{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,22]],"date-time":"2026-06-22T04:47:57Z","timestamp":1782103677614,"version":"3.54.5"},"reference-count":68,"publisher":"Springer Science and Business Media LLC","issue":"3","license":[{"start":{"date-parts":[[2026,3,9]],"date-time":"2026-03-09T00:00:00Z","timestamp":1773014400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2026,3,9]],"date-time":"2026-03-09T00:00:00Z","timestamp":1773014400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"name":"Vietnamese Government Scholarship"},{"DOI":"10.13039\/501100000265","name":"Medical Research Council","doi-asserted-by":"publisher","award":["MR\/Y50337X\/1"],"award-info":[{"award-number":["MR\/Y50337X\/1"]}],"id":[{"id":"10.13039\/501100000265","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000921","name":"European Cooperation in Science and Technology","doi-asserted-by":"publisher","award":["CA21115"],"award-info":[{"award-number":["CA21115"]}],"id":[{"id":"10.13039\/501100000921","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000288","name":"Royal Society","doi-asserted-by":"publisher","award":["IES\\R1\\221117 and RGS\\R1\\231135"],"award-info":[{"award-number":["IES\\R1\\221117 and RGS\\R1\\231135"]}],"id":[{"id":"10.13039\/501100000288","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["J Biol Inorg Chem"],"DOI":"10.1007\/s00775-026-02139-y","type":"journal-article","created":{"date-parts":[[2026,3,9]],"date-time":"2026-03-09T12:25:39Z","timestamp":1773059139000},"page":"119-130","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Emerging role of mitoNEET as mitochondrial sensor of hypoxia"],"prefix":"10.1007","volume":"31","author":[{"given":"Nghi Thao","family":"Hoang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kourosh Honarmand","family":"Ebrahimi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,3,9]]},"reference":[{"key":"2139_CR1","doi-asserted-by":"publisher","first-page":"253","DOI":"10.1038\/s41557-021-00882-0","volume":"14","author":"KH Ebrahimi","year":"2022","unstructured":"Ebrahimi KH, Ciofi-Baffoni S, Hagedoorn PL, Nicolet Y, Le Brun NE, Hagen WR, Armstrong FA (2022) Iron-sulphur clusters as inhibitors and catalysts of viral replication. Nat Chem 14:253\u2013266","journal-title":"Nat Chem"},{"key":"2139_CR2","doi-asserted-by":"publisher","first-page":"4921","DOI":"10.1021\/acs.chemrev.9b00489","volume":"120","author":"S Bur\u00e9n","year":"2020","unstructured":"Bur\u00e9n S, Jim\u00e9nez-Vicente E, Echavarri-Erasun C, Rubio LM (2020) Biosynthesis of nitrogenase cofactors. Chem Rev 120:4921\u20134968","journal-title":"Chem Rev"},{"key":"2139_CR3","doi-asserted-by":"publisher","first-page":"653","DOI":"10.1126\/science.277.5326.653","volume":"277","author":"H Beinert","year":"1997","unstructured":"Beinert H, Holm RH, Munck E (1997) Iron-sulfur clusters: nature\u2019s modular, multipurpose structures. Sci (80-) 277:653\u2013659","journal-title":"Sci (80-)"},{"key":"2139_CR4","doi-asserted-by":"publisher","first-page":"354","DOI":"10.1038\/nature19095","volume":"536","author":"J Zhu","year":"2016","unstructured":"Zhu J, Vinothkumar KR, Hirst J (2016) Structure of mammalian respiratory complex I. Nature 536:354\u2013358. https:\/\/doi.org\/10.1038\/nature19095","journal-title":"Nature"},{"key":"2139_CR5","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-020-18950-3","volume":"11","author":"HR Bridges","year":"2020","unstructured":"Bridges HR, Fedor JG, Blaza JN, Di Luca A, Jussupow A, Jarman OD, Wright JJ, Agip A-N, Gamiz-Hernandez AP, Roessler MM, Kaila VRI, Hirst J (2020) Structure of inhibitor-bound mammalian complex I. Nat Commun 11:5261. https:\/\/doi.org\/10.1038\/s41467-020-18950-3","journal-title":"Nat Commun"},{"key":"2139_CR6","doi-asserted-by":"publisher","first-page":"46","DOI":"10.1038\/nchembio.1976","volume":"12","author":"RM Evans","year":"2016","unstructured":"Evans RM, Brooke EJ, Wehlin SAM, Nomerotskaia E, Sargent F, Carr SB, Phillips SEV, Armstrong FA (2016) Mechanism of hydrogen activation by [NiFe] hydrogenases. Nat Chem Biol 12:46\u201350. https:\/\/doi.org\/10.1038\/nchembio.1976","journal-title":"Nat Chem Biol"},{"key":"2139_CR7","doi-asserted-by":"publisher","first-page":"337","DOI":"10.1038\/s41929-020-0448-7","volume":"3","author":"Y Nicolet","year":"2020","unstructured":"Nicolet Y (2020) Structure\u2013function relationships of radical SAM enzymes. Nat Catal 3:337\u2013350","journal-title":"Nat Catal"},{"key":"2139_CR8","doi-asserted-by":"publisher","first-page":"539","DOI":"10.1039\/C7MT00341B","volume":"10","author":"KH Ebrahimi","year":"2018","unstructured":"Ebrahimi KH (2018) A unifying view of the broad-spectrum antiviral activity of RSAD2 (viperin) based on its radical-SAM chemistry. Metallomics 10:539\u2013552","journal-title":"Metallomics"},{"key":"2139_CR9","doi-asserted-by":"publisher","first-page":"4229","DOI":"10.1021\/cr4004709","volume":"114","author":"JB Broderick","year":"2014","unstructured":"Broderick JB, Duffus BR, Duschene KS, Shepard EM (2014) Radical S-adenosylmethionine enzymes. Chem Rev 114:4229\u20134317","journal-title":"Chem Rev"},{"key":"2139_CR10","doi-asserted-by":"publisher","DOI":"10.3389\/fmolb.2022.1032220","volume":"19","author":"Y Ji","year":"2022","unstructured":"Ji Y, Li W, Da A, Stark H, Hagedoorn P-L, Ciofi-Baffoni S, Cowley SA, Louro RO, Todorovic S, Mroginski MA, Nicolet Y, Roessler MM, Le Brun NE, Piccioli M, James WS, Hagen WR, Ebrahimi KH (2022) Radical-SAM dependent nucleotide dehydratase (SAND), rectification of the names of an ancient iron-sulfur enzyme using NC-IUBMB recommendations. Front Mol Biosci 19:1032220","journal-title":"Front Mol Biosci"},{"key":"2139_CR11","doi-asserted-by":"publisher","first-page":"14598","DOI":"10.1074\/jbc.M700825200","volume":"282","author":"D Barthelme","year":"2007","unstructured":"Barthelme D, Scheele U, Dinkelaker S, Janoschka A, MacMillan F, Albers S-V, Driessen AJM, Stagni MS, Bill E, Meyer-Klaucke W, Schuonemann V, Tampe R (2007) Structural organization of essential iron-sulfur clusters in the evolutionarily highly conserved ATP-binding cassette protein ABCE1. J Biol Chem 282:14598\u201314607","journal-title":"J Biol Chem"},{"key":"2139_CR12","doi-asserted-by":"publisher","first-page":"760","DOI":"10.1038\/s41929-025-01367-w","volume":"8","author":"R Ushimaru","year":"2025","unstructured":"Ushimaru R, Zheng Z, Xiong J, Mori T, Abe I, Guo Y, Liu H (2025) Radical S-adenosyl-l-methionine FeS cluster implicated as the sulfur donor during albomycin biosynthesis. Nat Catal 8:760\u2013770. https:\/\/doi.org\/10.1038\/s41929-025-01367-w","journal-title":"Nat Catal"},{"key":"2139_CR13","doi-asserted-by":"publisher","first-page":"5713","DOI":"10.1021\/jacs.1c13626","volume":"144","author":"G Saudino","year":"2022","unstructured":"Saudino G, Ciofi-Baffoni S, Banci L (2022) Protein-interaction affinity gradient drives [4Fe\u20134S] cluster insertion in human lipoyl synthase. J Am Chem Soc 144:5713\u20135717. https:\/\/doi.org\/10.1021\/jacs.1c13626","journal-title":"J Am Chem Soc"},{"key":"2139_CR14","doi-asserted-by":"publisher","first-page":"1564","DOI":"10.1038\/s41559-022-01857-1","volume":"6","author":"PS Garcia","year":"2022","unstructured":"Garcia PS, D\u2019Angelo F, Ollagnier de Choudens S, Dussouchaud M, Bouveret E, Gribaldo S, Barras F (2022) An early origin of iron\u2013sulfur cluster biosynthesis machineries before Earth oxygenation. Nat Ecol Evol 6:1564\u20131572. https:\/\/doi.org\/10.1038\/s41559-022-01857-1","journal-title":"Nat Ecol Evol"},{"key":"2139_CR15","doi-asserted-by":"publisher","DOI":"10.3390\/inorganics10100174","volume":"10","author":"I Elchennawi","year":"2022","unstructured":"Elchennawi I, de Ollagnier Chouns S (2022) Iron\u2013sulfur clusters toward stresses: implication for understanding and fighting tuberculosis. Inorganics 10:174","journal-title":"Inorganics"},{"key":"2139_CR16","doi-asserted-by":"publisher","first-page":"3517","DOI":"10.1073\/pnas.022042899","volume":"99","author":"Winkler","year":"2002","unstructured":"Winkler G.S., Kristjuhan A, Erdjument-Bromage H, Tempst P, Svejstrup J.Q. (2002) Elongator is a histone H3 and H4 acetyltransferase important for normal histone acetylation levels in vivo. Proc Natl Acad Sci 99:3517\u20133522","journal-title":"Proc Natl Acad Sci"},{"key":"2139_CR17","doi-asserted-by":"publisher","first-page":"872","DOI":"10.1016\/j.cell.2015.07.041","volume":"162","author":"DJ Young","year":"2015","unstructured":"Young DJ, Guydosh NR, Zhang F, Hinnebusch AG, Green R (2015) Rli1\/ABCE1 Recycles Terminating Ribosomes and Controls Translation Reinitiation in 3\u2032UTRs In Vivo. Cell 162:872\u2013884","journal-title":"Cell"},{"key":"2139_CR18","doi-asserted-by":"publisher","first-page":"453","DOI":"10.1038\/nsmb.3396","volume":"24","author":"A Heuer","year":"2017","unstructured":"Heuer A, Gerovac M, Schmidt C, Trowitzsch S, Preis A, Kotter P, Berninghausen O, Becker T, Beckmann R, Tampe R (2017) Structure of the 40S\u2013ABCE1 post-splitting complex in ribosome recycling and translation initiation. Nat Struct Mol Biol 24:453\u2013460","journal-title":"Nat Struct Mol Biol"},{"key":"2139_CR19","first-page":"652","volume":"59","author":"MK Fenwick","year":"2020","unstructured":"Fenwick MK, Su D, Dong M, Lin H, Ealick SE (2020) Struct Basis Substrate Selectivity Viperin Biochem 59:652\u2013662","journal-title":"Struct Basis Substrate Selectivity Viperin Biochem"},{"key":"2139_CR20","doi-asserted-by":"publisher","first-page":"43345","DOI":"10.1074\/jbc.M401889200","volume":"279","author":"D Gonzalez","year":"2004","unstructured":"Gonzalez D, Drapier J-C, Bouton C (2004) Endogenous Nitration of Iron Regulatory Protein-1 (IRP-1) in Nitric Oxide-producing Murine Macrophages: FURTHER INSIGHT INTO THE MECHANISM OF NITRATION IN VIVO AND ITS IMPACT ON IRP-1 FUNCTIONS. J Biol Chem 279:43345\u201343351","journal-title":"J Biol Chem"},{"key":"2139_CR21","doi-asserted-by":"publisher","first-page":"106","DOI":"10.1016\/j.sbi.2007.12.010","volume":"18","author":"K Volz","year":"2008","unstructured":"Volz K (2008) The functional duality of iron regulatory protein 1, Curr. Opin Struct Biol 18:106\u2013111.\u00a0https:\/\/doi.org\/10.1016\/j.sbi.2007.12.010","journal-title":"Opin Struct Biol"},{"key":"2139_CR22","doi-asserted-by":"publisher","first-page":"118705","DOI":"10.1016\/j.bbamcr.2020.118705","volume":"1867","author":"AK Hern\u00e1ndez-Gallardo","year":"2020","unstructured":"Hern\u00e1ndez-Gallardo AK, Missirlis F (2020) Cellular iron sensing and regulation: Nuclear IRP1 extends a classic paradigm, Biochim. Biophys. Acta - Mol. Cell Res 1867:118705. https:\/\/doi.org\/10.1016\/j.bbamcr.2020.118705","journal-title":"Cell Res"},{"key":"2139_CR23","doi-asserted-by":"publisher","first-page":"952","DOI":"10.1002\/1873-3468.15097","volume":"599","author":"TN Hoang","year":"2025","unstructured":"Hoang TN, Wu-Lu M, Collauto A, Hagedoorn P-L, Alexandru M, Henschel M, Kordasti S, Mroginski MA, Roessler MM, Ebrahimi KH (2025) The [2Fe-2S] cluster of mitochondrial outer membrane protein mitoNEET has an O-regulated nitric oxide access tunnel. FEBS Lett 599:952\u2013970","journal-title":"FEBS Lett"},{"key":"2139_CR24","doi-asserted-by":"publisher","first-page":"2260","DOI":"10.1111\/febs.13270","volume":"282","author":"K Schaffer","year":"2015","unstructured":"Schaffer K, Taylor CT (2015) The impact of hypoxia on bacterial infection. FEBS J 282:2260\u20132266. https:\/\/doi.org\/10.1111\/febs.13270","journal-title":"FEBS J"},{"key":"2139_CR25","doi-asserted-by":"publisher","first-page":"3582","DOI":"10.1016\/j.febslet.2007.06.018","volume":"581","author":"MC Brahimi-Horn","year":"2007","unstructured":"Brahimi-Horn MC, Pouyss\u00e9gur J (2007) Oxygen, a source of life and stress. FEBS Lett 581:3582\u20133591.\u00a0https:\/\/doi.org\/10.1016\/j.febslet.2007.06.018","journal-title":"FEBS Lett"},{"key":"2139_CR26","doi-asserted-by":"publisher","first-page":"617","DOI":"10.1016\/j.bbrc.2005.08.111","volume":"338","author":"CJ Schofield","year":"2005","unstructured":"Schofield CJ, Ratcliffe PJ (2005) Signalling hypoxia by HIF hydroxylases, Biochem. Biophys Res Commun 338:617\u2013626","journal-title":"Biophys Res Commun"},{"key":"2139_CR27","doi-asserted-by":"publisher","first-page":"2448","DOI":"10.1038\/emboj.2012.125","volume":"31","author":"SN Greer","year":"2012","unstructured":"Greer SN, Metcalf JL, Wang Y, Ohh M (2012) The updated biology of hypoxia-inducible factor. EMBO J 31:2448\u20132460","journal-title":"EMBO J"},{"key":"2139_CR28","doi-asserted-by":"publisher","first-page":"281","DOI":"10.1016\/j.cmet.2017.10.005","volume":"27","author":"H Choudhry","year":"2018","unstructured":"Choudhry H, Harris AL (2018) Advances in hypoxia-inducible factor biology. Cell Metab 27:281\u2013298","journal-title":"Cell Metab"},{"key":"2139_CR29","doi-asserted-by":"crossref","unstructured":"Richter FC, Saliutina M, Hegazy AN, Bergthaler A (2024) Take my breath away\u2014mitochondrial dysfunction drives CD8\u2009+\u2009T cell exhaustion. Genes Immun. 1\u20133","DOI":"10.1038\/s41435-023-00233-8"},{"key":"2139_CR30","doi-asserted-by":"publisher","first-page":"165845","DOI":"10.1016\/j.bbadis.2020.165845","volume":"1866","author":"Faas","year":"2020","unstructured":"Faas M.M., De Vos P (2020) Mitochondrial function in immune cells in health and disease. Biochim Biophys Acta (BBA)-Molecular Basis Dis 1866:165845","journal-title":"Biochim Biophys Acta (BBA)-Molecular Basis Dis"},{"key":"2139_CR31","doi-asserted-by":"publisher","first-page":"208","DOI":"10.1016\/j.redox.2017.02.012","volume":"12","author":"DC Fuhrmann","year":"2017","unstructured":"Fuhrmann DC, Br\u00fcne B (2017) Mitochondrial composition and function under the control of hypoxia. Redox Biol 12:208\u2013215.\u00a0https:\/\/doi.org\/10.1016\/j.redox.2017.02.012","journal-title":"Redox Biol"},{"key":"2139_CR32","doi-asserted-by":"publisher","first-page":"1171","DOI":"10.1016\/j.bbabio.2010.02.011","volume":"1797","author":"G Solaini","year":"2010","unstructured":"Solaini G, Baracca A, Lenaz G, Sgarbi G (2010) Hypoxia and mitochondrial oxidative metabolism. Biochim Biophys Acta (BBA)-Bioenergetics 1797:1171\u20131177","journal-title":"Biochim Biophys Acta (BBA)-Bioenergetics"},{"key":"2139_CR33","doi-asserted-by":"publisher","first-page":"217","DOI":"10.1007\/s00109-012-0880-5","volume":"90","author":"JJD Ho","year":"2012","unstructured":"Ho JJD, Man HSJ, Marsden PA (2012) Nitric oxide signaling in hypoxia. J Mol Med 90:217\u2013231","journal-title":"J Mol Med"},{"key":"2139_CR34","doi-asserted-by":"publisher","first-page":"1609","DOI":"10.1016\/S0891-5849(01)00754-7","volume":"31","author":"Z Lacza","year":"2001","unstructured":"Lacza Z, Puskar M, Figueroa JP, Zhang J, Rajapakse N, Busija DW (2001) Mitochondrial nitric oxide synthase is constitutively active and is functionally upregulated in hypoxia. Free Radic Biol Med 31:1609\u20131615","journal-title":"Free Radic Biol Med"},{"key":"2139_CR35","doi-asserted-by":"publisher","first-page":"341","DOI":"10.1016\/S0169-328X(96)00222-7","volume":"43","author":"NR Prabhakar","year":"1996","unstructured":"Prabhakar NR, Pieramici SF, Premkumar DRD, Kumar GK, Kalaria RN (1996) Activation of nitric oxide synthase gene expression by hypoxia in central and peripheral neurons. Mol Brain Res 43:341\u2013346","journal-title":"Mol Brain Res"},{"key":"2139_CR36","doi-asserted-by":"publisher","first-page":"12430","DOI":"10.1074\/jbc.M604547200","volume":"282","author":"J Li Campian","year":"2007","unstructured":"Li Campian J, Gao X, Qian M, Eaton JW (2007) Cytochrome\u2009<\u2009em\u2009>\u2009c<\/em> oxidase activity and oxygen tolerance *. J Biol Chem 282:12430\u201312438. https:\/\/doi.org\/10.1074\/jbc.M604547200","journal-title":"J Biol Chem"},{"key":"2139_CR37","doi-asserted-by":"publisher","first-page":"718","DOI":"10.1128\/MCB.01338-07","volume":"28","author":"RD Guzy","year":"2008","unstructured":"Guzy RD, Sharma B, Bell E, Chandel NS, Schumacker PT (2008) Loss of the SdhB, but not the SdhA, subunit of complex II triggers reactive oxygen species-dependent hypoxia-inducible factor activation and tumorigenesis. Mol Cell Biol 28:718\u2013731","journal-title":"Mol Cell Biol"},{"key":"2139_CR38","doi-asserted-by":"publisher","first-page":"599","DOI":"10.1007\/s00775-018-1538-8","volume":"23","author":"O Karmi","year":"2018","unstructured":"Karmi O, Marjault H-B, Pesce L, Carloni P, Onuchic J, Jennings PA, Mittler R, Nechushtai R (2018) The unique fold and lability of the [2Fe-2S] clusters of NEET proteins mediate their key functions in health and disease. JBIC J Biol Inorg Chem 23:599\u2013612","journal-title":"JBIC J Biol Inorg Chem"},{"key":"2139_CR39","doi-asserted-by":"publisher","first-page":"8218","DOI":"10.3390\/molecules27238218","volume":"27","author":"F Camponeschi","year":"2022","unstructured":"Camponeschi F, Piccioli M, Banci L (2022) The intriguing mitoNEET: functional and spectroscopic properties of a unique [2Fe-2S] cluster coordination geometry. Molecules 27:8218","journal-title":"Molecules"},{"key":"2139_CR40","doi-asserted-by":"publisher","first-page":"763","DOI":"10.1007\/s00775-021-01890-8","volume":"26","author":"K Zuo","year":"2021","unstructured":"Zuo K, Marjault H-B, Bren KL, Rossetti G, Nechushtai R, Carloni P (2021) The two redox states of the human NEET proteins\u2019[2Fe\u20132S] clusters. JBIC J Biol Inorg Chem 26:763\u2013774","journal-title":"JBIC J Biol Inorg Chem"},{"key":"2139_CR41","doi-asserted-by":"publisher","first-page":"1083","DOI":"10.1089\/ars.2018.7502","volume":"30","author":"R Mittler","year":"2019","unstructured":"Mittler R, Darash-Yahana M, Sohn YS, Bai F, Song L, Cabantchik IZ, Jennings PA, Onuchic JN, Nechushtai R (2019) NEET proteins: a new link between iron metabolism, reactive oxygen species, and cancer. Antioxid Redox Signal 30:1083\u20131095","journal-title":"Antioxid Redox Signal"},{"key":"2139_CR42","first-page":"E252","volume":"286","author":"JR Colca","year":"2004","unstructured":"Colca JR, McDonald WG, Waldon DJ, Leone JW, Lull JM, Bannow CA, Lund ET, Mathews WR (2004) Identification of a novel mitochondrial protein (mitoNEET) cross-linked specifically by a thiazolidinedione photoprobe. Am J Physiol Metab 286:E252\u2013E260","journal-title":"Am J Physiol Metab"},{"key":"2139_CR43","doi-asserted-by":"publisher","first-page":"113","DOI":"10.1002\/path.5436","volume":"251","author":"A Nobili","year":"2020","unstructured":"Nobili A, Krashia P, D\u2019Amelio M (2020) Cisd2: a promising new target in Alzheimer\u2019s disease. J Pathol 251:113\u2013116","journal-title":"J Pathol"},{"key":"2139_CR44","doi-asserted-by":"publisher","first-page":"904","DOI":"10.1002\/emmm.201201429","volume":"5","author":"SE Wiley","year":"2013","unstructured":"Wiley SE, Andreyev AY, Divakaruni AS, Karisch R, Perkins G, Wall EA, van der Geer P, Chen Y, Tsai T, Simon MI (2013) Wolfram syndrome protein, Miner1, regulates sulphydryl redox status, the unfolded protein response, and Ca2\u2009+\u2009homeostasis. EMBO Mol. Med. 5:904\u2013918","journal-title":"EMBO Mol. Med."},{"key":"2139_CR45","doi-asserted-by":"publisher","DOI":"10.1016\/j.jbc.2024.105745","author":"D Grifagni","year":"2024","unstructured":"Grifagni D, Silva JM, Querci L, Lepoivre M, Valli\u00e8res C, Louro RO, Banci L, Piccioli M, Golinelli-Cohen M-P, Cantini F (2024) Biochemical and cellular characterization of the CISD3 protein: molecular bases of cluster release and destabilizing effects of nitric oxide. J Biol Chem. https:\/\/doi.org\/10.1016\/j.jbc.2024.105745","journal-title":"J Biol Chem"},{"key":"2139_CR46","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0245174","volume":"16","author":"SD King","year":"2021","unstructured":"King SD, Gray CF, Song L, Mittler R, Padilla PA (2021) The mitochondrial localized CISD-3.1\/CISD-3.2 proteins are required to maintain normal germline structure and function in Caenorhabditis elegans. PLoS One 16:e0245174","journal-title":"PLoS One"},{"key":"2139_CR47","doi-asserted-by":"publisher","DOI":"10.3389\/fmolb.2022.995421","volume":"9","author":"CR Fontenot","year":"2022","unstructured":"Fontenot CR, Cheng Z, Ding H (2022) Nitric oxide reversibly binds the reduced [2Fe-2S] cluster in mitochondrial outer membrane protein mitoNEET and inhibits its electron transfer activity. Front. Mol. Biosci. 9:995421","journal-title":"Front. Mol. Biosci."},{"key":"2139_CR48","doi-asserted-by":"publisher","DOI":"10.3390\/biomedicines9040384","author":"M Salameh","year":"2021","unstructured":"Salameh M, Riquier S, Guittet O, Huang M-E, Vernis L, Lepoivre M, Golinelli-Cohen M-P (2021) New insights of the NEET protein CISD2 reveals distinct features compared to its close mitochondrial homolog mitoNEET. Biomedicines. https:\/\/doi.org\/10.3390\/biomedicines9040384","journal-title":"Biomedicines"},{"key":"2139_CR49","doi-asserted-by":"publisher","first-page":"9479","DOI":"10.1021\/jacs.7b05003","volume":"139","author":"F Camponeschi","year":"2017","unstructured":"Camponeschi F, Ciofi-Baffoni S, Banci L (2017) Anamorsin\/Ndor1 complex reduces [2Fe\u20132S]-MitoNEET via a transient protein\u2013protein interaction. J Am Chem Soc 139:9479\u20139482","journal-title":"J Am Chem Soc"},{"key":"2139_CR50","doi-asserted-by":"publisher","first-page":"4307","DOI":"10.1074\/jbc.M113.542050","volume":"289","author":"AP Landry","year":"2014","unstructured":"Landry AP, Ding H (2014) Redox control of human mitochondrial outer membrane protein MitoNEET [2Fe-2S] clusters by biological thiols and hydrogen peroxide. J Biol Chem 289:4307\u20134315","journal-title":"J Biol Chem"},{"key":"2139_CR51","doi-asserted-by":"publisher","first-page":"1539","DOI":"10.1038\/nm.2899","volume":"18","author":"CM Kusminski","year":"2012","unstructured":"Kusminski CM, Holland WL, Sun K, Park J, Spurgin SB, Lin Y, Askew GR, Simcox JA, McClain DA, Li C, Scherer PE (2012) Mitoneet-driven alterations in adipocyte mitochondrial activity reveal a crucial adaptive process that preserves insulin sensitivity in obesity. Nat Med 18:1539\u20131549","journal-title":"Nat Med"},{"key":"2139_CR52","doi-asserted-by":"publisher","first-page":"19924","DOI":"10.1073\/pnas.1908271116","volume":"116","author":"CH Lipper","year":"2019","unstructured":"Lipper CH, Stofleth JT, Bai F, Sohn Y-S, Roy S, Mittler R, Nechushtai R, Onuchic JN, Jennings PA (2019) Redox-dependent gating of VDAC by mitoNEET. Proc Natl Acad Sci 116:19924\u201319929","journal-title":"Proc Natl Acad Sci"},{"key":"2139_CR53","doi-asserted-by":"publisher","first-page":"8277","DOI":"10.1073\/pnas.1706643114","volume":"114","author":"A Vernay","year":"2017","unstructured":"Vernay A, Marchetti A, Sabra A, Jauslin T.N., Rosselin M, Scherer P.E., Demaurex N, Orci L, Cosson P. (2017) MitoNEET-dependent formation of intermitochondrial junctions. Proc Natl Acad Sci 114:8277\u20138282","journal-title":"Proc Natl Acad Sci"},{"key":"2139_CR54","doi-asserted-by":"publisher","first-page":"4062","DOI":"10.1111\/febs.17214","volume":"291","author":"E Tam","year":"2024","unstructured":"Tam E, Nguyen K, Sung HK, Sweeney G (2024) MitoNEET preserves muscle insulin sensitivity during iron overload by regulating mitochondrial iron, reactive oxygen species and fission. FEBS J 291:4062\u20134075. https:\/\/doi.org\/10.1111\/febs.17214","journal-title":"FEBS J"},{"key":"2139_CR55","doi-asserted-by":"publisher","first-page":"28070","DOI":"10.1074\/jbc.M114.548438","volume":"289","author":"I Ferecatu","year":"2014","unstructured":"Ferecatu I, Gon\u00e7alves S, Golinelli-Cohen M-P, Cl\u00e9mancey M, Martelli A, Riquier S, Guittet E, Latour J-M, Puccio H, Drapier J-C, Lescop E, Bouton C (2014) The Diabetes Drug Target MitoNEET Governs a Novel Trafficking Pathway to Rebuild an Fe-S Cluster into Cytosolic Aconitase\/Iron Regulatory Protein 1*. J Biol Chem 289:28070\u201328086. https:\/\/doi.org\/10.1074\/jbc.M114.548438","journal-title":"J Biol Chem"},{"key":"2139_CR56","doi-asserted-by":"publisher","first-page":"1833","DOI":"10.1016\/j.bbabio.2012.02.033","volume":"1817","author":"B Westermann","year":"2012","unstructured":"Westermann B (2012) Bioenergetic role of mitochondrial fusion and fission, Biochim. Biophys. Acta - Bioenerg 1817:1833\u20131838.\u00a0https:\/\/doi.org\/10.1016\/j.bbabio.2012.02.033","journal-title":"Acta - Bioenerg"},{"key":"2139_CR57","doi-asserted-by":"publisher","first-page":"2641","DOI":"10.1039\/D2DT04047F","volume":"52","author":"OV Pokidova","year":"2023","unstructured":"Pokidova OV, Novikova VO, Emel\u2019yanova NS, Kormukhina AY, Kulikov AV, Utenyshev AN, Lazarenko VA, Ovanesyan NS, Starostina AA, Sanina NA (2023) A nitrosyl iron complex with 3.4-dichlorothiophenolyl ligands: synthesis, structures and its reactions with targets\u2013carriers of nitrogen oxide (NO) in vivo. Dalt Trans 52:2641\u20132662","journal-title":"Dalt Trans"},{"key":"2139_CR58","doi-asserted-by":"publisher","first-page":"3146","DOI":"10.1074\/jbc.M116.766774","volume":"292","author":"Z Cheng","year":"2017","unstructured":"Cheng Z, Landry AP, Wang Y, Ding H (2017) Binding of Nitric Oxide in CDGSH-type [2Fe-2S] Clusters of the Human Mitochondrial Protein Miner2. J Biol Chem 292:3146\u20133153","journal-title":"J Biol Chem"},{"key":"2139_CR59","doi-asserted-by":"publisher","first-page":"1355","DOI":"10.1016\/j.bbapap.2014.01.002","volume":"1844","author":"O Kabil","year":"2014","unstructured":"Kabil O, Motl N, Banerjee R (2014) H2S and its role in redox signaling, Biochim. Biophys. Acta - Proteins Proteom 1844:1355\u20131366. https:\/\/doi.org\/10.1016\/j.bbapap.2014.01.002","journal-title":"Acta - Proteins Proteom"},{"key":"2139_CR60","doi-asserted-by":"publisher","first-page":"13098","DOI":"10.1096\/fj.201901304R","volume":"33","author":"B Murphy","year":"2019","unstructured":"Murphy B, Bhattacharya R, Mukherjee P (2019) Hydrogen sulfide signaling in mitochondria and disease. FASEB J 33:13098","journal-title":"FASEB J"},{"key":"2139_CR61","doi-asserted-by":"publisher","DOI":"10.3390\/cells10020220","author":"C Szabo","year":"2021","unstructured":"Szabo C (2021) Hydrogen sulfide, an endogenous stimulator of mitochondrial function in cancer cells. Cells. https:\/\/doi.org\/10.3390\/cells10020220","journal-title":"Cells"},{"key":"2139_CR62","doi-asserted-by":"publisher","first-page":"14342","DOI":"10.1073\/pnas.0707189104","volume":"104","author":"ML Paddock","year":"2007","unstructured":"Paddock ML, Wiley SE, Axelrod HL, Cohen AE, Roy M, Abresch EC, Capraro D, Murphy AN, Nechushtai R, Dixon JE (2007) MitoNEET is a uniquely folded 2Fe\u20132S outer mitochondrial membrane protein stabilized by pioglitazone. Proc Natl Acad Sci 104:14342\u201314347","journal-title":"Proc Natl Acad Sci"},{"key":"2139_CR63","doi-asserted-by":"publisher","first-page":"933","DOI":"10.1083\/jcb.201008084","volume":"191","author":"SM Jin","year":"2010","unstructured":"Jin SM, Lazarou M, Wang C, Kane LA, Narendra DP, Youle RJ (2010) Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL. J Cell Biol 191:933\u2013942. https:\/\/doi.org\/10.1083\/jcb.201008084","journal-title":"J Cell Biol"},{"key":"2139_CR64","doi-asserted-by":"publisher","first-page":"95","DOI":"10.1016\/j.ceb.2015.01.002","volume":"33","author":"A Eiyama","year":"2015","unstructured":"Eiyama A, Okamoto K (2015) PINK1\/Parkin-mediated mitophagy in mammalian cells. Curr Opin Cell Biol 33:95\u2013101","journal-title":"Curr Opin Cell Biol"},{"key":"2139_CR65","doi-asserted-by":"publisher","first-page":"1073","DOI":"10.1016\/j.febslet.2010.02.016","volume":"584","author":"S Kawajiri","year":"2010","unstructured":"Kawajiri S, Saiki S, Sato S, Sato F, Hatano T, Eguchi H, Hattori N (2010) PINK1 is recruited to mitochondria with parkin and associates with LC3 in mitophagy. FEBS Lett 584:1073\u20131079","journal-title":"FEBS Lett"},{"key":"2139_CR66","doi-asserted-by":"publisher","first-page":"1386","DOI":"10.1016\/j.febslet.2010.02.060","volume":"584","author":"A Tanaka","year":"2010","unstructured":"Tanaka A (2010) Parkin-mediated selective mitochondrial autophagy, mitophagy: Parkin purges damaged organelles from the vital mitochondrial network. FEBS Lett 584:1386\u20131392","journal-title":"FEBS Lett"},{"key":"2139_CR67","doi-asserted-by":"publisher","first-page":"2168","DOI":"10.1016\/j.febslet.2007.01.095","volume":"581","author":"Y Zhang","year":"2007","unstructured":"Zhang Y, Chan DC (2007) New insights into mitochondrial fusion. FEBS Lett 581:2168\u20132173.\u00a0https:\/\/doi.org\/10.1016\/j.febslet.2007.01.095","journal-title":"FEBS Lett"},{"key":"2139_CR68","doi-asserted-by":"publisher","first-page":"872","DOI":"10.1038\/nrm3013","volume":"11","author":"B Westermann","year":"2010","unstructured":"Westermann B (2010) Mitochondrial fusion and fission in cell life and death. Nat Rev Mol Cell Biol 11:872\u2013884. https:\/\/doi.org\/10.1038\/nrm3013","journal-title":"Nat Rev Mol Cell Biol"}],"container-title":["JBIC Journal of Biological Inorganic Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s00775-026-02139-y.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s00775-026-02139-y","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s00775-026-02139-y.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,6,22]],"date-time":"2026-06-22T04:04:09Z","timestamp":1782101049000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s00775-026-02139-y"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,3,9]]},"references-count":68,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2026,4]]}},"alternative-id":["2139"],"URL":"https:\/\/doi.org\/10.1007\/s00775-026-02139-y","relation":{},"ISSN":["1432-1327"],"issn-type":[{"value":"1432-1327","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,3,9]]},"assertion":[{"value":"1 January 2026","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"26 February 2026","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"9 March 2026","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"The authors declare no competing interests.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}},{"value":"Not applicable","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethics approval and consent to participate"}},{"value":"All Authors have approved the submission of the work and consent to publication in the Journal of Biological Inorganic Chemistry","order":4,"name":"Ethics","group":{"name":"EthicsHeading","label":"<!--Emphasis Type='Bold' removed-->Consent for publication"}}]}}