{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,14]],"date-time":"2026-10-14T17:53:08Z","timestamp":1792000388138,"version":"4.4.0"},"reference-count":33,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2021,2,1]],"date-time":"2021-02-01T00:00:00Z","timestamp":1612137600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,2,1]],"date-time":"2021-02-01T00:00:00Z","timestamp":1612137600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["18K06215"],"award-info":[{"award-number":["18K06215"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100008886","name":"Princess Takamatsu Cancer Research Fund","doi-asserted-by":"publisher","award":["18\\u201325006"],"award-info":[{"award-number":["18\\u201325006"]}],"id":[{"id":"10.13039\/501100008886","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100008886","name":"Princess Takamatsu Cancer Research Fund","doi-asserted-by":"publisher","award":["25006"],"award-info":[{"award-number":["25006"]}],"id":[{"id":"10.13039\/501100008886","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochemical and Biophysical Research Communications"],"published-print":{"date-parts":[[2021,2]]},"DOI":"10.1016\/j.bbrc.2020.12.075","type":"journal-article","created":{"date-parts":[[2021,1,6]],"date-time":"2021-01-06T18:41:37Z","timestamp":1609958497000},"page":"56-63","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":39,"special_numbering":"C","title":["Role of ferritinophagy in cystine deprivation-induced cell death in glioblastoma cells"],"prefix":"10.1016","volume":"539","author":[{"given":"Kazuki","family":"Hayashima","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8778-145X","authenticated-orcid":false,"given":"Ikuo","family":"Kimura","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8191-8117","authenticated-orcid":false,"given":"Hironori","family":"Katoh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbrc.2020.12.075_bib1","doi-asserted-by":"crossref","first-page":"v1","DOI":"10.1093\/neuonc\/nos218","article-title":"CBTRUS statistical report: primary brain and central nervous system tumors diagnosed in the United States in 2005-2009","volume":"14","author":"Dolecek","year":"2012","journal-title":"Neuro Oncol."},{"key":"10.1016\/j.bbrc.2020.12.075_bib2","doi-asserted-by":"crossref","first-page":"218","DOI":"10.3389\/fphar.2018.00218","article-title":"Drug repositioning in glioblastoma: a pathway perspective","volume":"16","author":"Tan","year":"2018","journal-title":"Front. Pharmacol."},{"key":"10.1016\/j.bbrc.2020.12.075_bib3","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.bbrc.2020.12.075_bib4","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1016\/j.cell.2013.12.010","article-title":"Regulation of ferroptotic cancer death by GPX4","volume":"156","author":"Yang","year":"2014","journal-title":"Cell"},{"key":"10.1016\/j.bbrc.2020.12.075_bib5","doi-asserted-by":"crossref","first-page":"522","DOI":"10.1089\/ars.2011.4391","article-title":"The cystine\/glutamate antiporter system xc- in health and disease: from molecular mechanisms to novel therapeutic opportunities","volume":"18","author":"Lewerenz","year":"2013","journal-title":"Antioxidants Redox Signal."},{"key":"10.1016\/j.bbrc.2020.12.075_bib6","article-title":"Cystine transporter SLC7A11\/xCT in cancer: ferroptosis, nutrient dependency, and cancer therapy","author":"Koppula","year":"2020","journal-title":"Protein Cell"},{"key":"10.1016\/j.bbrc.2020.12.075_bib7","first-page":"35","article-title":"The hallmarks of ferroptosis","volume":"3","author":"Dixon","year":"2019","journal-title":"Annu. Rev. Cell Biol."},{"key":"10.1016\/j.bbrc.2020.12.075_bib8","doi-asserted-by":"crossref","first-page":"15074","DOI":"10.1038\/ncomms15074","article-title":"The glutamate\/cystine xCT antiporter antagonaizes glutamine metabolism and reduces nutrient flexibility","volume":"8","author":"Shin","year":"2017","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bbrc.2020.12.075_bib9","doi-asserted-by":"crossref","first-page":"14240","DOI":"10.1074\/jbc.M117.798405","article-title":"The glutamate\/cystine antiporter SLC7A11\/xCT enhances cancer cell dependency on glucose by exporting glutamate","volume":"292","author":"Koppula","year":"2017","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.bbrc.2020.12.075_bib10","doi-asserted-by":"crossref","first-page":"19721","DOI":"10.1074\/jbc.M117.814392","article-title":"Cystine uptake through the cystine\/glutamine antiporter xCT triggers glioblastoma cell death under glucose deprivation","volume":"292","author":"Goji","year":"2017","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.bbrc.2020.12.075_bib11","doi-asserted-by":"crossref","first-page":"830","DOI":"10.1016\/j.ccell.2019.04.002","article-title":"Targeting ferroptosis to iron out cancer","volume":"35","author":"Hassannia","year":"2019","journal-title":"Canc. Cell"},{"key":"10.1016\/j.bbrc.2020.12.075_bib12","doi-asserted-by":"crossref","first-page":"420","DOI":"10.1016\/j.chembiol.2020.02.005","article-title":"Autophagy-dependent ferroptosis: machinery and regulation","volume":"27","author":"Liu","year":"2020","journal-title":"Cell Chem. Biol."},{"key":"10.1016\/j.bbrc.2020.12.075_bib13","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1016\/j.chembiol.2008.02.010","article-title":"Synthetic lethal screening identifies compounds activating iron-dependent nonapoptotic cell death in oncogenic Ras harboring cancer cells","volume":"15","author":"Yang","year":"2008","journal-title":"Chem. Biol."},{"key":"10.1016\/j.bbrc.2020.12.075_bib14","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":"10.1016\/j.bbrc.2020.12.075_bib15","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":"10.1016\/j.bbrc.2020.12.075_bib16","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":"10.1016\/j.bbrc.2020.12.075_bib17","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1016\/j.freeradbiomed.2018.12.011","article-title":"DHA inhibits proliferation and induces ferroptosis of leukemia cells through autophagy dependent degradation of ferritin","volume":"131","author":"Du","year":"2019","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.bbrc.2020.12.075_bib18","doi-asserted-by":"crossref","first-page":"822","DOI":"10.1038\/s41419-019-2064-5","article-title":"ROS-mediated autophagy increases intracellular iron levels and ferroptosis by ferritin and transferrin receptor regulation","volume":"10","author":"Park","year":"2019","journal-title":"Cell Death Dis."},{"key":"10.1016\/j.bbrc.2020.12.075_bib19","first-page":"3826","article-title":"Knockdown of ferroportin accelerates erastin-induced ferroptosis in neuroblastoma cells","volume":"22","author":"Geng","year":"2018","journal-title":"Eur. Rev. Med. Pharmacol. Sci."},{"key":"10.1016\/j.bbrc.2020.12.075_bib20","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1016\/j.devcel.2019.10.007","article-title":"Prominin2 drives ferroptosis resistance by stimulating iron export","volume":"51","author":"Brown","year":"2019","journal-title":"Dev. Cell"},{"key":"10.1016\/j.bbrc.2020.12.075_bib21","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":"10.1016\/j.bbrc.2020.12.075_bib22","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1016\/j.canlet.2017.12.025","article-title":"Heme oxygenase-1 mediates BAY 11-7085 induced ferroptosis","volume":"416","author":"Chang","year":"2018","journal-title":"Canc. Lett."},{"key":"10.1016\/j.bbrc.2020.12.075_bib23","doi-asserted-by":"crossref","first-page":"898","DOI":"10.1091\/mbc.e17-01-0051","article-title":"Practical method for targeted disruption of cilia-related genes by using CRISPR\/Cas9-mediated homology-independent knock-in system","volume":"28","author":"Katoh","year":"2017","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.bbrc.2020.12.075_bib24","doi-asserted-by":"crossref","first-page":"2341","DOI":"10.1016\/j.celrep.2017.08.034","article-title":"Autophagy-independent lysosomal targeting regulated by ULK1\/2-FIP200 and ATG9","volume":"20","author":"Goodwin","year":"2017","journal-title":"Cell Rep."},{"key":"10.1016\/j.bbrc.2020.12.075_bib25","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.bbrc.2020.12.075_bib26","doi-asserted-by":"crossref","first-page":"114","DOI":"10.3390\/ph11040114","article-title":"The role of NCOA4-mediated ferritinophagy in health and disease","volume":"11","author":"Santana-Codina","year":"2018","journal-title":"Pharmaceuticals"},{"key":"10.1016\/j.bbrc.2020.12.075_bib27","doi-asserted-by":"crossref","first-page":"420","DOI":"10.1016\/j.chembiol.2020.02.005","article-title":"Autophagy-dependent ferroptosis: machinery and regulation","volume":"27","author":"Liu","year":"2020","journal-title":"Cell Chem. Biol."},{"key":"10.1016\/j.bbrc.2020.12.075_bib28","doi-asserted-by":"crossref","first-page":"5720","DOI":"10.1093\/emboj\/19.21.5720","article-title":"LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing","volume":"19","author":"Kabeya","year":"2000","journal-title":"EMBO J."},{"key":"10.1016\/j.bbrc.2020.12.075_bib29","doi-asserted-by":"crossref","first-page":"542","DOI":"10.4161\/auto.4600","article-title":"How to interpret LC3 immunoblotting","volume":"3","author":"Mizushima","year":"2007","journal-title":"Autophagy"},{"key":"10.1016\/j.bbrc.2020.12.075_bib30","doi-asserted-by":"crossref","first-page":"6228","DOI":"10.1038\/s41598-019-42370-z","article-title":"Intracellular Fe2+ accumulation in endothelial cells and pericytes induces blood-brain barrier dysfunction in secondary brain injury after brain hemorrhage","volume":"9","author":"Imai","year":"2019","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bbrc.2020.12.075_bib31","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":"10.1016\/j.bbrc.2020.12.075_bib32","doi-asserted-by":"crossref","first-page":"C445","DOI":"10.1152\/ajpcell.00505.2005","article-title":"Release of iron from ferritin requires lysosomal activity","volume":"291","author":"Kidane","year":"2006","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"10.1016\/j.bbrc.2020.12.075_bib33","doi-asserted-by":"crossref","first-page":"999","DOI":"10.1089\/ars.2010.3129","article-title":"Lysosomal proteolysis is the primary degradation pathway for cytosolic ferritin and cytosolic ferritin degradation is necessary for iron exit","volume":"13","author":"Zhang","year":"2010","journal-title":"Antioxidants Redox Signal."}],"container-title":["Biochemical and Biophysical Research Communications"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006291X2032252X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006291X2032252X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,5,13]],"date-time":"2026-05-13T02:20:50Z","timestamp":1778638850000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0006291X2032252X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,2]]},"references-count":33,"alternative-id":["S0006291X2032252X"],"URL":"https:\/\/doi.org\/10.1016\/j.bbrc.2020.12.075","relation":{},"ISSN":["0006-291X"],"issn-type":[{"value":"0006-291X","type":"print"}],"subject":[],"published":{"date-parts":[[2021,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Role of ferritinophagy in cystine deprivation-induced cell death in glioblastoma cells","name":"articletitle","label":"Article Title"},{"value":"Biochemical and Biophysical Research Communications","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbrc.2020.12.075","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}