{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,12]],"date-time":"2026-10-12T17:06:22Z","timestamp":1791824782852,"version":"4.3.4"},"reference-count":186,"publisher":"MDPI AG","issue":"4","license":[{"start":{"date-parts":[[2023,4,12]],"date-time":"2023-04-12T00:00:00Z","timestamp":1681257600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"The National Research Foundation of Korea (NRF) of the Korean Government","award":["NRF-2021R1F1A1051212"],"award-info":[{"award-number":["NRF-2021R1F1A1051212"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Antioxidants"],"abstract":"<jats:p>Iron is essential for life. Many enzymes require iron for appropriate function. However, dysregulation of intracellular iron homeostasis produces excessive reactive oxygen species (ROS) via the Fenton reaction and causes devastating effects on cells, leading to ferroptosis, an iron-dependent cell death. In order to protect against harmful effects, the intracellular system regulates cellular iron levels through iron regulatory mechanisms, including hepcidin\u2013ferroportin, divalent metal transporter 1 (DMT1)\u2013transferrin, and ferritin\u2013nuclear receptor coactivator 4 (NCOA4). During iron deficiency, DMT1\u2013transferrin and ferritin\u2013NCOA4 systems increase intracellular iron levels via endosomes and ferritinophagy, respectively. In contrast, repleting extracellular iron promotes cellular iron absorption through the hepcidin\u2013ferroportin axis. These processes are regulated by the iron-regulatory protein (IRP)\/iron-responsive element (IRE) system and nuclear factor erythroid 2-related factor 2 (Nrf2). Meanwhile, excessive ROS also promotes neuroinflammation by activating the nuclear factor kappa-light-chain-enhancer of activated B cells (NF-\u03baB). NF-\u03baB forms inflammasomes, inhibits silent information regulator 2-related enzyme 1 (SIRT1), and induces pro-inflammatory cytokines (IL-6, TNF-\u03b1, and IL-1\u03b2). Furthermore, 4-hydroxy-2,3-trans-nonenal (4-HNE), the end-product of ferroptosis, promotes the inflammatory response by producing amyloid-beta (A\u03b2) fibrils and neurofibrillary tangles in Alzheimer\u2019s disease, and alpha-synuclein aggregation in Parkinson\u2019s disease. This interplay shows that intracellular iron homeostasis is vital to maintain inflammatory homeostasis. Here, we review the role of iron homeostasis in inflammation based on recent findings.<\/jats:p>","DOI":"10.3390\/antiox12040918","type":"journal-article","created":{"date-parts":[[2023,4,13]],"date-time":"2023-04-13T02:29:15Z","timestamp":1681352955000},"page":"918","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":123,"title":["The Interplay between Intracellular Iron Homeostasis and Neuroinflammation in Neurodegenerative Diseases"],"prefix":"10.3390","volume":"12","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1184-1756","authenticated-orcid":false,"given":"Jaewang","family":"Lee","sequence":"first","affiliation":[{"name":"Department of Life Science, Ewha Womans University, Seoul 03760, Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0542-166X","authenticated-orcid":false,"given":"Dong-Hoon","family":"Hyun","sequence":"additional","affiliation":[{"name":"Department of Life Science, Ewha Womans University, Seoul 03760, Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,4,12]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"103","DOI":"10.2214\/ajr.147.1.103","article-title":"MRI of brain iron","volume":"147","author":"Drayer","year":"1986","journal-title":"AJR Am. J. Roentgenol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"414","DOI":"10.1016\/j.neurobiolaging.2006.02.005","article-title":"Brain ferritin iron may influence age- and gender-related risks of neurodegeneration","volume":"28","author":"Bartzokis","year":"2007","journal-title":"Neurobiol. Aging"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"598","DOI":"10.1016\/j.ebiom.2019.08.014","article-title":"New insights into the role of iron in inflammation and atherosclerosis","volume":"47","author":"Cornelissen","year":"2019","journal-title":"EBioMedicine"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1093\/intimm\/dxx031","article-title":"Hyperferritinemia and inflammation","volume":"29","author":"Kernan","year":"2017","journal-title":"Int. Immunol."},{"key":"ref_5","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_6","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_7","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1177\/107385840200800107","article-title":"Iron and Parkinson\u2019s disease","volume":"8","author":"Wolozin","year":"2002","journal-title":"Neuroscientist"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"632","DOI":"10.3389\/fnins.2018.00632","article-title":"Iron and Alzheimer\u2019s Disease: From Pathogenesis to Therapeutic Implications","volume":"12","author":"Liu","year":"2018","journal-title":"Front. Neurosci."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1038\/nrn3453","article-title":"Iron metabolism in the CNS: Implications for neurodegenerative diseases","volume":"14","author":"Rouault","year":"2013","journal-title":"Nat. Rev. Neurosci."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1146\/annurev-genom-090314-025011","article-title":"Neurodegeneration with Brain Iron Accumulation: Genetic Diversity and Pathophysiological Mechanisms","volume":"16","author":"Meyer","year":"2015","journal-title":"Annu. Rev. Genomics Hum. Genet."},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Reinert, A., Morawski, M., Seeger, J., Arendt, T., and Reinert, T. (2019). Iron concentrations in neurons and glial cells with estimates on ferritin concentrations. BMC Neurosci., 20.","DOI":"10.1186\/s12868-019-0507-7"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1007\/s12640-013-9435-y","article-title":"Neuromelanin of the human substantia nigra: An update","volume":"25","author":"Zucca","year":"2014","journal-title":"Neurotox. Res."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"e272","DOI":"10.1016\/j.lpm.2017.10.006","article-title":"Iron metabolism and the role of the iron-regulating hormone hepcidin in health and disease","volume":"46","author":"Daher","year":"2017","journal-title":"Presse. Med."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"1520","DOI":"10.1056\/NEJM198206243062504","article-title":"Perspectives in iron metabolism","volume":"306","author":"Finch","year":"1982","journal-title":"N. Engl. J. Med."},{"key":"ref_15","doi-asserted-by":"crossref","unstructured":"Vogt, A.S., Arsiwala, T., Mohsen, M., Vogel, M., Manolova, V., and Bachmann, M.F. (2021). On Iron Metabolism and Its Regulation. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22094591"},{"key":"ref_16","doi-asserted-by":"crossref","unstructured":"Crichton, R. (2009). Iron Metabolism-From Molecular Mechanisms to Clinical Consequences, Wiley and Sons, Ltd.","DOI":"10.1002\/9780470010303"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1146\/annurev.nutr.24.012003.132212","article-title":"Iron, ferritin, and nutrition","volume":"24","author":"Theil","year":"2004","journal-title":"Annu. Rev. Nutr."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1042\/bj1260151","article-title":"The formation of ferritin from apoferritin. Kinetics and mechanism of iron uptake","volume":"126","author":"Macara","year":"1972","journal-title":"Biochem. J."},{"key":"ref_19","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_20","doi-asserted-by":"crossref","first-page":"e10308","DOI":"10.7554\/eLife.10308","article-title":"Ferritinophagy via NCOA4 is required for erythropoiesis and is regulated by iron dependent HERC2-mediated proteolysis","volume":"4","author":"Mancias","year":"2015","journal-title":"Elife"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"17791","DOI":"10.1074\/jbc.M113.460253","article-title":"Each member of the poly-r(C)-binding protein 1 (PCBP) family exhibits iron chaperone activity toward ferritin","volume":"288","author":"Leidgens","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"1207","DOI":"10.1126\/science.1157643","article-title":"A cytosolic iron chaperone that delivers iron to ferritin","volume":"320","author":"Shi","year":"2008","journal-title":"Science"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"12764","DOI":"10.1074\/jbc.R117.791962","article-title":"Cytosolic iron chaperones: Proteins delivering iron cofactors in the cytosol of mammalian cells","volume":"292","author":"Philpott","year":"2017","journal-title":"J. Biol. Chem."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1146\/annurev.biochem.74.082803.133518","article-title":"Structure, function, and formation of biological iron-sulfur clusters","volume":"74","author":"Johnson","year":"2005","journal-title":"Annu. Rev. Biochem."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.freeradbiomed.2018.09.022","article-title":"Iron and redox cycling. Do\u2019s and don\u2019ts","volume":"133","author":"Koppenol","year":"2019","journal-title":"Free. Radic. Biol. Med."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"100860","DOI":"10.1016\/j.mam.2020.100860","article-title":"Iron: The cancer connection","volume":"75","author":"Torti","year":"2020","journal-title":"Mol. Asp. Med."},{"key":"ref_27","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_28","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1002\/(SICI)1098-1136(19990115)25:2<131::AID-GLIA4>3.0.CO;2-6","article-title":"Coordinate regulation of NAD(P)H:quinone oxidoreductase and glutathione-S-transferases in primary cultures of rat neurons and glia: Role of the antioxidant\/electrophile responsive element","volume":"25","author":"Reising","year":"1999","journal-title":"Glia"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1007\/s00018-011-0807-2","article-title":"Reactive oxygen species and the neuronal fate","volume":"69","author":"Kennedy","year":"2012","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"444","DOI":"10.1016\/j.pneurobio.2011.01.007","article-title":"Modulation of neuronal stem cell differentiation by hypoxia and reactive oxygen species","volume":"93","author":"Vieira","year":"2011","journal-title":"Prog. Neurobiol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/j.semcdb.2017.09.012","article-title":"From birth to death: A role for reactive oxygen species in neuronal development","volume":"80","author":"Wilson","year":"2018","journal-title":"Semin. Cell Dev. Biol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1002\/jnr.20280","article-title":"Peroxide detoxification by brain cells","volume":"79","author":"Dringen","year":"2005","journal-title":"J. Neurosci. Res."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1002\/jnr.10308","article-title":"Glutathione release from cultured brain cells: Multidrug resistance protein 1 mediates the release of GSH from rat astroglial cells","volume":"69","author":"Hirrlinger","year":"2002","journal-title":"J. Neurosci. Res."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1002\/hep.28251","article-title":"Activation of the p62-Keap1-NRF2 pathway protects against ferroptosis in hepatocellular carcinoma cells","volume":"63","author":"Sun","year":"2016","journal-title":"Hepatology"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"204","DOI":"10.1111\/imm.12922","article-title":"Inflammation in CNS neurodegenerative diseases","volume":"154","author":"Stephenson","year":"2018","journal-title":"Immunology"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1038\/nrd1279","article-title":"The IKK NF-kappa B system: A treasure trove for drug development","volume":"3","author":"Karin","year":"2004","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1016\/j.phrs.2012.07.004","article-title":"p62\/SQSTM1\/A170: Physiology and pathology","volume":"66","author":"Komatsu","year":"2012","journal-title":"Pharmacol. Res."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"S369","DOI":"10.3233\/JAD-2010-100543","article-title":"Mitochondria and the link between neuroinflammation and neurodegeneration","volume":"20","author":"Chiasserini","year":"2010","journal-title":"J. Alzheimers Dis."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/0014-5793(96)00347-X","article-title":"Effects of peroxynitrite-induced protein modifications on tyrosine phosphorylation and degradation","volume":"385","author":"Gow","year":"1996","journal-title":"FEBS Lett."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"746","DOI":"10.1016\/j.freeradbiomed.2004.11.005","article-title":"Alzheimer-specific epitopes of tau represent lipid peroxidation-induced conformations","volume":"38","author":"Liu","year":"2005","journal-title":"Free Radic. Biol. Med."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"770","DOI":"10.1089\/ars.2011.4429","article-title":"Lipid peroxidation product 4-hydroxy-2-nonenal promotes seeding-capable oligomer formation and cell-to-cell transfer of alpha-synuclein","volume":"18","author":"Bae","year":"2013","journal-title":"Antioxid. Redox Signal."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"232","DOI":"10.1039\/C4MT00164H","article-title":"Iron regulatory proteins and their role in controlling iron metabolism","volume":"7","author":"Kuhn","year":"2015","journal-title":"Metallomics"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1016\/S1097-2765(00)80282-8","article-title":"IRP-1 binding to ferritin mRNA prevents the recruitment of the small ribosomal subunit by the cap-binding complex eIF4F","volume":"2","author":"Muckenthaler","year":"1998","journal-title":"Mol. Cell"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"102276","DOI":"10.1016\/j.redox.2022.102276","article-title":"Poly(rC)-binding protein 1 represses ferritinophagy-mediated ferroptosis in head and neck cancer","volume":"51","author":"Lee","year":"2022","journal-title":"Redox Biol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"783","DOI":"10.1182\/blood-2003-03-0672","article-title":"Hepcidin, a key regulator of iron metabolism and mediator of anemia of inflammation","volume":"102","author":"Ganz","year":"2003","journal-title":"Blood"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1006\/bcmd.2002.0573","article-title":"Hepcidin, a new iron regulatory peptide","volume":"29","author":"Nicolas","year":"2002","journal-title":"Blood Cells Mol. Dis."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"2090","DOI":"10.1126\/science.1104742","article-title":"Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization","volume":"306","author":"Nemeth","year":"2004","journal-title":"Science"},{"key":"ref_48","doi-asserted-by":"crossref","unstructured":"Hawula, Z.J., Wallace, D.F., Subramaniam, V.N., and Rishi, G. (2019). Therapeutic Advances in Regulating the Hepcidin\/Ferroportin Axis. Pharmaceuticals, 12.","DOI":"10.3390\/ph12040170"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1053\/j.seminhematol.2009.06.001","article-title":"Iron sequestration and anemia of inflammation","volume":"46","author":"Ganz","year":"2009","journal-title":"Semin. Hematol."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"1271","DOI":"10.1172\/JCI200420945","article-title":"IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin","volume":"113","author":"Nemeth","year":"2004","journal-title":"J. Clin. Investig."},{"key":"ref_51","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 Gen. Subj."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"957","DOI":"10.1080\/1744666X.2021.1953981","article-title":"Pathological mechanisms of abnormal iron metabolism and mitochondrial dysfunction in systemic lupus erythematosus","volume":"17","author":"Wincup","year":"2021","journal-title":"Expert Rev. Clin. Immunol."},{"key":"ref_53","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_54","doi-asserted-by":"crossref","first-page":"129685","DOI":"10.1016\/j.bbagen.2020.129685","article-title":"The new role of poly (rC)-binding proteins as iron transport chaperones: Proteins that could couple with inter-organelle interactions to safely traffic iron","volume":"1864","author":"Yanatori","year":"2020","journal-title":"Biochim. Biophys. Acta Gen. Subj."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1016\/j.freeradbiomed.2018.10.411","article-title":"The ins and outs of iron: Escorting iron through the mammalian cytosol","volume":"133","author":"Philpott","year":"2019","journal-title":"Free Radic. Biol. Med."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"e2104666118","DOI":"10.1073\/pnas.2104666118","article-title":"The iron chaperone and nucleic acid-binding activities of poly(rC)-binding protein 1 are separable and independently essential","volume":"118","author":"Patel","year":"2021","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"7775","DOI":"10.7150\/thno.46903","article-title":"Inhibition of Glutaredoxin 5 predisposes Cisplatin-resistant Head and Neck Cancer Cells to Ferroptosis","volume":"10","author":"Lee","year":"2020","journal-title":"Theranostics"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"838","DOI":"10.1016\/j.bbrc.2016.08.034","article-title":"CISD1 inhibits ferroptosis by protection against mitochondrial lipid peroxidation","volume":"478","author":"Yuan","year":"2016","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1016\/j.canlet.2018.06.018","article-title":"CISD2 inhibition overcomes resistance to sulfasalazine-induced ferroptotic cell death in head and neck cancer","volume":"432","author":"Kim","year":"2018","journal-title":"Cancer Lett."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1128\/MCB.00936-15","article-title":"The Poly(C) Binding Protein Pcbp2 and Its Retrotransposed Derivative Pcbp1 Are Independently Essential to Mouse Development","volume":"36","author":"Ghanem","year":"2016","journal-title":"Mol. Cell. Biol."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"969","DOI":"10.1016\/0378-4274(95)03532-X","article-title":"Toxicity of iron and hydrogen peroxide: The Fenton reaction","volume":"82","author":"Winterbourn","year":"1995","journal-title":"Toxicol. Lett."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"910","DOI":"10.1002\/ejhf.1154","article-title":"Iron deficiency impairs contractility of human cardiomyocytes through decreased mitochondrial function","volume":"20","author":"Hoes","year":"2018","journal-title":"Eur. J. Heart Fail."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"1614","DOI":"10.1016\/j.celrep.2017.05.009","article-title":"Regnase-1 Maintains Iron Homeostasis via the Degradation of Transferrin Receptor 1 and Prolyl-Hydroxylase-Domain-Containing Protein 3 mRNAs","volume":"19","author":"Yoshinaga","year":"2017","journal-title":"Cell Rep."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"2171","DOI":"10.1073\/pnas.85.7.2171","article-title":"Cytoplasmic protein binds in vitro to a highly conserved sequence in the 5\u2019 untranslated region of ferritin heavy- and light-subunit mRNAs","volume":"85","author":"Leibold","year":"1988","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"22220","DOI":"10.1074\/jbc.M001478200","article-title":"Human NRAMP2\/DMT1, which mediates iron transport across endosomal membranes, is localized to late endosomes and lysosomes in HEp-2 cells","volume":"275","author":"Tabuchi","year":"2000","journal-title":"J. Biol. Chem."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1006\/bcmd.1998.0186","article-title":"The human Nramp2 gene: Characterization of the gene structure, alternative splicing, promoter region and polymorphisms","volume":"24","author":"Lee","year":"1998","journal-title":"Blood Cells Mol. Dis."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"821","DOI":"10.1083\/jcb.130.4.821","article-title":"Transport from late endosomes to lysosomes, but not sorting of integral membrane proteins in endosomes, depends on the vacuolar proton pump","volume":"130","author":"Dunn","year":"1995","journal-title":"J. Cell Biol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"1264","DOI":"10.1038\/ng1658","article-title":"Identification of a ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells","volume":"37","author":"Ohgami","year":"2005","journal-title":"Nat. Genet."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"18578","DOI":"10.1073\/pnas.0804373105","article-title":"Divalent metal transporter 1 (DMT1) contributes to neurodegeneration in animal models of Parkinson\u2019s disease","volume":"105","author":"Salazar","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"L24","DOI":"10.1152\/ajplung.00428.2003","article-title":"TNF, IFN-gamma, and endotoxin increase expression of DMT1 in bronchial epithelial cells","volume":"289","author":"Wang","year":"2005","journal-title":"Am. J. Physiol. Lung Cell. Mol. Physiol."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1111\/j.1749-6632.2003.tb07478.x","article-title":"The role of glial reaction and inflammation in Parkinson\u2019s disease","volume":"991","author":"Hirsch","year":"2003","journal-title":"Ann. N.Y. Acad. Sci."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"2247","DOI":"10.1523\/JNEUROSCI.21-07-02247.2001","article-title":"Caspase-8 is an effector in apoptotic death of dopaminergic neurons in Parkinson\u2019s disease, but pathway inhibition results in neuronal necrosis","volume":"21","author":"Hartmann","year":"2001","journal-title":"J. Neurosci."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1097\/00005072-199603000-00001","article-title":"Neuropathology of Parkinson\u2019s disease","volume":"55","author":"Forno","year":"1996","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1186\/s13024-017-0218-4","article-title":"Iron regulatory protein (IRP)-iron responsive element (IRE) signaling pathway in human neurodegenerative diseases","volume":"12","author":"Zhou","year":"2017","journal-title":"Mol. Neurodegener."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1146\/annurev.nutr.28.061807.155521","article-title":"Systemic iron homeostasis and the iron-responsive element\/iron-regulatory protein (IRE\/IRP) regulatory network","volume":"28","author":"Muckenthaler","year":"2008","journal-title":"Annu. Rev. Nutr."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"722","DOI":"10.1126\/science.1176326","article-title":"An E3 ligase possessing an iron-responsive hemerythrin domain is a regulator of iron homeostasis","volume":"326","author":"Salahudeen","year":"2009","journal-title":"Science"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"34365","DOI":"10.1074\/jbc.M700254200","article-title":"Bach1 repression of ferritin and thioredoxin reductase1 is heme-sensitive in cells and in vitro and coordinates expression with heme oxygenase1, beta-globin, and NADP(H) quinone (oxido) reductase1","volume":"282","author":"Hintze","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"46LT02","DOI":"10.1088\/0957-4484\/27\/46\/46LT02","article-title":"Morphology of the ferritin iron core by aberration corrected scanning transmission electron microscopy","volume":"27","author":"Jian","year":"2016","journal-title":"Nanotechnology"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"3900","DOI":"10.1021\/acs.biochem.7b00024","article-title":"Iron Oxidation and Core Formation in Recombinant Heteropolymeric Human Ferritins","volume":"56","author":"Mehlenbacher","year":"2017","journal-title":"Biochemistry"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"17801","DOI":"10.1021\/ja8054035","article-title":"Facilitated diffusion of iron(II) and dioxygen substrates into human H-chain ferritin. A fluorescence and absorbance study employing the ferroxidase center substitution Y34W","volume":"130","author":"Zhao","year":"2008","journal-title":"J. Am. Chem. Soc."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"1137","DOI":"10.1038\/s41589-019-0408-1","article-title":"The chemical basis of ferroptosis","volume":"15","author":"Conrad","year":"2019","journal-title":"Nat. Chem. Biol."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"100864","DOI":"10.1016\/j.mam.2020.100864","article-title":"Iron in infection and immunity","volume":"75","author":"Nairz","year":"2020","journal-title":"Mol. Aspects Med."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1182\/blood-2018-06-856500","article-title":"Anemia of inflammation","volume":"133","author":"Weiss","year":"2019","journal-title":"Blood"},{"key":"ref_84","doi-asserted-by":"crossref","unstructured":"Rosario, C., Zandman-Goddard, G., Meyron-Holtz, E.G., D\u2019Cruz, D.P., and Shoenfeld, Y. (2013). The hyperferritinemic syndrome: Macrophage activation syndrome, Still\u2019s disease, septic shock and catastrophic antiphospholipid syndrome. BMC Med., 11.","DOI":"10.1186\/1741-7015-11-185"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"296","DOI":"10.1002\/hep.1840080218","article-title":"Interactions between isolated hepatocytes and Kupffer cells in iron metabolism: A possible role for ferritin as an iron carrier protein","volume":"8","author":"Sibille","year":"1988","journal-title":"Hepatology"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"1211","DOI":"10.1002\/jcb.21499","article-title":"Macrophages function as a ferritin iron source for cultured human erythroid precursors","volume":"103","author":"Leimberg","year":"2008","journal-title":"J. Cell. Biochem."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"3505","DOI":"10.1073\/pnas.0913192107","article-title":"Binding and uptake of H-ferritin are mediated by human transferrin receptor-1","volume":"107","author":"Li","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"570","DOI":"10.1073\/pnas.0812010106","article-title":"Regulatory effects of ferritin on angiogenesis","volume":"106","author":"Coffman","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"760","DOI":"10.1016\/j.bbagen.2010.03.011","article-title":"Serum ferritin: Past, present and future","volume":"1800","author":"Wang","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"887","DOI":"10.1002\/hep.22716","article-title":"Ferritin functions as a proinflammatory cytokine via iron-independent protein kinase C zeta\/nuclear factor kappaB-regulated signaling in rat hepatic stellate cells","volume":"49","author":"Ruddell","year":"2009","journal-title":"Hepatology"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1111\/j.1365-2141.1979.tb01142.x","article-title":"Suppressive effect of ferritin on in vitro lymphocyte function","volume":"42","author":"Matzner","year":"1979","journal-title":"Br. J. Haematol."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1182\/blood.V73.1.74.74","article-title":"Suppressive effects in vivo of purified recombinant human H-subunit (acidic) ferritin on murine myelopoiesis","volume":"73","author":"Broxmeyer","year":"1989","journal-title":"Blood"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"37616","DOI":"10.1074\/jbc.M607266200","article-title":"Chemokine CXCL12 induces binding of ferritin heavy chain to the chemokine receptor CXCR4, alters CXCR4 signaling, and induces phosphorylation and nuclear translocation of ferritin heavy chain","volume":"281","author":"Li","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"3061","DOI":"10.1038\/s41598-020-59898-0","article-title":"H-Ferritin is essential for macrophages\u2019 capacity to store or detoxify exogenously added iron","volume":"10","author":"Mesquita","year":"2020","journal-title":"Sci. Rep."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1016\/j.jaut.2007.11.003","article-title":"New functions for an iron storage protein: The role of ferritin in immunity and autoimmunity","volume":"30","author":"Recalcati","year":"2008","journal-title":"J. Autoimmun."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1016\/j.autrev.2007.01.016","article-title":"Ferritin in autoimmune diseases","volume":"6","author":"Shoenfeld","year":"2007","journal-title":"Autoimmun. Rev."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.bcmd.2005.04.005","article-title":"Functional consequences of ferroportin 1 mutations","volume":"35","author":"Liu","year":"2005","journal-title":"Blood Cells Mol. Dis."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1016\/j.cmet.2005.01.003","article-title":"The iron exporter ferroportin\/Slc40a1 is essential for iron homeostasis","volume":"1","author":"Donovan","year":"2005","journal-title":"Cell Metab."},{"key":"ref_99","doi-asserted-by":"crossref","unstructured":"Ma, S., Dielschneider, R.F., Henson, E.S., Xiao, W., Choquette, T.R., Blankstein, A.R., Chen, Y., and Gibson, S.B. (2017). Ferroptosis and autophagy induced cell death occur independently after siramesine and lapatinib treatment in breast cancer cells. PLoS ONE, 12.","DOI":"10.1371\/journal.pone.0182921"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1016\/j.tibs.2015.11.012","article-title":"Regulators of Iron Homeostasis: New Players in Metabolism, Cell Death, and Disease","volume":"41","author":"Bogdan","year":"2016","journal-title":"Trends Biochem. Sci."},{"key":"ref_101","doi-asserted-by":"crossref","unstructured":"Abe, N., Nishihara, T., Yorozuya, T., and Tanaka, J. (2020). Microglia and Macrophages in the Pathological Central and Peripheral Nervous Systems. Cells, 9.","DOI":"10.3390\/cells9092132"},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"1045","DOI":"10.1016\/S1474-4422(14)70117-6","article-title":"The role of iron in brain ageing and neurodegenerative disorders","volume":"13","author":"Ward","year":"2014","journal-title":"Lancet. Neurol."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"360438","DOI":"10.1155\/2014\/360438","article-title":"Lipid peroxidation: Production, metabolism, and signaling mechanisms of malondialdehyde and 4-hydroxy-2-nonenal","volume":"2014","author":"Ayala","year":"2014","journal-title":"Oxid. Med. Cell. Longev."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1097\/01.pai.0000213130.63417.b3","article-title":"COX-2 expression in invasive breast cancer: Correlation with prognostic parameters and outcome","volume":"15","author":"Nassar","year":"2007","journal-title":"Appl. Immunohistochem. Mol. Morphol."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"28097","DOI":"10.1074\/jbc.M115.680090","article-title":"Ablation of the Ferroptosis Inhibitor Glutathione Peroxidase 4 in Neurons Results in Rapid Motor Neuron Degeneration and Paralysis","volume":"290","author":"Chen","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1038\/s41593-022-01221-3","article-title":"Microglia ferroptosis is regulated by SEC24B and contributes to neurodegeneration","volume":"26","author":"Ryan","year":"2023","journal-title":"Nat. Neurosci."},{"key":"ref_107","doi-asserted-by":"crossref","unstructured":"Martin, M., Sun, M., Motolani, A., and Lu, T. (2021). The Pivotal Player: Components of NF-kappaB Pathway as Promising Biomarkers in Colorectal Cancer. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22147429"},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1038\/cr.2010.177","article-title":"Non-canonical NF-kappaB signaling pathway","volume":"21","author":"Sun","year":"2011","journal-title":"Cell Res."},{"key":"ref_109","doi-asserted-by":"crossref","unstructured":"Chiarini, A., Armato, U., Hu, P., and Dal Pra, I. (2020). Danger-Sensing\/Patten Recognition Receptors and Neuroinflammation in Alzheimer\u2019s Disease. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21239036"},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1016\/j.jneuroim.2018.11.010","article-title":"Inhibitors of NF-kappaB and P2X7\/NLRP3\/Caspase 1 pathway in microglia: Novel therapeutic opportunities in neuroinflammation induced early-stage Alzheimer\u2019s disease","volume":"326","author":"Thawkar","year":"2019","journal-title":"J. Neuroimmunol."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1172\/JCI11916","article-title":"NF-kappaB in neuronal plasticity and neurodegenerative disorders","volume":"107","author":"Mattson","year":"2001","journal-title":"J. Clin. Investig."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"1208","DOI":"10.1016\/j.bbadis.2013.12.011","article-title":"Oxidative damage and the Nrf2-ARE pathway in neurodegenerative diseases","volume":"1842","author":"Gan","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"428","DOI":"10.1016\/j.freeradbiomed.2010.11.027","article-title":"The lipid peroxidation products 4-oxo-2-nonenal and 4-hydroxy-2-nonenal promote the formation of alpha-synuclein oligomers with distinct biochemical, morphological, and functional properties","volume":"50","author":"Nasstrom","year":"2011","journal-title":"Free Radic. Biol. Med."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1016\/j.cell.2004.10.017","article-title":"Ferritin heavy chain upregulation by NF-kappaB inhibits TNFalpha-induced apoptosis by suppressing reactive oxygen species","volume":"119","author":"Pham","year":"2004","journal-title":"Cell"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1042\/CS20120190","article-title":"Sirtuins and renal diseases: Relationship with aging and diabetic nephropathy","volume":"124","author":"Kitada","year":"2013","journal-title":"Clin. Sci. (Lond.)"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/BJ20070140","article-title":"Sirtuins in mammals: Insights into their biological function","volume":"404","author":"Michan","year":"2007","journal-title":"Biochem. J."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1038\/nature08197","article-title":"Recent progress in the biology and physiology of sirtuins","volume":"460","author":"Finkel","year":"2009","journal-title":"Nature"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1186\/s13148-016-0224-3","article-title":"Sirtuin functions and modulation: From chemistry to the clinic","volume":"8","author":"Carafa","year":"2016","journal-title":"Clin. Epigenetics"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1016\/j.cytogfr.2017.11.001","article-title":"Nuclear sirtuins and inflammatory signaling pathways","volume":"38","author":"Mendes","year":"2017","journal-title":"Cytokine Growth Factor Rev."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"101697","DOI":"10.1016\/j.redox.2020.101697","article-title":"Epigenetic reprogramming of epithelial-mesenchymal transition promotes ferroptosis of head and neck cancer","volume":"37","author":"Lee","year":"2020","journal-title":"Redox Biol."},{"key":"ref_121","doi-asserted-by":"crossref","unstructured":"Hao, C., Zhu, P.X., Yang, X., Han, Z.P., Jiang, J.H., Zong, C., Zhang, X.G., Liu, W.T., Zhao, Q.D., and Fan, T.T. (2014). Overexpression of SIRT1 promotes metastasis through epithelial-mesenchymal transition in hepatocellular carcinoma. BMC Cancer, 14.","DOI":"10.1186\/1471-2407-14-978"},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"4619","DOI":"10.1038\/onc.2011.612","article-title":"SIRT1 induces EMT by cooperating with EMT transcription factors and enhances prostate cancer cell migration and metastasis","volume":"31","author":"Byles","year":"2012","journal-title":"Oncogene"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"689","DOI":"10.15252\/embr.201439792","article-title":"MPP8 and SIRT1 crosstalk in E-cadherin gene silencing and epithelial-mesenchymal transition","volume":"16","author":"Sun","year":"2015","journal-title":"EMBO Rep."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"172847","DOI":"10.1016\/j.ejphar.2019.172847","article-title":"Review of the anti-inflammatory effect of SIRT1 and SIRT2 modulators on neurodegenerative diseases","volume":"867","author":"Zhang","year":"2020","journal-title":"Eur. J. Pharmacol."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"494","DOI":"10.1016\/j.tips.2012.05.007","article-title":"The neurobiology of sirtuins and their role in neurodegeneration","volume":"33","author":"Donmez","year":"2012","journal-title":"Trends Pharmacol. Sci."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"1939","DOI":"10.1016\/j.cellsig.2013.06.007","article-title":"Antagonistic crosstalk between NF-kappaB and SIRT1 in the regulation of inflammation and metabolic disorders","volume":"25","author":"Kauppinen","year":"2013","journal-title":"Cell. Signal."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1016\/j.biocel.2018.07.007","article-title":"Resveratrol alleviates ethanol-induced neuroinflammation in vivo and in vitro: Involvement of TLR2-MyD88-NF-kappaB pathway","volume":"103","author":"Qi","year":"2018","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"358","DOI":"10.1038\/nrn3880","article-title":"Immune attack: The role of inflammation in Alzheimer disease","volume":"16","author":"Heppner","year":"2015","journal-title":"Nat. Rev. Neurosci."},{"key":"ref_129","first-page":"7535472","article-title":"Nonpharmacological Modulation of Chronic Inflammation in Parkinson\u2019s Disease: Role of Diet Interventions","volume":"2019","author":"Kalampokini","year":"2019","journal-title":"Parkinsons Dis."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1016\/j.neuroscience.2015.10.006","article-title":"Resveratrol decreases the insoluble Abeta1-42 level in hippocampus and protects the integrity of the blood-brain barrier in AD rats","volume":"310","author":"Zhao","year":"2015","journal-title":"Neuroscience"},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1007\/s11011-018-0348-6","article-title":"Intracerebroventricular injection of resveratrol ameliorated Abeta-induced learning and cognitive decline in mice","volume":"34","author":"Qi","year":"2019","journal-title":"Metab. Brain Dis."},{"key":"ref_132","doi-asserted-by":"crossref","unstructured":"Feng, X., Liang, N., Zhu, D., Gao, Q., Peng, L., Dong, H., Yue, Q., Liu, H., Bao, L., and Zhang, J. (2013). Resveratrol inhibits beta-amyloid-induced neuronal apoptosis through regulation of SIRT1-ROCK1 signaling pathway. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0059888"},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"2429","DOI":"10.3892\/mmr.2014.3034","article-title":"Resveratrol inhibits beta-amyloid-induced neuronal apoptosis via regulation of p53 acetylation in PC12 cells","volume":"11","author":"Ai","year":"2015","journal-title":"Mol. Med. Rep."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"258","DOI":"10.1002\/biof.1149","article-title":"Neuroprotective effects of resveratrol on damages of mouse cortical neurons induced by beta-amyloid through activation of SIRT1\/Akt1 pathway","volume":"40","author":"Zhang","year":"2014","journal-title":"Biofactors"},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"2005","DOI":"10.4103\/1673-5374.239449","article-title":"SIRT1 facilitates amyloid beta peptide degradation by upregulating lysosome number in primary astrocytes","volume":"13","author":"Li","year":"2018","journal-title":"Neural. Regen. Res."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"5604","DOI":"10.1007\/s12035-016-0087-9","article-title":"SIRT1 Overexpression in Mouse Hippocampus Induces Cognitive Enhancement Through Proteostatic and Neurotrophic Mechanisms","volume":"54","author":"Corpas","year":"2017","journal-title":"Mol. Neurobiol."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"668","DOI":"10.1111\/jnc.13172","article-title":"Rotenone affects p53 transcriptional activity and apoptosis via targeting SIRT1 and H3K9 acetylation in SH-SY5Y cells","volume":"134","author":"Feng","year":"2015","journal-title":"J. Neurochem."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1159\/000328516","article-title":"Resveratrol-activated AMPK\/SIRT1\/autophagy in cellular models of Parkinson\u2019s disease","volume":"19","author":"Wu","year":"2011","journal-title":"Neurosignals"},{"key":"ref_139","doi-asserted-by":"crossref","unstructured":"Singh, P., Hanson, P.S., and Morris, C.M. (2017). SIRT1 ameliorates oxidative stress induced neural cell death and is down-regulated in Parkinson\u2019s disease. BMC Neurosci., 18.","DOI":"10.1186\/s12868-017-0364-1"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"2161","DOI":"10.1002\/mnfr.201600111","article-title":"Resveratrol alleviates MPTP-induced motor impairments and pathological changes by autophagic degradation of alpha-synuclein via SIRT1-deacetylated LC3","volume":"60","author":"Guo","year":"2016","journal-title":"Mol. Nutr. Food Res."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"8177","DOI":"10.1038\/s41598-021-87759-x","article-title":"SIRT1 promotes lipid metabolism and mitochondrial biogenesis in adipocytes and coordinates adipogenesis by targeting key enzymatic pathways","volume":"11","author":"Majeed","year":"2021","journal-title":"Sci. Rep."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1111\/imr.12297","article-title":"The inflammasome: Firing up innate immunity","volume":"265","author":"Kanneganti","year":"2015","journal-title":"Immunol. Rev."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"792","DOI":"10.1016\/j.cell.2016.03.046","article-title":"Inflammasome Complexes: Emerging Mechanisms and Effector Functions","volume":"165","author":"Rathinam","year":"2016","journal-title":"Cell"},{"key":"ref_144","first-page":"41","article-title":"Inflammasomes in CNS Diseases","volume":"108","author":"Albornoz","year":"2018","journal-title":"Exp. Suppl."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1186\/s12974-019-1670-6","article-title":"Systemic activation of NLRP3 inflammasome and plasma alpha-synuclein levels are correlated with motor severity and progression in Parkinson\u2019s disease","volume":"17","author":"Fan","year":"2020","journal-title":"J. Neuroinflammation"},{"key":"ref_146","first-page":"342ra378","article-title":"alpha-Synuclein binds to TOM20 and inhibits mitochondrial protein import in Parkinson\u2019s disease","volume":"8","author":"Barrett","year":"2016","journal-title":"Sci. Transl. Med."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"600","DOI":"10.1016\/j.redox.2017.11.010","article-title":"Integrin CD11b mediates alpha-synuclein-induced activation of NADPH oxidase through a Rho-dependent pathway","volume":"14","author":"Hou","year":"2018","journal-title":"Redox Biol."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1042\/BJ20150617","article-title":"Amyloid fibrils are the molecular trigger of inflammation in Parkinson\u2019s disease","volume":"471","author":"Gustot","year":"2015","journal-title":"Biochem. J."},{"key":"ref_149","doi-asserted-by":"crossref","unstructured":"Codolo, G., Plotegher, N., Pozzobon, T., Brucale, M., Tessari, I., Bubacco, L., and de Bernard, M. (2013). Triggering of inflammasome by aggregated alpha-synuclein, an inflammatory response in synucleinopathies. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0055375"},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/j.expneurol.2017.11.010","article-title":"Peripheral monocyte entry is required for alpha-Synuclein induced inflammation and Neurodegeneration in a model of Parkinson disease","volume":"300","author":"Harms","year":"2018","journal-title":"Exp. Neurol."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"896","DOI":"10.1016\/j.cell.2015.12.057","article-title":"NF-kappaB Restricts Inflammasome Activation via Elimination of Damaged Mitochondria","volume":"164","author":"Zhong","year":"2016","journal-title":"Cell"},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1016\/j.bcp.2017.12.021","article-title":"The P2X7 receptor: A main player in inflammation","volume":"151","author":"Adinolfi","year":"2018","journal-title":"Biochem. Pharmacol."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1111\/j.1399-0039.2011.01780.x","article-title":"The human P2X7 receptor and its role in innate immunity","volume":"78","author":"Wiley","year":"2011","journal-title":"Tissue Antigens"},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"340","DOI":"10.1016\/j.tips.2013.04.005","article-title":"Toward clinical application of the Keap1-Nrf2 pathway","volume":"34","author":"Suzuki","year":"2013","journal-title":"Trends Pharmacol. Sci."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1016\/j.neuropharm.2013.11.004","article-title":"NRF2-regulation in brain health and disease: Implication of cerebral inflammation","volume":"79","author":"Sandberg","year":"2014","journal-title":"Neuropharmacology"},{"key":"ref_156","doi-asserted-by":"crossref","unstructured":"Sajja, R.K., Green, K.N., and Cucullo, L. (2015). Altered Nrf2 signaling mediates hypoglycemia-induced blood-brain barrier endothelial dysfunction in vitro. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0122358"},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/j.freeradbiomed.2015.04.036","article-title":"The emerging role of Nrf2 in mitochondrial function","volume":"88","author":"Abramov","year":"2015","journal-title":"Free Radic. Biol. Med."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1101\/gad.13.1.76","article-title":"Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain","volume":"13","author":"Itoh","year":"1999","journal-title":"Genes. Dev."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"7130","DOI":"10.1128\/MCB.24.16.7130-7139.2004","article-title":"Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2","volume":"24","author":"Kobayashi","year":"2004","journal-title":"Mol. Cell. Biol."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/j.biopha.2016.11.118","article-title":"Cigarette smoke and related risk factors in neurological disorders: An update","volume":"85","author":"Choi","year":"2017","journal-title":"Biomed. Pharmacother."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"1201","DOI":"10.1016\/j.jnutbio.2012.03.005","article-title":"The Nrf2-antioxidant response element pathway: A target for regulating energy metabolism","volume":"23","author":"Picklo","year":"2012","journal-title":"J. Nutr. Biochem."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"101059","DOI":"10.1016\/j.redox.2018.11.017","article-title":"NRF2 and NF-\u049bB interplay in cerebrovascular and neurodegenerative disorders: Molecular mechanisms and possible therapeutic approaches","volume":"21","author":"Sivandzade","year":"2019","journal-title":"Redox Biol."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"883","DOI":"10.1016\/j.bbrc.2006.10.102","article-title":"Nrf2-dependent protection from LPS induced inflammatory response and mortality by CDDO-Imidazolide","volume":"351","author":"Thimmulappa","year":"2006","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"680","DOI":"10.4049\/jimmunol.181.1.680","article-title":"The transcription factor Nrf2 is a therapeutic target against brain inflammation","volume":"181","author":"Innamorato","year":"2008","journal-title":"J. Immunol."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1089\/ars.2015.6615","article-title":"Nuclear Factor E2-Related Factor-2 Negatively Regulates NLRP3 Inflammasome Activity by Inhibiting Reactive Oxygen Species-Induced NLRP3 Priming","volume":"26","author":"Liu","year":"2017","journal-title":"Antioxid. Redox Signal."},{"key":"ref_166","first-page":"229","article-title":"Ubiquitin-independent degradation: Lessons from the p53 model","volume":"8","author":"Asher","year":"2006","journal-title":"Isr. Med. Assoc. J."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"17020","DOI":"10.1074\/jbc.M114.563114","article-title":"Nuclear factor E2-related factor-2 (Nrf2) is required for NLRP3 and AIM2 inflammasome activation","volume":"289","author":"Zhao","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/j.molcel.2009.07.025","article-title":"KEAP1 E3 ligase-mediated downregulation of NF-kappaB signaling by targeting IKKbeta","volume":"36","author":"Lee","year":"2009","journal-title":"Mol. Cell"},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"2335","DOI":"10.1089\/ars.2010.3534","article-title":"Basic principles and emerging concepts in the redox control of transcription factors","volume":"15","author":"Flohe","year":"2011","journal-title":"Antioxid. Redox Signal."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1042\/BJ20050795","article-title":"Tumour necrosis factor alpha induces co-ordinated activation of rat GSH synthetic enzymes via nuclear factor kappaB and activator protein-1","volume":"391","author":"Yang","year":"2005","journal-title":"Biochem. J."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1016\/j.bbamcr.2008.01.002","article-title":"NF-kappaB\/p65 antagonizes Nrf2-ARE pathway by depriving CBP from Nrf2 and facilitating recruitment of HDAC3 to MafK","volume":"1783","author":"Liu","year":"2008","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"1583","DOI":"10.1016\/j.jnutbio.2011.10.012","article-title":"Inhibition of NF-kappaB nuclear translocation via HO-1 activation underlies alpha-tocopheryl succinate toxicity","volume":"23","author":"Bellezza","year":"2012","journal-title":"J. Nutr. Biochem."},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1097\/NEN.0b013e3181cb5af4","article-title":"Oxidative stress in the progression of Alzheimer disease in the frontal cortex","volume":"69","author":"Ansari","year":"2010","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1089\/ars.2015.6549","article-title":"Repurposing the NRF2 Activator Dimethyl Fumarate as Therapy Against Synucleinopathy in Parkinson\u2019s Disease","volume":"25","author":"Scannevin","year":"2016","journal-title":"Antioxid. Redox Signal."},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"3173","DOI":"10.1093\/hmg\/dds143","article-title":"alpha-Synuclein expression and Nrf2 deficiency cooperate to aggravate protein aggregation, neuronal death and inflammation in early-stage Parkinson\u2019s disease","volume":"21","author":"Ulusoy","year":"2012","journal-title":"Hum. Mol. Genet."},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"5718","DOI":"10.1093\/nar\/gkq212","article-title":"Global mapping of binding sites for Nrf2 identifies novel targets in cell survival response through ChIP-Seq profiling and network analysis","volume":"38","author":"Malhotra","year":"2010","journal-title":"Nucleic Acids Res."},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"10228","DOI":"10.1093\/nar\/gks827","article-title":"Nrf2-MafG heterodimers contribute globally to antioxidant and metabolic networks","volume":"40","author":"Hirotsu","year":"2012","journal-title":"Nucleic Acids Res."},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"7416","DOI":"10.1093\/nar\/gks409","article-title":"Identification of novel NRF2-regulated genes by ChIP-Seq: Influence on retinoid X receptor alpha","volume":"40","author":"Chorley","year":"2012","journal-title":"Nucleic Acids Res."},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1007\/BF03401947","article-title":"Role of transcription factor Nrf2 in the induction of hepatic phase 2 and antioxidative enzymes in vivo by the cancer chemoprotective agent, 3H-1, 2-dimethiole-3-thione","volume":"7","author":"Kwak","year":"2001","journal-title":"Mol. Med."},{"key":"ref_180","first-page":"5196","article-title":"Identification of Nrf2-regulated genes induced by the chemopreventive agent sulforaphane by oligonucleotide microarray","volume":"62","author":"Thimmulappa","year":"2002","journal-title":"Cancer Res."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"2361","DOI":"10.1074\/jbc.M210664200","article-title":"Nrf2 mediates the induction of ferritin H in response to xenobiotics and cancer chemopreventive dithiolethiones","volume":"278","author":"Pietsch","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"2835","DOI":"10.1093\/emboj\/20.11.2835","article-title":"Heme mediates derepression of Maf recognition element through direct binding to transcription repressor Bach1","volume":"20","author":"Ogawa","year":"2001","journal-title":"EMBO J."},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/j.abb.2011.02.001","article-title":"Nrf2 regulates ferroportin 1-mediated iron efflux and counteracts lipopolysaccharide-induced ferroportin 1 mRNA suppression in macrophages","volume":"508","author":"Harada","year":"2011","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"9722","DOI":"10.1073\/pnas.1221743110","article-title":"Pirin is an iron-dependent redox regulator of NF-kappaB","volume":"110","author":"Liu","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"1491","DOI":"10.1074\/jbc.M310022200","article-title":"Crystal structure of human pirin: An iron-binding nuclear protein and transcription cofactor","volume":"279","author":"Pang","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1007\/s11010-013-1931-0","article-title":"Basal PIR expression in HeLa cells is driven by NRF2 via evolutionary conserved antioxidant response element","volume":"389","author":"Brzoska","year":"2014","journal-title":"Mol. Cell. Biochem."}],"container-title":["Antioxidants"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2076-3921\/12\/4\/918\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T19:14:43Z","timestamp":1760123683000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2076-3921\/12\/4\/918"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,4,12]]},"references-count":186,"journal-issue":{"issue":"4","published-online":{"date-parts":[[2023,4]]}},"alternative-id":["antiox12040918"],"URL":"https:\/\/doi.org\/10.3390\/antiox12040918","relation":{},"ISSN":["2076-3921"],"issn-type":[{"value":"2076-3921","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,4,12]]}}}