{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T20:58:39Z","timestamp":1792789119138,"version":"4.5.0"},"reference-count":284,"publisher":"MDPI AG","issue":"9","license":[{"start":{"date-parts":[[2026,9,21]],"date-time":"2026-09-21T00:00:00Z","timestamp":1789948800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100015550","name":"Ministry of Health","doi-asserted-by":"publisher","award":["MH CZ-DRO-VFN64165"],"award-info":[{"award-number":["MH CZ-DRO-VFN64165"]}],"id":[{"id":"10.13039\/501100015550","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Czech Ministry of Education","award":["LUAUS26259"],"award-info":[{"award-number":["LUAUS26259"]}]},{"award":["LUAUS26259"],"award-info":[{"award-number":["LUAUS26259"]}],"id":[{"id":"https:\/\/ror.org\/00y6khe77","id-type":"ROR","asserted-by":"publisher"}]},{"name":"Italian Liver Foundation","id":[{"id":"https:\/\/ror.org\/00zpwa373","id-type":"ROR","asserted-by":"crossref"}]},{"id":[{"id":"https:\/\/ror.org\/00zpwa373","id-type":"ROR","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biomolecules"],"abstract":"<jats:p>Ferroptosis is a unique form of regulated lytic cell death driven by intracellular iron overload, excessive production of reactive oxygen species, failure of antioxidant defense systems, lipid peroxidation, and subsequent plasma membrane damage. Its initiation and progression involve complex signaling and regulatory networks. Although iron is a defining feature of ferroptosis, it also plays a central role in the heme oxygenase (HO)\u2013biliverdin reductase (BVR) system, a cellular machinery associated with a lower prevalence of chronic diseases and reduced all-cause mortality. The HO\u2013BVR cycle and its products biliverdin and bilirubin (together the yellow players: YPs) act as hormones and transcription factors on multiple signaling pathways, with powerful antioxidant, anti-inflammatory, and many more properties. The convergence between the two systems is suggestive of the existence of a finely tuned balance between the beneficial vs. exacerbating damage effects. Exploration of this equilibrium has just started. This review summarizes the current evidence on the interplay between ferroptosis and the HO\u2013BVR system, in the context of liver, cardiovascular and brain diseases. We also review the therapeutic strategies aimed at modulating these pathways, considering both their potential benefits and their possible adverse consequences within the context of these integrated cellular defense and injury mechanisms.<\/jats:p>","DOI":"10.3390\/biom16091371","type":"journal-article","created":{"date-parts":[[2026,9,21]],"date-time":"2026-09-21T09:01:38Z","timestamp":1789981298000},"page":"1371","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Bilirubin and the Yellow Players in Ferroptosis: A Delicate Balance in Human Health and Disease, with a Focus on the Liver, Cardiovascular System, and Brain"],"prefix":"10.3390","volume":"16","author":[{"ORCID":"https:\/\/orcid.org\/0009-0009-3678-8331","authenticated-orcid":false,"given":"Camilla","family":"Dalla Verde","sequence":"first","affiliation":[{"name":"Liver Brain Unit \u201cRita Moretti\u201d, Fondazione Italiana Fegato-Onlus, Bldg. Q, AREA Science Park, ss14, Km163.5, Basovizza, 34149 Trieste, Italy"},{"name":"Department of Life Sciences, University of Trieste, 34139 Trieste, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5318-0151","authenticated-orcid":false,"given":"Libor","family":"Vitek","sequence":"additional","affiliation":[{"name":"4th Department of Internal Medicine, Laboratory Diagnostic, Institute of Medical Biochemistry, 1st Faculty of Medicine, General University Hospital, Charles University, 12000 Prague, Czech Republic"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6596-7595","authenticated-orcid":false,"given":"Claudio","family":"Tiribelli","sequence":"additional","affiliation":[{"name":"Liver Brain Unit \u201cRita Moretti\u201d, Fondazione Italiana Fegato-Onlus, Bldg. Q, AREA Science Park, ss14, Km163.5, Basovizza, 34149 Trieste, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9403-3564","authenticated-orcid":false,"given":"Silvia","family":"Gazzin","sequence":"additional","affiliation":[{"name":"Liver Brain Unit \u201cRita Moretti\u201d, Fondazione Italiana Fegato-Onlus, Bldg. Q, AREA Science Park, ss14, Km163.5, Basovizza, 34149 Trieste, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,9,21]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1043","DOI":"10.1126\/science.3029864","article-title":"Bilirubin Is an Antioxidant of Possible Physiological Importance","volume":"235","author":"Stocker","year":"1987","journal-title":"Science"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"5171","DOI":"10.1073\/pnas.0813132106","article-title":"Bilirubin and Glutathione Have Complementary Antioxidant and Cytoprotective Roles","volume":"106","author":"Sedlak","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"16093","DOI":"10.1073\/pnas.252626999","article-title":"Biliverdin Reductase: A Major Physiologic Cytoprotectant","volume":"99","author":"Baranano","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"3221","DOI":"10.1007\/s00018-016-2223-0","article-title":"Role of Nrf2\/HO\u22121 System in Development, Oxidative Stress Response and Diseases: An Evolutionarily Conserved Mechanism","volume":"73","author":"Loboda","year":"2016","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"758","DOI":"10.1016\/j.molmed.2016.07.004","article-title":"A Novel Perspective on the Biology of Bilirubin in Health and Disease","volume":"22","author":"Gazzin","year":"2016","journal-title":"Trends Mol. Med."},{"key":"ref_6","doi-asserted-by":"crossref","unstructured":"Llido, J.P., Jayanti, S., Tiribelli, C., and Gazzin, S. (2023). Bilirubin and Redox Stress in Age-Related Brain Diseases. Antioxidants, 12.","DOI":"10.3390\/antiox12081525"},{"key":"ref_7","first-page":"92","article-title":"Bilirubin and Inflammation in Neurodegenerative and Other Neurological Diseases","volume":"7","author":"Jayanti","year":"2020","journal-title":"Neuroimmunol. Neuroinflamm."},{"key":"ref_8","doi-asserted-by":"crossref","unstructured":"Jayanti, S., V\u00edtek, L., Tiribelli, C., and Gazzin, S. (2020). The Role of Bilirubin and the Other \u201cYellow Players\u201d in Neurodegenerative Diseases. Antioxidants, 9.","DOI":"10.20517\/2347-8659.2019.14"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1152\/physrev.00011.2005","article-title":"Heme Oxygenase-1\/Carbon Monoxide: From Basic Science to Therapeutic Applications","volume":"86","author":"Ryter","year":"2006","journal-title":"Physiol. Rev."},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Ryter, S.W. (2021). Heme Oxgenase-1, a Cardinal Modulator of Regulated Cell Death and Inflammation. Cells, 10.","DOI":"10.3390\/cells10030515"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/CS20140566","article-title":"Looking to the Horizon: The Role of Bilirubin in the Development and Prevention of Age-Related Chronic Diseases","volume":"129","author":"Wagner","year":"2015","journal-title":"Clin. Sci."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"1060","DOI":"10.1016\/j.cell.2012.03.042","article-title":"Ferroptosis: An Iron-Dependent Form of Nonapoptotic Cell Death","volume":"149","author":"Dixon","year":"2012","journal-title":"Cell"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1083\/jcb.201605110","article-title":"Heat Stress Induces Ferroptosis-Like Cell Death in Plants","volume":"216","author":"Martin","year":"2017","journal-title":"J. Cell Biol."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"1831","DOI":"10.1111\/nph.16636","article-title":"Ferroptosis Contributes to Developmental Cell Death in Rice Blast","volume":"227","author":"Shen","year":"2020","journal-title":"New Phytol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"e56580","DOI":"10.7554\/eLife.56580","article-title":"Changes in Ferrous Iron and Glutathione Promote Ferroptosis and Frailty in Aging Caenorhabditis Elegans","volume":"9","author":"Jenkins","year":"2020","journal-title":"eLife"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"266","DOI":"10.1038\/s41580-020-00324-8","article-title":"Ferroptosis: Mechanisms, Biology and Role in Disease","volume":"22","author":"Jiang","year":"2021","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"6388","DOI":"10.1016\/S0021-9258(18)63477-5","article-title":"Microsomal Heme Oxygenase: Characterization of the Enzyme","volume":"244","author":"Tenhunen","year":"1969","journal-title":"J. Biol. Chem."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1021\/bi00804a016","article-title":"Reduced Nicotinamide Adenine Dinucleotide Phosphate Dependent Biliverdin Reductase. Partial Purification and Characterization","volume":"9","author":"Tenhunen","year":"1970","journal-title":"Biochemistry"},{"key":"ref_19","doi-asserted-by":"crossref","unstructured":"Ostrow, J.D. (1986). Bile Pigments and Jaundice: Molecular, Metabolic, and Medical Aspects, Dekker.","DOI":"10.1097\/00005176-198709000-00038"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1016\/j.taap.2012.03.010","article-title":"Metabolism of Bilirubin by Human Cytochrome P450 2A6","volume":"261","author":"Arthur","year":"2012","journal-title":"Toxicol. Appl. Pharmacol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1124\/pr.107.07104","article-title":"Pharmacological and Clinical Aspects of Heme Oxygenase","volume":"60","author":"Abraham","year":"2008","journal-title":"Pharmacol. Rev."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"174","DOI":"10.2174\/1567205012666150921103304","article-title":"The Pathophysiology of Heme in the Brain","volume":"13","author":"Gozzelino","year":"2016","journal-title":"Curr. Alzheimer Res."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1146\/annurev.pharmtox.37.1.517","article-title":"The Heme Oxygenase System: A Regulator of Second Messenger Gases","volume":"37","author":"Maines","year":"1997","journal-title":"Annu. Rev. Pharmacol. Toxicol."},{"key":"ref_24","doi-asserted-by":"crossref","unstructured":"Nitti, M., Piras, S., Brondolo, L., Marinari, U.M., Pronzato, M.A., and Furfaro, A.L. (2018). Heme Oxygenase 1 in the Nervous System: Does It Favor Neuronal Cell Survival or Induce Neurodegeneration?. Int. J. Mol. Sci., 19.","DOI":"10.3390\/ijms19082260"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1016\/j.pneurobio.2018.06.008","article-title":"The Sinister Face of Heme Oxygenase-1 in Brain Aging and Disease","volume":"172","author":"Schipper","year":"2019","journal-title":"Prog. Neurobiol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"E191","DOI":"10.1152\/ajpendo.00405.2020","article-title":"Bilirubin as a Metabolic Hormone: The Physiological Relevance of Low Levels","volume":"320","author":"Creeden","year":"2020","journal-title":"Am. J. Physiol.-Endocrinol. Metab."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"1485","DOI":"10.1016\/j.jhep.2021.06.010","article-title":"Bilirubin: The Yellow Hormone?","volume":"75","author":"Tiribelli","year":"2021","journal-title":"J. Hepatol."},{"key":"ref_28","doi-asserted-by":"crossref","unstructured":"Kong, E., Wang, H., Wang, X., Zhang, Y., Zhang, J., Yu, W., Feng, X., Sun, Y., and Wu, F. (2021). Bilirubin Induces Pain Desensitization in Cholestasis by Activating 5-Hydroxytryptamine 3A Receptor in Spinal Cord. Front. Cell Dev. Biol., 9.","DOI":"10.3389\/fcell.2021.605855"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1016\/S0014-5793(03)00420-4","article-title":"Interaction of Bilirubin and Biliverdin with Reactive Nitrogen Species","volume":"543","author":"Kaur","year":"2003","journal-title":"FEBS Lett."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/j.neulet.2012.04.062","article-title":"Inhibition of Lipid Peroxidation and Protein Oxidation by Endogenous and Exogenous Antioxidants in Rat Brain Microsomes in Vitro","volume":"518","author":"Mancuso","year":"2012","journal-title":"Neurosci. Lett."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"636","DOI":"10.1161\/HYPERTENSIONAHA.107.092296","article-title":"Induction of Heme Oxygenase-1 In Vivo Suppresses NADPH Oxidase\u2013Derived Oxidative Stress","volume":"50","author":"Datla","year":"2007","journal-title":"Hypertension"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"512","DOI":"10.1016\/j.cellsig.2013.11.029","article-title":"Bilirubin Mediated Oxidative Stress Involves Antioxidant Response Activation via Nrf2 Pathway","volume":"26","author":"Qaisiya","year":"2014","journal-title":"Cell. Signal."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"804","DOI":"10.1016\/j.neuint.2011.03.006","article-title":"Uptake, Metabolism and Toxicity of Hemin in Cultured Neurons","volume":"58","author":"Dang","year":"2011","journal-title":"Neurochem. Int."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1146\/annurev.pharmtox.010909.105600","article-title":"Mechanisms of Cell Protection by Heme Oxygenase-1","volume":"50","author":"Gozzelino","year":"2010","journal-title":"Annu. Rev. Pharmacol. Toxicol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"382","DOI":"10.1152\/physiol.00029.2005","article-title":"New Insights into Biliverdin Reductase Functions: Linking Heme Metabolism to Cell Signaling","volume":"20","author":"Maines","year":"2005","journal-title":"Physiology"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/j.tips.2008.12.003","article-title":"Pleiotropic Functions of Biliverdin Reductase: Cellular Signaling and Generation of Cytoprotective and Cytotoxic Bilirubin","volume":"30","author":"Kapitulnik","year":"2009","journal-title":"Trends Pharmacol. Sci."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"7109","DOI":"10.1073\/pnas.0502173102","article-title":"Human Biliverdin Reductase: A Member of the Insulin Receptor Substrate Family with Serine\/Threonine\/Tyrosine Kinase Activity","volume":"102","author":"Shen","year":"2005","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_38","doi-asserted-by":"crossref","unstructured":"Luu Hoang, K.N., Anstee, J.E., and Arnold, J.N. (2021). The Diverse Roles of Heme Oxygenase-1 in Tumor Progression. Front. Immunol., 12.","DOI":"10.3389\/fimmu.2021.658315"},{"key":"ref_39","doi-asserted-by":"crossref","unstructured":"Wang, H., Cheng, Q., Bao, L., Li, M., Chang, K., and Yi, X. (2023). Cytoprotective Role of Heme Oxygenase-1 in Cancer Chemoresistance: Focus on Antioxidant, Antiapoptotic, and Pro-Autophagy Properties. Antioxidants, 12.","DOI":"10.3390\/antiox12061217"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1165\/ajrcmb.27.1.4862","article-title":"Heme Oxygenase-1","volume":"27","author":"Morse","year":"2002","journal-title":"Am. J. Respir. Cell Mol. Biol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1089\/152308602760598891","article-title":"Heme Oxygenase-1: Redox Regulation and Role in the Hepatic Response to Oxidative Stress","volume":"4","author":"Bauer","year":"2002","journal-title":"Antioxid. Redox Signal."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1089\/ars.2005.7.80","article-title":"Heme Oxygenase-1: Redox Regulation of a Stress Protein in Lung and Cell Culture Models","volume":"7","author":"Ryter","year":"2005","journal-title":"Antioxid. Redox Signal."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"28","DOI":"10.3164\/jcbn.08-210-HO","article-title":"Heme Oxygenase-1 Is an Essential Cytoprotective Component in Oxidative Tissue Injury Induced by Hemorrhagic Shock","volume":"44","author":"Takahashi","year":"2009","journal-title":"J. Clin. Biochem. Nutr."},{"key":"ref_44","doi-asserted-by":"crossref","unstructured":"Jayanti, S., Vitek, L., Verde, C.D., Llido, J.P., Sukowati, C., Tiribelli, C., and Gazzin, S. (2024). Role of Natural Compounds Modulating Heme Catabolic Pathway in Gut, Liver, Cardiovascular, and Brain Diseases. Biomolecules, 14.","DOI":"10.3390\/biom14010063"},{"key":"ref_45","doi-asserted-by":"crossref","unstructured":"Choi, Y.K., and Kim, Y.-M. (2022). Beneficial and Detrimental Roles of Heme Oxygenase-1 in the Neurovascular System. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23137041"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1042\/BJ20080018","article-title":"Biliverdin Reductase Is a Transporter of Haem into the Nucleus and Is Essential for Regulation of HO-1 Gene Expression by Haematin","volume":"413","author":"Tudor","year":"2008","journal-title":"Biochem. J."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"26882","DOI":"10.1074\/jbc.M114.567685","article-title":"Nuclear Heme Oxygenase-1 (HO-1) Modulates Subcellular Distribution and Activation of Nrf2, Impacting Metabolic and Anti-Oxidant Defenses","volume":"289","author":"Biswas","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"1612","DOI":"10.2353\/ajpath.2006.060555","article-title":"Heme Oxygenase-2 Is a Critical Determinant for Execution of an Acute Inflammatory and Reparative Response","volume":"169","author":"Seta","year":"2006","journal-title":"Am. J. Pathol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1042\/bj1940273","article-title":"Reduction of Biliverdin and Placental Transfer of Bilirubin and Biliverdin in the Pregnant Guinea Pig","volume":"194","author":"McDonagh","year":"1981","journal-title":"Biochem. J."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1258\/0004563011900821","article-title":"Relationships between Serum (ZZ)-Bilirubin, Its Subfractions and Biliverdin Concentrations in Infants at 1-Month Check-Ups","volume":"38","author":"Itoh","year":"2001","journal-title":"Ann. Clin. Biochem."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"18849","DOI":"10.1073\/pnas.1108571108","article-title":"Biliverdin Inhibits Toll-like Receptor-4 (TLR4) Expression through Nitric Oxide-Dependent Nuclear Translocation of Biliverdin Reductase","volume":"108","author":"Wegiel","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"19916","DOI":"10.1074\/jbc.M314251200","article-title":"Biliverdin Reductase, a Novel Regulator for Induction of Activating Transcription Factor-2 and Heme Oxygenase-1","volume":"279","author":"Kravets","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"24698","DOI":"10.1074\/jbc.M111.326504","article-title":"The Human Biliverdin Reductase-Based Peptide Fragments and Biliverdin Regulate Protein Kinase C\u03b4 Activity: The Peptides are Inhibitors or Substrate for the Protein Kinase C","volume":"287","author":"Miralem","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"21369","DOI":"10.1074\/jbc.M109.027433","article-title":"Cell Surface Biliverdin Reductase Mediates Biliverdin-Induced Anti-Inflammatory Effects via Phosphatidylinositol 3-Kinase and Akt","volume":"284","author":"Wegiel","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1016\/j.nbd.2013.09.018","article-title":"The Janus Face of the Heme Oxygenase\/Biliverdin Reductase System in Alzheimer Disease: It\u2019s Time for Reconciliation","volume":"62","author":"Barone","year":"2014","journal-title":"Neurobiol. Dis."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/bj2190001","article-title":"Oxygen Toxicity, Oxygen Radicals, Transition Metals and Disease","volume":"219","author":"Halliwell","year":"1984","journal-title":"Biochem. J."},{"key":"ref_57","doi-asserted-by":"crossref","unstructured":"Zhong, M., Wang, Y., Min, J., and Wang, F. (2025). Iron Metabolism and Ferroptosis in Human Health and Disease. BMC Biol., 23.","DOI":"10.1186\/s12915-025-02378-6"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"14678","DOI":"10.1016\/S0021-9258(18)82386-9","article-title":"Oxidative Stress Resulting from Ultraviolet A Irradiation of Human Skin Fibroblasts Leads to a Heme Oxygenase-Dependent Increase in Ferritin","volume":"268","author":"Vile","year":"1993","journal-title":"J. Biol. Chem."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"2607","DOI":"10.1073\/pnas.91.7.2607","article-title":"Heme Oxygenase 1 Mediates an Adaptive Response to Oxidative Stress in Human Skin Fibroblasts","volume":"91","author":"Vile","year":"1994","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"C1105","DOI":"10.1152\/ajpcell.00023.2013","article-title":"CORM-A1 Prevents Blood-Brain Barrier Dysfunction Caused by Ionotropic Glutamate Receptor-Mediated Endothelial Oxidative Stress and Apoptosis","volume":"304","author":"Basuroy","year":"2013","journal-title":"Am. J. Physiol.-Cell Physiol."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"728","DOI":"10.1038\/nrd3228","article-title":"The Therapeutic Potential of Carbon Monoxide","volume":"9","author":"Motterlini","year":"2010","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1186\/s12974-018-1226-1","article-title":"Carbon Monoxide-Releasing Molecule-3 Protects against Ischemic Stroke by Suppressing Neuroinflammation and Alleviating Blood-Brain Barrier Disruption","volume":"15","author":"Wang","year":"2018","journal-title":"J. Neuroinflamm."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"2605","DOI":"10.1161\/STROKEAHA.110.607101","article-title":"Carbon Monoxide-Activated Nrf2 Pathway Leads to Protection against Permanent Focal Cerebral Ischemia","volume":"42","author":"Wang","year":"2011","journal-title":"Stroke"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"338","DOI":"10.1016\/j.bbrc.2009.06.029","article-title":"Bilirubin Inhibits the TNF\u03b1-Related Induction of Three Endothelial Adhesion Molecules","volume":"386","author":"Mazzone","year":"2009","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"15418","DOI":"10.1074\/jbc.M111.266510","article-title":"Essential Roles of Raf\/Extracellular Signal-Regulated Kinase\/Mitogen-Activated Protein Kinase Pathway, YY1, and Ca2+ Influx in Growth Arrest of Human Vascular Smooth Muscle Cells by Bilirubin","volume":"287","author":"Stoeckius","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"3078","DOI":"10.4161\/cc.6.24.5022","article-title":"Bilirubin Inhibits Tumor Cell Growth via Activation of ERK","volume":"6","author":"Ollinger","year":"2007","journal-title":"Cell Cycle"},{"key":"ref_67","first-page":"1890","article-title":"Bilirubin Decreases Nos2 Expression via Inhibition of NAD(P)H Oxidase: Implications for Protection against Endotoxic Shock in Rats","volume":"19","author":"Lanone","year":"2005","journal-title":"FASEB J. Off. Publ. Fed. Am. Soc. Exp. Biol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"1549","DOI":"10.1002\/ijc.27412","article-title":"Association of Serum Bilirubin and Promoter Variations in HMOX1 and UGT1A1 Genes with Sporadic Colorectal Cancer","volume":"131","author":"Pardini","year":"2012","journal-title":"Int. J. Cancer"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"1319","DOI":"10.1093\/carcin\/bgq028","article-title":"The Aryl Hydrocarbon Receptor (AhR) in the Regulation of Cell\u2013Cell Contact and Tumor Growth","volume":"31","author":"Dietrich","year":"2010","journal-title":"Carcinogenesis"},{"key":"ref_70","unstructured":"(2005). The Role of Ah Receptor in Induction of Human UDP-Glucuronosyltransferase 1A1. Methods in Enzymology, Academic Press."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1093\/toxsci\/kfp115","article-title":"Introducing the \u201cTCDD-Inducible AhR-Nrf2 Gene Battery\u201d","volume":"111","author":"Yeager","year":"2009","journal-title":"Toxicol. Sci."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"7188","DOI":"10.1128\/MCB.00915-07","article-title":"NRF2 Modulates Aryl Hydrocarbon Receptor Signaling: Influence on Adipogenesis","volume":"27","author":"Shin","year":"2007","journal-title":"Mol. Cell. Biol."},{"key":"ref_73","doi-asserted-by":"crossref","unstructured":"Stec, D.E., John, K., Trabbic, C.J., Luniwal, A., Hankins, M.W., Baum, J., and Hinds, T.D. (2016). Bilirubin Binding to PPAR\u03b1 Inhibits Lipid Accumulation. PLoS ONE, 11.","DOI":"10.1371\/journal.pone.0153427"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"7038","DOI":"10.1111\/febs.16059","article-title":"Signaling Pathways and Defense Mechanisms of Ferroptosis","volume":"289","author":"Liu","year":"2022","journal-title":"FEBS J."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"1398","DOI":"10.1016\/j.bbagen.2019.06.010","article-title":"Iron Homeostasis and Iron-Regulated ROS in Cell Death, Senescence and Human Diseases","volume":"1863","author":"Nakamura","year":"2019","journal-title":"Biochim. Biophys. Acta BBA-Gen. Subj."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"109888","DOI":"10.1016\/j.jnutbio.2025.109888","article-title":"Iron Metabolism and Ferroptosis in Health and Diseases: The Crucial Role of Mitochondria in Metabolically Active Tissues","volume":"140","author":"Catapano","year":"2025","journal-title":"J. Nutr. Biochem."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"316","DOI":"10.7762\/cnr.2022.11.4.316","article-title":"Iron Homeostasis and Energy Metabolism in Obesity","volume":"11","author":"Kim","year":"2022","journal-title":"Clin. Nutr. Res."},{"key":"ref_78","doi-asserted-by":"crossref","unstructured":"Radlowski, E.C., and Johnson, R.W. (2013). Perinatal Iron Deficiency and Neurocognitive Development. Front. Hum. Neurosci., 7.","DOI":"10.3389\/fnhum.2013.00585"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1002\/glia.20784","article-title":"Oligodendrocytes and Myelination: The Role of Iron","volume":"57","author":"Todorich","year":"2009","journal-title":"Glia"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1016\/j.spen.2006.08.004","article-title":"Iron Deficiency and Brain Development","volume":"13","author":"Lozoff","year":"2006","journal-title":"Semin. Pediatr. Neurol."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1016\/j.molcel.2015.06.011","article-title":"Glutaminolysis and Transferrin Regulate Ferroptosis","volume":"59","author":"Gao","year":"2015","journal-title":"Mol. Cell"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/S0300-483X(00)00231-6","article-title":"The Haber\u2013Weiss Reaction and Mechanisms of Toxicity","volume":"149","author":"Kehrer","year":"2000","journal-title":"Toxicology"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1038\/s41420-021-00579-w","article-title":"Ferroptosis: A Cell Death Connecting Oxidative Stress, Inflammation and Cardiovascular Diseases","volume":"7","author":"Yu","year":"2021","journal-title":"Cell Death Discov."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1021\/tx00031a001","article-title":"Mechanisms and Biological Relevance of Lipid Peroxidation Initiation","volume":"6","author":"Dix","year":"1993","journal-title":"Chem. Res. Toxicol."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1038\/nchembio.2239","article-title":"ACSL4 Dictates Ferroptosis Sensitivity by Shaping Cellular Lipid Composition","volume":"13","author":"Doll","year":"2017","journal-title":"Nat. Chem. Biol."},{"key":"ref_86","doi-asserted-by":"crossref","unstructured":"Feng, X., Zhang, W., Liu, X., Wang, Q., Dang, X., Han, J., and Zhang, X. (2025). Ferroptosis-Associated Signaling Pathways and Therapeutic Approaches in Depression. Front. Neurosci., 19.","DOI":"10.3389\/fnins.2025.1559597"},{"key":"ref_87","first-page":"880","article-title":"The Role of Redox-Active Iron, Copper, Manganese, and Redox-Inactive Zinc in Toxicity, Oxidative Stress, and Human Diseases","volume":"24","author":"Jomova","year":"2025","journal-title":"EXCLI J."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1124\/pr.57.4.2","article-title":"The Evolution of Iron Chelators for the Treatment of Iron Overload Disease and Cancer","volume":"57","author":"Kalinowski","year":"2005","journal-title":"Pharmacol. Rev."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"102650","DOI":"10.1016\/j.redox.2023.102650","article-title":"Redox Phospholipidomics Discovers Pro-Ferroptotic Death Signals in A375 Melanoma Cells in Vitro and in Vivo","volume":"61","author":"Tyurina","year":"2023","journal-title":"Redox Biol."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1038\/nchembio.2238","article-title":"Oxidized Arachidonic and Adrenic PEs Navigate Cells to Ferroptosis","volume":"13","author":"Kagan","year":"2017","journal-title":"Nat. Chem. Biol."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"1282","DOI":"10.1016\/j.cub.2023.02.060","article-title":"Lipid Peroxidation Increases Membrane Tension, Piezo1 Gating, and Cation Permeability to Execute Ferroptosis","volume":"33","author":"Hirata","year":"2023","journal-title":"Curr. Biol."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1021\/acscentsci.9b01063","article-title":"GTP Cyclohydrolase 1\/Tetrahydrobiopterin Counteract Ferroptosis through Lipid Remodeling","volume":"6","author":"Kraft","year":"2020","journal-title":"ACS Cent. Sci."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"278","DOI":"10.1016\/j.bbrc.2019.01.090","article-title":"The Release and Activity of HMGB1 in Ferroptosis","volume":"510","author":"Wen","year":"2019","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"1464","DOI":"10.1016\/j.bbrc.2020.10.035","article-title":"Cathepsin B Is a Mediator of Organelle-Specific Initiation of Ferroptosis","volume":"533","author":"Kuang","year":"2020","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/0076-6879(95)51106-7","article-title":"Glutathione Metabolism","volume":"Volume 251","author":"Meister","year":"1995","journal-title":"Methods in Enzymology"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"11455","DOI":"10.1074\/jbc.274.17.11455","article-title":"Cloning and Expression of a Plasma Membrane Cystine\/Glutamate Exchange Transporter Composed of Two Distinct Proteins","volume":"274","author":"Sato","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1080\/09168451.2015.1065172","article-title":"Biosynthesis of Coenzyme Q in Eukaryotes","volume":"80","author":"Kawamukai","year":"2016","journal-title":"Biosci. Biotechnol. Biochem."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"S62","DOI":"10.1016\/j.mito.2007.03.007","article-title":"Endogenous Synthesis of Coenzyme Q in Eukaryotes","volume":"7","author":"Tran","year":"2007","journal-title":"Mitochondrion"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1021\/acs.biochem.0c00030","article-title":"Ferroptosis Suppressor Protein 1 (FSP1) and Coenzyme Q10 Cooperatively Suppress Ferroptosis","volume":"59","author":"Hadian","year":"2020","journal-title":"Biochemistry"},{"key":"ref_100","doi-asserted-by":"crossref","unstructured":"Gon\u00e7alves, D.A., Jasiulionis, M.G., and Melo, F.H.M.d. (2021). The Role of the BH4 Cofactor in Nitric Oxide Synthase Activity and Cancer Progression: Two Sides of the Same Coin. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22179546"},{"key":"ref_101","doi-asserted-by":"crossref","unstructured":"Olmos, Y. (2022). The ESCRT Machinery: Remodeling, Repairing, and Sealing Membranes. Membranes, 12.","DOI":"10.3390\/membranes12060633"},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1016\/j.bbrc.2019.11.110","article-title":"ESCRT-III-Dependent Membrane Repair Blocks Ferroptosis","volume":"522","author":"Dai","year":"2020","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"1644","DOI":"10.1038\/s41418-020-00691-x","article-title":"Ferroptotic Pores Induce Ca2+ Fluxes and ESCRT-III Activation to Modulate Cell Death Kinetics","volume":"28","author":"Pedrera","year":"2021","journal-title":"Cell Death Differ."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41417-020-0200-0","article-title":"ESCRT-III-Mediated Membrane Repair in Cell Death and Tumor Resistance","volume":"28","author":"Liu","year":"2021","journal-title":"Cancer Gene Ther."},{"key":"ref_105","doi-asserted-by":"crossref","unstructured":"Yang, Y., Wang, M., Zhang, Y.-Y., Zhao, S.-Z., and Gu, S. (2022). The Endosomal Sorting Complex Required for Transport Repairs the Membrane to Delay Cell Death. Front. Oncol., 12.","DOI":"10.3389\/fonc.2022.1007446"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"R1292","DOI":"10.1016\/j.cub.2020.09.068","article-title":"Ferroptosis","volume":"30","author":"Tang","year":"2020","journal-title":"Curr. Biol."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1038\/s41422-020-00441-1","article-title":"Ferroptosis: Molecular Mechanisms and Health Implications","volume":"31","author":"Tang","year":"2021","journal-title":"Cell Res."},{"key":"ref_108","doi-asserted-by":"crossref","unstructured":"Zhang, D.-L., Ghosh, M.C., and Rouault, T.A. (2014). The Physiological Functions of Iron Regulatory Proteins in Iron Homeostasis\u2014An Update. Front. Pharmacol., 5.","DOI":"10.3389\/fphar.2014.00124"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1146\/annurev.physiol.69.031905.164337","article-title":"Iron Homeostasis","volume":"69","author":"Andrews","year":"2007","journal-title":"Annu. Rev. Physiol."},{"key":"ref_110","doi-asserted-by":"crossref","unstructured":"Shivangi, S., SharathBabu, B.N., and Mugesh, G. (2026). From Fenton Reaction to Ferroptosis: Chemistry of Metal Complexes in Regulated Cell Death by Lipid Peroxidation. Chem. Soc. Rev.","DOI":"10.1039\/D6CS00041J"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"354","DOI":"10.1016\/j.molcel.2018.10.042","article-title":"Role of Mitochondria in Ferroptosis","volume":"73","author":"Gao","year":"2019","journal-title":"Mol. Cell"},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"714","DOI":"10.14336\/AD.2023.0717","article-title":"Mitochondria-Mediated Ferroptosis in Diseases Therapy: From Molecular Mechanisms to Implications","volume":"15","author":"Feng","year":"2024","journal-title":"Aging Dis."},{"key":"ref_113","doi-asserted-by":"crossref","unstructured":"Liu, Y., Zhou, L., Xu, Y., Li, K., Zhao, Y., Qiao, H., Xu, Q., and Zhao, J. (2022). Heat Shock Proteins and Ferroptosis. Front. Cell Dev. Biol., 10.","DOI":"10.3389\/fcell.2022.864635"},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1016\/S0022-3476(66)80147-6","article-title":"The Distribution of Bilirubin between Albumin and Mitochondria","volume":"68","author":"Odell","year":"1966","journal-title":"J. Pediatr."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"948","DOI":"10.1080\/15548627.2020.1739447","article-title":"Mitochondrial DNA Stress Triggers Autophagy-Dependent Ferroptotic Death","volume":"17","author":"Li","year":"2021","journal-title":"Autophagy"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1038\/s41556-020-0461-8","article-title":"Energy-Stress-Mediated AMPK Activation Inhibits Ferroptosis","volume":"22","author":"Lee","year":"2020","journal-title":"Nat. Cell Biol."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"108767","DOI":"10.1016\/j.celrep.2021.108767","article-title":"PDK4 Dictates Metabolic Resistance to Ferroptosis by Suppressing Pyruvate Oxidation and Fatty Acid Synthesis","volume":"34","author":"Song","year":"2021","journal-title":"Cell Rep."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"151058","DOI":"10.1016\/j.ejcb.2019.151058","article-title":"Mitochondria Regulation in Ferroptosis","volume":"99","author":"Wang","year":"2020","journal-title":"Eur. J. Cell Biol."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"436","DOI":"10.1016\/j.chembiol.2020.03.011","article-title":"Breakdown of an Ironclad Defense System: The Critical Role of NRF2 in Mediating Ferroptosis","volume":"27","author":"Anandhan","year":"2020","journal-title":"Cell Chem. Biol."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1038\/cdd.2015.93","article-title":"Loss of Cysteinyl-tRNA Synthetase (CARS) Induces the Transsulfuration Pathway and Inhibits Ferroptosis Induced by Cystine Deprivation","volume":"23","author":"Hayano","year":"2016","journal-title":"Cell Death Differ."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1016\/j.cell.2017.09.021","article-title":"Ferroptosis: A Regulated Cell Death Nexus Linking Metabolism, Redox Biology, and Disease","volume":"171","author":"Stockwell","year":"2017","journal-title":"Cell"},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"104919","DOI":"10.1016\/j.phrs.2020.104919","article-title":"The Application of Ferroptosis in Diseases","volume":"159","author":"Qiu","year":"2020","journal-title":"Pharmacol. Res."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1097\/FBP.0000000000000143","article-title":"Antidepressant-like and Anxiolytic-like Effects of Hydrogen Sulfide in Streptozotocin-Induced Diabetic Rats through Inhibition of Hippocampal Oxidative Stress","volume":"26","author":"Tang","year":"2015","journal-title":"Behav. Pharmacol."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"117226","DOI":"10.1016\/j.jep.2023.117226","article-title":"Di-Huang-Yin-Zi Regulates P53\/SLC7A11 Signaling Pathway to Improve the Mechanism of Post-Stroke Depression","volume":"319","author":"Yang","year":"2024","journal-title":"J. Ethnopharmacol."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"530","DOI":"10.1038\/s41419-022-04971-x","article-title":"STAT6 Inhibits Ferroptosis and Alleviates Acute Lung Injury via Regulating P53\/SLC7A11 Pathway","volume":"13","author":"Yang","year":"2022","journal-title":"Cell Death Dis."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"1425","DOI":"10.1080\/15548627.2016.1187366","article-title":"Autophagy Promotes Ferroptosis by Degradation of Ferritin","volume":"12","author":"Hou","year":"2016","journal-title":"Autophagy"},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"1021","DOI":"10.1038\/cr.2016.95","article-title":"Ferroptosis Is an Autophagic Cell Death Process","volume":"26","author":"Gao","year":"2016","journal-title":"Cell Res."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1007\/s12026-025-09720-8","article-title":"BECN1 Activator Peptide Tat-Beclin 1 Promotes Ferroptosis via the BECN1-SLC7A11 Axis to Inhibit NSCLC Progression","volume":"73","author":"Gou","year":"2025","journal-title":"Immunol. Res."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"2173","DOI":"10.1080\/15548627.2018.1513758","article-title":"BECN1 Is a New Driver of Ferroptosis","volume":"14","author":"Kang","year":"2018","journal-title":"Autophagy"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1016\/j.freeradbiomed.2018.05.074","article-title":"The Tumor Suppressor Protein P53 and the Ferroptosis Network","volume":"133","author":"Kang","year":"2019","journal-title":"Free Radic. Biol. Med."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"6339","DOI":"10.1038\/s41467-020-20154-8","article-title":"Ferroptotic Damage Promotes Pancreatic Tumorigenesis through a TMEM173\/STING-Dependent DNA Sensor Pathway","volume":"11","author":"Dai","year":"2020","journal-title":"Nat. Commun."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"3084","DOI":"10.1016\/j.ymthe.2023.07.026","article-title":"STING\/ACSL4 Axis-Dependent Ferroptosis and Inflammation Promote Hypertension-Associated Chronic Kidney Disease","volume":"31","author":"Gao","year":"2023","journal-title":"Mol. Ther. J. Am. Soc. Gene Ther."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1186\/s13046-025-03520-6","article-title":"Targeting the Interplay of cGAS-STING and Ferroptosis by Nanomedicine in the Treatment of Cancer","volume":"44","author":"Li","year":"2025","journal-title":"J. Exp. Clin. Cancer Res."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"1692","DOI":"10.1016\/j.celrep.2017.07.055","article-title":"The Tumor Suppressor P53 Limits Ferroptosis by Blocking DPP4 Activity","volume":"20","author":"Xie","year":"2017","journal-title":"Cell Rep."},{"key":"ref_135","doi-asserted-by":"crossref","unstructured":"Taylor-Fishwick, D.A. (2013). NOX, NOX Who Is There? The Contribution of NADPH Oxidase One to Beta Cell Dysfunction. Front. Endocrinol., 4.","DOI":"10.3389\/fendo.2013.00040"},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1152\/physrev.00044.2005","article-title":"The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology","volume":"87","author":"Bedard","year":"2007","journal-title":"Physiol. Rev."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"1338","DOI":"10.1016\/j.bbrc.2016.08.124","article-title":"Identification of ACSL4 as a Biomarker and Contributor of Ferroptosis","volume":"478","author":"Yuan","year":"2016","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"2284","DOI":"10.1038\/s41418-019-0299-4","article-title":"Ischemia-Induced ACSL4 Activation Contributes to Ferroptosis-Mediated Tissue Injury in Intestinal Ischemia\/Reperfusion","volume":"26","author":"Li","year":"2019","journal-title":"Cell Death Differ."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1038\/s41422-019-0263-3","article-title":"The Role of Ferroptosis in Ionizing Radiation-Induced Cell Death and Tumor Suppression","volume":"30","author":"Lei","year":"2020","journal-title":"Cell Res."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"5355","DOI":"10.1158\/0008-5472.CAN-19-0369","article-title":"Stearoyl-CoA Desaturase 1 Protects Ovarian Cancer Cells from Ferroptotic Cell Death","volume":"79","author":"Tesfay","year":"2019","journal-title":"Cancer Res."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"420","DOI":"10.1016\/j.chembiol.2018.11.016","article-title":"Exogenous Monounsaturated Fatty Acids Promote a Ferroptosis-Resistant Cell State","volume":"26","author":"Magtanong","year":"2019","journal-title":"Cell Chem. Biol."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"11252","DOI":"10.1038\/s41467-025-66113-z","article-title":"AMP-Activated Protein Kinase-Driven Lipid Droplet Dynamics Govern Melanoma Sensitivity to Polyunsaturated Fatty Acid and Iron-Induced Ferroptosis","volume":"16","author":"Motamedi","year":"2025","journal-title":"Nat. Commun."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1186\/s12964-023-01170-9","article-title":"The Emerging Roles of MAPK-AMPK in Ferroptosis Regulatory Network","volume":"21","author":"Wang","year":"2023","journal-title":"Cell Commun. Signal."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"1617","DOI":"10.1038\/s41467-019-09277-9","article-title":"A GPX4-Dependent Cancer Cell State Underlies the Clear-Cell Morphology and Confers Sensitivity to Ferroptosis","volume":"10","author":"Zou","year":"2019","journal-title":"Nat. Commun."},{"key":"ref_145","doi-asserted-by":"crossref","unstructured":"K\u00fck\u00fcrt, A., Gelen, V., Ba\u015fer, \u00d6.F., Deveci, H.A., and Karapehlivan, M. (2021). Thiols: Role in Oxidative Stress-Related Disorders. Accenting Lipid Peroxidation, IntechOpen.","DOI":"10.5772\/intechopen.96682"},{"key":"ref_146","first-page":"270","article-title":"Dynamic Thiol\/Disulfide Homeostasis and Myeloperoxidase Levels in Gilbert\u2019s Syndrome with Mild Hyperbilirubinemia: Oxidant Status in Gilbert\u2019s Syndrome","volume":"17","author":"Demir","year":"2024","journal-title":"Gastroenterol. Hepatol. Bed Bench"},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"2120","DOI":"10.1016\/j.freeradbiomed.2012.03.002","article-title":"Reduced Circulating Oxidized LDL Is Associated with Hypocholesterolemia and Enhanced Thiol Status in Gilbert Syndrome","volume":"52","author":"Boon","year":"2012","journal-title":"Free Radic. Biol. Med."},{"key":"ref_148","doi-asserted-by":"crossref","unstructured":"Uzelac, T., Smiljani\u0107, K., Taki\u0107, M., \u0160arac, I., Oggiano, G., Nikoli\u0107, M., and Jovanovi\u0107, V. (2024). The Thiol Group Reactivity and the Antioxidant Property of Human Serum Albumin Are Controlled by the Joint Action of Fatty Acids and Glucose Binding. Int. J. Mol. Sci., 25.","DOI":"10.3390\/ijms25042335"},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"16712","DOI":"10.1016\/S0021-9258(19)89449-8","article-title":"Free and Albumin-Bound Bilirubin Are Efficient Co-Antioxidants for Alpha-Tocopherol, Inhibiting Plasma and Low Density Lipoprotein Lipid Peroxidation","volume":"269","author":"Neuzil","year":"1994","journal-title":"J. Biol. Chem."},{"key":"ref_150","doi-asserted-by":"crossref","unstructured":"Kajarabille, N., and Latunde-Dada, G.O. (2019). Programmed Cell-Death by Ferroptosis: Antioxidants as Mitigators. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20194968"},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"678","DOI":"10.1172\/JCI105383","article-title":"Experimental Bilirubin Encephalopathy. The Mode of Entry of Bilirubin-14C into the Central Nervous System","volume":"45","author":"Diamond","year":"1966","journal-title":"J. Clin. Investig."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"1094","DOI":"10.1111\/liv.13351","article-title":"The Molecular Basis of Jaundice: An Old Symptom Revisited","volume":"37","author":"Gazzin","year":"2016","journal-title":"Liver Int."},{"key":"ref_153","doi-asserted-by":"crossref","unstructured":"Tian, Y., Li, Z., Tian, T., Zhu, H., Zhou, M., Long, X., and Wang, S. (2026). Ferroptosis Suppressor Protein 1-Mediated Ferroptosis Suppression in Sepsis: Non-Canonical Antioxidant Pathways, Inflammatory Regulation, and Therapeutic Perspectives. Front. Immunol., 17.","DOI":"10.3389\/fimmu.2026.1892904"},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"1338","DOI":"10.1016\/j.jhep.2025.06.034","article-title":"Mevalonate Pathway Promotes Liver Cancer by Suppressing Ferroptosis through CoQ10 Production and Selenocysteine-tRNA Modification","volume":"83","author":"Chen","year":"2025","journal-title":"J. Hepatol."},{"key":"ref_155","doi-asserted-by":"crossref","unstructured":"Pic\u00f3n, D.F., and Skouta, R. (2023). Unveiling the Therapeutic Potential of Squalene Synthase: Deciphering Its Biochemical Mechanism, Disease Implications, and Intriguing Ties to Ferroptosis. Cancers, 15.","DOI":"10.3390\/cancers15143731"},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"688","DOI":"10.1038\/s41586-019-1705-2","article-title":"The CoQ Oxidoreductase FSP1 Acts Parallel to GPX4 to Inhibit Ferroptosis","volume":"575","author":"Bersuker","year":"2019","journal-title":"Nature"},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1038\/s41586-019-1707-0","article-title":"FSP1 Is a Glutathione-Independent Ferroptosis Suppressor","volume":"575","author":"Doll","year":"2019","journal-title":"Nature"},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"2206","DOI":"10.1038\/s41467-022-29905-1","article-title":"A Targetable CoQ-FSP1 Axis Drives Ferroptosis- and Radiation-Resistance in KEAP1 Inactive Lung Cancers","volume":"13","author":"Koppula","year":"2022","journal-title":"Nat. Commun."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"1136","DOI":"10.18632\/oncotarget.28301","article-title":"FSP1, a Novel KEAP1\/NRF2 Target Gene Regulating Ferroptosis and Radioresistance in Lung Cancers","volume":"13","author":"Emmanuel","year":"2022","journal-title":"Oncotarget"},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1007\/s00018-026-06082-8","article-title":"PPARa-FSP1 Axis Modulates Lipid Peroxidation-Induced Neuronal Ferroptosis to Promote Functional Recovery in Mouse Model of Traumatic Spinal Cord Injury","volume":"83","author":"Song","year":"2026","journal-title":"Cell. Mol. Life Sci. CMLS"},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"2501","DOI":"10.1016\/j.celrep.2019.07.107","article-title":"The Hippo Pathway Effector TAZ Regulates Ferroptosis in Renal Cell Carcinoma","volume":"28","author":"Yang","year":"2019","journal-title":"Cell Rep."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"729","DOI":"10.1016\/j.tcb.2022.05.005","article-title":"Roles of YAP\/TAZ in Ferroptosis","volume":"32","author":"Magesh","year":"2022","journal-title":"Trends Cell Biol."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"4124","DOI":"10.1038\/s44319-025-00515-4","article-title":"Hippo Pathway Controls Biopterin Metabolism to Shield Adjacent Cells from Ferroptosis in Lung Cancer","volume":"26","author":"Li","year":"2025","journal-title":"EMBO Rep."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"107583","DOI":"10.1016\/j.jbc.2024.107583","article-title":"Ferroptosis Regulation by Cap\u2019n\u2019collar Family Transcription Factors","volume":"300","author":"Murray","year":"2024","journal-title":"J. Biol. Chem."},{"key":"ref_165","doi-asserted-by":"crossref","unstructured":"Telorack, M., Meyer, M., Ingold, I., Conrad, M., Bloch, W., and Werner, S. (2016). A Glutathione-Nrf2-Thioredoxin Cross-Talk Ensures Keratinocyte Survival and Efficient Wound Repair. PLoS Genet., 12.","DOI":"10.1371\/journal.pgen.1005800"},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"24393","DOI":"10.18632\/oncotarget.5162","article-title":"Heme Oxygenase-1 Accelerates Erastin-Induced Ferroptotic Cell Death","volume":"6","author":"Kwon","year":"2015","journal-title":"Oncotarget"},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"F702","DOI":"10.1152\/ajprenal.00044.2017","article-title":"Heme Oxygenase-1 Mitigates Ferroptosis in Renal Proximal Tubule Cells","volume":"314","author":"Adedoyin","year":"2018","journal-title":"Am. J. Physiol. Ren. Physiol."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"9091879","DOI":"10.1155\/2017\/9091879","article-title":"Expression of the NRF2 Target Gene NQO1 Is Enhanced in Mononuclear Cells in Human Chronic Kidney Disease","volume":"2017","author":"Shen","year":"2017","journal-title":"Oxid. Med. Cell. Longev."},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1038\/s41514-020-00051-6","article-title":"NQO1 Protects Obese Mice through Improvements in Glucose and Lipid Metabolism","volume":"6","author":"Choi","year":"2020","journal-title":"npj Aging Mech. Dis."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"101160","DOI":"10.1016\/j.drup.2024.101160","article-title":"Targeting NQO1 Induces Ferroptosis and Triggers Anti-Tumor Immunity in Immunotherapy-Resistant KEAP1-Deficient Cancers","volume":"77","author":"Yuan","year":"2024","journal-title":"Drug Resist. Updat."},{"key":"ref_171","doi-asserted-by":"crossref","unstructured":"Song, X., and Long, D. (2020). Nrf2 and Ferroptosis: A New Research Direction for Neurodegenerative Diseases. Front. Neurosci., 14.","DOI":"10.3389\/fnins.2020.00267"},{"key":"ref_172","doi-asserted-by":"crossref","unstructured":"Yan, R., Lin, B., Jin, W., Tang, L., Hu, S., and Cai, R. (2023). NRF2, a Superstar of Ferroptosis. Antioxidants, 12.","DOI":"10.20944\/preprints202308.1554.v1"},{"key":"ref_173","first-page":"5405","article-title":"Metabolic Networks in Ferroptosis","volume":"15","author":"Hao","year":"2018","journal-title":"Oncol. Lett."},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1016\/j.canlet.2017.12.025","article-title":"Heme Oxygenase-1 Mediates BAY 11\u20137085 Induced Ferroptosis","volume":"416","author":"Chang","year":"2018","journal-title":"Cancer Lett."},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"1299","DOI":"10.1007\/s00109-025-02599-w","article-title":"Involvement of Ferroptosis in Metabolic Dysfunction-Associated Steatohepatitis-Related Liver Diseases","volume":"103","author":"Liu","year":"2025","journal-title":"J. Mol. Med."},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"105088","DOI":"10.1016\/j.ebiom.2024.105088","article-title":"Emerging Role of Ferroptosis in Metabolic Dysfunction-Associated Steatotic Liver Disease: Revisiting Hepatic Lipid Peroxidation","volume":"102","author":"Peleman","year":"2024","journal-title":"eBioMedicine"},{"key":"ref_177","doi-asserted-by":"crossref","unstructured":"Vairetti, M., Di Pasqua, L.G., Cagna, M., Richelmi, P., Ferrigno, A., and Berardo, C. (2021). Changes in Glutathione Content in Liver Diseases: An Update. Antioxidants, 10.","DOI":"10.3390\/antiox10030364"},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1038\/s41418-022-00941-0","article-title":"The Multifaceted Role of Ferroptosis in Liver Disease","volume":"29","author":"Chen","year":"2022","journal-title":"Cell Death Differ."},{"key":"ref_179","doi-asserted-by":"crossref","unstructured":"Kuang, F., Liu, J., Tang, D., and Kang, R. (2020). Oxidative Damage and Antioxidant Defense in Ferroptosis. Front. Cell Dev. Biol., 8.","DOI":"10.3389\/fcell.2020.586578"},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1080\/20014091084227","article-title":"Gamma Glutamyl Transferase","volume":"38","author":"Whitfield","year":"2001","journal-title":"Crit. Rev. Clin. Lab. Sci."},{"key":"ref_181","doi-asserted-by":"crossref","unstructured":"Minetti, E.T., Hamburg, N.M., and Matsui, R. (2024). Drivers of Cardiovascular Disease in Metabolic Dysfunction-Associated Steatotic Liver Disease: The Threats of Oxidative Stress. Front. Cardiovasc. Med., 11.","DOI":"10.3389\/fcvm.2024.1469492"},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"588","DOI":"10.1007\/BF02365440","article-title":"Dynamic Aspects of Glutathione Metabolism in Obstructive Jaundice","volume":"29","author":"Hirota","year":"1994","journal-title":"J. Gastroenterol."},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"608","DOI":"10.1172\/JCI113639","article-title":"Inhibition of Glutathione Efflux in the Perfused Rat Liver and Isolated Hepatocytes by Organic Anions and Bilirubin","volume":"82","author":"Ookhtens","year":"1988","journal-title":"Kinet. Sidedness Mol. Forms. J. Clin. Investig."},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1016\/j.atherosclerosis.2009.12.026","article-title":"Plasma Bilirubin and Gamma-Glutamyltransferase Activity Are Inversely Related in Dyslipidemic Patients with Metabolic Syndrome: Relevance to Oxidative Stress","volume":"210","author":"Giral","year":"2010","journal-title":"Atherosclerosis"},{"key":"ref_185","doi-asserted-by":"crossref","unstructured":"Wang, Y., and Wu, J. (2023). Ferroptosis: A New Strategy for Cardiovascular Disease. Front. Cardiovasc. Med., 10.","DOI":"10.3389\/fcvm.2023.1241282"},{"key":"ref_186","doi-asserted-by":"crossref","unstructured":"Vitek, L. (2012). The Role of Bilirubin in Diabetes, Metabolic Syndrome, and Cardiovascular Diseases. Front. Pharmacol., 3.","DOI":"10.3389\/fphar.2012.00055"},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"1821","DOI":"10.1016\/j.biochi.2012.04.026","article-title":"Intracellular Accumulation of Bilirubin as a Defense Mechanism against Increased Oxidative Stress","volume":"94","author":"Zelenka","year":"2012","journal-title":"Biochimie"},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"29240","DOI":"10.1038\/srep29240","article-title":"Bilirubin Is an Endogenous Antioxidant in Human Vascular Endothelial Cells","volume":"6","author":"Ziberna","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_189","first-page":"151","article-title":"Bilirubin Effect on Endothelial Adhesion Molecules Expression Is Mediated by the NF-kappaB Signaling Pathway","volume":"3","author":"Mazzone","year":"2009","journal-title":"Biosci. Trends"},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"481","DOI":"10.21037\/atm.2016.12.27","article-title":"Gamma-Glutamyl Transferase and Cardiovascular Disease","volume":"4","author":"Ndrepepa","year":"2016","journal-title":"Ann. Transl. Med."},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1177\/108155899904700311","article-title":"Gamma-Glutamyl Transpeptidase-Dependent Iron Reduction and LDL Oxidation\u2014A Potential Mechanism in Atherosclerosis","volume":"47","author":"Paolicchi","year":"1999","journal-title":"J. Investig. Med."},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"677","DOI":"10.1016\/j.numecd.2015.03.014","article-title":"Clinical Significance of Serum Bilirubin and Gamma-Glutamyltransferase Levels on Coronary Atherosclerosis Assessed by Multidetector Computed Tomography","volume":"25","author":"Cho","year":"2015","journal-title":"Nutr. Metab. Cardiovasc. Dis."},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"e70385","DOI":"10.1002\/fsn3.70385","article-title":"Emerging Links Between Ferroptosis and Neurodegeneration: Implications for Disease Mechanisms and Nutraceutical Interventions","volume":"13","author":"Ali","year":"2025","journal-title":"Food Sci. Nutr."},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1089\/ars.2021.0218","article-title":"Dysregulation of Iron Homeostasis in the Central Nervous System and the Role of Ferroptosis in Neurodegenerative Disorders","volume":"37","author":"David","year":"2022","journal-title":"Antioxid. Redox Signal."},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/j.nbd.2015.05.009","article-title":"Iron Accumulation Promotes TACE-Mediated TNF-\u03b1 Secretion and Neurodegeneration in a Mouse Model of ALS","volume":"80","author":"Lee","year":"2015","journal-title":"Neurobiol. Dis."},{"key":"ref_196","doi-asserted-by":"crossref","unstructured":"Yi, Y., Jia, P., Xie, P., Peng, X., Zhu, X., Yin, S., Luo, Y., Deng, Y., and Wan, L. (2025). Beyond Oxidative Stress: Ferroptosis as a Novel Orchestrator in Neurodegenerative Disorders. Front. Immunol., 16.","DOI":"10.3389\/fimmu.2025.1683876"},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"102077","DOI":"10.1016\/j.arr.2023.102077","article-title":"Ferroptosis in Parkinson\u2019s Disease: Molecular Mechanisms and Therapeutic Potential","volume":"91","author":"Ding","year":"2023","journal-title":"Ageing Res. Rev."},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1186\/s40035-024-00432-x","article-title":"Updates in Alzheimer\u2019s Disease: From Basic Research to Diagnosis and Therapies","volume":"13","author":"Liu","year":"2024","journal-title":"Transl. Neurodegener."},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"1219","DOI":"10.1016\/S0140-6736(87)91361-4","article-title":"Increased Nigral Iron Content in Postmortem Parkinsonian Brain","volume":"2","author":"Dexter","year":"1987","journal-title":"Lancet"},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"4130937","DOI":"10.1155\/2023\/4130937","article-title":"\u03b4-Opioid Receptor Activation Inhibits Ferroptosis by Activating the Nrf2 Pathway in MPTP-Induced Parkinson Disease Models","volume":"2023","author":"Cai","year":"2023","journal-title":"Evid. Based Complement. Altern. Med."},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"446","DOI":"10.1111\/j.1471-4159.1991.tb08170.x","article-title":"Iron and Aluminum Increase in the Substantia Nigra of Patients with Parkinson\u2019s Disease: An X-Ray Microanalysis","volume":"56","author":"Hirsch","year":"1991","journal-title":"J. Neurochem."},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1016\/0304-3940(92)90355-B","article-title":"Reduced and Oxidized Glutathione in the Substantia Nigra of Patients with Parkinson\u2019s Disease","volume":"142","author":"Sofic","year":"1992","journal-title":"Neurosci. Lett."},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1186\/1750-1326-6-8","article-title":"Glutathione Peroxidase 4 Is Associated with Neuromelanin in Substantia Nigra and Dystrophic Axons in Putamen of Parkinson\u2019s Brain","volume":"6","author":"Bellinger","year":"2011","journal-title":"Mol. Neurodegener."},{"key":"ref_204","doi-asserted-by":"crossref","unstructured":"Huang, Q., Zhang, H., Chen, S., Wang, Y., and Zhou, J. (2025). Ferroptosis in Central Nervous System Injuries: Molecular Mechanisms, Diagnostic Approaches, and Therapeutic Strategies. Front. Cell. Neurosci., 19.","DOI":"10.3389\/fncel.2025.1593963"},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"1026","DOI":"10.1093\/brain\/aww022","article-title":"Iron and Dopamine: A Toxic Couple","volume":"139","author":"Hare","year":"2016","journal-title":"Brain J. Neurol."},{"key":"ref_206","doi-asserted-by":"crossref","unstructured":"Nagatsu, T., Nakashima, A., Watanabe, H., Ito, S., and Wakamatsu, K. (2022). Neuromelanin in Parkinson\u2019s Disease: Tyrosine Hydroxylase and Tyrosinase. Int. J. Mol. Sci., 23.","DOI":"10.20944\/preprints202203.0274.v1"},{"key":"ref_207","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/bs.ircmb.2025.12.004","article-title":"Chapter Four\u2014Advances in Ferroptosis Research and Applications","volume":"Volume 405","author":"Spada","year":"2026","journal-title":"Advances in Biomedical Engineering\u2014Part B"},{"key":"ref_208","doi-asserted-by":"crossref","first-page":"1564","DOI":"10.1124\/mol.108.048611","article-title":"Overexpression of Heme Oxygenase-1 Protects Dopaminergic Neurons against 1-Methyl-4-Phenylpyridinium-Induced Neurotoxicity","volume":"74","author":"Hung","year":"2008","journal-title":"Mol. Pharmacol."},{"key":"ref_209","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1016\/S0169-328X(02)00586-7","article-title":"Oxidative Stress Regulated Genes in Nigral Dopaminergic Neuronal Cells: Correlation with the Known Pathology in Parkinson\u2019s Disease","volume":"110","author":"Yoo","year":"2003","journal-title":"Mol. Brain Res."},{"key":"ref_210","doi-asserted-by":"crossref","unstructured":"Ayuso, P., Mart\u00ednez, C., Pastor, P., Lorenzo-Betancor, O., Luengo, A., Jim\u00e9nez-Jim\u00e9nez, F.J., Alonso-Navarro, H., Ag\u00fandez, J.A.G., and Garc\u00eda-Mart\u00edn, E. (2014). An Association Study between Heme Oxygenase-1 Genetic Variants and Parkinson\u2019s Disease. Front. Cell. Neurosci., 8.","DOI":"10.3389\/fncel.2014.00298"},{"key":"ref_211","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1111\/j.1471-4159.2009.06160.x","article-title":"Heme Oxygenase-1 and Neurodegeneration: Expanding Frontiers of Engagement","volume":"110","author":"Schipper","year":"2009","journal-title":"J. Neurochem."},{"key":"ref_212","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1016\/j.parkreldis.2019.01.012","article-title":"Increased Bilirubin Levels in Parkinson\u2019s Disease","volume":"63","author":"Labrador","year":"2019","journal-title":"Park. Relat. Disord."},{"key":"ref_213","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1136\/jnnp-2014-309676","article-title":"Identification of Novel Biomarkers for Parkinson\u2019s Disease by Metabolomic Technologies","volume":"87","author":"Hatano","year":"2016","journal-title":"J. Neurol. Neurosurg. Psychiatry"},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"2314","DOI":"10.1046\/j.1523-1755.2000.00415.x","article-title":"Dopamine Induces the Expression of Heme Oxygenase-1 by Human Endothelial Cells in Vitro","volume":"58","author":"Berger","year":"2000","journal-title":"Kidney Int."},{"key":"ref_215","first-page":"288","article-title":"Dose-Effect Relationship of Bilirubin on Striatal Synaptosomes in Rats","volume":"66","author":"Amato","year":"1994","journal-title":"Biol. Neonate"},{"key":"ref_216","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1007\/BF00712990","article-title":"Interactions of Bilirubin with Isolated Presynaptic Nerve Terminals: Functional Effects on the Uptake and Release of Neurotransmitters","volume":"13","author":"Ochoa","year":"1993","journal-title":"Cell. Mol. Neurobiol."},{"key":"ref_217","first-page":"335","article-title":"In Vitro Effect of Bilirubin on Dopamine Synthesis in Adult Rat Brain Synaptosomes","volume":"19","author":"Brann","year":"1985","journal-title":"Pediatr. Res."},{"key":"ref_218","doi-asserted-by":"crossref","first-page":"312","DOI":"10.1203\/00006450-199809000-00008","article-title":"Bilirubin Inhibits Transport of Neurotransmitters in Synaptic Vesicles","volume":"44","author":"Roseth","year":"1998","journal-title":"Pediatr. Res."},{"key":"ref_219","doi-asserted-by":"crossref","unstructured":"Jayanti, S., Moretti, R., Tiribelli, C., and Gazzin, S. (2022). Bilirubin Prevents the TH+ Dopaminergic Neuron Loss in a Parkinson\u2019s Disease Model by Acting on TNF-\u03b1. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms232214276"},{"key":"ref_220","doi-asserted-by":"crossref","first-page":"e36053","DOI":"10.1016\/j.heliyon.2024.e36053","article-title":"Association between Serum Total Bilirubin with Parkinson\u2019s Disease among American Adults (NHANES 1999 to 2018)","volume":"10","author":"Su","year":"2024","journal-title":"Heliyon"},{"key":"ref_221","doi-asserted-by":"crossref","first-page":"702","DOI":"10.1016\/j.biopsych.2015.04.005","article-title":"Brain Glutathione Levels\u2014A Novel Biomarker for Mild Cognitive Impairment and Alzheimer\u2019s Disease","volume":"78","author":"Mandal","year":"2015","journal-title":"Biol. Psychiatry"},{"key":"ref_222","doi-asserted-by":"crossref","first-page":"1562","DOI":"10.1212\/WNL.51.6.1562","article-title":"Decreased Glutathione Transferase Activity in Brain and Ventricular Fluid in Alzheimer\u2019s Disease","volume":"51","author":"Lovell","year":"1998","journal-title":"Neurology"},{"key":"ref_223","first-page":"e20078","article-title":"Oxidative Stress Gated by Fenton and Haber Weiss Reactions and Its Association With Alzheimer\u2019s Disease","volume":"2","author":"Das","year":"2014","journal-title":"ResearchGate"},{"key":"ref_224","doi-asserted-by":"crossref","first-page":"480","DOI":"10.1016\/j.bbadis.2011.01.005","article-title":"Biliverdin Reductase-A Protein Levels and Activity in the Brains of Subjects with Alzheimer Disease and Mild Cognitive Impairment","volume":"1812","author":"Barone","year":"2011","journal-title":"Biochim. Biophys. Acta BBA-Mol. Basis Dis."},{"key":"ref_225","doi-asserted-by":"crossref","first-page":"3181","DOI":"10.1016\/j.bbadis.2018.07.005","article-title":"Biliverdin Reductase-A Impairment Links Brain Insulin Resistance with Increased A\u03b2 Production in an Animal Model of Aging: Implications for Alzheimer Disease","volume":"1864","author":"Triani","year":"2018","journal-title":"Biochim. Biophys. Acta BBA-Mol. Basis Dis."},{"key":"ref_226","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1111\/j.1471-4159.2011.07538.x","article-title":"Biliverdin Reductase-A: A Novel Drug Target for Atorvastatin in a Dog Pre-Clinical Model of Alzheimer Disease","volume":"120","author":"Barone","year":"2012","journal-title":"J. Neurochem."},{"key":"ref_227","doi-asserted-by":"crossref","first-page":"9886","DOI":"10.1038\/srep09886","article-title":"Bilirubin Increases Insulin Sensitivity by Regulating Cholesterol Metabolism, Adipokines and PPAR\u03b3 Levels","volume":"5","author":"Liu","year":"2015","journal-title":"Sci. Rep."},{"key":"ref_228","doi-asserted-by":"crossref","first-page":"2435","DOI":"10.1007\/s12035-024-04417-9","article-title":"Ferroptosis in Cognitive Impairment Associated with Diabetes and Alzheimer\u2019s Disease: Mechanistic Insights and New Therapeutic Opportunities","volume":"62","author":"Ma","year":"2025","journal-title":"Mol. Neurobiol."},{"key":"ref_229","doi-asserted-by":"crossref","unstructured":"Ding, H., Yan, C.-Z., Shi, H., Zhao, Y.-S., Chang, S.-Y., Yu, P., Wu, W.-S., Zhao, C.-Y., Chang, Y.-Z., and Duan, X.-L. (2011). Hepcidin Is Involved in Iron Regulation in the Ischemic Brain. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0025324"},{"key":"ref_230","doi-asserted-by":"crossref","unstructured":"Cui, Q., Guo, C., Luo, Y., Liu, D., Wang, D., Wang, Z., and Xu, Z. (2026). Hypoxia-Inducible Factor 1-Alpha: A Dual Regulator of Ferroptosis in Ischemic Stroke and a Promising Therapeutic Target. Front. Neurol., 17.","DOI":"10.3389\/fneur.2026.1859829"},{"key":"ref_231","doi-asserted-by":"crossref","first-page":"3329","DOI":"10.1007\/s10571-023-01388-8","article-title":"The Mechanisms of Ferroptosis Under Hypoxia","volume":"43","author":"Gao","year":"2023","journal-title":"Cell. Mol. Neurobiol."},{"key":"ref_232","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1111\/j.1742-7843.2010.00537.x","article-title":"Protective Effect of Sesamol against 3-Nitropropionic Acid-Induced Cognitive Dysfunction and Altered Glutathione Redox Balance in Rats","volume":"107","author":"Kumar","year":"2010","journal-title":"Basic Clin. Pharmacol. Toxicol."},{"key":"ref_233","doi-asserted-by":"crossref","first-page":"1676","DOI":"10.1007\/s00415-007-0611-y","article-title":"Oxidative Stress Parameters in Plasma of Huntington\u2019s Disease Patients, Asymptomatic Huntington\u2019s Disease Gene Carriers and Healthy Subjects: A Cross-Sectional Study","volume":"254","author":"Klepac","year":"2007","journal-title":"J. Neurol."},{"key":"ref_234","doi-asserted-by":"crossref","first-page":"1701","DOI":"10.1111\/j.1460-9568.2006.04686.x","article-title":"Cystamine and Cysteamine Prevent 3-NP-induced Mitochondrial Depolarization of Huntington\u2019s Disease Knock-in Striatal Cells","volume":"23","author":"Mao","year":"2006","journal-title":"Eur. J. Neurosci."},{"key":"ref_235","doi-asserted-by":"crossref","first-page":"204","DOI":"10.1101\/gad.350211.122","article-title":"ALOX5-Mediated Ferroptosis Acts as a Distinct Cell Death Pathway upon Oxidative Stress in Huntington\u2019s Disease","volume":"37","author":"Song","year":"2023","journal-title":"Genes Dev."},{"key":"ref_236","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/j.neuroscience.2014.12.018","article-title":"Neuroprotective Effect of Hemeoxygenase-1\/Glycogen Synthase Kinase-3\u03b2 Modulators in 3-Nitropropionic Acid-Induced Neurotoxicity in Rats","volume":"287","author":"Khan","year":"2015","journal-title":"Neuroscience"},{"key":"ref_237","doi-asserted-by":"crossref","first-page":"102941","DOI":"10.1016\/j.msard.2021.102941","article-title":"Serum Malondialdehyde as a Lipid Peroxidation Marker in Multiple Sclerosis Patients and Its Relation to Disease Characteristics","volume":"51","author":"Ghonimi","year":"2021","journal-title":"Mult. Scler. Relat. Disord."},{"key":"ref_238","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1155\/2009\/325847","article-title":"Oxidative Stress Is Increased in Serum from Mexican Patients with Relapsing-Remitting Multiple Sclerosis","volume":"26","author":"Ortiz","year":"2009","journal-title":"Dis. Markers"},{"key":"ref_239","doi-asserted-by":"crossref","first-page":"577995","DOI":"10.1016\/j.jneuroim.2022.577995","article-title":"Ferroptosis as a Mechanism of Oligodendrocyte Loss and Demyelination in Experimental Autoimmune Encephalomyelitis","volume":"373","author":"Li","year":"2022","journal-title":"J. Neuroimmunol."},{"key":"ref_240","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/S0165-5728(03)00132-2","article-title":"Bilirubin as a Potent Antioxidant Suppresses Experimental Autoimmune Encephalomyelitis: Implications for the Role of Oxidative Stress in the Development of Multiple Sclerosis","volume":"139","author":"Liu","year":"2003","journal-title":"J. Neuroimmunol."},{"key":"ref_241","doi-asserted-by":"crossref","first-page":"1841","DOI":"10.1097\/00001756-200107030-00016","article-title":"Heme Oxygenase-1 Plays an Important Protective Role in Experimental Autoimmune Encephalomyelitis","volume":"12","author":"Liu","year":"2001","journal-title":"NeuroReport"},{"key":"ref_242","doi-asserted-by":"crossref","first-page":"960","DOI":"10.1016\/j.freeradbiomed.2005.07.021","article-title":"Biliverdin Reductase, a Major Physiologic Cytoprotectant, Suppresses Experimental Autoimmune Encephalomyelitis","volume":"40","author":"Liu","year":"2006","journal-title":"Free Radic. Biol. Med."},{"key":"ref_243","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1021\/acscentsci.7b00589","article-title":"Resolving the Role of Lipoxygenases in the Initiation and Execution of Ferroptosis","volume":"4","author":"Shah","year":"2018","journal-title":"ACS Cent. Sci."},{"key":"ref_244","doi-asserted-by":"crossref","first-page":"1507","DOI":"10.1007\/s12035-023-03646-8","article-title":"Oxytosis\/Ferroptosis in Neurodegeneration: The Underlying Role of Master Regulator Glutathione Peroxidase 4 (GPX4)","volume":"61","author":"Dar","year":"2024","journal-title":"Mol. Neurobiol."},{"key":"ref_245","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1016\/j.cell.2013.12.010","article-title":"Regulation of Ferroptotic Cancer Cell Death by GPX4","volume":"156","author":"Yang","year":"2014","journal-title":"Cell"},{"key":"ref_246","doi-asserted-by":"crossref","unstructured":"Zhang, L., Luo, Y.L., Xiang, Y., Bai, X.Y., Qiang, R.R., Zhang, X., Yang, Y.L., and Liu, X.L. (2024). Ferroptosis Inhibitors: Past, Present and Future. Front. Pharmacol., 15.","DOI":"10.3389\/fphar.2024.1407335"},{"key":"ref_247","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1196\/annals.1345.018","article-title":"Recent Insights into Interactions of Deferoxamine with Cellular and Plasma Iron Pools: Implications for Clinical Use","volume":"1054","author":"Porter","year":"2005","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"ref_248","doi-asserted-by":"crossref","first-page":"606","DOI":"10.1016\/j.bbrc.2019.10.006","article-title":"Liproxstatin-1 Protects the Mouse Myocardium against Ischemia\/Reperfusion Injury by Decreasing VDAC1 Levels and Restoring GPX4 Levels","volume":"520","author":"Feng","year":"2019","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_249","doi-asserted-by":"crossref","first-page":"2054","DOI":"10.1080\/15548627.2020.1810918","article-title":"Ferroptosis: Machinery and Regulation","volume":"17","author":"Chen","year":"2021","journal-title":"Autophagy"},{"key":"ref_250","doi-asserted-by":"crossref","first-page":"4551","DOI":"10.1021\/ja411006a","article-title":"Ferrostatins Inhibit Oxidative Lipid Damage and Cell Death in Diverse Disease Models","volume":"136","author":"Skouta","year":"2014","journal-title":"J. Am. Chem. Soc."},{"key":"ref_251","doi-asserted-by":"crossref","first-page":"1520","DOI":"10.1038\/mp.2017.171","article-title":"Tau-Mediated Iron Export Prevents Ferroptotic Damage after Ischemic Stroke","volume":"22","author":"Tuo","year":"2017","journal-title":"Mol. Psychiatry"},{"key":"ref_252","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/j.brainres.2016.02.006","article-title":"Therapies Targeting Lipid Peroxidation in Traumatic Brain Injury","volume":"1640","author":"Anthonymuthu","year":"2016","journal-title":"Brain Res."},{"key":"ref_253","doi-asserted-by":"crossref","first-page":"528","DOI":"10.4103\/1673-5374.266060","article-title":"Ferrostatin-1 Protects HT-22 Cells from Oxidative Toxicity","volume":"15","author":"Chu","year":"2020","journal-title":"Neural Regen. Res."},{"key":"ref_254","doi-asserted-by":"crossref","first-page":"916","DOI":"10.1016\/j.drudis.2020.12.020","article-title":"Inhibiting Ferroptosis: A Novel Approach for Stroke Therapeutics","volume":"26","author":"Jin","year":"2021","journal-title":"Drug Discov. Today"},{"key":"ref_255","doi-asserted-by":"crossref","first-page":"778","DOI":"10.1038\/s41586-022-05022-3","article-title":"A Non-Canonical Vitamin K Cycle Is a Potent Ferroptosis Suppressor","volume":"608","author":"Mishima","year":"2022","journal-title":"Nature"},{"key":"ref_256","doi-asserted-by":"crossref","first-page":"821","DOI":"10.3109\/09637486.2011.585963","article-title":"Caffeic Acid Phenethyl Ester (CAPE): Correlation of Structure and Antioxidant Properties","volume":"62","year":"2011","journal-title":"Int. J. Food Sci. Nutr."},{"key":"ref_257","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1016\/j.brainresbull.2019.08.006","article-title":"Matrine Protects Oligodendrocytes by Inhibiting Their Apoptosis and Enhancing Mitochondrial Autophagy","volume":"153","author":"Wang","year":"2019","journal-title":"Brain Res. Bull."},{"key":"ref_258","doi-asserted-by":"crossref","first-page":"150651","DOI":"10.1016\/j.bbrc.2024.150651","article-title":"Matrine Protects against Experimental Autoimmune Encephalomyelitis through Modulating Microglial Ferroptosis","volume":"735","author":"Feng","year":"2024","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_259","doi-asserted-by":"crossref","first-page":"110186","DOI":"10.1016\/j.biopha.2020.110186","article-title":"A Review for Physiological Activities of EGCG and the Role in Improving Fertility in Humans\/Mammals","volume":"127","author":"Zhang","year":"2020","journal-title":"Biomed. Pharmacother."},{"key":"ref_260","doi-asserted-by":"crossref","first-page":"5440","DOI":"10.1002\/ptr.7176","article-title":"Sulforaphane: A Review of Its Therapeutic Potentials, Advances in Its Nanodelivery, Recent Patents, and Clinical Trials","volume":"35","author":"Mangla","year":"2021","journal-title":"Phytother. Res."},{"key":"ref_261","doi-asserted-by":"crossref","first-page":"656","DOI":"10.1111\/bph.14881","article-title":"CuII (Atsm) Inhibits Ferroptosis: Implications for Treatment of Neurodegenerative Disease","volume":"177","author":"Southon","year":"2020","journal-title":"Br. J. Pharmacol."},{"key":"ref_262","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1007\/BF02924441","article-title":"Protective Effect of AA-861 (5-Lipoxygenase Inhibitor) on Experimental Acute Necrotizing Pancreatitis in Rats","volume":"13","author":"Kiriyama","year":"1993","journal-title":"Int. J. Pancreatol."},{"key":"ref_263","doi-asserted-by":"crossref","first-page":"17590914211010647","DOI":"10.1177\/17590914211010647","article-title":"Paeonol Inhibits the Progression of Intracerebral Haemorrhage by Mediating the HOTAIR\/UPF1\/ACSL4 Axis","volume":"13","author":"Jin","year":"2021","journal-title":"ASN Neuro"},{"key":"ref_264","doi-asserted-by":"crossref","first-page":"854","DOI":"10.1002\/ana.25356","article-title":"N-acetylcysteine Targets 5 Lipoxygenase-derived, Toxic Lipids and Can Synergize with Prostaglandin E2 to Inhibit Ferroptosis and Improve Outcomes Following Hemorrhagic Stroke in Mice","volume":"84","author":"Karuppagounder","year":"2018","journal-title":"Ann. Neurol."},{"key":"ref_265","doi-asserted-by":"crossref","first-page":"561","DOI":"10.4103\/1673-5374.293157","article-title":"Liproxstatin-1 Is an Effective Inhibitor of Oligodendrocyte Ferroptosis Induced by Inhibition of Glutathione Peroxidase 4","volume":"16","author":"Fan","year":"2021","journal-title":"Neural Regen. Res."},{"key":"ref_266","doi-asserted-by":"crossref","unstructured":"Han, R., Wan, J., Han, X., Ren, H., Falck, J.R., Munnuri, S., Yang, Z.-J., and Koehler, R.C. (2021). 20-HETE Participates in Intracerebral Hemorrhage-Induced Acute Injury by Promoting Cell Ferroptosis. Front. Neurol., 12.","DOI":"10.3389\/fneur.2021.763419"},{"key":"ref_267","doi-asserted-by":"crossref","first-page":"969","DOI":"10.1016\/j.lfs.2003.06.042","article-title":"Neuroprotective Effect of Curcumin in Middle Cerebral Artery Occlusion Induced Focal Cerebral Ischemia in Rats","volume":"74","author":"Thiyagarajan","year":"2004","journal-title":"Life Sci."},{"key":"ref_268","doi-asserted-by":"crossref","unstructured":"Hinman, A., Holst, C.R., Latham, J.C., Bruegger, J.J., Ulas, G., McCusker, K.P., Amagata, A., Davis, D., Hoff, K.G., and Kahn-Kirby, A.H. (2018). Vitamin E Hydroquinone Is an Endogenous Regulator of Ferroptosis via Redox Control of 15-Lipoxygenase. PLoS ONE, 13.","DOI":"10.1371\/journal.pone.0201369"},{"key":"ref_269","doi-asserted-by":"crossref","first-page":"2836","DOI":"10.3390\/nu5082836","article-title":"Iron Deprivation in Cancer\u2013\u2013Potential Therapeutic Implications","volume":"5","author":"Heath","year":"2013","journal-title":"Nutrients"},{"key":"ref_270","doi-asserted-by":"crossref","first-page":"2048","DOI":"10.1038\/s41467-021-22336-4","article-title":"Ferroptosis Response Segregates Small Cell Lung Cancer (SCLC) Neuroendocrine Subtypes","volume":"12","author":"Bebber","year":"2021","journal-title":"Nat. Commun."},{"key":"ref_271","doi-asserted-by":"crossref","first-page":"1793","DOI":"10.1038\/jcbfm.2010.137","article-title":"Hemoglobin and Iron Handling in Brain after Subarachnoid Hemorrhage and the Effect of Deferoxamine on Early Brain Injury","volume":"30","author":"Lee","year":"2010","journal-title":"J. Cereb. Blood Flow Metab."},{"key":"ref_272","doi-asserted-by":"crossref","first-page":"2045","DOI":"10.1056\/NEJMoa2209254","article-title":"Trial of Deferiprone in Parkinson\u2019s Disease","volume":"387","author":"Devos","year":"2022","journal-title":"N. Engl. J. Med."},{"key":"ref_273","doi-asserted-by":"crossref","first-page":"3527","DOI":"10.1007\/s00210-024-03640-4","article-title":"Therapeutic Potential of Synthetic and Natural Iron Chelators against Ferroptosis","volume":"398","author":"Prabhune","year":"2025","journal-title":"Naunyn. Schmiedebergs Arch. Pharmacol."},{"key":"ref_274","doi-asserted-by":"crossref","first-page":"767","DOI":"10.1016\/j.chembiol.2025.04.002","article-title":"N-Acetyl-l-Cysteine Averts Ferroptosis by Fostering Glutathione Peroxidase 4","volume":"32","author":"Zheng","year":"2025","journal-title":"Cell Chem. Biol."},{"key":"ref_275","doi-asserted-by":"crossref","first-page":"1180","DOI":"10.1038\/ncb3064","article-title":"Inactivation of the Ferroptosis Regulator Gpx4 Triggers Acute Renal Failure in Mice","volume":"16","author":"Schneider","year":"2014","journal-title":"Nat. Cell Biol."},{"key":"ref_276","doi-asserted-by":"crossref","first-page":"1351","DOI":"10.1038\/s41589-020-0613-y","article-title":"Metabolic Determinants of Cancer Cell Sensitivity to Canonical Ferroptosis Inducers","volume":"16","author":"Soula","year":"2020","journal-title":"Nat. Chem. Biol."},{"key":"ref_277","doi-asserted-by":"crossref","first-page":"114930","DOI":"10.1016\/j.biopha.2023.114930","article-title":"Vitamin A Metabolites Inhibit Ferroptosis","volume":"164","author":"Jakaria","year":"2023","journal-title":"Biomed. Pharmacother."},{"key":"ref_278","doi-asserted-by":"crossref","first-page":"586","DOI":"10.1038\/s41586-021-03539-7","article-title":"DHODH-Mediated Ferroptosis Defence Is a Targetable Vulnerability in Cancer","volume":"593","author":"Mao","year":"2021","journal-title":"Nature"},{"key":"ref_279","doi-asserted-by":"crossref","first-page":"4497","DOI":"10.1038\/s41598-025-34673-1","article-title":"Tocotrienols Exhibit Superior Ferroptosis Inhibition over Tocopherols","volume":"16","author":"Yang","year":"2026","journal-title":"Sci. Rep."},{"key":"ref_280","doi-asserted-by":"crossref","first-page":"858","DOI":"10.1111\/1440-1681.13673","article-title":"Hemin Mitigates Contrast-induced Nephropathy by Inhibiting Ferroptosis via HO -1\/Nrf2\/ GPX4 Pathway","volume":"49","author":"Gao","year":"2022","journal-title":"Clin. Exp. Pharmacol. Physiol."},{"key":"ref_281","doi-asserted-by":"crossref","unstructured":"Pham, J., Refesse, M., Saeed, A., and Latunde-Dada, G.O. (2025). Haem Oxygenase-1, Ferroptosis and Disorders\u2014A Narrative Review. Nutrients, 17.","DOI":"10.3390\/nu17243921"},{"key":"ref_282","doi-asserted-by":"crossref","first-page":"105580","DOI":"10.1016\/j.phrs.2021.105580","article-title":"Regulation of Ferroptosis by Bioactive Phytochemicals: Implications for Medical Nutritional Therapy","volume":"168","author":"Zheng","year":"2021","journal-title":"Pharmacol. Res."},{"key":"ref_283","doi-asserted-by":"crossref","unstructured":"Ge, C., Zhang, S., Mu, H., Zheng, S., Tan, Z., Huang, X., Xu, C., Zou, J., Zhu, Y., and Feng, D. (2022). Emerging Mechanisms and Disease Implications of Ferroptosis: Potential Applications of Natural Products. Front. Cell Dev. Biol., 9.","DOI":"10.3389\/fcell.2021.774957"},{"key":"ref_284","doi-asserted-by":"crossref","unstructured":"Chen, X., Yu, C., Kang, R., and Tang, D. (2020). Iron Metabolism in Ferroptosis. Front. Cell Dev. Biol., 8.","DOI":"10.3389\/fcell.2020.590226"}],"container-title":["Biomolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2218-273X\/16\/9\/1371\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,23]],"date-time":"2026-09-23T04:14:39Z","timestamp":1790136879000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2218-273X\/16\/9\/1371"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9,21]]},"references-count":284,"journal-issue":{"issue":"9","published-online":{"date-parts":[[2026,9]]}},"alternative-id":["biom16091371"],"URL":"https:\/\/doi.org\/10.3390\/biom16091371","relation":{},"ISSN":["2218-273X"],"issn-type":[{"value":"2218-273X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,9,21]]}}}