] Z. Zhu, Q. Zhao, W. Song, et al., “A Novel Cuproptosis-related Molecular Pattern and Its Tumor Microenvironment Characterization in Colorectal Cancer,” Frontiers in Immunology 13 (2022): 940774.

[158] Q. Song, R. Zhou, F. Shu, and W. Fu, “Cuproptosis Scoring System to Predict the Clinical Outcome and Immune Response in Bladder Cancer,” Frontiers in Immunology 13 (2022): 958368.

[159] J. Zeng, H. Chen, X. Liu, et al., “Cuproptosis in Microsatellite Stable Colon Cancer Cells Affects the Cytotoxicity of CD8(+)T Through the WNT Signaling Pathway,” Chemico-Biological Interactions 403 (2024): 111239.

[160] Y. T. Liu, L. Chen, S. J. Li, et al., “Dysregulated Wnt/β-catenin Signaling Confers Resistance to Cuproptosis in Cancer Cells,” Cell Death and Differentiation 31, no. 11 (2024): 1452-1466.

[161] K. Wang, Y. Zhang, M. Ao, H. Luo, W. Mao, and B. Li, “Multi-omics Analysis Defines a Cuproptosis-related Prognostic Model for Ovarian Cancer: Implication of WASF2 in Cuproptosis Resistance,” Life Sciences 332 (2023): 122081.

[162] H. Nie, H. Wang, M. Zhang, et al., “Comprehensive Analysis of Cuproptosis-related Genes in Prognosis, Tumor Microenvironment Infiltration, and Immunotherapy Response in Gastric Cancer,” Journal of Cancer Research and Clinical Oncology 149, no. 8 (2023): 5453-5468.

[163] S. Song, M. Zhang, P. Xie, S. Wang, and Y. Wang, “Comprehensive Analysis of Cuproptosis-related Genes and Tumor Microenvironment Infiltration Characterization in Breast Cancer,” Frontiers in Immunology 13 (2022): 978909.

[164] W. Xie, Y. Zhang, Q. Xu, et al., “A Unique Approach: Biomimetic Graphdiyne-Based Nanoplatform to Treat Prostate Cancer by Combining Cuproptosis and Enhanced Chemodynamic Therapy,” International Journal of Nanomedicine 19 (2024): 3957-3972.

[165] X. Gao, H. Zhao, J. Liu, et al., “Enzalutamide Sensitizes Castration-Resistant Prostate Cancer to Copper-Mediated Cell Death,” Advanced Science (Weinh) 11, no. 30 (2024): e2401396.

[166] P. Koppula, L. Zhuang, and B. Gan, “Cystine Transporter SLC7A11/xCT in Cancer: Ferroptosis, Nutrient Dependency, and Cancer Therapy,” Protein Cell 12, no. 8 (2021): 599-620.

[167] Y. Yan, H. Teng, Q. Hang, et al., “SLC7A11 expression Level Dictates Differential Responses to Oxidative Stress in Cancer Cells,” Nature Communications 14, no. 1 (2023): 3673.

[168] G. Grasmann, E. Smolle, H. Olschewski, and K. Leithner, “Gluconeogenesis in Cancer Cells—Repurposing of a Starvation-induced Metabolic Pathway?,” Biochimica et Biophysica Acta: Reviews on Cancer 1872, no. 1 (2019): 24-36.

[169] T. Levy, K. Voeltzke, L. Hruby, et al., “mTORC1 regulates Cell Survival Under Glucose Starvation Through 4EBP1/2-mediated Translational Reprogramming of Fatty Acid Metabolism,” Nature Communications 15, no. 1 (2024): 4083.

[170] M. Kang, J. H. Kang, I. A. Sim, et al., “Glucose Deprivation Induces Cancer Cell Death Through Failure of ROS Regulation,” International Journal of Molecular Sciences 24, no. 15 (2023): 11969.

[171] J. Wang, J. Chen, K. Fan, et al., “Inhibition of Endoplasmic Reticulum Stress Cooperates With SLC7A11 to Promote Disulfidptosis and Suppress Tumor Growth Upon Glucose Limitation,” Advanced Science (Weinh) 12, no. 7 (2025): e2408789.

[172] A. Jiang, W. Liu, Y. Liu, et al., “DCS, a Novel Classifier System Based on Disulfidptosis Reveals Tumor Microenvironment Heterogeneity and Guides Frontline Therapy for Clear Cell Renal Carcinoma,” Journal of the National Cancer Institute 4, no. 3 (2024): 263-279.

[173] J. Xie, X. Deng, Y. Xie, et al., “Multi-omics Analysis of Disulfidptosis Regulators and Therapeutic Potential Reveals Glycogen Synthase 1 as a Disulfidptosis Triggering Target for Triple-negative Breast Cancer,” MedComm 5, no. 3 (2024): e502.

[174] D. Zhao, Y. Meng, Y. Dian, et al., “Molecular Landmarks of Tumor Disulfidptosis Across Cancer Types to Promote Disulfidptosis-target Therapy,” Redox Biology 68 (2023): 102966.

[175] C. Zhang, T. Xu, K. Ji, et al., “Development and Experimental Validation of a Machine Learning-based Disulfidptosis-related Ferroptosis Score for Hepatocellular Carcinoma,” Apoptosis 29, no. 1-2 (2024): 103-120.

[176] J. Wei, J. Wang, X. Chen, L. Zhang, and M. Peng, “Novel Application of the Ferroptosis-related Genes Risk Model Associated With Disulfidptosis in Hepatocellular Carcinoma Prognosis and Immune Infiltration,” PeerJ 12 (2024): e16819.

[177] K. Xu, D. Li, J. Qian, et al., “Single-cell Disulfidptosis Regulator Patterns Guide Intercellular Communication of Tumor Microenvironment That Contribute to Kidney Renal Clear Cell Carcinoma Progression and Immunotherapy,” Frontiers in immunology 15 (2024): 1288240.

[178] T. Jin, T. Yin, R. Xu, et al., “Exploring the Role of Disulfidptosis-related Signatures in Immune Microenvironment, Prognosis and Therapeutic Strategies of Cervical Cancer,” Translational Oncology 44 (2024): 101938.

[179] K. Newton, A. Strasser, N. Kayagaki, and V. M. Dixit, “Cell Death,” Cell 187, no. 2 (2024): 235-256.

[180] M. Zhu, D. Liu, G. Liu, M. Zhang, and F. Pan, “Caspase-Linked Programmed Cell Death in Prostate Cancer: From Apoptosis, Necroptosis, and Pyroptosis to PANoptosis,” Biomolecules 13, no. 12 (2023): 1715.

[181] Á. F. Fernández, S. Sebti, Y. Wei, et al., “Disruption of the Beclin 1-BCL2 Autophagy Regulatory Complex Promotes Longevity in Mice,” Nature 558, no. 7708 (2018): 136-140.

[182] S. Pattingre, A. Tassa, X. Qu, et al., “Bcl-2 Antiapoptotic Proteins Inhibit Beclin 1-dependent Autophagy,” Cell 122, no. 6 (2005): 927-939.

[183] R. Kang, H. J. Zeh, M. T. Lotze, and D. Tang, “The Beclin 1 Network Regulates Autophagy and Apoptosis,” Cell Death and Differentiation 18, no. 4 (2011): 571-580.

[184] W. Wang, K. Lu, X. Jiang, et al., “Ferroptosis Inducers Enhanced Cuproptosis Induced by Copper Ionophores in Primary Liver Cancer,” Journal of Experimental & Clinical Cancer Research 42, no. 1 (2023): 142.

[185] S. Zhang, Y. Wang, J. Gu, et al., “PPARγ Antagonists Exhibit Antitumor Effects by Regulating Ferroptosis and Disulfidptosis,” Biomolecules 14, no. 5 (2024): 596.

[186] C. Mao, M. Wang, L. Zhuang, and B. Gan, “Metabolic Cell Death in Cancer: Ferroptosis, Cuproptosis, Disulfidptosis, and Beyond,” Protein Cell 15, no. 9 (2024): 642-660.

[187] L. Li, T. Li, X. Qu, G. Sun, Q. Fu, and G. Han, “Stress/Cell Death Pathways, Neuroinflammation, and Neuropathic Pain,” Immunological Reviews 321, no. 1 (2024): 33-51.

[188] B. Wang, Y. Wang, J. Zhang, et al., “ROS-induced Lipid Peroxidation Modulates Cell Death Outcome: Mechanisms Behind Apoptosis, Autophagy, and Ferroptosis,” Archives of Toxicology 97, no. 6 (2023): 1439-1451.

[189] M. Kist and D. Vucic, “Cell Death Pathways: Intricate Connections and Disease Implications,” Embo Journal 40, no. 5 (2021): e106700.

[190] X. Tong, R. Tang, M. Xiao, et al., “Targeting Cell Death Pathways for Cancer Therapy: Recent Developments in Necroptosis, Pyroptosis, Ferroptosis, and Cuproptosis Research,” Journal of Hematology & Oncology 15, no. 1 (2022): 174.

[191] M. Wang, F. Yu, Y. Zhang, and P. Li, “Programmed Cell Death in Tumor Immunity: Mechanistic Insights and Clinical Implications,” Frontiers in Immunology 14 (2024): 1309635.

[192] S. Li, A. Wang, Y. Wu, et al., “Targeted Therapy for Non-small-cell Lung Cancer: New Insights Into Regulated Cell Death Combined With Immunotherapy,” Immunological Reviews 321, no. 1 (2024): 300-334.

[193] Y. Xia, J. Zhang, and G. Liu, “A Prospective Strategy Leveraging Nanomedicine for Cancer Therapy: Pouring Ferroptosis on Apoptosis,” Nano Today 48 (2023): 101740.

[194] M. Kciuk, A. Gielecińska, Ż. Kałuzińska-Kołat, E. B. Yahya, and R. Kontek, “Ferroptosis and Cuproptosis: Metal-dependent Cell Death Pathways Activated in Response to Classical Chemotherapy—Significance for Cancer Treatment?,” Biochimica et Biophysica Acta: Reviews on Cancer 1879, no. 4 (2024): 189124.

[195] N. Kyprianou, H. F. English, and J. T. Isaacs, “Programmed Cell Death During Regression of PC-82 human Prostate Cancer Following Androgen Ablation,” Cancer Research 50, no. 12 (1990): 3748-3753.

[196] C. Söhngen, D. J. Thomas, M. A. Skowron, et al., “CD24 targeting With NK-CAR Immunotherapy in Testis, Prostate, Renal and (luminal-type) Bladder Cancer and Identification of Direct CD24 Interaction Partners,” The FEBS Journal 290, no. 20 (2023): 4864-4876.

[197] X. Lu, F. Yang, D. Chen, et al., “Quercetin Reverses Docetaxel Resistance in Prostate Cancer via Androgen Receptor and PI3K/Akt Signaling Pathways,” International Journal of Biological Sciences 16, no. 7 (2020): 1121-1134.

[198] W. Wang, X. Yuan, J. Mu, et al., “Quercetin Induces MGMT(+) Glioblastoma Cells Apoptosis via Dual Inhibition of Wnt3a/β-Catenin and Akt/NF-κB Signaling Pathways,” Phytomedicine 118 (2023): 154933.

[199] A. Maugeri, A. Calderaro, G. T. Patanè, et al., “Targets Involved in the Anti-Cancer Activity of Quercetin in Breast, Colorectal and Liver Neoplasms,” International Journal of Molecular Sciences 24, no. 3 (2023): 2952.

[200] P. Maleki Dana, F. Sadoughi, Z. Asemi, and B. Yousefi, “Anti-cancer Properties of Quercetin in Osteosarcoma,” Cancer Cell International 21, no. 1 (2021): 349.

[201] C. He, Y. Zhou, Z. Li, et al., “Co-Expression of IL-7 Improves NKG2D-Based CAR T Cell Therapy on Prostate Cancer by Enhancing the Expansion and Inhibiting the Apoptosis and Exhaustion,” Cancers (Basel) 12, no. 7 (2020): 1969.

[202] D. Yang, B. Sun, H. Dai, et al., “T Cells Expressing NKG2D Chimeric Antigen Receptors Efficiently Eliminate Glioblastoma and Cancer Stem Cells,” Journal for ImmunoTherapy of Cancer 7, no. 1 (2019): 171.

[203] Y. Zhang, C. Zhang, M. He, W. Xing, R. Hou, and H. Zhang, “Co-expression of IL-21-Enhanced NKG2D CAR-NK Cell Therapy for Lung Cancer,” BMC Cancer 24, no. 1 (2024): 119.

[204] F. Almasri and R. Karshafian, “Synergistic Enhancement of Cell Death by Triple Combination Therapy of docetaxel, Ultrasound and Microbubbles, and Radiotherapy on PC3 a Prostate Cancer Cell Line,” Heliyon 8, no. 8 (2022): e10213.

[205] H. Wei, J. Huang, J. Yang, et al., “Ultrasound Exposure Improves the Targeted Therapy Effects of Galactosylated Docetaxel Nanoparticles on Hepatocellular Carcinoma Xenografts,” PLoS ONE 8, no. 3 (2013): e58133.

[206] T. Li, Z. Hu, C. Wang, et al., “PD-L1-targeted Microbubbles Loaded With Docetaxel Produce a Synergistic Effect for the Treatment of Lung Cancer Under Ultrasound Irradiation,” Biomaterials Science 8, no. 5 (2020): 1418-1430.

[207] F. Fontana, R. M. Moretti, M. Raimondi, et al., “δ-Tocotrienol Induces Apoptosis, Involving Endoplasmic Reticulum Stress and Autophagy, and Paraptosis in Prostate Cancer Cells,” Cell Proliferation 52, no. 3 (2019): e12576.

[208] F. Fontana, M. Marzagalli, M. Raimondi, V. Zuco, N. Zaffaroni, and P. Limonta, “δ-Tocotrienol Sensitizes and Re-sensitizes Ovarian Cancer Cells to Cisplatin via Induction of G1 Phase Cell Cycle Arrest and ROS/MAPK-mediated Apoptosis,” Cell Proliferation 54, no. 11 (2021): e13111.

[209] J. Shen, T. Yang, Y. Tang, et al., “δ-Tocotrienol Induces Apoptosis and Inhibits Proliferation of Nasopharyngeal Carcinoma Cells,” Food & Function 12, no. 14 (2021): 6374-6388.

[210] R. A. Francois, A. Zhang, K. Husain, et al., “Vitamin E δ-tocotrienol Sensitizes human Pancreatic Cancer Cells to TRAIL-induced Apoptosis Through Proteasome-mediated Down-regulation of c-FLIP(s),” Cancer Cell International 19 (2019): 189.

[211] C. Ye, W. Zhao, M. Li, et al., “δ-tocotrienol Induces human Bladder Cancer Cell Growth Arrest, Apoptosis and Chemosensitization Through Inhibition of STAT3 Pathway,” PLoS ONE 10, no. 4 (2015): e0122712.

[212] H. Hu, C. Jiang, T. Schuster, G. X. Li, P. T. Daniel, and J. Lü, “Inorganic Selenium Sensitizes Prostate Cancer Cells to TRAIL-induced Apoptosis Through Superoxide/p53/Bax-mediated Activation of Mitochondrial Pathway,” Molecular Cancer Therapeutics 5, no. 7 (2006): 1873-1882.

[213] B. Toubhans, S. A. Gazze, C. Bissardon, et al., “Selenium Nanoparticles Trigger Alterations in Ovarian Cancer Cell Biomechanics,” Nanomedicine 29 (2020): 102258.

[214] M. Pei, K. Liu, X. Qu, et al., “Enzyme-catalyzed Synthesis of Selenium-doped Manganese Phosphate for Synergistic Therapy of Drug-resistant Colorectal Cancer,” Journal of Nanobiotechnology 21, no. 1 (2023): 72.

[215] S. Nie, X. He, Z. Sun, et al., “Selenium Speciation-dependent Cancer Radiosensitization by Induction of G2/M Cell Cycle Arrest and Apoptosis,” Frontiers in Bioengineering and Biotechnology 11 (2023): 1168827.

[216] Z. Lu, C. Wu, M. Zhu, et al., “Ophiopogonin D' induces RIPK1‑Dependent Necroptosis in Androgen‑Dependent LNCaP Prostate Cancer Cells,” International Journal of Oncology 56, no. 2 (2020): 439-447.

[217] T. Xu, W. Zhang, Y. Zhang, F. Song, and P. Huang, “Ophiopogonin D' inhibited Tumour Growth and Metastasis of Anaplastic Thyroid Cancer by Modulating JUN/RGS4 Signalling,” Journal of Cellular and Molecular Medicine 28, no. 16 (2024): e70014.

[218] H. M. Ko, W. Jee, D. Lee, H. J. Jang, and J. H. Jung, “Ophiopogonin D Increase Apoptosis by Activating p53 via Ribosomal Protein L5 and L11 and Inhibiting the Expression of c-Myc via CNOT2,” Frontiers in Pharmacology 13 (2022): 974468.

[219] C. Yang, X. Ma, Z. Wang, et al., “Curcumin Induces Apoptosis and Protective Autophagy in Castration-resistant Prostate Cancer Cells Through Iron Chelation,” Drug Design, Development and Therapy 11 (2017): 431-439.

[220] W. Wang, M. Li, L. Wang, L. Chen, and B. C. Goh, “Curcumin in Cancer Therapy: Exploring Molecular Mechanisms and Overcoming Clinical Challenges,” Cancer Letters 570 (2023): 216332.

[221] M. F. Wu, Y. H. Huang, L. Y. Chiu, S. H. Cherng, G. T. Sheu, and T. Y. Yang, “Curcumin Induces Apoptosis of Chemoresistant Lung Cancer Cells via ROS-Regulated p38 MAPK Phosphorylation,” International Journal of Molecular Sciences 23, no. 15 (2022): 8248.

[222] C. Liu, M. Rokavec, Z. Huang, and H. Hermeking, “Curcumin Activates a ROS/KEAP1/NRF2/miR-34a/b/c Cascade to Suppress Colorectal Cancer Metastasis,” Cell Death and Differentiation 30, no. 7 (2023): 1771-1785.

[223] Y. Dai, J. Desano, W. Tang, et al., “Natural Proteasome Inhibitor Celastrol Suppresses Androgen-independent Prostate Cancer Progression by Modulating Apoptotic Proteins and NF-kappaB,” PLoS ONE 5, no. 12 (2010): e14153.

[224] H. Xu, H. Zhao, C. Ding, et al., “Celastrol Suppresses Colorectal Cancer via Covalent Targeting Peroxiredoxin 1,” Signal Transduction and Targeted Therapy 8, no. 1 (2023): 51.

[225] P. Luo, Q. Zhang, S. Shen, et al., “Mechanistic Engineering of Celastrol Liposomes Induces Ferroptosis and Apoptosis by Directly Targeting VDAC2 in Hepatocellular Carcinoma,” Asian Journal of Pharmaceutical Sciences 18, no. 6 (2023): 100874.

[226] X. Chen, Y. Zhao, W. Luo, et al., “Celastrol Induces ROS-mediated Apoptosis via Directly Targeting Peroxiredoxin-2 in Gastric Cancer Cells,” Theranostics 10, no. 22 (2020): 10290-10308.

[227] X. Chen, S. Wang, L. Zhang, et al., “Celastrol Inhibited Human Esophageal Cancer by Activating DR5-Dependent Extrinsic and Noxa/Bim-Dependent Intrinsic Apoptosis,” Frontiers in Pharmacology 13 (2022): 873166.

[228] B. Ma, H. Zhang, Y. Wang, et al., “Corosolic Acid, a Natural Triterpenoid, Induces ER Stress-dependent Apoptosis in human Castration Resistant Prostate Cancer Cells via Activation of IRE-1/JNK, PERK/CHOP and TRIB3,” Journal of Experimental & Clinical Cancer Research 37, no. 1 (2018): 210.

[229] X. Luo, Z. Ye, C. Xu, et al., “Corosolic Acid Enhances Oxidative Stress-induced Apoptosis and Senescence in Pancreatic Cancer Cells by Inhibiting the JAK2/STAT3 Pathway,” Molecular Biology Reports 51, no. 1 (2024): 176.

[230] S. A. Jasim, O. Z. Khalaf, S. H. Alshahrani, et al., “An in Vitro Investigation of the Apoptosis-inducing Activity of Corosolic Acid in Breast Cancer Cells,” Iranian Journal of Basic Medical Sciences 26, no. 4 (2023): 453-460.

[231] S. D. Markowitsch, K. M. Juetter, P. Schupp, et al., “Shikonin Reduces Growth of Docetaxel-Resistant Prostate Cancer Cells Mainly Through Necroptosis,” Cancers (Basel) 13, no. 4 (2021): 882.

[232] H. Tian, H. Shang, Y. Chen, et al., “Sonosensitizer Nanoplatforms Augmented Sonodynamic Therapy-Sensitizing Shikonin-Induced Necroptosis against Hepatocellular Carcinoma,” International Journal of Nanomedicine 18 (2023): 7079-7092.

[233] X. Liu, L. Liu, X. Wang, et al., “Necroptosis Inhibits Autophagy by Regulating the Formation of RIP3/p62/Keap1 Complex in shikonin-induced ROS Dependent Cell Death of human Bladder Cancer,” Phytomedicine 118 (2023): 154943.

[234] J. Liang, X. Tian, M. Zhou, et al., “Shikonin and Chitosan-silver Nanoparticles Synergize Against Triple-negative Breast Cancer Through RIPK3-triggered Necroptotic Immunogenic Cell Death,” Biomaterials 309 (2024): 122608.

[235] L. Wang, C. Hu, Y. Zhao, and X. Hu, “Novel Smac Mimetic ASTX660 (Tolinapant) and TNF-α Synergistically Induce Necroptosis in Bladder Cancer Cells in Vitro Upon Apoptosis Inhibition,” Biochemical and Biophysical Research Communications 602 (2022): 8-14.

[236] A. Koch, B. Jeiler, J. Roedig, S. J. L. van Wijk, N. Dolgikh, and S. Fulda, “Smac Mimetics and TRAIL Cooperate to Induce MLKL-dependent Necroptosis in Burkitt's Lymphoma Cell Lines,” Neoplasia 23, no. 5 (2021): 539-550.

[237] M. Montagnani Marelli, G. Beretta, and R. M. Moretti, “Necroptosis Induced by Delta-Tocotrienol Overcomes Docetaxel Chemoresistance in Prostate Cancer Cells,” International Journal of Molecular Sciences 24, no. 5 (2023): 4923.

[238] P. Sonkusre and S. S. Cameotra, “Biogenic Selenium Nanoparticles Induce ROS-mediated Necroptosis in PC-3 Cancer Cells Through TNF Activation,” Journal of Nanobiotechnology 15, no. 1 (2017): 43.

[239] L. C. de Melo Gomes, A. B. de Oliveira Cunha, L. F. F. Peixoto, et al., “Photodynamic Therapy Reduces Cell Viability, Migration and Triggers Necroptosis in Prostate Tumor Cells,” Photochemical & Photobiological Sciences 22, no. 6 (2023): 1341-1356.

[240] Q. Zheng, T. Zou, W. Wang, et al., “Necroptosis-Mediated Synergistic Photodynamic and Glutamine-Metabolic Therapy Enabled by a Biomimetic Targeting Nanosystem for Cholangiocarcinoma,” Advanced Science (Weinh) 11, no. 29 (2024): e2309203.

[241] Á. C. de Souza, A. L. Mencalha, A. S. D. Fonseca, and F. de Paoli, “Necroptosis as a Consequence of Photodynamic Therapy in Tumor Cells,” Lasers in Medical Science 39, no. 1 (2024): 267.

[242] W. Chen, X. Wang, B. Zhao, et al., “CuS-MnS(2) Nano-flowers for Magnetic Resonance Imaging Guided Photothermal/Photodynamic Therapy of Ovarian Cancer Through Necroptosis,” Nanoscale 11, no. 27 (2019): 12983-12989.

[243] M. Montagnani Marelli, C. Macchi, M. Ruscica, P. Sartori, and R. M. Moretti, “Anticancer Activity of Delta-Tocotrienol in Human Hepatocarcinoma: Involvement of Autophagy Induction,” Cancers (Basel) 16, no. 15 (2024): 2654.

[244] S. Cocco, A. Leone, M. S. Roca, et al., “Inhibition of Autophagy by Chloroquine Prevents Resistance to PI3K/AKT Inhibitors and Potentiates Their Antitumor Effect in Combination With paclitaxel in Triple Negative Breast Cancer Models,” Journal of Translational Medicine 20, no. 1 (2022): 290.

[245] P. M. P. Ferreira, R. W. R. Sousa, J. R. O. Ferreira, G. C. G. Militão, and D. P. Bezerra, “Chloroquine and Hydroxychloroquine in Antitumor Therapies Based on Autophagy-related Mechanisms,” Pharmacological Research 168 (2021): 105582.

[246] A. Brockmueller, V. Ruiz de Porras, and M. Shakibaei, “Curcumin and Its Anti-colorectal Cancer Potential: From Mechanisms of Action to Autophagy,” Phytotherapy Research 38, no. 7 (2024): 3525-3551.

[247] X. Tang, H. Ding, M. Liang, et al., “Curcumin Induces Ferroptosis in Non-small-cell Lung Cancer via Activating Autophagy,” Thoracic Cancer 12, no. 8 (2021): 1219-1230.

[248] W. B. Wang, L. X. Feng, Q. X. Yue, et al., “Paraptosis Accompanied by Autophagy and Apoptosis Was Induced by Celastrol, a Natural Compound With Influence on Proteasome, ER Stress and Hsp90,” Journal of Cellular Physiology 227, no. 5 (2012): 2196-2206.

[249] J. Guo, Y. Mei, K. Li, X. Huang, and H. Yang, “Downregulation of miR-17-92a Cluster Promotes Autophagy Induction in Response to Celastrol Treatment in Prostate Cancer Cells,” Biochemical and Biophysical Research Communications 478, no. 2 (2016): 804-810.

[250] J. Guo, X. Huang, H. Wang, and H. Yang, “Celastrol Induces Autophagy by Targeting AR/miR-101 in Prostate Cancer Cells,” PLoS ONE 10, no. 10 (2015): e0140745.

[251] W. Zhang, Z. Wu, H. Qi, et al., “Celastrol Upregulated ATG7 Triggers Autophagy via Targeting Nur77 in Colorectal Cancer,” Phytomedicine 104 (2022): 154280.

[252] Y. Feng, B. Zhang, J. Lv, et al., “Scaffold Hopping of Celastrol Provides Derivatives Containing Pepper Ring, Pyrazine and Oxazole Substructures as Potent Autophagy Inducers Against Breast Cancer Cell Line MCF-7,” European Journal of Medicinal Chemistry 234 (2022): 114254.

[253] L. Chen, Y. Sun, M. Tang, et al., “High-dose-androgen-induced Autophagic Cell Death to Suppress the Enzalutamide-resistant Prostate Cancer Growth via Altering the circRNA-BCL2/miRNA-198/AMBRA1 Signaling,” Cell Death Discovery 8, no. 1 (2022): 128.

[254] Z. Xiang, Y. Sun, B. You, et al., “Suppressing BCL-XL Increased the High Dose Androgens Therapeutic Effect to Better Induce the Enzalutamide-resistant Prostate Cancer Autophagic Cell Death,” Cell Death & Disease 12, no. 1 (2021): 68.

[255] W. K. Martins, R. Belotto, M. N. Silva, et al., “Autophagy Regulation and Photodynamic Therapy: Insights to Improve Outcomes of Cancer Treatment,” Frontiers in Oncology 10 (2020): 610472.

[256] C. Song, W. Xu, H. Wu, et al., “Photodynamic Therapy Induces Autophagy-mediated Cell Death in human Colorectal Cancer Cells via Activation of the ROS/JNK Signaling Pathway,” Cell Death & Disease 11, no. 10 (2020): 938.

[257] A. Ghoochani, E. C. Hsu, M. Aslan, et al., “Ferroptosis Inducers Are a Novel Therapeutic Approach for Advanced Prostate Cancer,” Cancer Research 81, no. 6 (2021): 1583-1594.

[258] Y. Yang, T. Liu, C. Hu, et al., “Ferroptosis Inducer Erastin Downregulates Androgen Receptor and Its Splice Variants in Castration‑Resistant Prostate Cancer,” Oncology Reports 45, no. 4 (2021): 25.

[259] W. Yangyun, S. Guowei, S. Shufen, Y. Jie, Y. Rui, and R. Yu, “Everolimus Accelerates Erastin and RSL3-induced Ferroptosis in Renal Cell Carcinoma,” Gene 809 (2022): 145992.

[260] D. Fu, C. Wang, L. Yu, and R. Yu, “Induction of Ferroptosis by ATF3 Elevation Alleviates Cisplatin Resistance in Gastric Cancer by Restraining Nrf2/Keap1/xCT Signaling,” Cellular & Molecular Biology Letters 26, no. 1 (2021).

[261] C. Desterke, Y. Xiang, R. Elhage, C. Duruel, Y. Chang, and A. Hamaï, “Ferroptosis Inducers Upregulate PD-L1 in Recurrent Triple-Negative Breast Cancer,” Cancers (Basel) 16, no. 1 (2023): 155.

[262] K. Chang, Y. Chen, X. Zhang, et al., “DPP9 Stabilizes NRF2 to Suppress Ferroptosis and Induce Sorafenib Resistance in Clear Cell Renal Cell Carcinoma,” Cancer Research 83, no. 23 (2023): 3940-3955.

[263] L. Li, J. Zeng, S. He, Y. Yang, and C. Wang, “METTL14 decreases FTH1 mRNA Stability via m6A Methylation to Promote Sorafenib-induced Ferroptosis of Cervical Cancer,” Cancer Biology & Therapy 25, no. 1 (2024): 2349429.

[264] Z. Wang, C. Zhou, Y. Zhang, et al., “From Synergy to Resistance: Navigating the Complex Relationship Between Sorafenib and Ferroptosis in Hepatocellular Carcinoma,” Biomedicine & Pharmacotherapy 170 (2024): 116074.

[265] Q. Li, K. Chen, T. Zhang, et al., “Understanding Sorafenib-induced Ferroptosis and Resistance Mechanisms: Implications for Cancer Therapy,” European Journal of Pharmacology 955 (2023): 175913.

[266] F. Maccarinelli, D. Coltrini, S. Mussi, et al., “Iron Supplementation Enhances RSL3-induced Ferroptosis to Treat Naïve and Prevent Castration-resistant Prostate Cancer,” Cell Death Discovery 9, no. 1 (2023): 81.

[267] J. Bordini, F. Morisi, A. R. Elia, et al., “Iron Induces Cell Death and Strengthens the Efficacy of Antiandrogen Therapy in Prostate Cancer Models,” Clinical Cancer Research 26, no. 23 (2020): 6387-6398.

[268] R. Rodriguez, S. L. Schreiber, and M. Conrad, “Persister Cancer Cells: Iron Addiction and Vulnerability to Ferroptosis,” Molecular Cell 82, no. 4 (2022): 728-740.

[269] X. Yao, R. Xie, Y. Cao, et al., “Simvastatin Induced Ferroptosis for Triple-negative Breast Cancer Therapy,” Journal of Nanobiotechnology 19, no. 1 (2021): 311.

[270] W. J. Tang, D. Xu, M. X. Liang, et al., “Pitavastatin Induces Autophagy-dependent Ferroptosis in MDA-MB-231 Cells via the Mevalonate Pathway,” Heliyon 10, no. 5 (2024): e27084.

[271] D. Sun, X. Cui, W. Yang, et al., “Simvastatin Inhibits PD-L1 via ILF3 to Induce Ferroptosis in Gastric Cancer Cells,” Cell Death & Disease 16, no. 1 (2025): 208.

[272] W. Mao, Y. Cai, D. Chen, et al., “Statin Shapes Inflamed Tumor Microenvironment and Enhances Immune Checkpoint Blockade in Non-small Cell Lung Cancer,” JCI Insight 7, no. 18 (2022): e161940.

[273] M. Shi, M. J. Zhang, Y. Yu, et al., “Curcumin Derivative NL01 Induces Ferroptosis in Ovarian Cancer Cells via HCAR1/MCT1 Signaling,” Cell Signalling 109 (2023): 110791.

[274] Z. Liu, H. Ma, and Z. Lai, “The Role of Ferroptosis and Cuproptosis in Curcumin Against Hepatocellular Carcinoma,” Molecules (Basel, Switzerland) 28, no. 4 (2023): 1623.

[275] X. Cao, Y. Li, Y. Wang, et al., “Curcumin Suppresses Tumorigenesis by Ferroptosis in Breast Cancer,” PLoS ONE 17, no. 1 (2022): e0261370.

[276] X. Zhou, L. Zou, W. Chen, et al., “Flubendazole, FDA-approved Anthelmintic, Elicits Valid Antitumor Effects by Targeting P53 and Promoting Ferroptosis in Castration-resistant Prostate Cancer,” Pharmacological Research 164 (2021): 105305.

[277] W. Teng, Y. Ling, N. Long, et al., “Repurposing Flubendazole for Glioblastoma Ferroptosis by Affecting xCT and TFRC Proteins,” Journal of Cellular and Molecular Medicine 28, no. 22 (2024): e70188.

[278] L. M. Khachigian, “Emerging Insights on Functions of the Anthelmintic Flubendazole as a Repurposed Anticancer Agent,” Cancer Letters 522 (2021): 57-62.

[279] L. Wu, F. Liu, L. Yin, et al., “The Establishment of Polypeptide PSMA-targeted Chimeric Antigen Receptor-engineered Natural Killer Cells for Castration-resistant Prostate Cancer and the Induction of Ferroptosis-related Cell Death,” Cancer Communications (London) 42, no. 8 (2022): 768-783.

[280] H. Wang, L. Zhang, Z. Miao, et al., “PSMA-targeted Arsenic Nanosheets: A Platform for Prostate Cancer Therapy via Ferroptosis and ATM Deficiency-triggered Chemosensitization,” Materials Horizons 8, no. 8 (2021): 2216-2229.

[281] B. Tao, R. Du, X. Zhang, et al., “Engineering CAR-NK Cell Derived Exosome Disguised Nano-bombs for Enhanced HER2 Positive Breast Cancer Brain Metastasis Therapy,” Journal of Controlled Release 363 (2023): 692-706.

[282] K. S. Kim, B. Choi, H. Choi, M. J. Ko, D. H. Kim, and D. H. Kim, “Enhanced Natural Killer Cell Anti-tumor Activity With Nanoparticles Mediated Ferroptosis and Potential Therapeutic Application in Prostate Cancer,” Journal of Nanobiotechnology 20, no. 1 (2022): 428.

[283] J. Chen, Y. Wang, L. Han, et al., “A Ferroptosis-inducing Biomimetic Nanocomposite for the Treatment of Drug-resistant Prostate Cancer,” Materials Today Bio 17 (2022): 100484.

[284] Q. T. Huang, Q. Q. Hu, Z. F. Wen, and Y. L. Li, “Iron Oxide Nanoparticles Inhibit Tumor Growth by Ferroptosis in Diffuse Large B-cell Lymphoma,” American Journal of Cancer Research 13, no. 2 (2023): 498-508.

[285] Q. Li, R. Su, X. Bao, et al., “Glycyrrhetinic Acid Nanoparticles Combined With Ferrotherapy for Improved Cancer Immunotherapy,” Acta Biomaterialia 144 (2022): 109-120.

[286] P. Zou, Z. Chen, Q. He, and Y. Zhuo, “Polyphyllin I Induces Ferroptosis in Castration-resistant Prostate Cancer Cells Through the ERK/DNMT1/ACSL4 Axis,” Prostate 84, no. 1 (2024): 64-73.

[287] F. Zheng, Y. Wang, Q. Zhang, et al., “Polyphyllin I Suppresses the Gastric Cancer Growth by Promoting Cancer Cell Ferroptosis,” Frontiers in Pharmacology 14 (2023): 1145407.

[288] R. Yang, W. Gao, Z. Wang, et al., “Polyphyllin I Induced Ferroptosis to Suppress the Progression of Hepatocellular Carcinoma Through Activation of the Mitochondrial Dysfunction via Nrf2/HO-1/GPX4 Axis,” Phytomedicine 122 (2024): 155135.

[289] S. Liu, Y. Tao, S. Wu, et al., “Sanguinarine Chloride Induces Ferroptosis by Regulating ROS/BACH1/HMOX1 Signaling Pathway in Prostate Cancer,” Chinese Medicine 19, no. 1 (2024): 7.

[290] A. Alakkal, F. Thayyullathil, S. Pallichankandy, K. Subburayan, A. R. Cheratta, and S. Galadari, “Sanguinarine Induces H(2)O(2)-Dependent Apoptosis and Ferroptosis in Human Cervical Cancer,” Biomedicines 10, no. 8 (2022): 1795.

[291] R. Xu, J. Wu, Y. Luo, et al., “Sanguinarine Represses the Growth and Metastasis of Non-small Cell Lung Cancer by Facilitating Ferroptosis,” Current Pharmaceutical Design 28, no. 9 (2022): 760-768.

[292] W. Yang, Y. Wang, Y. Huang, et al., “4-Octyl Itaconate Inhibits Aerobic Glycolysis by Targeting GAPDH to Promote Cuproptosis in Colorectal Cancer,” Biomedicine & Pharmacotherapy 159 (2023): 114301.

[293] X. Lu, W. Deng, S. Wang, et al., “PEGylated Elesclomol@Cu(II)-based Metal‒Organic Framework With Effective Nanozyme Performance and Cuproptosis Induction Efficacy for Enhanced PD-L1-based Immunotherapy,” Materials Today Bio 29 (2024): 101317.

[294] N. J. S. Bontempo, D. A. Paixão, P. Lima, et al., “Copper(II) Complex Containing 4-Fluorophenoxyacetic Acid Hydrazide and 1,10-Phenanthroline: A Prostate Cancer Cell-Selective and Low-Toxic Copper(II) Compound,” Molecules (Basel, Switzerland) 27, no. 20 (2022): 7097.

[295] W. Lei, J. Xu, Y. Ya, et al., “Disulfiram-copper Activates Chloride Currents and Induces Apoptosis With Tyrosine Kinase in Prostate Cancer Cells,” Asia-Pacific Journal of Clinical Oncology 18, no. 2 (2022): e46-e55.

[296] J. F. Machado, D. Sequeira, F. Marques, et al., “New Copper(I) Complexes Selective for Prostate Cancer Cells,” Dalton Transactions 49, no. 35 (2020): 12273-12286.

[297] Y. Liao, D. Wang, C. Gu, et al., “A Cuproptosis Nanocapsule for Cancer Radiotherapy,” Nature Nanotechnology 19, no. 12 (2024): 1892-1902.

[298] Y. Li, J. Liu, Y. Chen, R. R. Weichselbaum, and W. Lin, “Nanoparticles Synergize Ferroptosis and Cuproptosis to Potentiate Cancer Immunotherapy,” Advanced Science (Weinh) 11, no. 23 (2024): e2310309.

[299] F. Hu, J. Huang, T. Bing, et al., “Stimulus-Responsive Copper Complex Nanoparticles Induce Cuproptosis for Augmented Cancer Immunotherapy,” Advanced Science (Weinh) 11, no. 13 (2024): e2309388.

[300] B. Guo, F. Yang, L. Zhang, et al., “Cuproptosis Induced by ROS Responsive Nanoparticles With Elesclomol and Copper Combined With αPD-L1 for Enhanced Cancer Immunotherapy,” Advanced Materials 35, no. 22 (2023): e2212267.

[301] D. Zhang, Y. Chen, Y. Sun, et al., “Gambogic Acid Induces GSDME Dependent Pyroptotic Signaling Pathway via ROS/P53/Mitochondria/Caspase-3 in Ovarian Cancer Cells,” Biochemical Pharmacology 232 (2025): 116695.

[302] H. Xu, D. Zhang, R. Wei, et al., “Gambogic Acid Induces Pyroptosis of Colorectal Cancer Cells Through the GSDME-Dependent Pathway and Elicits an Antitumor Immune Response,” Cancers (Basel) 14, no. 22 (2022): 5505.

[303] B. Ouyang, C. Shan, S. Shen, et al., “AI-powered Omics-based Drug Pair Discovery for Pyroptosis Therapy Targeting Triple-negative Breast Cancer,” Nature Communications 15, no. 1 (2024): 7560.

[304] W. Xuzhang, T. Lu, W. Jin, et al., “Cisplatin-induced Pyroptosis Enhances the Efficacy of PD-L1 Inhibitor in Small-Cell Lung Cancer via GSDME/IL12/CD4Tem Axis,” International Journal of Biological Sciences 20, no. 2 (2024): 537-553.

[305] R. Y. Li, Z. Y. Zheng, Z. M. Li, et al., “Cisplatin-induced Pyroptosis Is Mediated via the CAPN1/CAPN2-BAK/BAX-caspase-9-caspase-3-GSDME Axis in Esophageal Cancer,” Chemico-Biological Interactions 361 (2022): 109967.

[306] X. Hou, J. Xu, Y. Wang, et al., “Triggering Pyroptosis by Doxorubicin-Loaded Multifunctional Nanoparticles in Combination With Decitabine for Breast Cancer Chemoimmunotherapy,” ACS Applied Materials & Interfaces 16, no. 43 (2024): 58392-58404.

[307] X. Hou, J. Xia, Y. Feng, et al., “USP47-Mediated Deubiquitination and Stabilization of TCEA3 Attenuates Pyroptosis and Apoptosis of Colorectal Cancer Cells Induced by Chemotherapeutic Doxorubicin,” Frontiers in Pharmacology 12 (2021): 713322.

[308] J. Wu, C. Ding, C. Zhang, et al., “Methionine Metabolite Spermidine Inhibits Tumor Pyroptosis by Enhancing MYO6-mediated Endocytosis,” Nature Communications 16, no. 1 (2025): 2184.

[309] R. Chen, A. Ram, J. G. Albeck, and M. Overholtzer, “Entosis Is Induced by Ultraviolet Radiation,” Iscience 24, no. 8 (2021): 102902.

[310] X. Li, J. Xu, L. Yan, et al., “Targeting Disulfidptosis With Potentially Bioactive Natural Products in Metabolic Cancer Therapy,” Metabolites 14, no. 11 (2024): 604.

[311] W. Denmeade and J. T. Isaacs, “Programmed Cell Death (Apoptosis) and Cancer Chemotherapy,” Cancer Control: Journal of the Moffitt Cancer Center 3 (1996): 303-309.

[312] S. Maniam, “Small Molecules Targeting Programmed Cell Death in Breast Cancer Cells,” International Journal of Molecular Sciences 22, no. 18 (2021): 9722.

[313] Y. Zhang, S. Sun, W. Xu, et al., “Thioredoxin Reductase 1 Inhibitor Shikonin Promotes Cell Necroptosis via Sectraps Generation and Oxygen-Coupled Redox Cycling,” Free Radical Biology and Medicine 180 (2022): 52-62.

[314] P. Chittineedi, S. L. Pandrangi, J. A. Neira Mosquera, S. N. Sánchez Llaguno, and G. J. Mohiddin, “Aqueous Nyctanthes Arbortristis and Doxorubicin Conjugated Gold Nanoparticles Synergistically Induced mTOR-dependent Autophagy-mediated Ferritinophagy in Paclitaxel-resistant Breast Cancer Stem Cells,” Frontiers in Pharmacology 14 (2023): 1201319.

[315] Y. Chen, Q. Zhou, H. Zhang, et al., “Qingdai Decoction Suppresses Prostate Cancer Growth in Lethal-stage Prostate Cancer Models,” Journal of Ethnopharmacology 308 (2023): 116333.

[316] J. Wang, J. Li, J. Liu, et al., “Interplay of Ferroptosis and Cuproptosis in Cancer: Dissecting Metal-Driven Mechanisms for Therapeutic Potentials,” Cancers (Basel) 16, no. 3 (2024): 512.

[317] L. Lin, W. He, Y. Guo, et al., “Nanomedicine-induced Programmed Cell Death in Cancer Therapy: Mechanisms and Perspectives,” Cell Death Discovery 10 (2024): Article number: 386.

[318] F. Yang, G. Zhang, N. An, et al., “Interplay of Ferroptosis, Cuproptosis, and PANoptosis in Cancer Treatment-induced Cardiotoxicity: Mechanisms and Therapeutic Implications,” Seminars in Cancer Biology 106-107 (2024): 106-122.

[319] M. Imam, J. Ji, Z. Zhang, and S. Yan, “Targeting the Initiator to Activate both Ferroptosis and Cuproptosis for Breast Cancer Treatment: Progress and Possibility for Clinical Application,” Frontiers in Pharmacology 15 (2024): 1493188.

[320] Y. Shen, D. Li, Q. Liang, M. Yang, Y. Pan, and H. Li, “Cross-talk Between Cuproptosis and Ferroptosis Regulators Defines the Tumor Microenvironment for the Prediction of Prognosis and Therapies in Lung Adenocarcinoma,” Frontiers in Immunology 13 (2022): 1029092.

[321] K. Yamashita, M. Iwatsuki, N. Yasuda-Yoshihara, et al., “Trastuzumab Upregulates Programmed Death Ligand-1 Expression Through Interaction With NK Cells in Gastric Cancer,” British Journal of Cancer 124, no. 3 (2021): 595-603.

[322] J. Peng, J. Hamanishi, N. Matsumura, et al., “Chemotherapy Induces Programmed Cell Death-Ligand 1 Overexpression via the Nuclear Factor-κB to Foster an Immunosuppressive Tumor Microenvironment in Ovarian Cancer,” Cancer Research 75 (2015): 5034-5045.

[323] L. Yu, K. Huang, Y. Liao, L. Wang, G. Sethi, and Z. Ma, “Targeting Novel Regulated Cell Death: Ferroptosis, Pyroptosis and Necroptosis in Anti-PD-1/PD-L1 Cancer Immunotherapy,” Cell Proliferation 57, no. 8 (2024): e13644.

[324] G. Xie, H. Dong, Y. Liang, J. D. Ham, R. Rizwan, and J. Chen, “CAR-NK Cells: A Promising Cellular Immunotherapy for Cancer,” EBioMedicine 59 (2020): 102975.

[325] Z. Pang, Z. Wang, F. Li, C. Feng, and X. Mu, “Current Progress of CAR-NK Therapy in Cancer Treatment,” Cancers (Basel) 14, no. 17 (2022).

[326] W. Li, X. Wang, X. Zhang, A. U. R. Aziz, and D. Wang, “CAR-NK Cell Therapy: A Transformative Approach to Overcoming Oncological Challenges,” Biomolecules 14, no. 8 (2024).

[327] A. B. Dezfouli, M. Yazdi, A. G. Pockley, et al., “NK Cells Armed With Chimeric Antigen Receptors (CAR): Roadblocks to Successful Development,” Cells 10, no. 12 (2021).

[328] Z. Mao, Y. Hu, and Y. Zhao, “The Mutual Regulatory Role of Ferroptosis and Immunotherapy in Anti-tumor Therapy,” Apoptosis 29 (2024): 1291-1308.

[329] S. Li, J. Shapiro, and H. Shah, “Abstract 5350: Decr2 Regulates Tumor Cell Ferroptosis and Immunotherapy Efficacy,” Cancer Research 84, no. 6_Supplement (2024): 5350.

[330] L. Xie, J. Li, G. Wang, et al., “Phototheranostic Metal-Phenolic Networks With Antiexosomal PD-L1 Enhanced Ferroptosis for Synergistic Immunotherapy,” Journal of the American Chemical Society 144, no. 2 (2022): 787-797.

[331] P. Liu, X. Shi, Y.-Y. Peng, J. Hu, J. Ding, and W. Zhou, “Anti-PD-L1 DNAzyme Loaded Photothermal Mn2+/Fe3+ Hybrid Metal-Phenolic Networks for Cyclically Amplified Tumor Ferroptosis-Immunotherapy,” Advanced Healthcare Materials 11, no. 8 (2021): e2102315.

[332] S. Jeong, B. Jung, D. Lee, et al., “Enhanced Immunogenic Cell Death by Apoptosis/Ferroptosis Hybrid Pathway Potentiates PD-L1 Blockade Cancer Immunotherapy,” ACS Biomaterials Science & Engineering 8, no. 12 (2022): 5188-5198.

[333] C. Yan, Y. Liu, G. Zhao, et al., “Inhalable Metal-organic Framework-mediated Cuproptosis Combined With PD-L1 Checkpoint Blockade for Lung Metastasis Synergistic Immunotherapy,” Acta Pharmaceutica Sinica B 14 (2024): 2281-2297.

[334] X. Lu, W. Deng, and S. Wang, “PEGylated Elesclomol@Cu(II)-based Metal‒Organic Framework With Effective Nanozyme Performance and Cuproptosis Induction Efficacy for Enhanced PD-L1-based Immunotherapy,” Materials Today Bio 29 (2024): 101317.

[335] C. He, N. Zhu, Y. Chen, et al., “Reshaping Immunosuppressive Tumor Microenvironment Using Ferroptosis/Cuproptosis Nanosensitizers for Enhanced Radioimmunotherapy,” Advanced Functional Materials 34, no. 51 (2024): 2409966.

[336] F. Wang, L. Wu, L. Yin, H. Shi, Y. Gu, and N. Xing, “Combined Treatment With Anti-PSMA CAR NK-92 Cell and Anti-PD-L1 Monoclonal Antibody Enhances the Antitumour Efficacy Against Castration-resistant Prostate Cancer,” Clinical and Translational Medicine 12, no. 6 (2022): e901.

[337] H. Wu, “Multiple Cancer Treatment Advances With CAR-NK,” Highlights in Science, Engineering and Technology, no. 36 (2023): 930-938.

[338] M. Gang, N. D. Marin, P. Wong, et al., “CAR-Modified Memory-Like NK Cells Exhibit Potent Responses to NK-Resistant Lymphomas,” Blood 136, no. 20 (2020): 2308-2318.

[339] C. Belka, V. Heinrich, P. Marini, et al., “Ionizing Radiation and the Activation of Caspase-8 in Highly Apoptosis-sensitive Lymphoma Cells,” International Journal of Radiation Biology 75, no. 10 (1999): 1257-1264.

[340] H. Li, T. Yang, J. Zhang, et al., “Pyroptotic Cell Death: An Emerging Therapeutic Opportunity for Radiotherapy,” Cell Death Discovery 10 (2024): Article number: 32.

[341] E. Mališić, N. Petrović, M. Brengues, et al., “Association of Polymorphisms in TGFB1, XRCC1, XRCC3 Genes and CD8 T-lymphocyte Apoptosis With Adverse Effect of Radiotherapy for Prostate Cancer,” Scientific Reports 12, no. 1 (2022): 21306.

[342] M. I. Koukourakis, D. Kalamida, A. Mitrakas, et al., “Intensified Autophagy Compromises the Efficacy of Radiotherapy Against Prostate Cancer,” Biochemical and Biophysical Research Communications 461, no. 2 (2015): 268-274.

[343] A. Mishra, B. Salehi, M. Sharifi-Rad, et al., “Programmed Cell Death, From a Cancer Perspective: An Overview,” Molecular Diagnosis & Therapy 22 (2018): 281-295.

[344] D. Feng, L. Li, D. Li, et al., “Prolyl 4-hydroxylase Subunit Beta (P4HB) Could Serve as a Prognostic and Radiosensitivity Biomarker for Prostate Cancer Patients,” European Journal of Medical Research 28, no. 1 (2023): 245.

[345] X. Shi, D. Feng, P. Han, and W. Wei, “Ferroptosis-related ACSL3 and ACTC1 Predict Metastasis-free Survival for Prostate Cancer Patients Undergoing Radical Radiotherapy,” Asian Journal of Surgery 46, no. 6 (2023): 2489-2490.

[346] N. Liu and M. Chen, “Crosstalk Between Ferroptosis and Cuproptosis: From Mechanism to Potential Clinical Application,” Biomedicine & Pharmacotherapy 171 (2024): 116115.

[347] G. Liu, X. Lv, Y. Ding, and Y. Guo, “Precise Medicine of Programmed Cell Death-1/Programmed Cell Death 1 Ligand 1 Inhibitor Immunotherapy Combined Radiotherapy for Inoperable Advanced Lung Cancer,” Medicine 100, no. 24 (2021): e26367.

[348] Y. Huang, H. Li, L. Peng, et al., “Programmed Cell Death 1 Inhibitors With or Without Concurrent Brain Radiotherapy for Lung Cancer Patients With Brain Metastases,” Annals of Palliative Medicine 10 (2021): 9974-9983.

[349] R. Rosell, A. Jain, J. Codony-Servat, E. Jantus-Lewintre, B. Morrison, and J. B. Ginesta, “González-Cao M: Biological Insights in Non-small Cell Lung Cancer,” Cancer Biology & Medicine 20, no. 7 (2023): 500-518.

[350] P. Seneci, “Small Molecules as Pro-apoptotic Anticancer Agents,” Pharmaceutical Patent Analyst 1, no. 4 (2012): 483-505.

[351] S. Jin, H. Wang, Z. Zhang, and M. Yan, “Targeting Ferroptosis: Small-Molecule Inducers as Novel Anticancer Agents,” Anti-Cancer Agents in Medicinal Chemistry 25, no. 8 (2025): 517-532.

[352] B. Sun, L. Zhang, B. Wu, and X. Luo, “A Morpholine Derivative N-(4-morpholinomethylene)ethanesulfonamide Induces Ferroptosis in Tumor Cells by Targeting NRF2,” Biological & Pharmaceutical Bulletin 47, no. 2 (2024): 417-426.

[353] X. Ning, H. Qi, Y. Yuan, et al., “Identification of a New Small Molecule That Initiates Ferroptosis in Cancer Cells by Inhibiting the System Xc- to Deplete GSH,” European Journal of Pharmacology 934 (2022): 175304.

[354] W. Taylor, S. R. Fedorka, I. Gad, et al., “Small-Molecule Ferroptotic Agents With Potential to Selectively Target Cancer Stem Cells,” Scientific Reports 9 (2019): 5926.

[355] Y. Vinik, A. Maimon, V. Dubey, et al., “Programming a Ferroptosis-to-Apoptosis Transition Landscape Revealed Ferroptosis Biomarkers and Repressors for Cancer Therapy,” Advanced Science 11, no. 17 (2024): e2307263.

[356] X. Liu, L. Zhuang, and B. Gan, “Disulfidptosis: Disulfide Stress-Induced Cell Death,” Trends in Cell Biology 34, no. 4 (2024): 327-337.

[357] D. Liang, Y. Feng, F. Zandkarimi, et al., “Ferroptosis Surveillance Independent of GPX4 and Differentially Regulated by Sex Hormones,” Cell 186, no. 13 (2023): 2748-2764.e2722.

[358] R. R. Chhipa, Y. Wu, and C. Ip, “AMPK-mediated Autophagy Is a Survival Mechanism in Androgen-dependent Prostate Cancer Cells Subjected to Androgen Deprivation and Hypoxia,” Cell Signalling 23, no. 9 (2011): 1466-1472.

[359] H. L. Bennett, J. Stockley, J. T. Fleming, et al., “Does Androgen-ablation Therapy (AAT) Associated Autophagy Have a Pro-survival Effect in LNCaP human Prostate Cancer Cells?,” Bju International 111, no. 4 (2013): 672-682.

[360] Y. Feng, H. Cao, Z. Song, L. Chen, D. Wang, and R. Gao, “Qi Ling Decoction Enhances Abiraterone Treatment via Suppression of Autophagy in Castration Resistant Prostate Cancer,” Aging (Albany NY) 14, no. 24 (2022): 9942-9950.

[361] T. Ueno, N. Masuda, S. Kamigaki, et al., “Differential Involvement of Autophagy and Apoptosis in Response to Chemoendocrine and Endocrine Therapy in Breast Cancer: Jbcrg-07tr,” International Journal of Molecular Science 20, no. 4 (2019).

[362] H.-M. Wu, J.-C. Cheng, H. S. Wang, H. Y. Huang, C. D. MacCalman, and P. C. Leung, “Gonadotropin-Releasing Hormone Type II Induces Apoptosis of Human Endometrial Cancer Cells,” Cancer Research 69, no. 10 (2009): 4202-4208.

[363] H. M. Wu, A. V. Schally, J. C. Cheng, M. Zarandi, J. Varga, and P. C. Leung, “Growth Hormone-Releasing Hormone Antagonist Induces Apoptosis of Human Endometrial Cancer Cells Through Pkcδ-Mediated Activation of P53/P21,” Cancer Letters 298, no. 1 (2010): 16-25.

[364] H. Wang, Y. Wu, S. Chen, M. Hou, Y. Yang, and M. Xie, “Construction and Validation of a Ferroptosis-Related Prognostic Model for Endometrial Cancer,” Frontiers in Genetics 12 (2021): 729046.

[365] Y. Qian, H. Chen, P. Miao, et al., “Integrated Identification and Immunotherapy Response Analysis of the Prognostic Signature Associated With M6a, Cuproptosis-Related, Ferroptosis-Related Lncrna in Endometrial Cancer,” Cancer Reports (Hoboken) 7, no. 9 (2024): e70009.

[366] A. Hagege, D. Ambrosetti, J. Boyer, et al., “The Polo-Like Kinase 1 Inhibitor onvansertib Represents a Relevant Treatment for Head and Neck Squamous Cell Carcinoma Resistant to Cisplatin and Radiotherapy,” Theranostics 11, no. 19 (2021): 9571-9586.

[367] G. M. Springett, K. Husain, A. Neuger, et al., “A Phase I Safety, Pharmacokinetic, and Pharmacodynamic Presurgical Trial of Vitamin E δ-tocotrienol in Patients With Pancreatic Ductal Neoplasia,” EBioMedicine 2, no. 12 (2015): 1987-1995.

[368] A. Colville, J. Y. Liu, C. Rodriguez-Mateo, et al., “Death-seq Identifies Regulators of Cell Death and Senolytic Therapies,” Cell Metabolism 35, no. 10 (2023): 1814-1829.e1816.

[369] L. Hao, A. Zhang, D. Lv, L. Cong, Z. Sun, and L. Liu, “EGCG Activates Keap1/P62/Nrf2 Pathway, Inhibits Iron Deposition and Apoptosis in Rats With Cerebral Hemorrhage,” Scientific Reports 14, no. 1 (2024): 31474.

[370] R. Yang, D. Yu, J. Ren, et al., “CD44 Deficiency Induces Combinatory NRF2 Inhibition and Endoplasmic Reticulum Stress-Associated Dyserythropoiesis,” FASEB Journal: Official Publication of the Federation of American Societies for Experimental Biology 39, no. 11 (2025): e70695.

RIGHTS & PERMISSIONS

2025 The Author(s). MedComm published by Sichuan International Medical Exchange & Promotion Association (SCIMEA) and John Wiley & Sons Australia, Ltd.