{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T13:56:16Z","timestamp":1790776576940,"version":"4.1.0"},"reference-count":200,"publisher":"MDPI AG","issue":"19","license":[{"start":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T00:00:00Z","timestamp":1790726400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Int. J. Mol. Sci.","IJMS"],"abstract":"<jats:p>Cuproptosis is a copper-dependent form of regulated cell death driven by disrupted copper homeostasis and mitochondrial metabolic reprogramming. It is distinct from other cell death pathways and has been increasingly linked to vascular endothelial dysfunction and neurodegenerative diseases such as Alzheimer\u2019s and Parkinson\u2019s disease. This article comprehensively reviews the core molecular mechanisms of cuproptosis and its emerging roles in endothelial dysfunction and neurodegeneration, synthesizing recent findings from cellular, animal, and human studies. Cuproptosis exacerbates vascular pathology by impairing endothelial barrier function, inducing oxidative stress, and promoting inflammation and senescence. In the brain, it drives neurodegeneration both directly\u2014via mitochondrial damage and neuronal loss\u2014and indirectly by interacting with pathological proteins such as amyloid-beta and \u03b1-synuclein, creating a vicious cycle of copper dysregulation and protein aggregation. This review provides new insights into the pathophysiology of vascular endothelial dysfunction and neurodegenerative diseases by highlighting the pivotal role of cuproptosis. Understanding how cuproptosis links copper metabolism to cell death pathways opens avenues for identifying novel therapeutic targets. Interventions that restore copper homeostasis or block cuproptosis-specific molecular events may offer promising strategies for treating these devastating diseases.<\/jats:p>","DOI":"10.3390\/ijms27198765","type":"journal-article","created":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T13:01:19Z","timestamp":1790773279000},"page":"8765","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Cuproptosis: New Mechanisms Linking Endothelial Dysfunction to Neurodegenerative Diseases and Therapeutic Prospects"],"prefix":"10.3390","volume":"27","author":[{"ORCID":"https:\/\/orcid.org\/0009-0005-1294-840X","authenticated-orcid":false,"given":"Tianyi","family":"Gu","sequence":"first","affiliation":[{"name":"College of Traditional Chinese Medicine, Tianjin University of Traditional Chinese Medicine, Tianjin 301617, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiaoyu","family":"Wei","sequence":"additional","affiliation":[{"name":"College of Traditional Chinese Medicine, Tianjin University of Traditional Chinese Medicine, Tianjin 301617, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8690-3918","authenticated-orcid":false,"given":"Shengyu","family":"Hua","sequence":"additional","affiliation":[{"name":"College of Traditional Chinese Medicine, Tianjin University of Traditional Chinese Medicine, Tianjin 301617, China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,9,30]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1038\/s41392-022-01014-x","article-title":"Cuproptosis: Lipoylated TCA Cycle Proteins-Mediated Novel Cell Death Pathway","volume":"7","author":"Li","year":"2022","journal-title":"Signal Transduct. Target. Ther."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"1254","DOI":"10.1126\/science.abf0529","article-title":"Copper Induces Cell Death by Targeting Lipoylated TCA Cycle Proteins","volume":"375","author":"Tsvetkov","year":"2022","journal-title":"Science"},{"key":"ref_3","first-page":"337","article-title":"Cuproptosis and Physical Training","volume":"88","author":"Kordi","year":"2024","journal-title":"Clin. Hemorheol. Microcirc."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"114830","DOI":"10.1016\/j.biopha.2023.114830","article-title":"The Molecular Mechanisms of Cuproptosis and Its Relevance to Cardiovascular Disease","volume":"163","author":"Wang","year":"2023","journal-title":"Biomed. Pharmacother."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1186\/s12967-025-06163-5","article-title":"MT2A Promotes Angiogenesis in Chronically Ischemic Brains through a Copper-Mitochondria Regulatory Mechanism","volume":"23","author":"Mo","year":"2025","journal-title":"J. Transl. Med."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"115802","DOI":"10.1016\/j.biopha.2023.115802","article-title":"Different Types of Cell Death in Diabetic Endothelial Dysfunction","volume":"168","author":"Shen","year":"2023","journal-title":"Biomed. Pharmacother."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1097\/FJC.0000000000001728","article-title":"Types, Molecular Mechanisms, and Potential Therapeutic Targets of Programmed Endothelial Cell Death in Atherosclerosis","volume":"86","author":"Kuang","year":"2025","journal-title":"J. Cardiovasc. Pharmacol."},{"key":"ref_8","doi-asserted-by":"crossref","unstructured":"Genchi, G., Catalano, A., Carocci, A., Sinicropi, M.S., and Lauria, G. (2025). Copper, Cuproptosis, and Neurodegenerative Diseases. Int. J. Mol. Sci., 26.","DOI":"10.3390\/ijms26189173"},{"key":"ref_9","doi-asserted-by":"crossref","unstructured":"Chen, G., Xi, E., Gu, X., Wang, H., and Tang, Q. (2024). The Study on Cuproptosis in Alzheimer\u2019s Disease Based on the Cuproptosis Key Gene FDX1. Front. Aging Neurosci., 16.","DOI":"10.3389\/fnagi.2024.1480332"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"102214","DOI":"10.1016\/j.arr.2024.102214","article-title":"The Mechanism of Cuproptosis in Parkinson\u2019s Disease","volume":"95","author":"Huang","year":"2024","journal-title":"Ageing Res. Rev."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1038\/s41531-025-01250-2","article-title":"Multi-Omic Insight into the Molecular Mechanism of Cuproptosis-Related Genes in the Pathogenesis of Parkinson\u2019s Disease","volume":"12","author":"Zhang","year":"2026","journal-title":"npj Park. Dis."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"112236","DOI":"10.1016\/j.cellsig.2025.112236","article-title":"The Molecular Mechanisms of Cuproptosis and Its Role in Central Nervous System Diseases","volume":"138","author":"Xu","year":"2026","journal-title":"Cell. Signal."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1038\/s41419-020-2404-5","article-title":"Elevated Intracellular Copper Contributes a Unique Role to Kidney Fibrosis by Lysyl Oxidase Mediated Matrix Crosslinking","volume":"11","author":"Niu","year":"2020","journal-title":"Cell Death Dis."},{"key":"ref_14","doi-asserted-by":"crossref","unstructured":"Greco, M., Spinelli, C.C., De Riccardis, L., Buccolieri, A., Di Giulio, S., Musar\u00f2, D., Pagano, C., Manno, D., and Maffia, M. (2021). Copper Dependent Modulation of \u03b1-Synuclein Phosphorylation in Differentiated SHSY5Y Neuroblastoma Cells. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22042038"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"113065","DOI":"10.1016\/j.celrep.2023.113065","article-title":"A Co-Opted Endogenous Retroviral Envelope Promotes Cell Survival by Controlling CTR1-Mediated Copper Transport and Homeostasis","volume":"42","author":"Tury","year":"2023","journal-title":"Cell Rep."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"2175","DOI":"10.1080\/15548627.2023.2200554","article-title":"Copper Metabolism in Cell Death and Autophagy","volume":"19","author":"Xue","year":"2023","journal-title":"Autophagy"},{"key":"ref_17","doi-asserted-by":"crossref","unstructured":"Gromadzka, G., Wilkaniec, A., Tarnacka, B., Hadrian, K., Bendykowska, M., Przyby\u0142kowski, A., and Litwin, T. (2024). The Role of Glia in Wilson\u2019s Disease: Clinical, Neuroimaging, Neuropathological and Molecular Perspectives. Int. J. Mol. Sci., 25.","DOI":"10.3390\/ijms25147545"},{"key":"ref_18","doi-asserted-by":"crossref","unstructured":"Ma\u0142yszko, M., and Przyby\u0142kowski, A. (2024). Copper and Colorectal Cancer. Cancers, 16.","DOI":"10.3390\/cancers16213691"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"110401","DOI":"10.1016\/j.biopha.2020.110401","article-title":"The Contribution of Copper Efflux Transporters ATP7A and ATP7B to Chemoresistance and Personalized Medicine in Ovarian Cancer","volume":"129","author":"Herzog","year":"2020","journal-title":"Biomed. Pharmacother."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"15330338211039127","DOI":"10.1177\/15330338211039127","article-title":"MiR-495 Inhibits Cisplatin Resistance and Angiogenesis in Esophageal Cancer by Targeting ATP7A","volume":"20","author":"Li","year":"2021","journal-title":"Technol. Cancer Res. Treat."},{"key":"ref_21","doi-asserted-by":"crossref","unstructured":"Kitala-Ta\u0144ska, K., Socha, K., Ju\u015bkiewicz, J., Krajewska-W\u0142odarczyk, M., and Majewski, M. (2024). The Effect of an Elevated Dietary Copper Level on the Vascular Contractility and Oxidative Stress in Middle-Aged Rats. Nutrients, 16.","DOI":"10.3390\/nu16081172"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1007\/s10495-025-02211-z","article-title":"Copper Modulates Cell Fate through the PLK1-FOXO3a-\u03b2-Catenin Signaling Pathway by Differentially Regulating Cuproptosis and EMT","volume":"31","author":"Lee","year":"2026","journal-title":"Apoptosis"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"113206","DOI":"10.1016\/j.jinorgbio.2025.113206","article-title":"Developing a Novel Binuclear Copper Complex for Enhanced Cellular Copper Uptake and Cancer Treatment","volume":"277","author":"Liu","year":"2026","journal-title":"J. Inorg. Biochem."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"e2202949","DOI":"10.1002\/adhm.202202949","article-title":"Tumor Microenvironment Responsive Hollow Nanoplatform for Triple Amplification of Oxidative Stress to Enhance Cuproptosis-Based Synergistic Cancer Therapy","volume":"12","author":"Xu","year":"2023","journal-title":"Adv. Healthc. Mater."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"394","DOI":"10.1186\/s40001-025-02640-1","article-title":"Tetrathiomolybdate Alleviates Bleomycin-Induced Pulmonary Fibrosis by Reducing Copper Concentration and Suppressing EMT","volume":"30","author":"Wang","year":"2025","journal-title":"Eur. J. Med. Res."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"35334","DOI":"10.1074\/jbc.M404747200","article-title":"Specific Copper Transfer from the Cox17 Metallochaperone to Both Sco1 and Cox11 in the Assembly of Yeast Cytochrome C Oxidase","volume":"279","author":"Horng","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"3124","DOI":"10.4103\/NRR.NRR-D-24-00642","article-title":"Copper Homeostasis and Neurodegenerative Diseases","volume":"20","author":"Wang","year":"2025","journal-title":"Neural Regen. Res."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"2067","DOI":"10.1016\/j.jmb.2020.01.036","article-title":"COA6 Facilitates Cytochrome c Oxidase Biogenesis as Thiol-Reductase for Copper Metallochaperones in Mitochondria","volume":"432","author":"Wasilewski","year":"2020","journal-title":"J. Mol. Biol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"4114","DOI":"10.1016\/j.celrep.2019.11.054","article-title":"COA6 Is Structurally Tuned to Function as a Thiol-Disulfide Oxidoreductase in Copper Delivery to Mitochondrial Cytochrome c Oxidase","volume":"29","author":"Soma","year":"2019","journal-title":"Cell Rep."},{"key":"ref_30","doi-asserted-by":"crossref","unstructured":"Swaminathan, A.B., and Gohil, V.M. (2022). The Role of COA6 in the Mitochondrial Copper Delivery Pathway to Cytochrome c Oxidase. Biomolecules, 12.","DOI":"10.3390\/biom12010125"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"10233","DOI":"10.1074\/jbc.M610082200","article-title":"Characterization of the Cytochrome c Oxidase Assembly Factor Cox19 of Saccharomyces Cerevisiae","volume":"282","author":"Rigby","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"683","DOI":"10.1091\/mbc.e12-09-0705","article-title":"COX19 Mediates the Transduction of a Mitochondrial Redox Signal from SCO1 That Regulates ATP7A-Mediated Cellular Copper Efflux","volume":"24","author":"Leary","year":"2013","journal-title":"Mol. Biol. Cell"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"31943","DOI":"10.1074\/jbc.M405014200","article-title":"COX23, a Homologue of COX17, Is Required for Cytochrome Oxidase Assembly","volume":"279","author":"Barros","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"e2206905119","DOI":"10.1073\/pnas.2206905119","article-title":"Memo1 Binds Reduced Copper Ions, Interacts with Copper Chaperone Atox1, and Protects against Copper-Mediated Redox Activity In Vitro","volume":"119","author":"Zhang","year":"2022","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1080\/01902148.2026.2649073","article-title":"Copper Homeostasis Dysregulation and Cuproptosis in Respiratory Diseases","volume":"52","author":"Gao","year":"2026","journal-title":"Exp. Lung Res."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"e70807","DOI":"10.1002\/jbt.70807","article-title":"Progress in the Research of Cuproptosis and Possible Targets for Gynecological Cancers","volume":"40","author":"Tian","year":"2026","journal-title":"J. Biochem. Mol. Toxicol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"1393","DOI":"10.1007\/s10495-024-01978-x","article-title":"Cuproptosis in Lung Cancer: Therapeutic Options and Prognostic Models","volume":"29","author":"Jawed","year":"2024","journal-title":"Apoptosis"},{"key":"ref_38","doi-asserted-by":"crossref","unstructured":"Huo, S., Wang, Q., Shi, W., Peng, L., Jiang, Y., Zhu, M., Guo, J., Peng, D., Wang, M., and Men, L. (2023). ATF3\/SPI1\/SLC31A1 Signaling Promotes Cuproptosis Induced by Advanced Glycosylation End Products in Diabetic Myocardial Injury. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms24021667"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"115788","DOI":"10.1016\/j.intimp.2025.115788","article-title":"Cuproptosis as a Regulator in Human Diseases: From Basic Mechanisms to Clinical Relevance","volume":"168","author":"Chen","year":"2026","journal-title":"Int. Immunopharmacol."},{"key":"ref_40","doi-asserted-by":"crossref","unstructured":"Zhang, L., Deng, R., Guo, R., Jiang, Y., Guan, Y., Chen, C., Zhao, W., Huang, G., Liu, L., and Du, H. (2024). Recent Progress of Methods for Cuproptosis Detection. Front. Mol. Biosci., 11.","DOI":"10.3389\/fmolb.2024.1460987"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1016\/j.freeradbiomed.2023.05.017","article-title":"Copper Exerts Cytotoxicity through Inhibition of Iron-Sulfur Cluster Biogenesis on ISCA1\/ISCA2\/ISCU Assembly Proteins","volume":"204","author":"Du","year":"2023","journal-title":"Free Radic. Biol. Med."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"eabj9889","DOI":"10.1126\/sciadv.abj9889","article-title":"A Pathogenic Role for Histone H3 Copper Reductase Activity in a Yeast Model of Friedreich\u2019s Ataxia","volume":"7","author":"Campos","year":"2021","journal-title":"Sci. Adv."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"876","DOI":"10.1038\/s41418-023-01125-0","article-title":"Cuproptosis: P53-Regulated Metabolic Cell Death?","volume":"30","author":"Xiong","year":"2023","journal-title":"Cell Death Differ."},{"key":"ref_44","first-page":"17663","article-title":"Cuproptosis as the New Kryptonite of Cancer: A Copper-Dependent Novel Cell Death Mechanism with Promising Implications for the Treatment of Hepatocellular Carcinoma","volume":"149","author":"Ozkan","year":"2023","journal-title":"J. Cancer Res. Clin. Oncol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"4195","DOI":"10.1038\/s41467-024-48433-8","article-title":"Ferritinophagy Mediates Adaptive Resistance to EGFR Tyrosine Kinase Inhibitors in Non-Small Cell Lung Cancer","volume":"15","author":"Wang","year":"2024","journal-title":"Nat. Commun."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1016\/j.trecan.2025.12.002","article-title":"Cuproptosis in Cancer: From Molecular Mechanisms to Therapeutic Intervention","volume":"12","author":"Jiang","year":"2026","journal-title":"Trends Cancer"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"558","DOI":"10.1038\/s41401-023-01174-8","article-title":"ASH2L Upregulation Contributes to Diabetic Endothelial Dysfunction in Mice through STEAP4-Mediated Copper Uptake","volume":"45","author":"Zhong","year":"2024","journal-title":"Acta Pharmacol. Sin."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"107433","DOI":"10.1016\/j.vph.2024.107433","article-title":"Altered Copper Transport in Oxidative Stress-Dependent Brain Endothelial Barrier Dysfunction Associated with Alzheimer\u2019s Disease","volume":"157","author":"Hossain","year":"2024","journal-title":"Vasc. Pharmacol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"3091","DOI":"10.1038\/s41467-021-23408-1","article-title":"The P-Type ATPase Transporter ATP7A Promotes Angiogenesis by Limiting Autophagic Degradation of VEGFR2","volume":"12","author":"Ash","year":"2021","journal-title":"Nat. Commun."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"C933","DOI":"10.1152\/ajpcell.00151.2020","article-title":"Caveolin-1 Stabilizes ATP7A, a Copper Transporter for Extracellular SOD, in Vascular Tissue to Maintain Endothelial Function","volume":"319","author":"Sudhahar","year":"2020","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"17089","DOI":"10.2147\/JIR.S561184","article-title":"Cuproptosis and Immune Microenvironment Interplay in Temporal Lobe Epilepsy: Identification of Key Molecular Signatures and Therapeutic Targets","volume":"18","author":"Li","year":"2025","journal-title":"J. Inflamm. Res."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"9312","DOI":"10.1021\/acsnano.5c20888","article-title":"A Multifunctional Calcium Phosphate Nanoplatform Inducing Synergistic Copper\/Calcium Overload and Antiangiogenesis for Enhanced Cancer Therapy","volume":"20","author":"Zhao","year":"2026","journal-title":"ACS Nano"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1007\/s11011-025-01559-0","article-title":"Edaravone Dextranol Alleviates Ferroptosis, Cuproptosis, and Blood-Brain Barrier Damage after Acute Cerebral Infarction","volume":"40","author":"Jin","year":"2025","journal-title":"Metab. Brain Dis."},{"key":"ref_54","doi-asserted-by":"crossref","unstructured":"Dang, Y., Yan, C., Rui, H., Yan, X., Li, M., Dong, X., and Ma, L. (2026). Cell-Specific Exosomes in Sepsis-Associated ARDS: From Immunometabolic Reprogramming to Precision Medicine. Front. Immunol., 17.","DOI":"10.3389\/fimmu.2026.1799086"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1186\/s43556-023-00131-5","article-title":"A Novel Cuproptosis-Related Diagnostic Gene Signature and Differential Expression Validation in Atherosclerosis","volume":"4","author":"Cui","year":"2023","journal-title":"Mol. Biomed."},{"key":"ref_56","doi-asserted-by":"crossref","unstructured":"Han, Z., Lu, X., He, Y., Zhang, T., Zhou, Z., Zhang, J., and Zhou, H. (2024). Integration of Bulk\/scRNA-Seq and Multiple Machine Learning Algorithms Identifies PIM1 as a Biomarker Associated with Cuproptosis and Ferroptosis in Abdominal Aortic Aneurysm. Front. Immunol., 15.","DOI":"10.3389\/fimmu.2024.1486209"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"115839","DOI":"10.1016\/j.biopha.2023.115839","article-title":"Copper Homeostasis and Copper-Induced Cell Death: Novel Targeting for Intervention in the Pathogenesis of Vascular Aging","volume":"169","author":"Chen","year":"2023","journal-title":"Biomed. Pharmacother."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"4481","DOI":"10.2147\/IJN.S378727","article-title":"Respiratory Exposure to Copper Oxide Particles Causes Multiple Organ Injuries via Oxidative Stress in a Rat Model","volume":"17","author":"Wang","year":"2022","journal-title":"Int. J. Nanomed."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"123334","DOI":"10.1016\/j.lfs.2024.123334","article-title":"Unc5b Prevents Macrophage-Derived Foam Cell Migration and Promotes Atherosclerotic Development via the P53-Cuproptosis Signaling Pathway","volume":"361","author":"Wang","year":"2025","journal-title":"Life Sci."},{"key":"ref_60","doi-asserted-by":"crossref","unstructured":"Zhang, F., Wang, L., and Zhou, Y. (2025). Mitochondria as the Central Regulator of Cell Death in Bronchopulmonary Dysplasia. Front. Physiol., 16.","DOI":"10.3389\/fphys.2025.1685526"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1186\/s10020-024-00997-3","article-title":"Elabela Alleviates Cuproptosis and Vascular Calcification in vitaminD3- Overloaded Mice via Regulation of the PPAR-\u03b3\/FDX1 Signaling","volume":"30","author":"Qi","year":"2024","journal-title":"Mol. Med."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"e11630","DOI":"10.1002\/advs.202511630","article-title":"Engineered Multifunctional Hydrogel Delivering Novel CBX7 Inhibitor Modulates Cuproptosis Via Liquid-Liquid Phase Separation to Restore Cardiac Function in Aged Myocardial Infarction","volume":"13","author":"Liu","year":"2026","journal-title":"Adv. Sci."},{"key":"ref_63","doi-asserted-by":"crossref","unstructured":"Solito, E., and Sastre, M. (2012). Microglia Function in Alzheimer\u2019s Disease. Front. Pharmacol., 3.","DOI":"10.3389\/fphar.2012.00014"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1186\/s40035-022-00326-w","article-title":"Dual Role of Brain-Derived Extracellular Vesicles in Dementia-Related Neurodegenerative Disorders: Cargo of Disease Spreading Signals and Diagnostic-Therapeutic Molecules","volume":"11","author":"Natale","year":"2022","journal-title":"Transl. Neurodegener."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"454","DOI":"10.1186\/s13071-025-07107-0","article-title":"Cuproptosis-Driven Astrocyte Reactivity Exacerbates Experimental Cerebral Malaria Pathogenesis","volume":"18","author":"Hou","year":"2025","journal-title":"Parasites Vectors"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"103872","DOI":"10.1016\/j.redox.2025.103872","article-title":"Copper Overload Worsens the Inflammatory Response of Microglia to Amyloid Beta (A\u03b2) by Impairing Phagocytosis and Promoting Mitochondrial DNA-Mediated NLRP3 Inflammasome Activation","volume":"87","author":"Zubillaga","year":"2025","journal-title":"Redox Biol."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1007\/s12012-026-10094-y","article-title":"Cuproptosis and Its Impact on Cardiovascular Health: Mechanisms and Therapeutic Opportunities","volume":"26","author":"Huang","year":"2026","journal-title":"Cardiovasc. Toxicol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"172","DOI":"10.3892\/ijmm.2025.5613","article-title":"Copper Homeostasis and Cuproptosis in Alzheimer\u2019s Disease (Review)","volume":"56","author":"Cong","year":"2025","journal-title":"Int. J. Mol. Med."},{"key":"ref_69","doi-asserted-by":"crossref","unstructured":"Neely, C.L.C., Lippi, S.L.P., Lanzirotti, A., and Flinn, J.M. (2019). Localization of Free and Bound Metal Species through X-Ray Synchrotron Fluorescence Microscopy in the Rodent Brain and Their Relation to Behavior. Brain Sci., 9.","DOI":"10.3390\/brainsci9040074"},{"key":"ref_70","first-page":"580005","article-title":"Copper Homeostasis and Cuproptosis in Neurological Disorders","volume":"20","author":"Liu","year":"2026","journal-title":"Drug Des. Dev. Ther."},{"key":"ref_71","doi-asserted-by":"crossref","unstructured":"Tabb\u00ec, G., Cucci, L.M., Pinzino, C., Munzone, A., Marzo, T., Pizzanelli, S., Satriano, C., Magr\u00ec, A., and La Mendola, D. (2021). Peptides Derived from Angiogenin Regulate Cellular Copper Uptake. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22179530"},{"key":"ref_72","doi-asserted-by":"crossref","unstructured":"Peng, G., Huang, Y., Xie, G., and Tang, J. (2024). Exploring Copper\u2019s Role in Stroke: Progress and Treatment Approaches. Front. Pharmacol., 15.","DOI":"10.3389\/fphar.2024.1409317"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"mfac018","DOI":"10.1093\/mtomcs\/mfac018","article-title":"Copper-Mediated \u03b2-Amyloid Toxicity and Its Chelation Therapy in Alzheimer\u2019s Disease","volume":"14","author":"Singh","year":"2022","journal-title":"Metallomics"},{"key":"ref_74","doi-asserted-by":"crossref","unstructured":"Sasanian, N., Bernson, D., Horvath, I., Wittung-Stafshede, P., and Esbj\u00f6rner, E.K. (2020). Redox-Dependent Copper Ion Modulation of Amyloid-\u03b2 (1-42) Aggregation In Vitro. Biomolecules, 10.","DOI":"10.3390\/biom10060924"},{"key":"ref_75","doi-asserted-by":"crossref","unstructured":"Toader, C., Tataru, C.P., Munteanu, O., Serban, M., Covache-Busuioc, R.-A., Ciurea, A.V., and Enyedi, M. (2024). Decoding Neurodegeneration: A Review of Molecular Mechanisms and Therapeutic Advances in Alzheimer\u2019s, Parkinson\u2019s, and ALS. Int. J. Mol. Sci., 25.","DOI":"10.3390\/ijms252312613"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1038\/srep00011","article-title":"Mechanism of Copper(II)-Induced Misfolding of Parkinson\u2019s Disease Protein","volume":"1","author":"Rose","year":"2011","journal-title":"Sci. Rep."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"858","DOI":"10.1016\/j.neurobiolaging.2013.09.034","article-title":"Copper Pathology in Vulnerable Brain Regions in Parkinson\u2019s Disease","volume":"35","author":"Davies","year":"2014","journal-title":"Neurobiol. Aging"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"1410","DOI":"10.1021\/acschemneuro.2c00021","article-title":"Single-Particle Resolution of Copper-Associated Annular \u03b1-Synuclein Oligomers Reveals Potential Therapeutic Targets of Neurodegeneration","volume":"13","author":"Synhaivska","year":"2022","journal-title":"ACS Chem. Neurosci."},{"key":"ref_79","doi-asserted-by":"crossref","unstructured":"Patel, R., and Aschner, M. (2021). Commonalities between Copper Neurotoxicity and Alzheimer\u2019s Disease. Toxics, 9.","DOI":"10.3390\/toxics9010004"},{"key":"ref_80","doi-asserted-by":"crossref","unstructured":"An, Y., Li, S., Huang, X., Chen, X., Shan, H., and Zhang, M. (2022). The Role of Copper Homeostasis in Brain Disease. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms232213850"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"111493","DOI":"10.1016\/j.jinorgbio.2021.111493","article-title":"Interactions of Copper and Copper Chelate Compounds with the Amyloid Beta Peptide: An Investigation into Electrochemistry, Reactive Oxygen Species and Peptide Aggregation","volume":"222","author":"Crnich","year":"2021","journal-title":"J. Inorg. Biochem."},{"key":"ref_82","doi-asserted-by":"crossref","unstructured":"Metaxas, A. (2021). Imbalances in Copper or Zinc Concentrations Trigger Further Trace Metal Dyshomeostasis in Amyloid-Beta Producing Caenorhabditis Elegans. Front. Neurosci., 15.","DOI":"10.3389\/fnins.2021.755475"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1007\/s00395-026-01163-y","article-title":"Amyloid Beta 42 Disrupts Cardiac Function in Alzheimer\u2019s Disease Mice via SLC31A1 Upregulation-Mediated Cuproptosis","volume":"121","author":"Xiong","year":"2026","journal-title":"Basic Res. Cardiol."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"850","DOI":"10.1038\/s41419-024-07206-3","article-title":"Copper Homeostasis and Cuproptosis in Central Nervous System Diseases","volume":"15","author":"Zhu","year":"2024","journal-title":"Cell Death Dis."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"1897","DOI":"10.1039\/d0mt00168f","article-title":"Neuron-Glia: Understanding Cellular Copper Homeostasis, Its Cross-Talk and Their Contribution towards Neurodegenerative Diseases","volume":"12","author":"Bhattacharjee","year":"2020","journal-title":"Metallomics"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"126711","DOI":"10.1016\/j.jtemb.2021.126711","article-title":"Characterizing Effects of Excess Copper Levels in a Human Astrocytic Cell Line with Focus on Oxidative Stress Markers","volume":"65","author":"Witt","year":"2021","journal-title":"J. Trace Elem. Med. Biol."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"115747","DOI":"10.1016\/j.expneurol.2026.115747","article-title":"Nrf2 Modulates the IRF7-SLC31A1 Axis to Suppress Neuronal Cuproptosis after Traumatic Brain Injury","volume":"401","author":"Feng","year":"2026","journal-title":"Exp. Neurol."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"106150","DOI":"10.1016\/j.neuint.2026.106150","article-title":"Copper Depletion Ameliorates Neuronal Damage after Intracerebral Hemorrhage","volume":"196","author":"Zhang","year":"2026","journal-title":"Neurochem. Int."},{"key":"ref_89","doi-asserted-by":"crossref","unstructured":"Zhang, Y., Zhou, Q., Lu, L., Su, Y., Shi, W., Zhang, H., Liu, R., Pu, Y., and Yin, L. (2023). Copper Induces Cognitive Impairment in Mice via Modulation of Cuproptosis and CREB Signaling. Nutrients, 15.","DOI":"10.3390\/nu15040972"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"123809","DOI":"10.1016\/j.biomaterials.2025.123809","article-title":"Targeting Neuronal Cuproptosis and Neuroinflammation with Biomimetic Nanoparticle for the Therapy of Radiotherapy-Induced Brain Injury","volume":"328","author":"Wu","year":"2026","journal-title":"Biomaterials"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1136\/svn-2025-004248","article-title":"Brain-Targeted Extracellular Vesicles for Anti-Cuproptosis Therapy in Subarachnoid Haemorrhage","volume":"11","author":"Xu","year":"2025","journal-title":"Stroke Vasc. Neurol."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"e24237","DOI":"10.1002\/anie.202524237","article-title":"Simultaneous Imaging of Cu+ and Cu2+ in Neural Cells Using DNAzyme Probes Reveals Mechanistic Link Between Copper Redox Imbalance and Amyloid Pathology","volume":"65","author":"Shao","year":"2026","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"111245","DOI":"10.1016\/j.brainresbull.2025.111245","article-title":"Peripheral Mitochondrial Transplantation Alleviates Diabetes-Associated Cognitive Dysfunction by Suppressing Cuproptosis","volume":"222","author":"Hu","year":"2025","journal-title":"Brain Res. Bull."},{"key":"ref_94","doi-asserted-by":"crossref","unstructured":"Squitti, R., Pal, A., Ivanova, I.D., Marianetti, M., and Rongioletti, M. (2025). CLSI Validation of Exchangeable Copper Determination in Serum by ICP-MS: A Focus on Alzheimer\u2019s Disease and Wilson Disease. Biomolecules, 15.","DOI":"10.3390\/biom15060788"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1038\/s41422-022-00653-7","article-title":"Cuproptosis: A Copper-Triggered Modality of Mitochondrial Cell Death","volume":"32","author":"Tang","year":"2022","journal-title":"Cell Res."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"803","DOI":"10.1038\/s41380-021-01361-1","article-title":"Age-Related Immune Alterations and Cerebrovascular Inflammation","volume":"27","author":"Finger","year":"2022","journal-title":"Mol. Psychiatry"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"2835","DOI":"10.7150\/ijbs.84060","article-title":"Ability of Local Clearance of Senescent Cells in Ipsilateral Hemisphere to Mitigate Acute Ischemic Brain Injury in Mice","volume":"19","author":"Lu","year":"2023","journal-title":"Int. J. Biol. Sci."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1021\/acschemneuro.1c00707","article-title":"Semax, a Synthetic Regulatory Peptide, Affects Copper-Induced Abeta Aggregation and Amyloid Formation in Artificial Membrane Models","volume":"13","author":"Sciacca","year":"2022","journal-title":"ACS Chem. Neurosci."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1186\/s12964-023-01267-1","article-title":"Iron and Copper: Critical Executioners of Ferroptosis, Cuproptosis and Other Forms of Cell Death","volume":"21","author":"Li","year":"2023","journal-title":"Cell Commun. Signal"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1186\/s12964-024-01625-7","article-title":"Cuproptosis: Unveiling a New Frontier in Cancer Biology and Therapeutics","volume":"22","author":"Feng","year":"2024","journal-title":"Cell Commun. Signal"},{"key":"ref_101","doi-asserted-by":"crossref","unstructured":"Huang, X. (2023). A Concise Review on Oxidative Stress-Mediated Ferroptosis and Cuproptosis in Alzheimer\u2019s Disease. Cells, 12.","DOI":"10.3390\/cells12101369"},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"14594","DOI":"10.1021\/acs.chemrev.1c00371","article-title":"The Bioinorganic Chemistry of Mammalian Metallothioneins","volume":"121","author":"Maret","year":"2021","journal-title":"Chem. Rev."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"1221","DOI":"10.24976\/Discov.Med.202436185.112","article-title":"Metallothionein III Decreases the Proliferation of Astrocytes and Enhances Pathological Improvements in a Mouse Model of Alzheimer\u2019s Disease","volume":"36","author":"Lv","year":"2024","journal-title":"Discov. Med."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1186\/s40478-024-01760-9","article-title":"Gene-Expression Profiling of Individuals Resilient to Alzheimer\u2019s Disease Reveals Higher Expression of Genes Related to Metallothionein and Mitochondrial Processes and No Changes in the Unfolded Protein Response","volume":"12","author":"Jongejan","year":"2024","journal-title":"Acta Neuropathol. Commun."},{"key":"ref_105","doi-asserted-by":"crossref","unstructured":"Kong, A.H.-Y., Wu, A.J., Ho, O.K.-Y., Leung, M.M.-K., Huang, A.S., Yu, Y., Zhang, G., Lyu, A., Li, M., and Cheung, K.-H. (2023). Exploring the Potential of Aptamers in Targeting Neuroinflammation and Neurodegenerative Disorders: Opportunities and Challenges. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms241411780"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"3497","DOI":"10.1021\/acschemneuro.5c00160","article-title":"Divalent and Trivalent Metallic Ions Differentially Affect Alpha-Synuclein Aggregation","volume":"16","author":"Graves","year":"2025","journal-title":"ACS Chem. Neurosci."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"977","DOI":"10.1042\/EBC20220043","article-title":"Crossroads between Copper Ions and Amyloid Formation in Parkinson\u2019s Disease","volume":"66","year":"2022","journal-title":"Essays Biochem."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"113229","DOI":"10.1016\/j.jinorgbio.2026.113229","article-title":"Impact of N-Terminal Acetylation on Cu(I) Coordination by Alpha Synuclein Protein","volume":"278","author":"Lim","year":"2026","journal-title":"J. Inorg. Biochem."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"112068","DOI":"10.1016\/j.jinorgbio.2022.112068","article-title":"How Cu(II) Binding Affects Structure and Dynamics of \u03b1-Synuclein Revealed by Molecular Dynamics Simulations","volume":"239","author":"Savva","year":"2023","journal-title":"J. Inorg. Biochem."},{"key":"ref_110","doi-asserted-by":"crossref","unstructured":"Blacher, C., Abramov-Harpaz, K., and Miller, Y. (2024). Primary Nucleation of Polymorphic \u03b1-Synuclein Dimers Depends on Copper Concentrations and Definite Copper-Binding Site. Biomolecules, 14.","DOI":"10.3390\/biom14060627"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"111945","DOI":"10.1016\/j.jinorgbio.2022.111945","article-title":"Cu2+ Ions Modulate the Interaction between \u03b1-Synuclein and Lipid Membranes","volume":"236","author":"Wang","year":"2022","journal-title":"J. Inorg. Biochem."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"2380","DOI":"10.1002\/cphc.202100796","article-title":"Acetylation Rather than H50Q Mutation Impacts the Kinetics of Cu(II) Binding to \u03b1-Synuclein","volume":"22","author":"Teng","year":"2021","journal-title":"Chemphyschem"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"16252","DOI":"10.1039\/D0DT01138J","article-title":"X1INH, an Improved next-Generation Affinity-Optimized Hydrazonic Ligand, Attenuates Abnormal Copper(I)\/Copper(II)-\u03b1-Syn Interactions and Affects Protein Aggregation in a Cellular Model of Synucleinopathy","volume":"49","author":"Cukierman","year":"2020","journal-title":"Dalton Trans."},{"key":"ref_114","doi-asserted-by":"crossref","unstructured":"Gonzalez-Alcocer, A., Duarte-Jurado, A.P., Soto-Dominguez, A., Loera-Arias, M.d.J., Villarreal-Silva, E.E., Saucedo-Cardenas, O., de Oca-Luna, R.M., Garcia-Garcia, A., and Rodriguez-Rocha, H. (2023). Unscrambling the Role of Redox-Active Biometals in Dopaminergic Neuronal Death and Promising Metal Chelation-Based Therapy for Parkinson\u2019s Disease. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms24021256"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"738","DOI":"10.1111\/jnc.14019","article-title":"Copper Increases the Ability of 6-Hydroxydopamine to Generate Oxidative Stress and the Ability of Ascorbate and Glutathione to Potentiate This Effect: Potential Implications in Parkinson\u2019s Disease","volume":"141","year":"2017","journal-title":"J. Neurochem."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"5202","DOI":"10.1007\/s12035-024-04609-3","article-title":"Copper Mitigates Atrazine-Induced Neurotoxicity in Parkinson\u2019s Disease Models","volume":"62","author":"Li","year":"2025","journal-title":"Mol. Neurobiol."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/j.neuro.2023.02.002","article-title":"Combined Chronic Copper Exposure and Aging Lead to Neurotoxicity In Vivo","volume":"95","year":"2023","journal-title":"Neurotoxicology"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"254","DOI":"10.1093\/toxsci\/kfae092","article-title":"Copper-Mediated Neurotoxicity and Genetic Vulnerability in the Background of Neurodegenerative Diseases in C. elegans","volume":"201","author":"Weishaupt","year":"2024","journal-title":"Toxicol. Sci."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"103787","DOI":"10.1016\/j.redox.2025.103787","article-title":"Decoding Parkinson\u2019s Disease: The Interplay of Cell Death Pathways, Oxidative Stress, and Therapeutic Innovations","volume":"85","author":"Liu","year":"2025","journal-title":"Redox Biol."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1007\/s11011-025-01574-1","article-title":"Investigating Cuproptosis and Mitochondrial Dysfunction in Brain Cells: Uncovering Novel Mechanisms and Biomarkers for Parkinson\u2019s Disease","volume":"40","author":"Li","year":"2025","journal-title":"Metab. Brain Dis."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"123378","DOI":"10.1016\/j.biomaterials.2025.123378","article-title":"\u03b1-Synuclein Targeted Therapy with Multiple Pathological Improvement for Parkinson\u2019s Disease by Macrocyclic Amphiphile Nanomedicine","volume":"322","author":"Gao","year":"2025","journal-title":"Biomaterials"},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"1025","DOI":"10.1038\/cr.2014.79","article-title":"Phosphorylated Ubiquitin: A New Shade of PINK1 in Parkin Activation","volume":"24","author":"Gehring","year":"2014","journal-title":"Cell Res."},{"key":"ref_123","doi-asserted-by":"crossref","unstructured":"Ruiz-Pozo, V.A., Tamayo-Trujillo, R., Cadena-Ullauri, S., Frias-Toral, E., Guevara-Ram\u00edrez, P., Paz-Cruz, E., Chapela, S., Montalv\u00e1n, M., Morales-L\u00f3pez, T., and Simancas-Racines, D. (2023). The Molecular Mechanisms of the Relationship between Insulin Resistance and Parkinson\u2019s Disease Pathogenesis. Nutrients, 15.","DOI":"10.3390\/nu15163585"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"1351","DOI":"10.1016\/j.cell.2013.11.009","article-title":"Isogenic Human iPSC Parkinson\u2019s Model Shows Nitrosative Stress-Induced Dysfunction in MEF2-PGC1\u03b1 Transcription","volume":"155","author":"Ryan","year":"2013","journal-title":"Cell"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"111207","DOI":"10.1016\/j.mad.2020.111207","article-title":"Mitophagy and DNA Damage Signaling in Human Aging","volume":"186","author":"Babbar","year":"2020","journal-title":"Mech. Ageing Dev."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"859","DOI":"10.1111\/cns.13140","article-title":"Mechanisms and Roles of Mitophagy in Neurodegenerative Diseases","volume":"25","author":"Wang","year":"2019","journal-title":"CNS Neurosci. Ther."},{"key":"ref_127","doi-asserted-by":"crossref","unstructured":"Limanaqi, F., Biagioni, F., Busceti, C.L., Ryskalin, L., Polzella, M., Frati, A., and Fornai, F. (2019). Phytochemicals Bridging Autophagy Induction and Alpha-Synuclein Degradation in Parkinsonism. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20133274"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"1893","DOI":"10.1002\/stem.499","article-title":"Efficient Generation of Functional Dopaminergic Neurons from Human Induced Pluripotent Stem Cells under Defined Conditions","volume":"28","author":"Swistowski","year":"2010","journal-title":"Stem Cells"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1038\/s41531-025-00928-x","article-title":"Linking Parkinson\u2019s Disease and Melanoma: The Impact of Copper-Driven Cuproptosis and Related Mechanisms","volume":"11","author":"Wang","year":"2025","journal-title":"npj Park. Dis."},{"key":"ref_130","doi-asserted-by":"crossref","unstructured":"Fan, H., Wang, K., Zhao, X., Song, B., Yao, T., Liu, T., Gao, G., Lu, W., and Liu, C. (2024). Emerging Insights into Cuproptosis and Copper Metabolism: Implications for Age-Related Diseases and Potential Therapeutic Strategies. Front. Aging Neurosci., 16.","DOI":"10.3389\/fnagi.2024.1335122"},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"2808","DOI":"10.1093\/hmg\/ddad102","article-title":"Mitochondrial Dysfunction and Mitophagy Defects in LRRK2-R1441C Parkinson\u2019s Disease Models","volume":"32","author":"Williamson","year":"2023","journal-title":"Hum. Mol. Genet."},{"key":"ref_132","doi-asserted-by":"crossref","unstructured":"Curtis, W.M., Seeds, W.A., Mattson, M.P., and Bradshaw, P.C. (2022). NADPH and Mitochondrial Quality Control as Targets for a Circadian-Based Fasting and Exercise Therapy for the Treatment of Parkinson\u2019s Disease. Cells, 11.","DOI":"10.3390\/cells11152416"},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"592","DOI":"10.5483\/BMBRep.2021.54.12.107","article-title":"Precise Control of Mitophagy through Ubiquitin Proteasome System and Deubiquitin Proteases and Their Dysfunction in Parkinson\u2019s Disease","volume":"54","author":"Park","year":"2021","journal-title":"BMB Rep."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"686","DOI":"10.1016\/j.devcel.2014.04.033","article-title":"Wilson Disease Protein ATP7B Utilizes Lysosomal Exocytosis to Maintain Copper Homeostasis","volume":"29","author":"Polishchuk","year":"2014","journal-title":"Dev. Cell"},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"eabl5508","DOI":"10.1126\/sciadv.abl5508","article-title":"Structure of the Wilson Disease Copper Transporter ATP7B","volume":"8","author":"Bitter","year":"2022","journal-title":"Sci. Adv."},{"key":"ref_136","doi-asserted-by":"crossref","unstructured":"Springer, C., Humayun, D., and Skouta, R. (2024). Cuproptosis: Unraveling the Mechanisms of Copper-Induced Cell Death and Its Implication in Cancer Therapy. Cancers, 16.","DOI":"10.3390\/cancers16030647"},{"key":"ref_137","doi-asserted-by":"crossref","unstructured":"Jiang, A., Handley, R.R., Lehnert, K., and Snell, R.G. (2023). From Pathogenesis to Therapeutics: A Review of 150 Years of Huntington\u2019s Disease Research. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms241613021"},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"dmm049492","DOI":"10.1242\/dmm.049492","article-title":"Integrated Multi-Omics Analysis of Huntington Disease Identifies Pathways That Modulate Protein Aggregation","volume":"15","author":"Pradhan","year":"2022","journal-title":"Dis. Model. Mech."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/j.freeradbiomed.2020.11.031","article-title":"Mitochondrial SIRT3 Confers Neuroprotection in Huntington\u2019s Disease by Regulation of Oxidative Challenges and Mitochondrial Dynamics","volume":"163","author":"Naia","year":"2021","journal-title":"Free Radic. Biol. Med."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"e15851","DOI":"10.15252\/emmm.202215851","article-title":"Mitochondrial HSF1 Triggers Mitochondrial Dysfunction and Neurodegeneration in Huntington\u2019s Disease","volume":"14","author":"Liu","year":"2022","journal-title":"EMBO Mol. Med."},{"key":"ref_141","doi-asserted-by":"crossref","unstructured":"Li, L., Lv, L., Wang, Z., Liu, X., Wang, Q., Zhu, H., Jiang, B., Han, Y., Pan, X., and Zhou, X. (2025). From Copper Homeostasis to Cuproptosis: A New Perspective on CNS Immune Regulation and Neurodegenerative Diseases. Front. Neurol., 16, Correction in Front. Neurol. 2025, 16, 1664184. https:\/\/doi.org\/ 10.3389\/fneur.2025.1664184.","DOI":"10.3389\/fneur.2025.1664184"},{"key":"ref_142","doi-asserted-by":"crossref","unstructured":"Tao, F., Lin, M., Meng, X., Huang, L., Zhuo, B., Jiang, S., Deng, S., Meng, Z., and Shi, J. (2025). Copper Homeostasis and Cuproptosis: Implications for Neurodegenerative Diseases. Front. Aging Neurosci., 17.","DOI":"10.3389\/fnagi.2025.1688554"},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"e2014610118","DOI":"10.1073\/pnas.2014610118","article-title":"Accelerated Expansion of Pathogenic Mitochondrial DNA Heteroplasmies in Huntington\u2019s Disease","volume":"118","author":"Wang","year":"2021","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"103930","DOI":"10.1016\/j.redox.2025.103930","article-title":"Ferredoxins: Master Regulators in Mitochondrial Redox Homeostasis and Programmed Cell Death","volume":"88","author":"Lu","year":"2025","journal-title":"Redox Biol."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"183663","DOI":"10.1016\/j.bbamem.2021.183663","article-title":"Mitochondrial Membranes Modify Mutant Huntingtin Aggregation","volume":"1863","author":"Adegbuyiro","year":"2021","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"ref_146","doi-asserted-by":"crossref","unstructured":"van den Bos, M.A.J., Geevasinga, N., Higashihara, M., Menon, P., and Vucic, S. (2019). Pathophysiology and Diagnosis of ALS: Insights from Advances in Neurophysiological Techniques. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20112818"},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"428","DOI":"10.1038\/s41598-019-57366-y","article-title":"High Neutrophil-to-Lymphocyte Ratio Predicts Short Survival Duration in Amyotrophic Lateral Sclerosis","volume":"10","author":"Choi","year":"2020","journal-title":"Sci. Rep."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"750","DOI":"10.1590\/S0004-282X2009000400040","article-title":"Amyotrophic Lateral Sclerosis (ALS): Three Letters That Change the People\u2019s Life. For ever","volume":"67","author":"Oliveira","year":"2009","journal-title":"Arq. Neuropsiquiatr."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"831","DOI":"10.1016\/j.nbd.2011.08.031","article-title":"Mutant SOD1 Forms Ion Channel: Implications for ALS Pathophysiology","volume":"45","author":"Allen","year":"2012","journal-title":"Neurobiol. Dis."},{"key":"ref_150","doi-asserted-by":"crossref","unstructured":"Tokuda, E., and Furukawa, Y. (2016). Copper Homeostasis as a Therapeutic Target in Amyotrophic Lateral Sclerosis with SOD1 Mutations. Int. J. Mol. Sci., 17.","DOI":"10.3390\/ijms17050636"},{"key":"ref_151","doi-asserted-by":"crossref","unstructured":"Xing, L., Wang, Z., Hao, Z., Pan, P., Yang, A., and Wang, J. (2024). Cuproptosis in Stroke: Focusing on Pathogenesis and Treatment. Front. Mol. Neurosci., 17.","DOI":"10.3389\/fnmol.2024.1349123"},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"358","DOI":"10.1038\/s41392-025-02439-w","article-title":"Navigating the Landscape of Protein Folding and Proteostasis: From Molecular Chaperones to Therapeutic Innovations","volume":"10","author":"Kuzu","year":"2025","journal-title":"Signal Transduct. Target. Ther."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"105228","DOI":"10.1016\/j.nbd.2020.105228","article-title":"The M1311V Variant of ATP7A Is Associated with Impaired Trafficking and Copper Homeostasis in Models of Motor Neuron Disease","volume":"149","author":"Bakkar","year":"2021","journal-title":"Neurobiol. Dis."},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1007\/s11596-024-2832-z","article-title":"Copper Metabolism and Cuproptosis: Molecular Mechanisms and Therapeutic Perspectives in Neurodegenerative Diseases","volume":"44","author":"Ban","year":"2024","journal-title":"Curr. Med. Sci."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"101262","DOI":"10.1016\/j.redox.2019.101262","article-title":"Copper Ion\/H2O2 Oxidation of Cu\/Zn-Superoxide Dismutase: Implications for Enzymatic Activity and Antioxidant Action","volume":"26","author":"Tiwari","year":"2019","journal-title":"Redox Biol."},{"key":"ref_156","doi-asserted-by":"crossref","unstructured":"Malik, L., and Hedrich, S. (2021). Ferric Iron Reduction in Extreme Acidophiles. Front. Microbiol., 12.","DOI":"10.3389\/fmicb.2021.818414"},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"15521","DOI":"10.1523\/JNEUROSCI.0755-12.2012","article-title":"Neuroprotective Effects of Reactive Oxygen Species Mediated by BDNF-Independent Activation of TrkB","volume":"32","author":"Huang","year":"2012","journal-title":"J. Neurosci."},{"key":"ref_158","doi-asserted-by":"crossref","unstructured":"Lovejoy, D.B., and Guillemin, G.J. (2014). The Potential for Transition Metal-Mediated Neurodegeneration in Amyotrophic Lateral Sclerosis. Front. Aging Neurosci., 6.","DOI":"10.3389\/fnagi.2014.00173"},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1186\/s41747-021-00221-5","article-title":"Studying Alzheimer Disease, Parkinson Disease, and Amyotrophic Lateral Sclerosis with 7-T Magnetic Resonance","volume":"5","author":"Costagli","year":"2021","journal-title":"Eur. Radiol. Exp."},{"key":"ref_160","doi-asserted-by":"crossref","unstructured":"Kon\u00ed\u010dkov\u00e1, D., Men\u0161\u00edkov\u00e1, K., Tu\u010dkov\u00e1, L., H\u00e9nykov\u00e1, E., Strnad, M., Friedeck\u00fd, D., Stejskal, D., Mat\u011bj, R., and Ka\u0148ovsk\u00fd, P. (2022). Biomarkers of Neurodegenerative Diseases: Biology, Taxonomy, Clinical Relevance, and Current Research Status. Biomedicines, 10.","DOI":"10.3390\/biomedicines10071760"},{"key":"ref_161","doi-asserted-by":"crossref","unstructured":"Zhang, L., Deng, R., Liu, L., Du, H., and Tang, D. (2024). Novel Insights into Cuproptosis Inducers and Inhibitors. Front. Mol. Biosci., 11.","DOI":"10.3389\/fmolb.2024.1477971"},{"key":"ref_162","doi-asserted-by":"crossref","unstructured":"Jia, F., Han, W., Gao, S., Huang, J., Zhao, W., Lu, Z., Zhao, W., Li, Z., Wang, Z., and Guo, Y. (2024). Novel Cuproptosis Metabolism-Related Molecular Clusters and Diagnostic Signature for Alzheimer\u2019s Disease. Front. Mol. Biosci., 11.","DOI":"10.3389\/fmolb.2024.1478611"},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1186\/s40001-024-02093-y","article-title":"Identification of Cuproptosis-Related Genes in Alzheimer\u2019s Disease Based on Bioinformatic Analysis","volume":"29","author":"Ma","year":"2024","journal-title":"Eur. J. Med. Res."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"3496","DOI":"10.4103\/NRR.NRR-D-25-00813","article-title":"N6-Methyladenosine Modification Regulates Cell Death in Cognitive Impairment","volume":"21","author":"Li","year":"2025","journal-title":"Neural Regen. Res."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"30928","DOI":"10.1073\/pnas.2014058117","article-title":"Design of a Multivalent Bifunctional Chelator for Diagnostic 64Cu PET Imaging in Alzheimer\u2019s Disease","volume":"117","author":"Cho","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1186\/s40001-025-02818-7","article-title":"Identifying the Important Involvement of Cuproptosis in the Pathophysiology of Age-Related Macular Degeneration","volume":"30","author":"Lei","year":"2025","journal-title":"Eur. J. Med. Res."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"e202300078","DOI":"10.1002\/open.202300078","article-title":"Current and Future of \u201cTurn-On\u201d Based Small-Molecule Copper Probes for Cuproptosis","volume":"12","author":"Peng","year":"2023","journal-title":"ChemistryOpen"},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"1853","DOI":"10.1152\/jn.00370.2025","article-title":"Cuproptosis: Mechanisms and Links with Alzheimer\u2019s Disease","volume":"134","author":"Zheng","year":"2025","journal-title":"J. Neurophysiol."},{"key":"ref_169","doi-asserted-by":"crossref","unstructured":"El-Nablaway, M., Sonpol, H.M.A., Elewa, Y.H.A., Ali, M.A.M., Adel, M., Zayed, E.S., Alhelf, M., Didamoony, M.A., Dawood, A.F., and Embaby, E.M. (2025). Copper Chelation by Penicillamine Protects Against Doxorubicin-Induced Cardiomyopathy by Suppressing FDX1-Mediated Cuproptosis. Biomolecules, 15.","DOI":"10.3390\/biom15091320"},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"101903","DOI":"10.1016\/j.mito.2024.101903","article-title":"Chelating Mitochondrial Iron and Copper: Recipes, Pitfalls and Promise","volume":"78","author":"Trnka","year":"2024","journal-title":"Mitochondrion"},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"3291","DOI":"10.2147\/IJN.S241157","article-title":"Copper Oxide Nanoparticles Induce Oxidative DNA Damage and Cell Death via Copper Ion-Mediated P38 MAPK Activation in Vascular Endothelial Cells","volume":"15","author":"He","year":"2020","journal-title":"Int. J. Nanomed."},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"103331","DOI":"10.1016\/j.redox.2024.103331","article-title":"A New Paradigm in Intracellular Immunology: Mitochondria Emerging as Leading Immune Organelles","volume":"76","author":"Xu","year":"2024","journal-title":"Redox Biol."},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"e24150","DOI":"10.1002\/advs.202524150","article-title":"Copper Depletion Nanoparticles Potentiate Cancer Immunotherapy by Avoiding Innate and Adaptive Immune Resistance","volume":"13","author":"Zhou","year":"2026","journal-title":"Adv. Sci."},{"key":"ref_174","doi-asserted-by":"crossref","unstructured":"Min, J.-H., Sarlus, H., and Harris, R.A. (2024). Copper Toxicity and Deficiency: The Vicious Cycle at the Core of Protein Aggregation in ALS. Front. Mol. Neurosci., 17.","DOI":"10.3389\/fnmol.2024.1408159"},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"1058","DOI":"10.4103\/NRR.NRR-D-24-00110","article-title":"Role of Copper in Central Nervous System Physiology and Pathology","volume":"20","author":"Locatelli","year":"2025","journal-title":"Neural Regen. Res."},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"e12919","DOI":"10.1111\/nan.12919","article-title":"Treatment with the Copper Compound CuATSM Has No Significant Effect on Motor Neuronal Pathology in Patients with ALS","volume":"49","author":"Yang","year":"2023","journal-title":"Neuropathol. Appl. Neurobiol."},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"e12938","DOI":"10.1111\/nan.12938","article-title":"CuII(Atsm) Significantly Decreases Microglial Reactivity in Patients with Sporadic Amyotrophic Lateral Sclerosis","volume":"49","author":"Liddell","year":"2023","journal-title":"Neuropathol. Appl. Neurobiol."},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1016\/j.freeradbiomed.2025.09.044","article-title":"Targeting FDX1 with Icaritin Attenuates Neuronal Cuproptosis by Reconciling Mitochondrial Fission-Fusion Dynamics and Bioenergetic Homeostasis","volume":"241","author":"He","year":"2025","journal-title":"Free Radic. Biol. Med."},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"542","DOI":"10.1016\/j.freeradbiomed.2025.06.017","article-title":"Phillygenin Ameliorates Myocardial Ischemia-Reperfusion Injury by Inhibiting Cuproptosis via the Autophagy-Lysosome Degradation of CTR1","volume":"237","author":"Chen","year":"2025","journal-title":"Free Radic. Biol. Med."},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"114262","DOI":"10.1016\/j.jconrel.2025.114262","article-title":"Copper Ionophore-Autophagy Interference Nanoregulators for Tumor Self-Defense Reprograming to Amplify Cuproptotic Stress and Antitumor Immunity","volume":"388","author":"Li","year":"2025","journal-title":"J. Control. Release"},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1016\/j.actbio.2025.06.018","article-title":"Janus Hydrogels Delivering Low-Density Lipoprotein Receptor-Related Protein 6 Inhibitor Enhance Myocardial Repair via m6A-Dependent Cuproptosis in Bama Pigs","volume":"201","author":"Liu","year":"2025","journal-title":"Acta Biomater."},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"1281","DOI":"10.7150\/thno.120455","article-title":"Precision Targeting of FDX1-Mediated Cuproptosis by a ROS-Responsive Hydrogel for Myocardial Ischemia-Reperfusion Injury Treatment","volume":"16","author":"Hu","year":"2026","journal-title":"Theranostics"},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"284","DOI":"10.1016\/j.freeradbiomed.2025.12.019","article-title":"Mitochondrial Uncoupling Sensitizes Gastric Cancer Cells to Elesclomol-Induced Cuproptosis via FDX1\/DLAT Upregulation","volume":"244","author":"Lu","year":"2026","journal-title":"Free Radic. Biol. Med."},{"key":"ref_184","doi-asserted-by":"crossref","unstructured":"Gromadzka, G., Tarnacka, B., Flaga, A., and Adamczyk, A. (2020). Copper Dyshomeostasis in Neurodegenerative Diseases-Therapeutic Implications. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21239259"},{"key":"ref_185","first-page":"CD005380","article-title":"Metal Protein Attenuating Compounds for the Treatment of Alzheimer\u2019s Dementia","volume":"2014","author":"Sampson","year":"2014","journal-title":"Cochrane Database Syst. Rev."},{"key":"ref_186","doi-asserted-by":"crossref","unstructured":"Squitti, R., Pal, A., Picozza, M., Avan, A., Ventriglia, M., Rongioletti, M.C., and Hoogenraad, T. (2020). Zinc Therapy in Early Alzheimer\u2019s Disease: Safety and Potential Therapeutic Efficacy. Biomolecules, 10.","DOI":"10.3390\/biom10081164"},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1021\/acschemneuro.0c00621","article-title":"TDMQ20, a Specific Copper Chelator, Reduces Memory Impairments in Alzheimer\u2019s Disease Mouse Models","volume":"12","author":"Zhao","year":"2021","journal-title":"ACS Chem. Neurosci."},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1038\/s41420-023-01796-1","article-title":"Copper Homeostasis and Cuproptosis in Atherosclerosis: Metabolism, Mechanisms and Potential Therapeutic Strategies","volume":"10","author":"Yang","year":"2024","journal-title":"Cell Death Discov."},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1186\/s12964-024-01726-3","article-title":"The Crosstalk between Copper-Induced Oxidative Stress and Cuproptosis: A Novel Potential Anticancer Paradigm","volume":"22","author":"Vo","year":"2024","journal-title":"Cell Commun. Signal"},{"key":"ref_190","doi-asserted-by":"crossref","unstructured":"Wang, J., Li, J., Liu, J., Chan, K.-Y., Lee, H.-S., Lin, K.N., Wang, C.-C., and Lau, T.-S. (2024). Interplay of Ferroptosis and Cuproptosis in Cancer: Dissecting Metal-Driven Mechanisms for Therapeutic Potentials. Cancers, 16.","DOI":"10.3390\/cancers16030512"},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"386","DOI":"10.1016\/j.tips.2026.02.004","article-title":"Cuproptosis in Cancer: Emerging Mechanism and Therapeutic Opportunities","volume":"47","author":"Qin","year":"2026","journal-title":"Trends Pharmacol. Sci."},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"e1800311","DOI":"10.1002\/pmic.201800311","article-title":"GPX4 at the Crossroads of Lipid Homeostasis and Ferroptosis","volume":"19","author":"Forcina","year":"2019","journal-title":"Proteomics"},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"2665","DOI":"10.1111\/cas.14496","article-title":"Ferroptosis at the Crossroads of Infection, Aging and Cancer","volume":"111","author":"Toyokuni","year":"2020","journal-title":"Cancer Sci."},{"key":"ref_194","doi-asserted-by":"crossref","unstructured":"Xu, D., Hu, L., Zhou, J., Deng, X., Zhu, Y., and Liu, C. (2025). The Emerging Role of Cuproptosis in Spinal Cord Injury. Front. Immunol., 16.","DOI":"10.3389\/fimmu.2025.1595852"},{"key":"ref_195","doi-asserted-by":"crossref","unstructured":"Zhang, M., Meng, W., Liu, C., Wang, H., Li, R., Wang, Q., Gao, Y., Zhou, S., Du, T., and Yuan, T. (2023). Identification of Cuproptosis Clusters and Integrative Analyses in Parkinson\u2019s Disease. Brain Sci., 13.","DOI":"10.3390\/brainsci13071015"},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1111\/jnc.15961","article-title":"Copper Induces Neuron-Sparing, Ferredoxin 1-Independent Astrocyte Toxicity Mediated by Oxidative Stress","volume":"167","author":"Gale","year":"2023","journal-title":"J. Neurochem."},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"5938","DOI":"10.1021\/ja100714p","article-title":"Development of Highly Sensitive Fluorescent Probes for Detection of Intracellular Copper(I) in Living Systems","volume":"132","author":"Taki","year":"2010","journal-title":"J. Am. Chem. Soc."},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"11179","DOI":"10.1073\/pnas.0406547102","article-title":"Imaging of the Intracellular Topography of Copper with a Fluorescent Sensor and by Synchrotron X-Ray Fluorescence Microscopy","volume":"102","author":"Yang","year":"2005","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"eaau6977","DOI":"10.1126\/science.aau6977","article-title":"The Biology, Function, and Biomedical Applications of Exosomes","volume":"367","author":"Kalluri","year":"2020","journal-title":"Science"},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1038\/nbt.1807","article-title":"Delivery of siRNA to the Mouse Brain by Systemic Injection of Targeted Exosomes","volume":"29","author":"Seow","year":"2011","journal-title":"Nat. Biotechnol."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/27\/19\/8765\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T13:03:35Z","timestamp":1790773415000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/27\/19\/8765"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9,30]]},"references-count":200,"journal-issue":{"issue":"19","published-online":{"date-parts":[[2026,10]]}},"alternative-id":["ijms27198765"],"URL":"https:\/\/doi.org\/10.3390\/ijms27198765","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,9,30]]}}}