{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,25]],"date-time":"2026-10-25T12:35:23Z","timestamp":1792931723052,"version":"4.5.0"},"reference-count":70,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,11,1]],"date-time":"2026-11-01T00:00:00Z","timestamp":1793491200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,11,1]],"date-time":"2026-11-01T00:00:00Z","timestamp":1793491200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T00:00:00Z","timestamp":1790553600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["461705066"],"award-info":[{"award-number":["461705066"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["461705388"],"award-info":[{"award-number":["461705388"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["461705208"],"award-info":[{"award-number":["461705208"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Redox Biology"],"published-print":{"date-parts":[[2026,11]]},"DOI":"10.1016\/j.redox.2026.104418","type":"journal-article","created":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T16:04:55Z","timestamp":1790611495000},"page":"104418","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"special_numbering":"C","title":["The fruitfly Drosophila melanogaster as an in vivo model of ferroptosis"],"prefix":"10.1016","volume":"97","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-6339-6087","authenticated-orcid":false,"given":"Li","family":"Zhang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0004-9499-3468","authenticated-orcid":false,"given":"Felix","family":"Schmidt","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fatih","family":"Yasar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yasminn","family":"Akele","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bernhard","family":"Michalke","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Konstantin","family":"Becksch\u00e4fer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christoph","family":"Thiele","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eva-Maria","family":"Hanschmann","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vivek","family":"Venkataramani","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8774-0057","authenticated-orcid":false,"given":"Axel","family":"Methner","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.redox.2026.104418_bib1","doi-asserted-by":"crossref","first-page":"2401","DOI":"10.1016\/j.cell.2022.06.003","article-title":"Ferroptosis turns 10: emerging mechanisms, physiological functions, and therapeutic applications","volume":"185","author":"Stockwell","year":"2022","journal-title":"Cell"},{"key":"10.1016\/j.redox.2026.104418_bib2","doi-asserted-by":"crossref","DOI":"10.1016\/j.redox.2024.103211","article-title":"Ferroptosis in health and disease","volume":"75","author":"Berndt","year":"2024","journal-title":"Redox Biol."},{"key":"10.1016\/j.redox.2026.104418_bib3","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1016\/j.cmet.2008.07.005","article-title":"Glutathione peroxidase 4 senses and translates oxidative stress into 12\/15-lipoxygenase dependent- and AIF-mediated cell death","volume":"8","author":"Seiler","year":"2008","journal-title":"Cell Metab."},{"key":"10.1016\/j.redox.2026.104418_bib4","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":"10.1016\/j.redox.2026.104418_bib5","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":"10.1016\/j.redox.2026.104418_bib6","doi-asserted-by":"crossref","first-page":"628","DOI":"10.1084\/jem.165.3.628","article-title":"Induction of cystine transport activity in mouse peritoneal macrophages","volume":"165","author":"Watanabe","year":"1987","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.redox.2026.104418_bib7","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":"10.1016\/j.redox.2026.104418_bib8","doi-asserted-by":"crossref","first-page":"864","DOI":"10.1038\/nature05859","article-title":"RAS-RAF-MEK-dependent oxidative cell death involving voltage-dependent anion channels","volume":"447","author":"Yagoda","year":"2007","journal-title":"Nature"},{"key":"10.1016\/j.redox.2026.104418_bib9","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":"10.1016\/j.redox.2026.104418_bib10","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.2006203","article-title":"Unsolved mysteries: how does lipid peroxidation cause ferroptosis?","volume":"16","author":"Feng","year":"2018","journal-title":"PLoS Biol."},{"key":"10.1016\/j.redox.2026.104418_bib11","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":"10.1016\/j.redox.2026.104418_bib12","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":"10.1016\/j.redox.2026.104418_bib13","doi-asserted-by":"crossref","first-page":"4402","DOI":"10.1038\/s41467-021-24712-6","article-title":"Dysfunction of the key ferroptosis-surveilling systems hypersensitizes mice to tubular necrosis during acute kidney injury","volume":"12","author":"Tonnus","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.redox.2026.104418_bib14","doi-asserted-by":"crossref","first-page":"2672","DOI":"10.1073\/pnas.1821022116","article-title":"Ferroptosis as a target for protection against cardiomyopathy","volume":"116","author":"Fang","year":"2019","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.redox.2026.104418_bib15","doi-asserted-by":"crossref","first-page":"2293","DOI":"10.1172\/JCI126428","article-title":"Ferroptotic cell death and TLR4\/Trif signaling initiate neutrophil recruitment after heart transplantation","volume":"129","author":"Li","year":"2019","journal-title":"J. Clin. Investig."},{"key":"10.1016\/j.redox.2026.104418_bib16","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. Psychiatr."},{"key":"10.1016\/j.redox.2026.104418_bib17","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":"10.1016\/j.redox.2026.104418_bib18","doi-asserted-by":"crossref","first-page":"1009","DOI":"10.1038\/s41419-021-04284-5","article-title":"Inhibition of keratinocyte ferroptosis suppresses psoriatic inflammation","volume":"12","author":"Shou","year":"2021","journal-title":"Cell Death Dis."},{"key":"10.1016\/j.redox.2026.104418_bib19","article-title":"Ferroptosis activation contributes to the formation of skin lesions in psoriasis vulgaris","volume":"12","author":"Li","year":"2023","journal-title":"Antioxidants"},{"key":"10.1016\/j.redox.2026.104418_bib20","doi-asserted-by":"crossref","first-page":"913","DOI":"10.1038\/s41423-022-00883-0","article-title":"Ferroptosis promotes T-cell activation-induced neurodegeneration in multiple sclerosis, cell","volume":"19","author":"Luoqian","year":"2022","journal-title":"Mol. Immunol."},{"key":"10.1016\/j.redox.2026.104418_bib21","doi-asserted-by":"crossref","DOI":"10.1038\/s41418-023-01195-0","article-title":"Ferroptosis contributes to multiple sclerosis and its pharmacological targeting suppresses experimental disease progression","author":"Van San","year":"2023","journal-title":"Cell Death Differ."},{"key":"10.1016\/j.redox.2026.104418_bib22","first-page":"1","article-title":"TNF antagonist sensitizes synovial fibroblasts to ferroptotic cell death in collagen-induced arthritis mouse models","volume":"13","author":"Wu","year":"2022","journal-title":"Nat. Commun."},{"key":"10.1016\/j.redox.2026.104418_bib23","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1038\/s41420-023-01446-6","article-title":"Patient-derived zebrafish xenografts of uveal melanoma reveal ferroptosis as a drug target","volume":"9","author":"Groenewoud","year":"2023","journal-title":"Cell Death Discov."},{"key":"10.1016\/j.redox.2026.104418_bib24","doi-asserted-by":"crossref","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":"10.1016\/j.redox.2026.104418_bib25","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1016\/j.devcel.2020.06.019","article-title":"Dietary lipids induce ferroptosis in caenorhabditiselegans and human cancer cells","volume":"54","author":"Perez","year":"2020","journal-title":"Dev. Cell"},{"key":"10.1016\/j.redox.2026.104418_bib26","doi-asserted-by":"crossref","first-page":"308","DOI":"10.3389\/fnagi.2016.00308","article-title":"The protective role of mitochondrial ferritin on erastin-induced ferroptosis","volume":"8","author":"Wang","year":"2016","journal-title":"Front. Aging Neurosci."},{"key":"10.1016\/j.redox.2026.104418_bib27","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pgen.1008396","article-title":"Ferritin heavy chain protects the developing wing from reactive oxygen species and ferroptosis","volume":"15","author":"Mumbauer","year":"2019","journal-title":"PLoS Genet."},{"key":"10.1016\/j.redox.2026.104418_bib28","doi-asserted-by":"crossref","DOI":"10.1016\/j.scitotenv.2022.161183","article-title":"Cadmium chloride exposure impairs the growth and behavior of drosophila via ferroptosis","volume":"865","author":"Hu","year":"2023","journal-title":"Sci. Total Environ."},{"key":"10.1016\/j.redox.2026.104418_bib29","doi-asserted-by":"crossref","first-page":"261","DOI":"10.3390\/antiox12020261","article-title":"\u0391-synuclein toxicity in Drosophila melanogaster is enhanced by the presence of iron: implications for Parkinson's disease","volume":"12","author":"Agostini","year":"2023","journal-title":"Antioxidants"},{"key":"10.1016\/j.redox.2026.104418_bib30","doi-asserted-by":"crossref","DOI":"10.1155\/2023\/7222462","article-title":"Increased iron levels and oxidative stress mediate age-related impairments in male and female Drosophila melanogaster","volume":"2023","author":"Gomes","year":"2023","journal-title":"Oxid. Med. Cell. Longev."},{"key":"10.1016\/j.redox.2026.104418_bib31","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/j.freeradbiomed.2023.12.005","article-title":"Inhibition of ferroptosis underlies EGCG mediated protection against Parkinson's disease in a drosophila model","volume":"211","author":"Xia","year":"2024","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.redox.2026.104418_bib32","doi-asserted-by":"crossref","DOI":"10.1096\/fj.202400119RR","article-title":"Fat body-derived juvenile hormone acid methyltransferase functions to maintain iron homeostasis in Drosophila melanogaster","volume":"38","author":"Ye","year":"2024","journal-title":"FASEB J."},{"key":"10.1016\/j.redox.2026.104418_bib33","doi-asserted-by":"crossref","DOI":"10.1038\/s41556-024-01450-7","article-title":"Ferroptosis-like cell death promotes and prolongs inflammation in drosophila","author":"Davidson","year":"2024","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.redox.2026.104418_bib34","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.35574","article-title":"A gene-specific T2A-GAL4 library for drosophila","volume":"7","author":"Lee","year":"2018","journal-title":"eLife"},{"key":"10.1016\/j.redox.2026.104418_bib35","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.76077","article-title":"An expanded toolkit for Drosophila gene tagging using synthesized homology donor constructs for CRISPR-mediated homologous recombination","volume":"11","author":"Kanca","year":"2022","journal-title":"eLife"},{"key":"10.1016\/j.redox.2026.104418_bib36","article-title":"The evolutionary conserved transmembrane BAX inhibitor motif (TMBIM) containing protein family members 5 and 6 are essential for the development and survival of Drosophila melanogaster","volume":"9","author":"Zhang","year":"2021","journal-title":"Front. Cell Dev. Biol."},{"key":"10.1016\/j.redox.2026.104418_bib37","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.97027","article-title":"Iron-sulfur cluster loss in mitochondrial CISD1 mediates PINK1 loss-of-function phenotypes","volume":"13","author":"Bitar","year":"2024","journal-title":"eLife"},{"key":"10.1016\/j.redox.2026.104418_bib38","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/S0165-6147(02)00004-4","article-title":"Techniques: fruit flies as models for neuropharmacological research","volume":"24","author":"Manev","year":"2003","journal-title":"Trends Pharmacol. Sci."},{"key":"10.1016\/j.redox.2026.104418_bib39","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1006\/meth.2001.1262","article-title":"Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method","volume":"25","author":"Livak","year":"2001","journal-title":"Methods"},{"key":"10.1016\/j.redox.2026.104418_bib40","doi-asserted-by":"crossref","first-page":"1123","DOI":"10.1038\/s41592-019-0593-6","article-title":"Multiplexed and single cell tracing of lipid metabolism","volume":"16","author":"Thiele","year":"2019","journal-title":"Nat. Methods"},{"key":"10.1016\/j.redox.2026.104418_bib41","doi-asserted-by":"crossref","first-page":"R8","DOI":"10.1186\/gb-2011-12-1-r8","article-title":"A novel informatics concept for high-throughput shotgun lipidomics based on the molecular fragmentation query language","volume":"12","author":"Herzog","year":"2011","journal-title":"Genome Biol."},{"key":"10.1016\/j.redox.2026.104418_bib42","doi-asserted-by":"crossref","first-page":"136","DOI":"10.3389\/fchem.2019.00136","article-title":"Iron redox speciation analysis using capillary electrophoresis coupled to inductively coupled plasma mass spectrometry (CE-ICP-MS)","volume":"7","author":"Michalke","year":"2019","journal-title":"Front. Chem."},{"key":"10.1016\/j.redox.2026.104418_bib43","doi-asserted-by":"crossref","DOI":"10.3791\/61055","article-title":"Setup of capillary electrophoresis-inductively coupled plasma mass spectrometry (CE-ICP-MS) for quantification of iron redox species (Fe(II), Fe(III))","author":"Michalke","year":"2020","journal-title":"J. Vis. Exp."},{"key":"10.1016\/j.redox.2026.104418_bib44","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1038\/msb.2011.75","article-title":"Fast, scalable generation of high-quality protein multiple sequence alignments using clustal omega","volume":"7","author":"Sievers","year":"2011","journal-title":"Mol. Syst. Biol."},{"key":"10.1016\/j.redox.2026.104418_bib45","doi-asserted-by":"crossref","first-page":"W232","DOI":"10.1093\/nar\/gkw256","article-title":"W-IQ-TREE: a fast online phylogenetic tool for maximum likelihood analysis","volume":"44","author":"Trifinopoulos","year":"2016","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.redox.2026.104418_bib46","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1093\/biomet\/93.3.491","article-title":"Adaptive linear step-up procedures that control the false discovery rate","volume":"93","author":"Benjamini","year":"2006","journal-title":"Biometrika"},{"key":"10.1016\/j.redox.2026.104418_bib47","doi-asserted-by":"crossref","first-page":"1622","DOI":"10.3390\/nu5051622","article-title":"Iron absorption in Drosophila melanogaster","volume":"5","author":"Mandilaras","year":"2013","journal-title":"Nutrients"},{"key":"10.1016\/j.redox.2026.104418_bib48","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":"10.1016\/j.redox.2026.104418_bib49","doi-asserted-by":"crossref","first-page":"1604","DOI":"10.1021\/acschembio.5b00245","article-title":"Human haploid cell genetics reveals roles for lipid metabolism genes in nonapoptotic cell death","volume":"10","author":"Dixon","year":"2015","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.redox.2026.104418_bib50","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1126\/science.291.5504.643","article-title":"Substitution of the thioredoxin system for glutathione reductase in Drosophila melanogaster","volume":"291","author":"Kanzok","year":"2001","journal-title":"Science"},{"key":"10.1016\/j.redox.2026.104418_bib51","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1515\/BC.2003.052","article-title":"A putative glutathione peroxidase of drosophila encodes a thioredoxin peroxidase that provides resistance against oxidative stress but fails to complement a lack of catalase activity","volume":"384","author":"Missirlis","year":"2003","journal-title":"Biol. Chem."},{"key":"10.1016\/j.redox.2026.104418_bib52","doi-asserted-by":"crossref","first-page":"11521","DOI":"10.1074\/jbc.M111692200","article-title":"Mitochondrial and cytoplasmic thioredoxin reductase variants encoded by a single drosophila gene are both essential for viability","volume":"277","author":"Missirlis","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.redox.2026.104418_bib53","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1042\/BJ20082198","article-title":"Drosophila expresses a CD98 transporter with an evolutionarily conserved structure and amino acid-transport properties","volume":"420","author":"Reynolds","year":"2009","journal-title":"Biochem. J."},{"key":"10.1016\/j.redox.2026.104418_bib54","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1523\/JNEUROSCI.4770-06.2007","article-title":"Nonvesicular release of glutamate by glial xCT transporters suppresses glutamate receptor clustering in vivo","volume":"27","author":"Augustin","year":"2007","journal-title":"J. Neurosci."},{"key":"10.1016\/j.redox.2026.104418_bib55","doi-asserted-by":"crossref","first-page":"1340","DOI":"10.3390\/cells13161340","article-title":"A LAT1-like amino acid transporter regulates neuronal activity in the drosophila mushroom bodies","volume":"13","author":"Delescluse","year":"2024","journal-title":"Cells"},{"key":"10.1016\/j.redox.2026.104418_bib56","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2018.08.067","article-title":"Sobremesa L-type amino acid transporter expressed in glia is essential for proper timing of development and brain growth","volume":"24","author":"Galagovsky","year":"2018","journal-title":"Cell Rep."},{"key":"10.1016\/j.redox.2026.104418_bib57","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":"10.1016\/j.redox.2026.104418_bib58","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":"10.1016\/j.redox.2026.104418_bib59","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1038\/s41586-020-2732-8","article-title":"Plasticity of ether lipids promotes ferroptosis susceptibility and evasion","volume":"585","author":"Zou","year":"2020","journal-title":"Nature"},{"key":"10.1016\/j.redox.2026.104418_bib60","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1038\/nature12962","article-title":"Diversity and dynamics of the Drosophila transcriptome","volume":"512","author":"Brown","year":"2014","journal-title":"Nature"},{"key":"10.1016\/j.redox.2026.104418_bib61","doi-asserted-by":"crossref","first-page":"916","DOI":"10.1111\/j.1471-4159.2006.03921.x","article-title":"Cooperative action of glutamate transporters and cystine\/glutamate antiporter system Xc- protects from oxidative glutamate toxicity","volume":"98","author":"Lewerenz","year":"2006","journal-title":"J. Neurochem."},{"key":"10.1016\/j.redox.2026.104418_bib62","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2022.111610","article-title":"Sex differences in resilience to ferroptosis underlie sexual dimorphism in kidney injury and repair","volume":"41","author":"Ide","year":"2022","journal-title":"Cell Rep."},{"key":"10.1016\/j.redox.2026.104418_bib63","doi-asserted-by":"crossref","first-page":"2748","DOI":"10.1016\/j.cell.2023.05.003","article-title":"Ferroptosis surveillance independent of GPX4 and differentially regulated by sex hormones","volume":"186","author":"Liang","year":"2023","journal-title":"Cell"},{"key":"10.1016\/j.redox.2026.104418_bib64","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1007\/s00726-011-0862-x","article-title":"Regulation of xCT expression and system x (c) (-) function in neuronal cells","volume":"42","author":"Lewerenz","year":"2012","journal-title":"Amino Acids"},{"key":"10.1016\/j.redox.2026.104418_bib65","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1038\/nature13148","article-title":"Quantitative proteomics identifies NCOA4 as the cargo receptor mediating ferritinophagy","volume":"509","author":"Mancias","year":"2014","journal-title":"Nature"},{"key":"10.1016\/j.redox.2026.104418_bib66","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-022-18779-4","article-title":"N-glycosylation is crucial for trafficking and stability of SLC3A2 (CD98)","volume":"12","author":"Console","year":"2022","journal-title":"Sci. Rep."},{"key":"10.1016\/j.redox.2026.104418_bib67","doi-asserted-by":"crossref","first-page":"11920","DOI":"10.1074\/jbc.M112.433847","article-title":"Voltage-dependent anion channels modulate mitochondrial metabolism in cancer cells: regulation by free tubulin and erastin","volume":"288","author":"Maldonado","year":"2013","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.redox.2026.104418_bib68","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1007\/s10571-018-0634-1","article-title":"Inhibition of VDAC1 protects against glutamate-induced oxytosis and mitochondrial fragmentation in hippocampal HT22 cells","volume":"39","author":"Nagakannan","year":"2019","journal-title":"Cell. Mol. Neurobiol."},{"key":"10.1016\/j.redox.2026.104418_bib69","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0154605","article-title":"Erastin disrupts mitochondrial permeability transition pore (mPTP) and induces apoptotic death of colorectal cancer cells","volume":"11","author":"Huo","year":"2016","journal-title":"PLoS One"},{"key":"10.1016\/j.redox.2026.104418_bib70","doi-asserted-by":"crossref","first-page":"204","DOI":"10.1016\/S0005-2736(97)00059-X","article-title":"Cloning and molecular characterization of a voltage-dependent anion-selective channel (VDAC) from Drosophila melanogaster","volume":"1327","author":"Ryerse","year":"1997","journal-title":"Biochim. Biophys. Acta"}],"container-title":["Redox Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2213231726004179?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2213231726004179?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,10,25]],"date-time":"2026-10-25T12:23:51Z","timestamp":1792931031000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S2213231726004179"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,11]]},"references-count":70,"alternative-id":["S2213231726004179"],"URL":"https:\/\/doi.org\/10.1016\/j.redox.2026.104418","relation":{},"ISSN":["2213-2317"],"issn-type":[{"value":"2213-2317","type":"print"}],"subject":[],"published":{"date-parts":[[2026,11]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The fruitfly Drosophila melanogaster as an in vivo model of ferroptosis","name":"articletitle","label":"Article Title"},{"value":"Redox Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.redox.2026.104418","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 The Authors. Published by Elsevier B.V.","name":"copyright","label":"Copyright"}],"article-number":"104418"}}