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(Camb.)"},{"key":"10.1016\/j.bbamcr.2015.01.021_rf9380","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1016\/j.tcb.2013.11.005","article-title":"Maturation of cytosolic and nuclear iron\u2013sulfur proteins","volume":"24","author":"Netz","year":"2014","journal-title":"Trends Cell Biol."},{"key":"10.1016\/j.bbamcr.2015.01.021_rf9900","doi-asserted-by":"crossref","first-page":"26745","DOI":"10.1074\/jbc.R110.122218","article-title":"Cytosolic iron-sulfur cluster assembly (CIA) system: factors, mechanism, and relevance to cellular iron regulation","volume":"285","author":"Sharma","year":"2010","journal-title":"J. Biol. 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Pharmacol."},{"key":"10.1016\/j.bbamcr.2015.01.021_bb0400","doi-asserted-by":"crossref","first-page":"20590","DOI":"10.1073\/pnas.1215349109","article-title":"Identification of nonferritin mitochondrial iron deposits in a mouse model of Friedreich ataxia","volume":"109","author":"Whitnall","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamcr.2015.01.021_bb0405","doi-asserted-by":"crossref","first-page":"1771","DOI":"10.1093\/hmg\/6.11.1771","article-title":"Frataxin is reduced in Friedreich ataxia patients and is associated with mitochondrial membranes","volume":"6","author":"Campuzano","year":"1997","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbamcr.2015.01.021_bb0410","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1038\/ng0897-345","article-title":"Studies of human, mouse and yeast homologues indicate a mitochondrial function for frataxin","volume":"16","author":"Koutnikova","year":"1997","journal-title":"Nat. Genet."},{"key":"10.1016\/j.bbamcr.2015.01.021_bb0415","doi-asserted-by":"crossref","first-page":"1219","DOI":"10.1093\/hmg\/9.8.1219","article-title":"Inactivation of the Friedreich ataxia mouse gene leads to early embryonic lethality without iron accumulation","volume":"9","author":"Cossee","year":"2000","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbamcr.2015.01.021_bb0420","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1042\/BJ20130079","article-title":"Biochemistry of cardiomyopathy in the mitochondrial disease Friedreich's ataxia","volume":"453","author":"Lane","year":"2013","journal-title":"Biochem. J."},{"issue":"Suppl. 1","key":"10.1016\/j.bbamcr.2015.01.021_bb0425","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1007\/s00415-009-1003-2","article-title":"The pathogenesis of Friedreich ataxia and the structure and function of frataxin","volume":"256","author":"Pandolfo","year":"2009","journal-title":"J. Neurol."},{"key":"10.1016\/j.bbamcr.2015.01.021_bb0430","doi-asserted-by":"crossref","first-page":"6078","DOI":"10.1021\/ja027967i","article-title":"Iron-sulfur cluster biosynthesis. Characterization of frataxin as an iron donor for assembly of [2Fe\u20132S] clusters in ISU-type proteins","volume":"125","author":"Yoon","year":"2003","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbamcr.2015.01.021_bb0435","doi-asserted-by":"crossref","first-page":"25943","DOI":"10.1074\/jbc.C400107200","article-title":"Frataxin-mediated iron delivery to ferrochelatase in the final step of heme biosynthesis","volume":"279","author":"Yoon","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2015.01.021_bb0440","doi-asserted-by":"crossref","first-page":"12674","DOI":"10.1074\/jbc.M800399200","article-title":"Binding of yeast frataxin to the scaffold for Fe\u2013S cluster biogenesis, Isu","volume":"283","author":"Wang","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2015.01.021_bb0445","doi-asserted-by":"crossref","first-page":"1798","DOI":"10.1039\/B703195E","article-title":"Human frataxin: iron and ferrochelatase binding surface","author":"Bencze","year":"2007","journal-title":"Chem. Commun. (Camb.)"},{"key":"10.1016\/j.bbamcr.2015.01.021_bb0450","doi-asserted-by":"crossref","first-page":"390","DOI":"10.1038\/nsmb.1579","article-title":"Bacterial frataxin CyaY is the gatekeeper of iron-sulfur cluster formation catalyzed by IscS","volume":"16","author":"Adinolfi","year":"2009","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.bbamcr.2015.01.021_bb0455","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1038\/ncomms1097","article-title":"Structural bases for the interaction of frataxin with the central components of iron\u2013sulphur cluster assembly","volume":"1","author":"Prischi","year":"2010","journal-title":"Nat. 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Mol. Genet."},{"key":"10.1016\/j.bbamcr.2015.01.021_bb0490","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1080\/10409230701322298","article-title":"Molecular chaperones HscA\/Ssq1 and HscB\/Jac1 and their roles in iron\u2013sulfur protein maturation","volume":"42","author":"Vickery","year":"2007","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"key":"10.1016\/j.bbamcr.2015.01.021_bb0495","doi-asserted-by":"crossref","first-page":"1660","DOI":"10.1016\/j.cub.2006.06.069","article-title":"Evolution of mitochondrial chaperones utilized in Fe\u2013S cluster biogenesis","volume":"16","author":"Schilke","year":"2006","journal-title":"Curr. Biol."},{"key":"10.1016\/j.bbamcr.2015.01.021_bb0500","doi-asserted-by":"crossref","first-page":"1457","DOI":"10.1093\/hmg\/ddr582","article-title":"HSC20 interacts with frataxin and is involved in iron\u2013sulfur cluster biogenesis and iron homeostasis","volume":"21","author":"Shan","year":"2012","journal-title":"Hum. Mol. 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Hum. Genet."},{"key":"10.1016\/j.bbamcr.2015.01.021_bb0520","doi-asserted-by":"crossref","first-page":"3816","DOI":"10.1093\/hmg\/ddq301","article-title":"Characterization of the human HSC20, an unusual DnaJ type III protein, involved in iron\u2013sulfur cluster biogenesis","volume":"19","author":"Uhrigshardt","year":"2010","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbamcr.2015.01.021_bb0525","first-page":"1","article-title":"The diverse roles of J-proteins, the obligate Hsp70 co-chaperone","volume":"156","author":"Craig","year":"2006","journal-title":"Rev. Physiol. Biochem. Pharmacol."},{"key":"10.1016\/j.bbamcr.2015.01.021_bb0530","doi-asserted-by":"crossref","first-page":"1335","DOI":"10.1042\/BST20130116","article-title":"The superfamily of mitochondrial Complex1_LYR motif-containing (LYRM) proteins","volume":"41","author":"Angerer","year":"2013","journal-title":"Biochem. Soc. 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