{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,7]],"date-time":"2026-08-07T15:13:47Z","timestamp":1786115627111,"version":"build-2736575974"},"reference-count":491,"publisher":"MDPI AG","issue":"15","license":[{"start":{"date-parts":[[2026,8,3]],"date-time":"2026-08-03T00:00:00Z","timestamp":1785715200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Int. J. Mol. Sci.","IJMS"],"abstract":"<jats:p>The increased activity of \u03b4-aminolevulinic acid synthase-1 (ALAS1) leads to the accumulation of \u03b4-aminolevulinic acid (ALA), which may reduce the iron(III) retention ability of ferritin, resulting in iron(III) overload. The accumulation of ALA occurs in the condition of attenuation of the heme negative feedback loop over ALAS1 activity in concert with the induction of ALAS1 expression. Attenuation of the heme negative feedback loop is maintained by elevated quantities of the heme catabolizing enzyme, heme oxygenase-1 (HO-1), which, in turn, may be induced by highly increased heme concentration. The upregulation of brain HO-1 occurs in patients with Alzheimer\u2019s and Parkinson\u2019s diseases. A mouse with overexpressed human HMOX1 is a model of schizophrenia with concurrent iron overload. HO-1 inhibitors reduce oxidative damage to whole cells and mitochondrial compartments of rat astrocytes transfected with the HMOX1 gene. Iron reduction within the heme prosthetic moiety of P450 cytochromes in microsomes is facilitated by NADPH-cytochrome P450 oxidoreductase (CPR), while adrenodoxin reductase performs this function in the mitochondria. In partial CPR-deficient conditions, the half-life of apocytochromes is prolonged while HO-1 is induced due to the elevated heme release from unreduced cytochromes. This study posits that, before being degraded by HO-1, the released hemin triggers the oligomerization of cytochromes, as well as other oxidative damages, by producing hydroperoxyl radicals from hydrogen peroxide produced in uncoupling reaction. After reaching a specific level, iron(III) overload may trigger the saturation of CPR, resulting in the development of neuropathologies.<\/jats:p>","DOI":"10.3390\/ijms27156971","type":"journal-article","created":{"date-parts":[[2026,8,3]],"date-time":"2026-08-03T14:16:27Z","timestamp":1785766587000},"page":"6971","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["The Role of Cytochrome P450 Holoenzyme Metabolism in the Origin of Neuropathologies"],"prefix":"10.3390","volume":"27","author":[{"given":"Snje\u017eana","family":"\u0160tambuk","sequence":"first","affiliation":[{"name":"Faculty of Forensic Sciences, University of Split, Ru\u0111era Bo\u0161kovi\u0107a 33, 21000 Split, Croatia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,8,3]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"94","DOI":"10.3390\/jox11030007","article-title":"The Central Role of Cytochrome P450 in Xenobiotic Metabolism-A Brief Review on a Fascinating Enzyme Family","volume":"11","author":"Esteves","year":"2021","journal-title":"J. Xenobiot."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1021\/tx500444e","article-title":"Survey of Human Oxidoreductases and Cytochrome P450 Enzymes Involved in the Metabolism of Xenobiotic and Natural Chemicals","volume":"28","author":"Rendic","year":"2014","journal-title":"Chem. Res. Toxicol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"1223","DOI":"10.1016\/j.bbrc.2012.12.072","article-title":"Oxidase uncoupling in heme monooxygenases: Human cytochrome P450 CYP3A4 in Nanodiscs","volume":"430","author":"Grinkova","year":"2013","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1042\/bj3400453","article-title":"Relationship between cytochrome P450 catalytic cycling and stability: Fast degradation of ethanol-inducible cytochrome P450 2E1 (CYP2E1) in hepatoma cells is abolished by inactivation of its electron donor NADPH-cytochrome P450 reductase","volume":"340","author":"Zhukov","year":"1999","journal-title":"Biochem. J."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1111\/j.1471-4159.2009.06160.x","article-title":"Heme oxygenase-1 and neurodegeneration: Expanding frontiers of engagement","volume":"110","author":"Schipper","year":"2009","journal-title":"J. Neurochem."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"1399","DOI":"10.1046\/j.1471-4159.1995.65031399.x","article-title":"Induction of heme oxygenase-1 mRNA and protein in neocortex and cerebral vessels in Alzheimer\u2019s disease","volume":"65","author":"Premkumar","year":"1995","journal-title":"J. Neurochem."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1111\/j.1471-4159.2012.07914.x","article-title":"Unregulated brain iron deposition in transgenic mice over-expressing HMOX1 in the astrocytic compartment","volume":"123","author":"Song","year":"2012","journal-title":"J. Neurochem."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"10841","DOI":"10.1523\/JNEUROSCI.6469-11.2012","article-title":"Schizophrenia-like features in transgenic mice overexpressing human HO-1 in the astrocytic compartment","volume":"32","author":"Song","year":"2012","journal-title":"J. Neurosci."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1111\/j.1744-9987.2010.00824.x","article-title":"Pathological role of aminolevulinate in uremic patients","volume":"15","author":"Hasuike","year":"2011","journal-title":"Ther. Apher. Dial."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1006\/abbi.1995.1080","article-title":"5-Aminolevulinic acid induces iron release from ferritin","volume":"316","author":"Oteiza","year":"1995","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"1272","DOI":"10.1016\/S0891-5849(00)00437-8","article-title":"Roles of phosphate and an enoyl radical in ferritin iron mobilization by 5-aminolevulinic acid","volume":"29","author":"Rocha","year":"2000","journal-title":"Free Radic. Biol. Med."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1016\/S0003-9861(02)00633-1","article-title":"Oxidative damage to ferritin by 5-aminolevulinic acid","volume":"409","author":"Rocha","year":"2003","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"997","DOI":"10.1089\/ars.2007.1893","article-title":"Intracellular iron transport and storage: From molecular mechanisms to health implications","volume":"10","author":"MacKenzie","year":"2008","journal-title":"Antioxid. Redox Signal."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1016\/j.pharmthera.2011.06.001","article-title":"Drugs in porphyria: From observation to a modern algorithm-based system for the prediction of porphyrogenicity","volume":"132","author":"Hift","year":"2011","journal-title":"Pharmacol. Ther."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"S43","DOI":"10.33549\/physiolres.930000.55.S2.43","article-title":"(Far) Outside the box: Genomic approach to acute porphyria","volume":"55","author":"Thunell","year":"2006","journal-title":"Physiol. Res."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3109\/03602532.2010.515222","article-title":"Cytochrome P450 regulation: The interplay between its heme and apoprotein moieties in synthesis, assembly, repair, and disposal","volume":"43","author":"Correia","year":"2011","journal-title":"Drug Metab. Rev."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1042\/cs0720103","article-title":"\u03b4-Aminolaevulinic acid in plasma, cerebrospinal fluid, saliva and erythrocytes: Studies in normal, uraemic and porphyric subjects","volume":"72","author":"Gorchein","year":"1987","journal-title":"Clin. Sci."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/0009-8981(86)90258-5","article-title":"Measurement of 5-aminolaevulinic acid by reversed phase HPLC and fluorescence detection","volume":"161","author":"Minder","year":"1986","journal-title":"Clin. Chim. Acta"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"2592","DOI":"10.1172\/JCI78031","article-title":"ATF4-dependent induction of heme oxygenase 1 prevents anoikis and promotes metastasis","volume":"125","author":"Dey","year":"2015","journal-title":"J. Clin. Investig."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"7777","DOI":"10.1073\/pnas.1406228111","article-title":"RNAi-mediated silencing of hepatic Alas1 effectively prevents and treats the induced acute attacks in acute intermittent porphyria mice","volume":"111","author":"Yasuda","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1023\/B:BOLI.0000016613.75677.05","article-title":"Homozygous acute intermittent porphyria in a 7-year-old boy with massive excretions of porphyrins and porphyrin precursors","volume":"27","author":"Hessels","year":"2004","journal-title":"J. Inherit. Metab. Dis."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1007\/BF00207051","article-title":"Homozygous acute intermittent porphyria: Compound heterozygosity for adjacent base transitions in the same codon of the porphobilinogen deaminase gene","volume":"89","author":"Llewellyn","year":"1992","journal-title":"Hum. Genet."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"452","DOI":"10.1046\/j.1523-1747.1998.00148.x","article-title":"Homozygous variegate porphyria: Identification of mutations on both alleles of the protoporphyrinogen oxidase gene in a severely affected proband","volume":"110","author":"Frank","year":"1998","journal-title":"J. Investig. Dermatol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"1921","DOI":"10.1093\/hmg\/7.12.1921","article-title":"Molecular characterization of homozygous variegate porphyria","volume":"7","author":"Roberts","year":"1998","journal-title":"Hum. Mol. Genet."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"610","DOI":"10.1046\/j.1523-1747.2001.01293.x","article-title":"Homozygous variegate porphyria: 20 y follow-up and characterization of molecular defect","volume":"116","author":"Kauppinen","year":"2001","journal-title":"J. Investig. Dermatol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"3024","DOI":"10.1073\/pnas.91.8.3024","article-title":"Molecular cloning, sequencing, and functional expression of a cDNA encoding human coproporphyrinogen oxidase","volume":"91","author":"Martasek","year":"1994","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"3089","DOI":"10.1093\/hmg\/ddi342","article-title":"Mutations in human CPO gene predict clinical expression of either hepatic hereditary coproporphyria or erythropoietic harderoporphyria","volume":"14","author":"Schmitt","year":"2005","journal-title":"Hum. Mol. Genet."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1453","DOI":"10.1182\/blood.V91.4.1453","article-title":"Neonatal hemolytic anemia due to inherited harderoporphyria: Clinical characteristics and molecular basis","volume":"91","author":"Lamoril","year":"1998","journal-title":"Blood"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1086\/511444","article-title":"ALAD porphyria is a conformational disease","volume":"80","author":"Jaffe","year":"2007","journal-title":"Am. J. Hum. Genet."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"924","DOI":"10.1016\/S0140-6736(09)61925-5","article-title":"Porphyrias","volume":"375","author":"Puy","year":"2010","journal-title":"Lancet"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"701","DOI":"10.1080\/15287391003614000","article-title":"Porphyrinuria in Korean children with autism: Correlation with oxidative stress","volume":"73","author":"Youn","year":"2010","journal-title":"J. Toxicol. Environ. Health Part A"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1016\/j.taap.2006.04.008","article-title":"Porphyrinuria in childhood autistic disorder: Implications for environmental toxicity","volume":"214","author":"Nataf","year":"2006","journal-title":"Toxicol. Appl. Pharmacol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1349","DOI":"10.1080\/15287390802271723","article-title":"An investigation of porphyrinuria in Australian children with autism","volume":"71","author":"Austin","year":"2008","journal-title":"J. Toxicol. Environ. Health Part A"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1585","DOI":"10.1080\/15287390903232475","article-title":"A prospective blinded evaluation of urinary porphyrins verses the clinical severity of autism spectrum disorders","volume":"72","author":"Geier","year":"2009","journal-title":"J. Toxicol. Environ. Health Part A"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1111\/j.1442-200X.2010.03196.x","article-title":"Toxicity biomarkers in autism spectrum disorder: A blinded study of urinary porphyrins","volume":"53","author":"Kern","year":"2011","journal-title":"Pediatr. Int."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1002\/aur.236","article-title":"Disordered porphyrin metabolism: A potential biological marker for autism risk assessment","volume":"5","author":"Heyer","year":"2012","journal-title":"Autism Res."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1016\/0891-5849(95)02035-7","article-title":"The prooxidant effect of 5-aminolevulinic acid in the brain tissue of rats: Implications in neuropsychiatric manifestations in porphyrias","volume":"20","author":"Demasi","year":"1996","journal-title":"Free Radic. Biol. Med."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1677\/JOE-07-0131","article-title":"Increased metastatic lymph node 64 and CYP17 expression are associated with high stage prostate cancer","volume":"194","author":"Stigliano","year":"2007","journal-title":"J. Endocrinol."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1016\/j.bbamcr.2006.05.005","article-title":"Biosynthesis of heme in mammals","volume":"1763","author":"Ajioka","year":"2006","journal-title":"Biochim. Biophys. Acta (BBA)-Mol. Cell Res."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"831","DOI":"10.1038\/nature08301","article-title":"Function and biogenesis of iron-sulphur proteins","volume":"460","author":"Lill","year":"2009","journal-title":"Nature"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"282","DOI":"10.1006\/abbi.1993.1424","article-title":"5-aminolevulinic acid induces lipid peroxidation in cardiolipin-rich liposomes","volume":"305","author":"Oteiza","year":"1993","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_42","first-page":"201","article-title":"Calcium-dependent mitochondrial oxidative damage promoted by 5-aminolevulinic acid","volume":"1180","author":"Castilho","year":"1992","journal-title":"Biochim. Biophys. Acta (BBA)-Mol. Basis Dis."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/S0005-2728(05)80072-6","article-title":"Damage to rat liver mitochondria promoted by \u03b4-aminolevulinic acid-generated reactive oxygen species: Connections with acute intermittent porphyria and lead-poisoning","volume":"1056","author":"Valle","year":"1991","journal-title":"Biochim. Biophys. Acta (BBA)-Bioenerg."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1016\/0891-5849(95)00015-P","article-title":"How do Ca2+ and 5-aminolevulinic acid-derived oxyradicals promote injury to isolated mitochondria?","volume":"19","year":"1995","journal-title":"Free Radic. Biol. Med."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1006\/abbi.1996.0481","article-title":"\u03b4-Aminolevulinic acid-induced synaptosomal Ca2+ uptake and mitochondrial permeabilization","volume":"335","author":"Penatti","year":"1996","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1146\/annurev.med.49.1.407","article-title":"Angiogenesis and tumor metastasis","volume":"49","author":"Zetter","year":"1998","journal-title":"Annu. Rev. Med."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"726","DOI":"10.1016\/j.molcel.2014.01.013","article-title":"MICU1 and MICU2 Finely Tune the Mitochondrial Ca2+ Uniporter by Exerting Opposite Effects on MCU Activity","volume":"53","author":"Patron","year":"2014","journal-title":"Mol. Cell"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"10479","DOI":"10.1073\/pnas.1300410110","article-title":"Mitochondrial calcium uptake","volume":"110","author":"Williams","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1016\/0005-2728(94)90025-6","article-title":"Oxidative damage of mitochondria induced by 5-aminolevulinic acid: Role of Ca2+ and membrane protein thiols","volume":"1188","author":"Vercesi","year":"1994","journal-title":"Biochim. Biophys. Acta (BBA)-Bioenerg."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"19955","DOI":"10.1016\/S0021-9258(17)45467-6","article-title":"Membrane protein thiol cross-linking associated with the permeabilization of the inner mitochondrial membrane by Ca2+ plus prooxidants","volume":"265","author":"Fagian","year":"1990","journal-title":"J. Biol. Chem."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/j.biocel.2014.03.032","article-title":"Acute intermittent porphyria causes hepatic mitochondrial energetic failure in a mouse model","volume":"51","author":"Homedan","year":"2014","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1016\/j.biochi.2014.08.014","article-title":"Pro-oxidant effect of ALA is implicated in mitochondrial dysfunction of HepG2 cells","volume":"106","author":"Laafi","year":"2014","journal-title":"Biochimie"},{"key":"ref_53","first-page":"2162","article-title":"Autophagy inhibition promotes epithelial-mesenchymal transition through ROS\/HO-1 pathway in ovarian cancer cells","volume":"6","author":"Zhao","year":"2016","journal-title":"Am. J. Cancer Res."},{"key":"ref_54","doi-asserted-by":"crossref","unstructured":"Sripetchwandee, J., Pipatpiboon, N., Chattipakorn, N., and Chattipakorn, S. (2014). Combined therapy of iron chelator and antioxidant completely restores brain dysfunction induced by iron toxicity. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0085115"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"985","DOI":"10.1016\/0006-291X(82)91067-1","article-title":"Evidence for the transcriptional inhibition by heme of the synthesis of \u03b4-aminolevulinate synthase in rat liver","volume":"105","author":"Yamamoto","year":"1982","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"1746","DOI":"10.1016\/S0021-9258(19)86095-7","article-title":"Translocation of delta-aminolevulinate synthase from the cytosol to the mitochondria and its regulation by hemin in the rat liver","volume":"255","author":"Yamauchi","year":"1980","journal-title":"J. Biol. Chem."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1042\/BJ20040570","article-title":"Examination of mitochondrial protein targeting of haem synthetic enzymes: In vivo identification of three functional haem-responsive motifs in 5-aminolaevulinate synthase","volume":"386","author":"Dailey","year":"2005","journal-title":"Biochem. J."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1016\/0006-291X(89)91968-2","article-title":"Regulation of the stability of chicken embryo liver \u03b4-aminolevulinate synthase mRNA by hemin","volume":"162","author":"Drew","year":"1989","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1016\/0003-9861(91)90428-L","article-title":"Heme regulates hepatic 5-aminolevulinate synthase mRNA expression by decreasing mRNA half-life and not by altering its rate of transcription","volume":"289","author":"Hamilton","year":"1991","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1006\/abbi.2000.2117","article-title":"Regulation of heme metabolism in rat hepatocytes and hepatocyte cell lines: \u03b4-aminolevulinic acid synthase and heme oxygenase are regulated by different heme-dependent mechanisms","volume":"384","author":"Cable","year":"2000","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"26424","DOI":"10.1074\/jbc.M110.215772","article-title":"Lon peptidase 1 (LONP1)-dependent breakdown of mitochondrial 5-aminolevulinic acid synthase protein by heme in human liver cells","volume":"286","author":"Tian","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"2391","DOI":"10.1158\/1055-9965.EPI-05-0343","article-title":"Polymorphisms and haplotypes in the cytochrome P450 17A1, prolactin, and catechol-O-methyltransferase genes and non-Hodgkin lymphoma risk","volume":"14","author":"Skibola","year":"2005","journal-title":"Cancer Epidemiol. Biomark. Prev."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"1149","DOI":"10.1042\/bj1261149","article-title":"Stimulation of liver 5-aminolaevulinate synthetase by drugs and its relevance to drug-induced accumulation of cytochrome P-450. Studies with phenylbutazone and 3,5-diethoxycarbonyl-1,4-dihydrocollidine","volume":"126","author":"Gibbs","year":"1972","journal-title":"Biochem. J."},{"key":"ref_64","first-page":"267","article-title":"Expression of 5-aminolaevulinate synthase and cytochrome P-450 mRNAs in chicken embryo hepatocytes in vivo and in culture. Effect of porphyrinogenic drugs and haem","volume":"255","author":"Hamilton","year":"1988","journal-title":"Biochem. J."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"7128","DOI":"10.1046\/j.1432-1327.2000.01815.x","article-title":"Limited heme synthesis in porphobilinogen deaminase-deficient mice impairs transcriptional activation of specific cytochrome P450 genes by phenobarbital","volume":"267","author":"Jover","year":"2000","journal-title":"Eur. J. Biochem."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1042\/bj1960285","article-title":"Effect of allylisopropylacetamide on glutathione metabolism in the rat liver. The possible role of glutathione in the induction of 5-aminolaevulinate synthase","volume":"196","author":"Maines","year":"1981","journal-title":"Biochem. J."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"5466","DOI":"10.1016\/S0021-9258(19)69224-0","article-title":"Cytochrome P-450 heme moiety. The specific target in drug-induced heme alkylation","volume":"256","author":"Correia","year":"1981","journal-title":"J. Biol. Chem."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.1016\/0006-291X(76)90774-9","article-title":"Site of biosynthesis of cytochrome P450 in hepatocytes of phenobarbital treated rats","volume":"71","author":"Negishi","year":"1976","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"965","DOI":"10.1073\/pnas.77.2.965","article-title":"Synthesis and insertion of cytochrome P-450 into endoplasmic reticulum membranes","volume":"77","author":"Kreibich","year":"1980","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1042\/bj2810577","article-title":"Phenobarbital induction of cytochrome P-450 gene expression","volume":"281","author":"Waxman","year":"1992","journal-title":"Biochem. J."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"1025","DOI":"10.1016\/0020-711X(89)90235-8","article-title":"Coordinate elevations of liver \u03b4-aminolevulinate synthase and cytochrome P-450 RNA by phenobarbital in chicken embryos: The effects of heme","volume":"21","author":"Ryan","year":"1989","journal-title":"Int. J. Biochem."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1146\/annurev.pharmtox.41.1.123","article-title":"Phenobarbital response elements of cytochrome P450 genes and nuclear receptors","volume":"41","author":"Sueyoshi","year":"2001","journal-title":"Annu. Rev. Pharmacol. Toxicol."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"7559","DOI":"10.1074\/jbc.M008090200","article-title":"Chromatin assembly enhances binding to the CYP2B1 phenobarbital-responsive unit (PBRU) of nuclear factor-1, which binds simultaneously with constitutive androstane receptor (CAR)\/retinoid X receptor (RXR) and enhances CAR\/RXR-mediated activation of the PBRU","volume":"276","author":"Kim","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1007\/BF02353475","article-title":"Cytochrome P4503A (CYP3A) metabolism: Prediction of in vivo activity in humans","volume":"24","author":"Wilkinson","year":"1996","journal-title":"J. Pharmacokinet. Biopharm."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"9127","DOI":"10.1073\/pnas.0401845101","article-title":"Identification of the xenosensors regulating human 5-aminolevulinate synthase","volume":"101","author":"Podvinec","year":"2004","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"34717","DOI":"10.1074\/jbc.M204699200","article-title":"Drugs mediate the transcriptional activation of the 5-aminolevulinic acid synthase (ALAS1) gene via the chicken xenobiotic-sensing nuclear receptor (CXR)","volume":"277","author":"Fraser","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"39392","DOI":"10.1074\/jbc.M306148200","article-title":"Nuclear receptors constitutive androstane receptor and pregnane X receptor activate a drug-responsive enhancer of the murine 5-aminolevulinic acid synthase gene","volume":"278","author":"Fraser","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"5522","DOI":"10.1210\/en.2012-1334","article-title":"Nuclear receptor 5A (NR5A) family regulates 5-aminolevulinic acid synthase 1 (ALAS1) gene expression in steroidogenic cells","volume":"153","author":"Ju","year":"2012","journal-title":"Endocrinology"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"1960","DOI":"10.1002\/hep.21879","article-title":"Regulation of human liver \u03b4-aminolevulinic acid synthase by bile acids","volume":"46","author":"Peyer","year":"2007","journal-title":"Hepatology"},{"key":"ref_80","first-page":"20","article-title":"Functional analysis of the 5\u2032 regulatory region of the 5-aminolevulinate synthase (ALAS1) gene in response to estrogen","volume":"55","author":"Kimberg","year":"2009","journal-title":"Cell. Mol. Biol."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"2750","DOI":"10.1016\/S0021-9258(19)41665-7","article-title":"Induction of delta-aminolevulinic acid synthetase in isolated rat liver cells by steroids","volume":"250","author":"Edwards","year":"1975","journal-title":"J. Biol. Chem."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1016\/0014-5793(83)80430-X","article-title":"The effect of N-methylprotoporphyrin and succinyl-acetone on the regulation of heme biosynthesis in chicken hepatocytes in culture","volume":"159","author":"Marks","year":"1983","journal-title":"FEBS Lett."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"5216","DOI":"10.1093\/emboj\/cdf516","article-title":"Hemoprotein Bach1 regulates enhancer availability of heme oxygenase-1 gene","volume":"21","author":"Sun","year":"2002","journal-title":"EMBO J."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1042\/bj2500189","article-title":"Regulation of hepatic haem metabolism. Disparate mechanisms of induction of haem oxygenase by drugs and metals","volume":"250","author":"Lincoln","year":"1988","journal-title":"Biochem. J."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1111\/joim.12750","article-title":"Recurrent attacks of acute hepatic porphyria: Major role of the chronic inflammatory response in the liver","volume":"284","author":"Schmitt","year":"2018","journal-title":"J. Intern. Med."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"e0013","DOI":"10.5041\/RMMJ.10333","article-title":"Porphyria: What Is It and Who Should Be Evaluated?","volume":"9","author":"Edel","year":"2018","journal-title":"Rambam Maimonides Med. J."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"500","DOI":"10.1016\/0016-5085(93)90726-S","article-title":"Tin protoporphyrin prolongs the biochemical remission produced by heme arginate in acute hepatic porphyria","volume":"105","author":"Dover","year":"1993","journal-title":"Gastroenterology"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"1325","DOI":"10.1053\/j.gastro.2014.01.053","article-title":"Heme exporter FLVCR1a regulates heme synthesis and degradation and controls activity of cytochromes P450","volume":"146","author":"Vinchi","year":"2014","journal-title":"Gastroenterology"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"366","DOI":"10.1016\/j.freeradbiomed.2012.03.007","article-title":"Sustained expression of heme oxygenase-1 alters iron homeostasis in nonerythroid cells","volume":"53","author":"Li","year":"2012","journal-title":"Free Radic. Biol. Med."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"532","DOI":"10.1111\/j.1471-4159.2006.04230.x","article-title":"Induction of haem oxygenase-1 causes cortical non-haem iron increase in experimental pneumococcal meningitis: Evidence that concomitant ferritin up-regulation prevents iron-induced oxidative damage","volume":"100","author":"Ren","year":"2007","journal-title":"J. Neurochem."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"14807","DOI":"10.1073\/pnas.192585799","article-title":"Heme deficiency may be a factor in the mitochondrial and neuronal decay of aging","volume":"99","author":"Atamna","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1007\/BF03033339","article-title":"Glial HO-1 expression, iron deposition and oxidative stress in neurodegenerative diseases","volume":"1","author":"Schipper","year":"1999","journal-title":"Neurotox. Res."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"4896","DOI":"10.3390\/ijms13044896","article-title":"Risk-association of CYP11A1 polymorphisms and breast cancer among Han Chinese women in Southern China","volume":"13","author":"Sun","year":"2012","journal-title":"Int. J. Mol. Sci."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"655","DOI":"10.1002\/jcp.20509","article-title":"Over-expression of heme oxygenase-1 promotes oxidative mitochondrial damage in rat astroglia","volume":"206","author":"Song","year":"2006","journal-title":"J. Cell. Physiol."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"424","DOI":"10.2174\/156720509789207985","article-title":"Suppression of glial HO-1 activity as a potential neurotherapeutic intervention in AD","volume":"6","author":"Schipper","year":"2009","journal-title":"Curr. Alzheimer Res."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"758","DOI":"10.1002\/ana.410370609","article-title":"Expression of heme oxygenase-1 in the senescent and Alzheimer-diseased brain","volume":"37","author":"Schipper","year":"1995","journal-title":"Ann. Neurol."},{"key":"ref_97","first-page":"42","article-title":"Heme oxygenase-1 is associated with the neurofibrillary pathology of Alzheimer\u2019s disease","volume":"145","author":"Smith","year":"1994","journal-title":"Am. J. Pathol."},{"key":"ref_98","first-page":"955","article-title":"Variation in the CYP19A1 gene and risk of colon and rectal cancer","volume":"22","author":"Slattery","year":"2011","journal-title":"Cancer Causes Control"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"299","DOI":"10.3233\/JAD-2011-102061","article-title":"Long-term overexpression of heme oxygenase 1 promotes tau aggregation in mouse brain by inducing tau phosphorylation","volume":"26","author":"Hui","year":"2011","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"519","DOI":"10.3233\/JAD-140567","article-title":"Overexpression of Heme Oxygenase 1 Causes Cognitive Decline and Affects Pathways for Tauopathy in Mice","volume":"43","author":"Wang","year":"2014","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1016\/j.expneurol.2014.01.006","article-title":"Astroglial heme oxygenase-1 and the origin of corpora amylacea in aging and degenerating neural tissues","volume":"254","author":"Song","year":"2014","journal-title":"Exp. Neurol."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"778","DOI":"10.1111\/jnc.12927","article-title":"Neurotherapeutic effects of novel HO-1 inhibitors in vitro and in a transgenic mouse model of Alzheimer\u2019s disease","volume":"131","author":"Gupta","year":"2014","journal-title":"J. Neurochem."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"3017","DOI":"10.1523\/JNEUROSCI.21-09-03017.2001","article-title":"Mitochondrial abnormalities in Alzheimer\u2019s disease","volume":"21","author":"Hirai","year":"2001","journal-title":"J. Neurosci."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1016\/j.freeradbiomed.2012.11.014","article-title":"Mitochondrial defects and oxidative stress in Alzheimer disease and Parkinson disease","volume":"62","author":"Yan","year":"2013","journal-title":"Free Radic. Biol. Med."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"1217","DOI":"10.1089\/ars.2017.7134","article-title":"Multifaceted Roles of Glutathione and Glutathione-Based Systems in Carcinogenesis and Anticancer Drug Resistance","volume":"27","author":"Hatem","year":"2017","journal-title":"Antioxid. Redox Signal."},{"key":"ref_106","first-page":"201","article-title":"Evidence of Mitochondrial Dysfunction within the Complex Genetic Etiology of Schizophrenia","volume":"1","author":"Hjelm","year":"2015","journal-title":"Mol. Neuropsychiatry"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1016\/j.bbadis.2009.10.006","article-title":"Mitochondrial dysfunction is a trigger of Alzheimer\u2019s disease pathophysiology","volume":"1802","author":"Moreira","year":"2010","journal-title":"Biochim. Biophys. Acta (BBA)-Mol. Basis Dis."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1158\/1078-0432.CCR-12-2812","article-title":"Molecular markers in key steroidogenic pathways, circulating steroid levels, and prostate cancer progression","volume":"19","author":"Huang","year":"2013","journal-title":"Clin. Cancer Res."},{"key":"ref_109","doi-asserted-by":"crossref","unstructured":"Cho, L.Y., Yang, J.J., Ko, K.P., Ma, S.H., Shin, A., Choi, B.Y., Han, D.S., Song, K.S., Kim, Y.S., and Chang, S.H. (2012). Genetic susceptibility factors on genes involved in the steroid hormone biosynthesis pathway and progesterone receptor for gastric cancer risk. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0047603"},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"879","DOI":"10.3233\/JAD-2009-1010","article-title":"Iron toxicity in diseases of aging: Alzheimer\u2019s disease, Parkinson\u2019s disease and atherosclerosis","volume":"16","author":"Altamura","year":"2009","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"S551","DOI":"10.3233\/JAD-2010-100354","article-title":"Mitochondrial iron metabolism and its role in neurodegeneration","volume":"20","author":"Horowitz","year":"2010","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1016\/j.bcp.2013.11.022","article-title":"Common defects of mitochondria and iron in neurodegeneration and diabetes (MIND): A paradigm worth exploring","volume":"88","author":"Stroh","year":"2014","journal-title":"Biochem. Pharmacol."},{"key":"ref_113","doi-asserted-by":"crossref","unstructured":"Ashraf, A., Clark, M., and So, P.W. (2018). The Aging of Iron Man. Front. Aging Neurosci., 10.","DOI":"10.3389\/fnagi.2018.00065"},{"key":"ref_114","doi-asserted-by":"crossref","unstructured":"Chen, J., Marks, E., Lai, B., Zhang, Z., Duce, J.A., Lam, L.Q., Volitakis, I., Bush, A.I., Hersch, S., and Fox, J.H. (2013). Iron accumulates in Huntington\u2019s disease neurons: Protection by deferoxamine. PLoS ONE, 8, Correction in PLoS ONE\u00a02013, 8, 11.","DOI":"10.1371\/annotation\/67f555f5-35b7-4468-8bab-26d518942803"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.jsbmb.2007.05.021","article-title":"Aromatase and COX in breast cancer: Enzyme inhibitors and beyond","volume":"106","author":"Brueggemeier","year":"2007","journal-title":"J. Steroid Biochem. Mol. Biol."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1111\/j.1471-4159.2011.07536.x","article-title":"Pathogenic implications of iron accumulation in multiple sclerosis","volume":"120","author":"Williams","year":"2012","journal-title":"J. Neurochem."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1016\/0022-510X(95)00037-3","article-title":"Aluminum, calcium, and iron in the spinal cord of patients with sporadic amyotrophic lateral sclerosis using laser microprobe mass spectroscopy: A preliminary study","volume":"130","author":"Kasarskis","year":"1995","journal-title":"J. Neurol. Sci."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1176\/jnp.4.1.36","article-title":"Staining intensity of brain iron in patients with schizophrenia: A postmortem study","volume":"4","author":"Casanova","year":"1992","journal-title":"J. Neuropsychiatry Clin. Neurosci."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"S360","DOI":"10.1016\/S1344-6223(02)00133-5","article-title":"Age-associated increases in heme oxygenase-1 and ferritin immunoreactivity in the autopsied brain","volume":"5","author":"Hirose","year":"2003","journal-title":"Leg. Med."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"36","DOI":"10.3109\/02699052.2015.1084648","article-title":"Dual effects of heme oxygenase-1 on astrocyte injury induced by hemin in vitro","volume":"30","author":"Chen","year":"2016","journal-title":"Brain Inj."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1007\/s11064-015-1795-7","article-title":"Uptake and Toxicity of Hemin and Iron in Cultured Mouse Astrocytes","volume":"41","author":"Owen","year":"2016","journal-title":"Neurochem. Res."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"3381","DOI":"10.1073\/pnas.0600134103","article-title":"Amyloid-\u03b2 peptide binds with heme to form a peroxidase: Relationship to the cytopathologies of Alzheimer\u2019s disease","volume":"103","author":"Atamna","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"3359","DOI":"10.1007\/s00216-014-7822-8","article-title":"Characterization of the enhanced peroxidatic activity of amyloid \u03b2 peptide-hemin complexes towards neurotransmitters","volume":"406","author":"Neumann","year":"2014","journal-title":"Anal. Bioanal. Chem."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1186\/2051-5960-1-83","article-title":"A central role for dityrosine crosslinking of Amyloid-\u03b2 in Alzheimer\u2019s disease","volume":"1","author":"Williams","year":"2013","journal-title":"Acta Neuropathol. Commun."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"3765","DOI":"10.1016\/0006-2952(83)90147-8","article-title":"Effect of heme on allylisopropylacetamide-induced changes in heme and drug metabolism in the rhesus monkey (Macaca mulatta)","volume":"32","author":"Eiseman","year":"1983","journal-title":"Biochem. Pharmacol."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1111\/j.1600-0773.1987.tb01718.x","article-title":"Barbiturate and ethanol sleeping times and pharmacokinetics of propranolol in mice after intravenous administration of haem arginate","volume":"60","author":"Tokola","year":"1987","journal-title":"Pharmacol. Toxicol."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1111\/j.1476-5381.1987.tb11218.x","article-title":"Effects of repeated intravenous administration of haem arginate upon hepatic metabolism of foreign compounds in rats and dogs","volume":"90","author":"Tokola","year":"1987","journal-title":"Br. J. Pharmacol."},{"key":"ref_128","first-page":"39","article-title":"The induction of heme oxidation in various tissues by trace metals: Evidence for the catabolism of endogenous heme by hepatic heme oxygenase","volume":"8","author":"Maines","year":"1976","journal-title":"Ann. Clin. Res."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1056\/NEJM198408233110818","article-title":"Instability of hematin solutions","volume":"311","author":"Mendenhall","year":"1984","journal-title":"N. Engl. J. Med."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1016\/S0021-9673(00)96276-9","article-title":"High-performance liquid chromatographic analysis of \u201cavailable\u201d hemin in hematin solutions","volume":"283","author":"Bauer","year":"1984","journal-title":"J. Chromatogr. A"},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1056\/NEJM198607243150406","article-title":"Instability of hematin used in the treatment of acute hepatic porphyria","volume":"315","author":"Goetsch","year":"1986","journal-title":"N. Engl. J. Med."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"213","DOI":"10.2131\/jts.25.3_213","article-title":"Sex-related effect of hemin on cytochrome P450 and drug-metabolizing enzymes in rat liver","volume":"25","author":"Kobayashi","year":"2000","journal-title":"J. Toxicol. Sci."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"4685","DOI":"10.1046\/j.1432-1327.2000.01519.x","article-title":"Regulation of the expression of human ferrochelatase by intracellular iron levels","volume":"267","author":"Taketani","year":"2000","journal-title":"Eur. J. Biochem."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"31340","DOI":"10.1074\/jbc.M303158200","article-title":"Yeast frataxin sequentially chaperones and stores iron by coupling protein assembly with iron oxidation","volume":"278","author":"Park","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_135","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":"ref_136","doi-asserted-by":"crossref","first-page":"853","DOI":"10.1042\/CS20160072","article-title":"Frataxin and the molecular mechanism of mitochondrial iron-loading in Friedreich\u2019s ataxia","volume":"130","author":"Chiang","year":"2016","journal-title":"Clin. Sci."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"1709","DOI":"10.1126\/science.276.5319.1709","article-title":"Regulation of mitochondrial iron accumulation by Yfh1p, a putative homolog of frataxin","volume":"276","author":"Babcock","year":"1997","journal-title":"Science"},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"16381","DOI":"10.1073\/pnas.0906784106","article-title":"Elucidation of the mechanism of mitochondrial iron loading in Friedreich\u2019s ataxia by analysis of a mouse mutant","volume":"106","author":"Huang","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/j.freeradbiomed.2015.03.014","article-title":"Mitoferrin modulates iron toxicity in a Drosophila model of Friedreich\u2019s ataxia","volume":"85","author":"Navarro","year":"2015","journal-title":"Free Radic. Biol. Med."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1016\/0891-5849(94)90095-7","article-title":"Hydrogen peroxide-mediated inactivation of microsomal cytochrome P450 during monooxygenase reactions","volume":"17","author":"Karuzina","year":"1994","journal-title":"Free Radic. Biol. Med."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"620","DOI":"10.1016\/S0891-5849(98)00252-4","article-title":"Heme and apoprotein modification of cytochrome P450 2B4 during its oxidative inactivation in monooxygenase reconstituted system","volume":"26","author":"Karuzina","year":"1999","journal-title":"Free Radic. Biol. Med."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"14741","DOI":"10.1021\/bi9719399","article-title":"Kinetics of ferric cytochrome P450 reduction by NADPH-cytochrome P450 reductase: Rapid reduction in the absence of substrate and variations among cytochrome P450 systems","volume":"36","author":"Guengerich","year":"1997","journal-title":"Biochemistry"},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/j.pharmthera.2013.01.010","article-title":"NADPH P450 oxidoreductase: Structure, function, and pathology of diseases","volume":"138","author":"Pandey","year":"2013","journal-title":"Pharmacol. Ther."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"1375","DOI":"10.1016\/S0021-9258(18)60338-2","article-title":"A new cytochrome in liver microsomes","volume":"237","author":"Omura","year":"1962","journal-title":"J. Biol. Chem."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1016\/S0021-9258(19)43095-0","article-title":"Cytochrome P-450cam: I. Crystalization and properties","volume":"249","author":"Yu","year":"1974","journal-title":"J. Biol. Chem."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"25895","DOI":"10.1074\/jbc.M303125200","article-title":"Liver-specific deletion of the NADPH-cytochrome P450 reductase gene: Impact on plasma cholesterol homeostasis and the function and regulation of microsomal cytochrome P450 and heme oxygenase","volume":"278","author":"Gu","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"6536","DOI":"10.1074\/jbc.M111408200","article-title":"Association of multiple developmental defects and embryonic lethality with loss of microsomal NADPH-cytochrome P450 oxidoreductase","volume":"277","author":"Shen","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1124\/jpet.104.073353","article-title":"Transgenic mice with a hypomorphic NADPH-cytochrome P450 reductase gene: Effects on development, reproduction, and microsomal cytochrome P450","volume":"312","author":"Wu","year":"2005","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1016\/j.neulet.2013.05.043","article-title":"Suppression of cytochrome P450 reductase expression promotes astrocytosis in subventricular zone of adult mice","volume":"548","author":"Yao","year":"2013","journal-title":"Neurosci. Lett."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1016\/0896-6273(91)90052-2","article-title":"The molecular pathology of Alzheimer\u2019s disease","volume":"6","author":"Selkoe","year":"1991","journal-title":"Neuron"},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"722","DOI":"10.1177\/0004867414531078","article-title":"Increased expression of astrocyte markers in schizophrenia: Association with neuroinflammation","volume":"48","author":"Catts","year":"2014","journal-title":"Aust. N. Z. J. Psychiatry"},{"key":"ref_152","first-page":"397","article-title":"Trapezoidocephaly, midfacial hypoplasia and cartilage abnormalities with multiple synostoses and skeletal fractures","volume":"11","author":"Antley","year":"1975","journal-title":"Birth Defects Orig. Artic. Ser."},{"key":"ref_153","doi-asserted-by":"crossref","unstructured":"Panda, S.P., Guntur, A.R., Polusani, S.R., Fajardo, R.J., Gakunga, P.T., Roman, L.J., and Masters, B.S. (2013). Conditional deletion of cytochrome p450 reductase in osteoprogenitor cells affects long bone and skull development in mice recapitulating antley-bixler syndrome: Role of a redox enzyme in development. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0075638"},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"919","DOI":"10.1530\/EJE-10-0764","article-title":"Impaired hepatic drug and steroid metabolism in congenital adrenal hyperplasia due to P450 oxidoreductase deficiency","volume":"163","author":"Maiter","year":"2010","journal-title":"Eur. J. Endocrinol."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"E453","DOI":"10.1210\/jc.2010-1607","article-title":"Pubertal presentation in seven patients with congenital adrenal hyperplasia due to P450 oxidoreductase deficiency","volume":"96","author":"Idkowiak","year":"2011","journal-title":"J. Clin. Endocrinol. Metab."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"859","DOI":"10.1016\/j.psyneuen.2009.01.002","article-title":"Cortisol response to a psychosocial stressor in schizophrenia: Blunted, delayed, or normal?","volume":"34","author":"Brenner","year":"2009","journal-title":"Psychoneuroendocrinology"},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1016\/j.psychres.2012.12.021","article-title":"Hypothalamic-pituitary-adrenal axis dysfunction in non-clinical psychosis","volume":"206","author":"Mittal","year":"2013","journal-title":"Psychiatry Res."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1093\/schbul\/sbq062","article-title":"Impaired neuroendocrine and immune response to acute stress in medication-naive patients with a first episode of psychosis","volume":"38","author":"Fluitman","year":"2012","journal-title":"Schizophr. Bull."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1007\/s12094-017-1738-7","article-title":"High expression of HO-1 predicts poor prognosis of ovarian cancer patients and promotes proliferation and aggressiveness of ovarian cancer cells","volume":"20","author":"Zhao","year":"2017","journal-title":"Clin. Transl. Oncol."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"3063","DOI":"10.1016\/0006-2952(83)90250-2","article-title":"Selenium and drug metabolism\u2014I: Multiple modulations of mouse liver enzymes","volume":"32","author":"Reiter","year":"1983","journal-title":"Biochem. Pharmacol."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"6203","DOI":"10.1016\/S0021-9258(17)34600-8","article-title":"Rapid stimulation of hepatic microsomal heme oxygenase in selenium-deficient rats. An effect of phenobarbital","volume":"253","author":"Correia","year":"1978","journal-title":"J. Biol. Chem."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1042\/bj1680105","article-title":"Accelerated hepatic haem catabolism in the selenium-deficient rat","volume":"168","author":"Burk","year":"1977","journal-title":"Biochem. J."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"3294","DOI":"10.1016\/S0021-9258(19)50730-X","article-title":"Thyroid hormone stimulation of NADPH P450 reductase expression in liver and extrahepatic tissues. Regulation by multiple mechanisms","volume":"267","author":"Ram","year":"1992","journal-title":"J. Biol. Chem."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"9557","DOI":"10.1016\/S0021-9258(17)42736-0","article-title":"Dissociation of heme metabolic activities from the microsomal cytochrome P-450 turnover in testis of hypophysectomized rats","volume":"259","author":"Maines","year":"1984","journal-title":"J. Biol. Chem."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1016\/S0026-895X(25)11248-0","article-title":"Hypophysectomy differentially alters P-450 protein levels and enzyme activities in rat liver: Pituitary control of hepatic NADPH cytochrome P-450 reductase","volume":"35","author":"Waxman","year":"1989","journal-title":"Mol. Pharmacol."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"715","DOI":"10.1210\/me.2010-0236","article-title":"Transcriptional regulation of the human P450 oxidoreductase gene: Hormonal regulation and influence of promoter polymorphisms","volume":"25","author":"Tee","year":"2011","journal-title":"Mol. Endocrinol."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1124\/mol.52.1.46","article-title":"Thyroid regulation of NADPH:cytochrome P450 oxidoreductase: Identification of a thyroid-responsive element in the 5\u2032-flank of the oxidoreductase gene","volume":"52","author":"Li","year":"1997","journal-title":"Mol. Pharmacol."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1016\/0304-4165(91)90057-N","article-title":"Studies on the decrease of liver cytochrome P-450 content by triiodothyronine","volume":"1074","author":"Sancovich","year":"1991","journal-title":"Biochim. Biophys. Acta (BBA)-Gen. Subj."},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1016\/0006-291X(89)92476-5","article-title":"Thyroid hormone suppression of hepatic levels of phenobarbital-inducible P-450b and P-450e and other neonatal P-450s in hypophysectomized rats","volume":"160","author":"Yamazoe","year":"1989","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1042\/bj3560613","article-title":"Human NADPH-P450 oxidoreductase modulates the level of cytochrome P450 CYP2D6 holoprotein via haem oxygenase-dependent and -independent pathways","volume":"356","author":"Ding","year":"2001","journal-title":"Biochem. J."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1006\/abbi.1996.0468","article-title":"Expression and coupling of human cytochrome P450 2E1 and NADPH-cytochrome P450 oxidoreductase in dual expression and co-infection systems with baculovirus in insect cells","volume":"334","author":"Wang","year":"1996","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1006\/abbi.1997.0405","article-title":"High levels of recombinant CYP3A4 expression in Chinese hamster ovary cells are modulated by coexpressed human P450 reductase and hemin supplementation","volume":"348","author":"Ding","year":"1997","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/j.tem.2011.10.003","article-title":"Aromatase, breast cancer and obesity: A complex interaction","volume":"23","author":"Bulun","year":"2012","journal-title":"Trends Endocrinol. Metab."},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1080\/00498250412331281089","article-title":"Comparative inhibition of inducible and constitutive CYPs in rat hepatic microsomes by parathion","volume":"34","author":"Murray","year":"2004","journal-title":"Xenobiotica"},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1124\/jpet.102.033837","article-title":"Expression and induction of CYP2C P450 enzymes in primary cultures of human hepatocytes","volume":"302","author":"Raucy","year":"2002","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/0026-0495(71)90091-6","article-title":"Biochemical and genetic factors influencing drug metabolism. Influence of hepatic microsomal mixed function oxidation reactions on cellular metabolic control","volume":"20","author":"Estabrook","year":"1971","journal-title":"Metabolism"},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"579","DOI":"10.2217\/pgs.09.7","article-title":"Pharmacogenomics of human liver cytochrome P450 oxidoreductase: Multifactorial analysis and impact on microsomal drug oxidation","volume":"10","author":"Gomes","year":"2009","journal-title":"Pharmacogenomics"},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"6","DOI":"10.2174\/187231211794455253","article-title":"Inhibition of cytochrome P450 1A2-mediated metabolism and production of reactive oxygen species by heme oxygenase-1 in rat liver microsomes","volume":"5","author":"Reed","year":"2011","journal-title":"Drug Metab. Lett."},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1016\/j.abb.2011.06.008","article-title":"Mutations of human cytochrome P450 reductase differentially modulate heme oxygenase-1 activity and oligomerization","volume":"513","author":"Marohnic","year":"2011","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"1321","DOI":"10.1093\/oxfordjournals.jbchem.a135399","article-title":"Incorporation of heme to microsomal cytochrome P-450 in the absence of protein biosynthesis","volume":"98","author":"Sadano","year":"1985","journal-title":"J. Biochem."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"1808","DOI":"10.1111\/j.1476-5381.2009.00461.x","article-title":"3-methylcholanthrene and benzo(a)pyrene modulate cardiac cytochrome P-450 gene expression and arachidonic acid metabolism in male Sprague Dawley rats","volume":"158","author":"Aboutabl","year":"2009","journal-title":"Br. J. Pharmacol."},{"key":"ref_182","first-page":"633","article-title":"Hydrodynamic studies on the association of cytochrome P-450","volume":"42","author":"Wendel","year":"1983","journal-title":"Biomed. Biochim. Acta"},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1016\/0014-5793(86)80861-4","article-title":"Quaternary structure of the liver microsomal cytochrome P-450","volume":"205","author":"Tsuprun","year":"1986","journal-title":"FEBS Lett."},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"717","DOI":"10.3109\/00498258209038946","article-title":"Cytochrome P-450 rotamers control mixed-function oxygenation in reconstituted membranes. Rotational diffusion studied by delayed fluorescence depolarizationd`","volume":"12","author":"Greinert","year":"1982","journal-title":"Xenobiotica"},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"7023","DOI":"10.1016\/S0021-9258(18)34532-0","article-title":"Rotation of cytochrome P-450. I. Investigations of protein-protein interactions of cytochrome P-450 in phospholipid vesicles and liver microsomes","volume":"257","author":"Kawato","year":"1982","journal-title":"J. Biol. Chem."},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1016\/0006-291X(90)91373-Z","article-title":"Membrane topology of microsomal cytochrome P-450: Saturation transfer EPR and freeze-fracture electron microscopy studies","volume":"171","author":"Schwarz","year":"1990","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1016\/S0021-9258(17)35233-X","article-title":"Interactions among cytochromes P-450 in the endoplasmic reticulum. Detection of chemically cross-linked complexes with monoclonal antibodies","volume":"266","author":"Alston","year":"1991","journal-title":"J. Biol. Chem."},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"31269","DOI":"10.1074\/jbc.M301489200","article-title":"Fluorescence resonance energy transfer analysis of cytochromes P450 2C2 and 2E1 molecular interactions in living cells","volume":"278","author":"Mallah","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"9456","DOI":"10.1021\/bi990584l","article-title":"Complex formation in vesicle-reconstituted mitochondrial cytochrome P450 systems (CYP11A1 and CYP11B1) as evidenced by rotational diffusion experiments using EPR and ST-EPR","volume":"38","author":"Schwarz","year":"1999","journal-title":"Biochemistry"},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/0006-291X(82)91699-0","article-title":"Hydrodynamic properties of monomeric cytochromes P-450LM2 and P-450LM4 in n-octylglucoside solution","volume":"107","author":"Dean","year":"1982","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"3850","DOI":"10.1074\/jbc.M114.615443","article-title":"Interactions among cytochromes P450 in microsomal membranes: Oligomerization of cytochromes P450 3A4, 3A5, and 2E1 and its functional consequences","volume":"290","author":"Davydov","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1042\/BJ20120636","article-title":"Effect of homomeric P450-P450 complexes on P450 function","volume":"446","author":"Reed","year":"2012","journal-title":"Biochem. J."},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"8588","DOI":"10.1016\/S0021-9258(18)32096-9","article-title":"Rotation of cytochrome P-450. Complex formation of cytochrome P-450 with NADPH-cytochrome P-450 reductase in liposomes demonstrated by combining protein rotation with antibody-induced cross-linking","volume":"258","author":"Gut","year":"1983","journal-title":"J. Biol. Chem."},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"10113","DOI":"10.1021\/bi00032a003","article-title":"Dynamic interactions of rabbit liver cytochromes P450IA2 and P450IIB4 with cytochrome b5 and NADPH-cytochrome P450 reductase in proteoliposomes","volume":"34","author":"Yamada","year":"1995","journal-title":"Biochemistry"},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"12852","DOI":"10.1021\/bi980674a","article-title":"Interactions among P450 enzymes when combined in reconstituted systems: Formation of a 2B4-1A2 complex with a high affinity for NADPH-cytochrome P450 reductase","volume":"37","author":"Backes","year":"1998","journal-title":"Biochemistry"},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1124\/dmd.117.078642","article-title":"Characterization of Interactions Among CYP1A2, CYP2B4, and NADPH-cytochrome P450 Reductase: Identification of Specific Protein Complexes","volume":"46","author":"Connick","year":"2018","journal-title":"Drug Metab. Dispos."},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1042\/bj2220453","article-title":"Formation of cytochrome P-450 containing haem or cobalt-protoporphyrin in liver homogenates of rats treated with phenobarbital and allylisopropylacetamide","volume":"222","author":"Bonkovsky","year":"1984","journal-title":"Biochem. J."},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"2379","DOI":"10.1016\/S0021-9258(20)82245-5","article-title":"The carbon monoxide-binding pigment of liver microsomes: II. Solubilization, purification, and protperties","volume":"239","author":"Omura","year":"1964","journal-title":"J. Biol. Chem."},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1016\/S0021-9258(19)43096-2","article-title":"Cytochrome P-450cam. II. Interconversion with P-420","volume":"249","author":"Yu","year":"1974","journal-title":"J. Biol. Chem."},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"14530","DOI":"10.1021\/bi961511u","article-title":"Probing the heme iron coordination structure of pressure-induced cytochrome P420cam","volume":"35","author":"Martinis","year":"1996","journal-title":"Biochemistry"},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"253","DOI":"10.3109\/10408363.2015.1136259","article-title":"Glutathione in metastases: From mechanisms to clinical applications","volume":"53","author":"Estrela","year":"2016","journal-title":"Crit. Rev. Clin. Lab. Sci."},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"11287","DOI":"10.1158\/0008-5472.CAN-05-2737","article-title":"Aromatase inhibitors in human lung cancer therapy","volume":"65","author":"Weinberg","year":"2005","journal-title":"Cancer Res."},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"4417","DOI":"10.1158\/1078-0432.CCR-07-1950","article-title":"Intratumoral estrogens and estrogen receptors in human non-small cell lung carcinoma","volume":"14","author":"Niikawa","year":"2008","journal-title":"Clin. Cancer Res."},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1016\/S0021-9258(19)43097-4","article-title":"Cytochrome P-450cam. III. Removal and replacement of ferriprotoporphyrin IX","volume":"249","author":"Yu","year":"1974","journal-title":"J. Biol. Chem."},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"460","DOI":"10.1016\/S0090-9556(25)07748-7","article-title":"Selective inactivation of rat lung and liver microsomal NADPH-cytochrome c reductase by acrolein","volume":"12","author":"Patel","year":"1984","journal-title":"Drug Metab. Dispos."},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"39872","DOI":"10.1074\/jbc.M406912200","article-title":"Glutathione is required to regulate the formation of native disulfide bonds within proteins entering the secretory pathway","volume":"279","author":"Chakravarthi","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_207","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1016\/0005-2736(80)90188-1","article-title":"Incorporation of purified components of the rabbit liver microsomal hydroxylase system into phospholipid vesicles","volume":"599","author":"Glaumann","year":"1980","journal-title":"Biochim. Biophys. Acta (BBA)-Biomembr."},{"key":"ref_208","doi-asserted-by":"crossref","first-page":"204","DOI":"10.1016\/S0026-895X(25)13845-5","article-title":"Studies on heme transfer from microsomal hemoproteins to heme-binding plasma proteins","volume":"10","author":"Maines","year":"1974","journal-title":"Mol. Pharmacol."},{"key":"ref_209","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1016\/0003-9861(95)90017-9","article-title":"High-pressure-induced transitions in microsomal cytochrome P450 2B4 in solution: Evidence for conformational inhomogeneity in the oligomers","volume":"320","author":"Davydov","year":"1995","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_210","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1042\/bj1640295","article-title":"Role of haem in the synthesis and assembly of cytochrome P-450","volume":"164","author":"Bhat","year":"1977","journal-title":"Biochem. J."},{"key":"ref_211","doi-asserted-by":"crossref","first-page":"1013","DOI":"10.1016\/S0006-291X(83)80243-5","article-title":"Reversible transfer of heme between different molecular species of microsome-bound cytochrome P-450 in rat liver","volume":"116","author":"Sadano","year":"1983","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_212","doi-asserted-by":"crossref","first-page":"1375","DOI":"10.1093\/oxfordjournals.jbchem.a134272","article-title":"Turnover of two drug-inducible forms of microsomal cytochrome P-450 in rat liver","volume":"93","author":"Sadano","year":"1983","journal-title":"J. Biochem."},{"key":"ref_213","doi-asserted-by":"crossref","first-page":"4421","DOI":"10.1016\/S0021-9258(17)33313-6","article-title":"Effect of cobalt on synthesis of heme and cytochrome P-450 in the liver. Studies of adult rat hepatocytes in primary monolayer culture and in vivo","volume":"251","author":"Guzelian","year":"1976","journal-title":"J. Biol. Chem."},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"1095","DOI":"10.1042\/bj1291095","article-title":"The effect of exogenous \u03b4-aminolaevulinate on rat liver haem and cytochromes","volume":"129","author":"Druyan","year":"1972","journal-title":"Biochem. J."},{"key":"ref_215","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.ejphar.2018.05.009","article-title":"Oral administration of 5-aminolevulinic acid induces heme oxygenase-1 expression in peripheral blood mononuclear cells of healthy human subjects in combination with ferrous iron","volume":"833","author":"Ito","year":"2018","journal-title":"Eur. J. Pharmacol."},{"key":"ref_216","doi-asserted-by":"crossref","first-page":"688","DOI":"10.1073\/pnas.88.3.688","article-title":"Regulation of ferritin and heme oxygenase synthesis in rat fibroblasts by different forms of iron","volume":"88","author":"Eisenstein","year":"1991","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_217","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1042\/bj2000035","article-title":"Control of \u03b4-aminolaevulinate synthase and haem oxygenase in chroniciron-overloaded rats","volume":"200","author":"Ibrahim","year":"1981","journal-title":"Biochem. J."},{"key":"ref_218","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1042\/bj1960057","article-title":"Iron and the liver. Acute and long-term effects of iron-loading on hepatic haem metabolism","volume":"196","author":"Bonkowsky","year":"1981","journal-title":"Biochem. J."},{"key":"ref_219","doi-asserted-by":"crossref","first-page":"348","DOI":"10.1016\/S0022-5347(05)68050-0","article-title":"Urinary hyaluronic acid and hyaluronidase: Markers for bladder cancer detection and evaluation of grade","volume":"163","author":"Lokeshwar","year":"2000","journal-title":"J. Urol."},{"key":"ref_220","doi-asserted-by":"crossref","first-page":"2213","DOI":"10.1016\/S0021-9258(18)63141-2","article-title":"\u03b4-aminolevulinic acid synthetase: III. Synergistic effect of chelated iron on induction","volume":"245","author":"Stein","year":"1970","journal-title":"J. Biol. Chem."},{"key":"ref_221","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1023\/A:1025803600840","article-title":"Heme oxygenase-1 accelerates tumor angiogenesis of human pancreatic cancer","volume":"6","author":"Sunamura","year":"2003","journal-title":"Angiogenesis"},{"key":"ref_222","doi-asserted-by":"crossref","first-page":"2181","DOI":"10.2353\/ajpath.2006.051365","article-title":"Overexpression of heme oxygenase-1 in murine melanoma: Increased proliferation and viability of tumor cells, decreased survival of mice","volume":"169","author":"Was","year":"2006","journal-title":"Am. J. Pathol."},{"key":"ref_223","first-page":"13","article-title":"Hepatic heme metabolism and its control","volume":"52","author":"Bonkowsky","year":"1979","journal-title":"Yale J. Biol. Med."},{"key":"ref_224","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1042\/bj1540125","article-title":"Studies on the mechanism of induction of haem oxygenase by cobalt and other metal ions","volume":"154","author":"Maines","year":"1976","journal-title":"Biochem. J."},{"key":"ref_225","doi-asserted-by":"crossref","first-page":"4293","DOI":"10.1073\/pnas.71.11.4293","article-title":"Cobalt induction of hepatic heme oxygenase; with evidence that cytochrome P-450 is not essential for this enzyme activity","volume":"71","author":"Maines","year":"1974","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_226","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1016\/S0021-5198(19)42443-8","article-title":"Acute effect of amitriptyline, phenobarbital or cobaltous chloride on \u03b4-aminolevulinic acid synthetase, heme oxygenase and microsomal heme content and drug metabolism in rat liver","volume":"50","author":"Hoshi","year":"1989","journal-title":"Jpn. J. Pharmacol."},{"key":"ref_227","doi-asserted-by":"crossref","first-page":"4171","DOI":"10.1016\/S0021-9258(19)41402-6","article-title":"Cobalt stimulation of heme degradation in the liver. Dissociation of microsomal oxidation of heme from cytochrome P-450","volume":"250","author":"Maines","year":"1975","journal-title":"J. Biol. Chem."},{"key":"ref_228","doi-asserted-by":"crossref","first-page":"S196","DOI":"10.1002\/mnfr.200900550","article-title":"Resveratrol inhibits human lung adenocarcinoma cell metastasis by suppressing heme oxygenase 1-mediated nuclear factor-\u03baB pathway and subsequently downregulating expression of matrix metalloproteinases","volume":"54","author":"Liu","year":"2010","journal-title":"Mol. Nutr. Food Res."},{"key":"ref_229","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1042\/bj1130507","article-title":"The structural organization of haem synthesis in rat liver mitochondria","volume":"113","author":"Jones","year":"1969","journal-title":"Biochem. J."},{"key":"ref_230","doi-asserted-by":"crossref","first-page":"40750","DOI":"10.1074\/jbc.M111.300871","article-title":"Cytochrome P450 is present in both ferrous and ferric forms in the resting state within intact Escherichia coli and hepatocytes","volume":"286","author":"Johnston","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_231","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1016\/j.bbabio.2009.12.008","article-title":"Electron transfer in the complex of membrane-bound human cytochrome P450 3A4 with the flavin domain of P450BM-3: The effect of oligomerization of the heme protein and intermittent modulation of the spin equilibrium","volume":"1797","author":"Davydov","year":"2010","journal-title":"Biochim. Biophys. Acta (BBA)-Bioenerg."},{"key":"ref_232","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1016\/j.abb.2007.11.020","article-title":"Kinetics of electron transfer in the complex of cytochrome P450 3A4 with the flavin domain of cytochrome P450BM-3 as evidence of functional heterogeneity of the heme protein","volume":"471","author":"Fernando","year":"2008","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_233","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1517\/17425255.2011.562194","article-title":"Microsomal monooxygenase as a multienzyme system: The role of P450-P450 interactions","volume":"7","author":"Davydov","year":"2011","journal-title":"Expert Opin. Drug Metab. Toxicol."},{"key":"ref_234","first-page":"3489","article-title":"Functional vitamin B12 deficiency in advanced malignancy: Implications for the management of neuropathy and neuropathic pain","volume":"24","author":"Solomon","year":"2016","journal-title":"Support. Care Cancer"},{"key":"ref_235","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1016\/0005-2736(85)90023-9","article-title":"Lipid peroxidation decreases the rotational mobility of cytochrome P-450 in rat liver microsomes","volume":"817","author":"Gut","year":"1985","journal-title":"Biochim. Biophys. Acta (BBA)-Biomembr."},{"key":"ref_236","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/0005-2760(88)90243-3","article-title":"The involvement of superoxide and iron ions in the NADPH-dependent lipid peroxidation in human placental mitochondria","volume":"958","author":"Klimek","year":"1988","journal-title":"Biochim. Biophys. Acta (BBA)-Lipids Lipid Metab."},{"key":"ref_237","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1016\/0005-2760(90)90231-L","article-title":"Cytochrome P-450 involvement in the NADPH-dependent lipid peroxidation in human placental mitochondria","volume":"1044","author":"Klimek","year":"1990","journal-title":"Biochim. Biophys. Acta (BBA)-Lipids Lipid Metab."},{"key":"ref_238","doi-asserted-by":"crossref","first-page":"729","DOI":"10.1016\/0960-0760(92)90114-X","article-title":"The influence of NADPH-dependent lipid peroxidation on the progesterone biosynthesis in human placental mitochondria","volume":"42","author":"Klimek","year":"1992","journal-title":"J. Steroid Biochem. Mol. Biol."},{"key":"ref_239","doi-asserted-by":"crossref","first-page":"1168","DOI":"10.1016\/S0891-5849(97)00442-5","article-title":"Inhibitory effect of free radicals derived from organic hydroperoxide on progesterone synthesis in human term placental mitochondria","volume":"24","author":"Klimek","year":"1998","journal-title":"Free Radic. Biol. Med."},{"key":"ref_240","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1007\/s11010-006-9279-3","article-title":"The NADPH- and iron-dependent lipid peroxidation in human placental microsomes","volume":"295","author":"Milczarek","year":"2007","journal-title":"Mol. Cell. Biochem."},{"key":"ref_241","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1016\/j.jsbmb.2007.11.004","article-title":"NADPH- and iron-dependent lipid peroxidation inhibit aromatase activity in human placental microsomes","volume":"110","author":"Milczarek","year":"2008","journal-title":"J. Steroid Biochem. Mol. Biol."},{"key":"ref_242","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.placenta.2016.04.019","article-title":"Paraquat inhibits progesterone synthesis in human placental mitochondria","volume":"43","author":"Milczarek","year":"2016","journal-title":"Placenta"},{"key":"ref_243","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/0014-5793(73)80545-9","article-title":"Iron-dependent loss of liver cytochrome P-450 haem in vivo and in vitro","volume":"29","author":"Sparks","year":"1973","journal-title":"FEBS Lett."},{"key":"ref_244","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/S0003-9861(02)00489-7","article-title":"Hemin-mediated restoration of allylisopropylacetamide-inactivated CYP2B1: A role for glutathione and GRP94 in the heme-protein assembly","volume":"408","author":"Zgoda","year":"2002","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_245","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1006\/bbrc.1997.7861","article-title":"Influence of glutathione on the catalytic activity of reconstituted cytochrome P450 3A4","volume":"242","author":"Kim","year":"1998","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_246","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1111\/j.1600-0714.2004.00258.x","article-title":"Microarray gene expression profiling of cell lines from primary and metastatic tongue squamous cell carcinoma: Possible insights from emerging technology","volume":"34","author":"Vigneswaran","year":"2005","journal-title":"J. Oral Pathol. Med."},{"key":"ref_247","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1006\/bbrc.1996.0593","article-title":"High rates of substrate hydroxylation by human cytochrome P450 3A4 in reconstituted membranous vesicles: Influence of membrane charge","volume":"221","author":"Ueng","year":"1996","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_248","doi-asserted-by":"crossref","first-page":"1512","DOI":"10.1111\/j.1471-4159.1993.tb03315.x","article-title":"Glutathione depletion induces heme oxygenase-1 (HSP32) mRNA and protein in rat brain","volume":"60","author":"Ewing","year":"1993","journal-title":"J. Neurochem."},{"key":"ref_249","first-page":"974","article-title":"Induction of heme oxygenase: A general response to oxidant stress in cultured mammalian cells","volume":"51","author":"Applegate","year":"1991","journal-title":"Cancer Res."},{"key":"ref_250","doi-asserted-by":"crossref","first-page":"1913","DOI":"10.1073\/pnas.88.5.1913","article-title":"Glutathione deficiency leads to mitochondrial damage in brain","volume":"88","author":"Jain","year":"1991","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_251","doi-asserted-by":"crossref","first-page":"1428","DOI":"10.1089\/ars.2012.4858","article-title":"Redox dysregulation in the pathophysiology of schizophrenia and bipolar disorder: Insights from animal models","volume":"18","author":"Kulak","year":"2013","journal-title":"Antioxid. Redox Signal."},{"key":"ref_252","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1016\/j.abb.2008.01.001","article-title":"Effect of glutathione on homo- and heterotropic cooperativity in cytochrome P450 3A4","volume":"471","author":"Davydov","year":"2008","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_253","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1016\/j.biocel.2010.09.025","article-title":"Cellular iron depletion weakens induction of heme oxygenase-1 by cadmium","volume":"43","author":"Lai","year":"2011","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_254","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1002\/jbt.10062","article-title":"Mediation of cadmium-induced oxidative damage and glucose-6-phosphate dehydrogenase expression through glutathione depletion","volume":"17","author":"Xu","year":"2003","journal-title":"J. Biochem. Mol. Toxicol."},{"key":"ref_255","doi-asserted-by":"crossref","first-page":"2790","DOI":"10.1093\/hmg\/ddn178","article-title":"Glutathione-dependent redox status of frataxin-deficient cells in a yeast model of Friedreich\u2019s ataxia","volume":"17","author":"Santos","year":"2008","journal-title":"Hum. Mol. Genet."},{"key":"ref_256","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1186\/1750-1172-9-54","article-title":"Adrenal hormonal imbalance in acute intermittent porphyria patients: Results of a case control study","volume":"9","author":"Pozo","year":"2014","journal-title":"Orphanet J. Rare Dis."},{"key":"ref_257","doi-asserted-by":"crossref","first-page":"889","DOI":"10.1006\/bbrc.1993.2128","article-title":"Rotation of cytochrome P450SCC (CYP11A1) in proteoliposomes studied by delayed fluorescence depolarization","volume":"195","author":"Schwarz","year":"1993","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_258","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1006\/jsbi.1994.1055","article-title":"Direct visualization of a cardiolipin-dependent cytochrome P450scc-induced vesicle aggregation","volume":"113","author":"Schwarz","year":"1994","journal-title":"J. Struct. Biol."},{"key":"ref_259","doi-asserted-by":"crossref","first-page":"3057","DOI":"10.1016\/S0021-9258(19)85851-9","article-title":"Mitochondrial cytochrome P-450sec. Mechanism of electron transport by adrenodoxin","volume":"255","author":"Hanukoglu","year":"1980","journal-title":"J. Biol. Chem."},{"key":"ref_260","doi-asserted-by":"crossref","first-page":"506","DOI":"10.1002\/iub.1029","article-title":"Adrenodoxin\u2014A versatile ferredoxin","volume":"64","author":"Ewen","year":"2012","journal-title":"IUBMB Life"},{"key":"ref_261","doi-asserted-by":"crossref","first-page":"484","DOI":"10.1016\/j.bbamcr.2011.11.002","article-title":"Both human ferredoxins 1 and 2 and ferredoxin reductase are important for iron-sulfur cluster biogenesis","volume":"1823","author":"Shi","year":"2012","journal-title":"Biochim. Biophys. Acta (BBA)-Mol. Cell Res."},{"key":"ref_262","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1046\/j.1432-1327.1999.00483.x","article-title":"The concentration of adrenodoxin reductase limits cytochrome p450scc activity in the human placenta","volume":"263","author":"Tuckey","year":"1999","journal-title":"Eur. J. Biochem."},{"key":"ref_263","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/S0960-0760(02)00058-4","article-title":"Placental cytochrome P450scc (CYP11A1): Comparison of catalytic properties between conditions of limiting and saturating adrenodoxin reductase","volume":"81","author":"Tuckey","year":"2002","journal-title":"J. Steroid Biochem. Mol. Biol."},{"key":"ref_264","doi-asserted-by":"crossref","first-page":"4937","DOI":"10.1093\/hmg\/ddx377","article-title":"Biallelic mutations in the ferredoxin reductase gene cause novel mitochondriopathy with optic atrophy","volume":"26","author":"Peng","year":"2017","journal-title":"Hum. Mol. Genet."},{"key":"ref_265","doi-asserted-by":"crossref","first-page":"H1394","DOI":"10.1152\/ajpheart.00584.2011","article-title":"Hemin causes mitochondrial dysfunction in endothelial cells through promoting lipid peroxidation: The protective role of autophagy","volume":"302","author":"Higdon","year":"2012","journal-title":"Am. J. Physiol. Heart Circ. Physiol."},{"key":"ref_266","doi-asserted-by":"crossref","first-page":"1700","DOI":"10.1161\/01.ATV.11.6.1700","article-title":"Hemin: A possible physiological mediator of low density lipoprotein oxidation and endothelial injury","volume":"11","author":"Balla","year":"1991","journal-title":"Arterioscler. Thromb. J. Vasc. Biol."},{"key":"ref_267","doi-asserted-by":"crossref","first-page":"6033","DOI":"10.1038\/srep06033","article-title":"Transformation of membrane nanosurface of red blood cells under hemin action","volume":"4","author":"Kozlova","year":"2014","journal-title":"Sci. Rep."},{"key":"ref_268","doi-asserted-by":"crossref","first-page":"1197","DOI":"10.1038\/ncb2837","article-title":"Cardiolipin externalization to the outer mitochondrial membrane acts as an elimination signal for mitophagy in neuronal cells","volume":"15","author":"Chu","year":"2013","journal-title":"Nat. Cell Biol."},{"key":"ref_269","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1089\/dna.2014.2757","article-title":"Alzheimer\u2019s disease-related misfolded proteins and dysfunctional organelles on autophagy menu","volume":"34","author":"Correia","year":"2015","journal-title":"DNA Cell Biol."},{"key":"ref_270","doi-asserted-by":"crossref","unstructured":"Permenter, M.G., Lewis, J.A., and Jackson, D.A. (2011). Exposure to nickel, chromium, or cadmium causes distinct changes in the gene expression patterns of a rat liver derived cell line. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0027730"},{"key":"ref_271","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1002\/tox.22082","article-title":"Oral exposure of mice to cadmium (II), chromium (VI) and their mixture induce oxidative- and endoplasmic reticulum-stress mediated apoptosis in the livers","volume":"31","author":"Jin","year":"2014","journal-title":"Environ. Toxicol."},{"key":"ref_272","doi-asserted-by":"crossref","first-page":"1021","DOI":"10.1158\/1940-6207.CAPR-11-0110","article-title":"Inflammation and increased aromatase expression occur in the breast tissue of obese women with breast cancer","volume":"4","author":"Morris","year":"2011","journal-title":"Cancer Prev. Res."},{"key":"ref_273","doi-asserted-by":"crossref","first-page":"434","DOI":"10.3390\/ijms14010434","article-title":"An involvement of oxidative stress in endoplasmic reticulum stress and its associated diseases","volume":"14","author":"Bhandary","year":"2012","journal-title":"Int. J. Mol. Sci."},{"key":"ref_274","doi-asserted-by":"crossref","first-page":"496","DOI":"10.1016\/j.ygyno.2009.05.041","article-title":"Elevated aromatase expression correlates with cervical carcinoma progression","volume":"114","author":"Veerapaneni","year":"2009","journal-title":"Gynecol. Oncol."},{"key":"ref_275","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/j.taap.2012.09.021","article-title":"Acrolein cytotoxicity in hepatocytes involves endoplasmic reticulum stress, mitochondrial dysfunction and oxidative stress","volume":"265","author":"Mohammad","year":"2012","journal-title":"Toxicol. Appl. Pharmacol."},{"key":"ref_276","doi-asserted-by":"crossref","first-page":"21618","DOI":"10.1074\/jbc.M700053200","article-title":"Bax inhibitor-1 regulates endoplasmic reticulum stress-associated reactive oxygen species and heme oxygenase-1 expression","volume":"282","author":"Lee","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_277","doi-asserted-by":"crossref","first-page":"872","DOI":"10.1074\/jbc.M410413200","article-title":"Endoplasmic reticulum stress stimulates heme oxygenase-1 gene expression in vascular smooth muscle: Role in cell survival","volume":"280","author":"Liu","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_278","doi-asserted-by":"crossref","first-page":"1496","DOI":"10.1126\/science.1523409","article-title":"Oxidized redox state of glutathione in the endoplasmic reticulum","volume":"257","author":"Hwang","year":"1992","journal-title":"Science"},{"key":"ref_279","doi-asserted-by":"crossref","first-page":"612","DOI":"10.1111\/j.1440-1681.2008.05114.x","article-title":"Endoplasmic reticulum stress involved in heart and liver injury in iron-loaded rats","volume":"36","author":"Lou","year":"2009","journal-title":"Clin. Exp. Pharmacol. Physiol."},{"key":"ref_280","doi-asserted-by":"crossref","first-page":"13161","DOI":"10.1074\/jbc.M110.170944","article-title":"Mutant HFE H63D protein is associated with prolonged endoplasmic reticulum stress and increased neuronal vulnerability","volume":"286","author":"Liu","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_281","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1111\/j.1474-9726.2010.00652.x","article-title":"Iron handling in hippocampal neurons: Activity-dependent iron entry and mitochondria-mediated neurotoxicity","volume":"10","author":"Pelizzoni","year":"2011","journal-title":"Aging Cell"},{"key":"ref_282","doi-asserted-by":"crossref","first-page":"1686","DOI":"10.1007\/s11064-007-9313-1","article-title":"Voltage-gated calcium channels provide an alternate route for iron uptake in neuronal cell cultures","volume":"32","author":"Gaasch","year":"2007","journal-title":"Neurochem. Res."},{"key":"ref_283","doi-asserted-by":"crossref","first-page":"939","DOI":"10.1001\/archgenpsychiatry.2010.96","article-title":"Genetic variation in CACNA1C affects brain circuitries related to mental illness","volume":"67","author":"Bigos","year":"2010","journal-title":"Arch. Gen. Psychiatry"},{"key":"ref_284","doi-asserted-by":"crossref","first-page":"1657","DOI":"10.1038\/nm.2576","article-title":"Using iPSC-derived neurons to uncover cellular phenotypes associated with Timothy syndrome","volume":"17","author":"Portmann","year":"2011","journal-title":"Nat. Med."},{"key":"ref_285","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1111\/j.1749-6632.2008.03572.x","article-title":"Genetic calcium signaling abnormalities in the central nervous system: Seizures, migraine, and autism","volume":"1151","author":"Gargus","year":"2009","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"ref_286","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.cell.2004.09.011","article-title":"CaV1.2 calcium channel dysfunction causes a multisystem disorder including arrhythmia and autism","volume":"119","author":"Splawski","year":"2004","journal-title":"Cell"},{"key":"ref_287","doi-asserted-by":"crossref","first-page":"936","DOI":"10.4088\/JCP.10m06244gry","article-title":"Sudden deaths in psychiatric patients","volume":"72","author":"Manu","year":"2011","journal-title":"J. Clin. Psychiatry"},{"key":"ref_288","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.eurpsy.2011.02.009","article-title":"Type-2 diabetes mellitus in schizophrenia: Increased prevalence and major risk factor of excess mortality in a naturalistic 7-year follow-up","volume":"27","author":"Schoepf","year":"2012","journal-title":"Eur. Psychiatry"},{"key":"ref_289","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1007\/s00406-013-0436-x","article-title":"Physical comorbidity and its relevance on mortality in schizophrenia: A naturalistic 12-year follow-up in general hospital admissions","volume":"264","author":"Schoepf","year":"2014","journal-title":"Eur. Arch. Psychiatry Clin. Neurosci."},{"key":"ref_290","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1111\/j.1365-2133.2011.10401.x","article-title":"The association between porphyria cutanea tarda and diabetes mellitus: Analysis of a long-term follow-up cohort","volume":"165","author":"Guilabert","year":"2011","journal-title":"Br. J. Dermatol."},{"key":"ref_291","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1016\/S1357-2725(98)00145-9","article-title":"Delta aminolevulinate dehydratase (ALA-D) activity in human and experimental diabetes mellitus","volume":"31","author":"Rebollar","year":"1999","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_292","doi-asserted-by":"crossref","first-page":"25","DOI":"10.2174\/157339913804143225","article-title":"Regulation of insulin synthesis and secretion and pancreatic Beta-cell dysfunction in diabetes","volume":"9","author":"Fu","year":"2013","journal-title":"Curr. Diabetes Rev."},{"key":"ref_293","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1007\/s00702-010-0426-3","article-title":"The link between iron, metabolic syndrome, and Alzheimer\u2019s disease","volume":"118","author":"Bartl","year":"2011","journal-title":"J. Neural Transm."},{"key":"ref_294","doi-asserted-by":"crossref","first-page":"734","DOI":"10.2337\/dc06-1539","article-title":"Spectrum of liver disease in type 2 diabetes and management of patients with diabetes and liver disease","volume":"30","author":"Tolman","year":"2007","journal-title":"Diabetes Care"},{"key":"ref_295","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1111\/j.1478-3231.2008.01718.x","article-title":"Prevalence and associated factors of non-alcoholic fatty liver disease in patients with type-2 diabetes mellitus","volume":"29","author":"Leite","year":"2009","journal-title":"Liver Int."},{"key":"ref_296","doi-asserted-by":"crossref","first-page":"S99","DOI":"10.1002\/hep.20973","article-title":"Nonalcoholic fatty liver disease: From steatosis to cirrhosis","volume":"43","author":"Farrell","year":"2006","journal-title":"Hepatology"},{"key":"ref_297","doi-asserted-by":"crossref","first-page":"S67","DOI":"10.1192\/bjp.184.47.s67","article-title":"Prevalence of diabetes and impaired glucose tolerance in patients with schizophrenia","volume":"184","author":"Bushe","year":"2004","journal-title":"Br. J. Psychiatry"},{"key":"ref_298","doi-asserted-by":"crossref","first-page":"752","DOI":"10.1016\/j.psyneuen.2012.09.009","article-title":"Schizophrenia: Metabolic aspects of aetiology, diagnosis and future treatment strategies","volume":"38","author":"Harris","year":"2013","journal-title":"Psychoneuroendocrinology"},{"key":"ref_299","doi-asserted-by":"crossref","first-page":"1035","DOI":"10.1016\/j.psychres.2012.03.043","article-title":"Prevalence of metabolic syndrome in patients with schizophrenia in India","volume":"200","author":"Grover","year":"2012","journal-title":"Psychiatry Res."},{"key":"ref_300","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1177\/2045125312464385","article-title":"The prevalence and mechanisms of metabolic syndrome in schizophrenia: A review","volume":"3","author":"Papanastasiou","year":"2013","journal-title":"Ther. Adv. Psychopharmacol."},{"key":"ref_301","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1016\/j.jad.2013.03.010","article-title":"A prospective, longitudinal study of metabolic syndrome in patients with bipolar disorder and schizophrenia","volume":"150","author":"Malhotra","year":"2013","journal-title":"J. Affect. Disord."},{"key":"ref_302","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1038\/mp.2009.81","article-title":"Increased levels of circulating insulin-related peptides in first-onset, antipsychotic na\u00efve schizophrenia patients","volume":"15","author":"Guest","year":"2010","journal-title":"Mol. Psychiatry"},{"key":"ref_303","doi-asserted-by":"crossref","first-page":"284","DOI":"10.1176\/appi.ajp.160.2.284","article-title":"Impaired fasting glucose tolerance in first-episode, drug-naive patients with schizophrenia","volume":"160","author":"Ryan","year":"2003","journal-title":"Am. J. Psychiatry"},{"key":"ref_304","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1111\/j.1464-5491.2007.02092.x","article-title":"Impaired glucose tolerance in first-episode drug-na\u00efve patients with schizophrenia","volume":"24","author":"Spelman","year":"2007","journal-title":"Diabet. Med."},{"key":"ref_305","doi-asserted-by":"crossref","first-page":"1557","DOI":"10.1176\/appi.ajp.2007.07020233","article-title":"Insulin and insulin-like growth factor-1 abnormalities in antipsychotic-naive schizophrenia","volume":"164","author":"Venkatasubramanian","year":"2007","journal-title":"Am. J. Psychiatry"},{"key":"ref_306","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1016\/j.schres.2008.04.017","article-title":"Glucose abnormalities in the siblings of people with schizophrenia","volume":"103","author":"Bernardo","year":"2008","journal-title":"Schizophr. Res."},{"key":"ref_307","doi-asserted-by":"crossref","first-page":"1335","DOI":"10.4088\/JCP.v65n1007","article-title":"Insulin resistance and increased leptin concentrations in noncompliant schizophrenia patients but not in antipsychotic-naive first-episode schizophrenia patients","volume":"65","author":"Arranz","year":"2004","journal-title":"J. Clin. Psychiatry"},{"key":"ref_308","doi-asserted-by":"crossref","first-page":"382","DOI":"10.1177\/070674370605100608","article-title":"Insulin resistance and adiponectin levels in drug-free patients with schizophrenia: A preliminary report","volume":"51","author":"Cohn","year":"2006","journal-title":"Can. J. Psychiatry"},{"key":"ref_309","doi-asserted-by":"crossref","unstructured":"Holmes, E., Tsang, T.M., Huang, J.T., Leweke, F.M., Koethe, D., Gerth, C.W., Nolden, B.M., Gross, S., Schreiber, D., and Nicholson, J.K. (2006). Metabolic profiling of CSF: Evidence that early intervention may impact on disease progression and outcome in schizophrenia. PLoS Med., 3.","DOI":"10.1371\/journal.pmed.0030327"},{"key":"ref_310","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1038\/mp.2011.131","article-title":"Potential metabolite markers of schizophrenia","volume":"18","author":"Yang","year":"2013","journal-title":"Mol. Psychiatry"},{"key":"ref_311","doi-asserted-by":"crossref","first-page":"282","DOI":"10.1007\/s00125-004-1627-9","article-title":"Functional and morphological alterations of mitochondria in pancreatic beta cells from type 2 diabetic patients","volume":"48","author":"Anello","year":"2005","journal-title":"Diabetologia"},{"key":"ref_312","doi-asserted-by":"crossref","first-page":"1739","DOI":"10.1002\/mnfr.201300747","article-title":"Targeting mitochondrial alterations to prevent type 2 diabetes-Evidence from studies of dietary redox-active compounds","volume":"58","author":"Cheng","year":"2014","journal-title":"Mol. Nutr. Food Res."},{"key":"ref_313","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1016\/j.cmet.2013.02.007","article-title":"Iron and diabetes risk","volume":"17","author":"Simcox","year":"2013","journal-title":"Cell Metab."},{"key":"ref_314","first-page":"308","article-title":"Clinical aspects of diabetes secondary to idiopathic haemochromatosis in French-speaking Belgium","volume":"23","author":"Buysschaert","year":"1997","journal-title":"Diabetes Metab."},{"key":"ref_315","first-page":"478","article-title":"Factors determining glucose tolerance in patients with thalassemia major","volume":"77","author":"Dmochowski","year":"1993","journal-title":"J. Clin. Endocrinol. Metab."},{"key":"ref_316","doi-asserted-by":"crossref","first-page":"809","DOI":"10.1056\/NEJM198803313181303","article-title":"Insulin resistance and hyperinsulinemia in patients with thalassemia major treated by hypertransfusion","volume":"318","author":"Merkel","year":"1988","journal-title":"N. Engl. J. Med."},{"key":"ref_317","doi-asserted-by":"crossref","first-page":"1765","DOI":"10.1182\/blood-2006-05-022335","article-title":"Diabetes, hypertension, and cardiovascular events in survivors of hematopoietic cell transplantation: A report from the bone marrow transplantation survivor study","volume":"109","author":"Baker","year":"2007","journal-title":"Blood"},{"key":"ref_318","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1111\/jnc.12216","article-title":"Diabetes in Friedreich ataxia","volume":"126","author":"Cnop","year":"2013","journal-title":"J. Neurochem."},{"key":"ref_319","doi-asserted-by":"crossref","first-page":"1661","DOI":"10.1007\/s00125-006-0200-0","article-title":"High prevalence of abnormal glucose homeostasis secondary to decreased insulin secretion in individuals with hereditary haemochromatosis","volume":"49","author":"McClain","year":"2006","journal-title":"Diabetologia"},{"key":"ref_320","doi-asserted-by":"crossref","first-page":"5305","DOI":"10.1210\/en.2004-0392","article-title":"Oxidative stress, \u03b2-cell apoptosis, and decreased insulin secretory capacity in mouse models of hemochromatosis","volume":"145","author":"Cooksey","year":"2004","journal-title":"Endocrinology"},{"key":"ref_321","doi-asserted-by":"crossref","first-page":"2546","DOI":"10.1007\/s00125-006-0445-7","article-title":"Increased insulin secretory capacity but decreased insulin sensitivity after correction of iron overload by phlebotomy in hereditary haemochromatosis","volume":"49","author":"Abraham","year":"2006","journal-title":"Diabetologia"},{"key":"ref_322","doi-asserted-by":"crossref","first-page":"2181","DOI":"10.1016\/S0140-6736(00)02397-7","article-title":"Insulin resistance, iron, and the liver","volume":"355","author":"Ferrannini","year":"2000","journal-title":"Lancet"},{"key":"ref_323","doi-asserted-by":"crossref","first-page":"1155","DOI":"10.1016\/S0016-5085(99)70401-4","article-title":"Insulin resistance-associated hepatic iron overload","volume":"117","author":"Mendler","year":"1999","journal-title":"Gastroenterology"},{"key":"ref_324","doi-asserted-by":"crossref","first-page":"3782","DOI":"10.3748\/wjg.v18.i29.3782","article-title":"Diagnostic and therapeutic implications of the association between ferritin level and severity of nonalcoholic fatty liver disease","volume":"18","author":"Valenti","year":"2012","journal-title":"World J. Gastroenterol."},{"key":"ref_325","doi-asserted-by":"crossref","first-page":"4699","DOI":"10.3748\/wjg.v13.i35.4699","article-title":"Iron overload and cofactors with special reference to alcohol, hepatitis C virus infection and steatosis\/insulin resistance","volume":"13","author":"Kohgo","year":"2007","journal-title":"World J. Gastroenterol."},{"key":"ref_326","doi-asserted-by":"crossref","first-page":"1227","DOI":"10.1111\/j.1872-034X.2010.00719.x","article-title":"Iron state in association with retinoid metabolism in non-alcoholic fatty liver disease","volume":"40","author":"Tsuchiya","year":"2010","journal-title":"Hepatol. Res."},{"key":"ref_327","doi-asserted-by":"crossref","first-page":"1186","DOI":"10.3748\/wjg.15.1186","article-title":"Is the iron regulatory hormone hepcidin a risk factor for alcoholic liver disease?","volume":"15","year":"2009","journal-title":"World J. Gastroenterol."},{"key":"ref_328","doi-asserted-by":"crossref","first-page":"931","DOI":"10.1053\/gast.2002.32403","article-title":"Effect of iron depletion in carbohydrate-intolerant patients with clinical evidence of nonalcoholic fatty liver disease","volume":"122","author":"Facchini","year":"2002","journal-title":"Gastroenterology"},{"key":"ref_329","doi-asserted-by":"crossref","first-page":"1188","DOI":"10.1111\/j.1872-034X.2010.00724.x","article-title":"Restriction of calorie and iron intake results in reduction of visceral fat and serum alanine aminotransferase and ferritin levels in patients with chronic liver disease","volume":"40","author":"Iwasa","year":"2010","journal-title":"Hepatol. Res."},{"key":"ref_330","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1016\/j.jhep.2009.11.030","article-title":"Mitochondrial dysfunction precedes insulin resistance and hepatic steatosis and contributes to the natural history of non-alcoholic fatty liver disease in an obese rodent model","volume":"52","author":"Rector","year":"2010","journal-title":"J. Hepatol."},{"key":"ref_331","doi-asserted-by":"crossref","first-page":"S20","DOI":"10.1111\/j.1440-1746.2006.04640.x","article-title":"Role of mitochondria in non-alcoholic fatty liver disease","volume":"22","author":"Pessayre","year":"2007","journal-title":"J. Gastroenterol. Hepatol."},{"key":"ref_332","doi-asserted-by":"crossref","first-page":"837","DOI":"10.1111\/j.1572-0241.2005.41287.x","article-title":"Duration of hepatic iron exposure increases the risk of significant fibrosis in hereditary hemochromatosis: A new role for magnetic resonance imaging","volume":"100","author":"Olynyk","year":"2005","journal-title":"Am. J. Gastroenterol."},{"key":"ref_333","doi-asserted-by":"crossref","first-page":"294","DOI":"10.1001\/archinte.166.3.294","article-title":"Screening for hemochromatosis in asymptomatic subjects with or without a family history","volume":"166","author":"Powell","year":"2006","journal-title":"Arch. Intern. Med."},{"key":"ref_334","doi-asserted-by":"crossref","first-page":"729S","DOI":"10.3945\/jn.110.130351","article-title":"HFE gene variants affect iron in the brain","volume":"141","author":"Nandar","year":"2011","journal-title":"J. Nutr."},{"key":"ref_335","doi-asserted-by":"crossref","first-page":"448","DOI":"10.1139\/y04-052","article-title":"Heme-oxygenase-mediated iron accumulation in the liver","volume":"82","author":"Khan","year":"2004","journal-title":"Can. J. Physiol. Pharmacol."},{"key":"ref_336","doi-asserted-by":"crossref","first-page":"1593","DOI":"10.3748\/wjg.v19.i10.1593","article-title":"Heme status affects human hepatic messenger RNA and microRNA expression","volume":"19","author":"Bonkovsky","year":"2013","journal-title":"World J. Gastroenterol."},{"key":"ref_337","doi-asserted-by":"crossref","unstructured":"Bao, W., Song, F., Li, X., Rong, S., Yang, W., Zhang, M., Yao, P., Hao, L., Yang, N., and Hu, F.B. (2010). Plasma heme oxygenase-1 concentration is elevated in individuals with type 2 diabetes mellitus. PLoS ONE, 5.","DOI":"10.1371\/journal.pone.0012371"},{"key":"ref_338","doi-asserted-by":"crossref","first-page":"2921","DOI":"10.3748\/wjg.v19.i19.2921","article-title":"Inhibiting heme oxygenase-1 attenuates rat liver fibrosis by removing iron accumulation","volume":"19","author":"Wang","year":"2013","journal-title":"World J. Gastroenterol."},{"key":"ref_339","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.cell.2014.04.043","article-title":"Heme oxygenase-1 drives metaflammation and insulin resistance in mouse and man","volume":"158","author":"Jais","year":"2014","journal-title":"Cell"},{"key":"ref_340","doi-asserted-by":"crossref","first-page":"1636S","DOI":"10.1093\/jn\/136.6.1636S","article-title":"The sulfur-containing amino acids: An overview","volume":"136","author":"Brosnan","year":"2006","journal-title":"J. Nutr."},{"key":"ref_341","doi-asserted-by":"crossref","first-page":"51","DOI":"10.2143\/AC.61.1.2005140","article-title":"Influence of methionine synthase (A2756G) and methionine synthase reductase (A66G) polymorphisms on plasma homocysteine levels and relation to risk of coronary artery disease","volume":"61","author":"Laraqui","year":"2006","journal-title":"Acta Cardiol."},{"key":"ref_342","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1042\/BJ20120731","article-title":"Human cystathionine \u03b2-synthase (CBS) contains two classes of binding sites for S-adenosylmethionine (SAM): Complex regulation of CBS activity and stability by SAM","volume":"449","author":"Pey","year":"2013","journal-title":"Biochem. J."},{"key":"ref_343","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/S0006-291X(75)80297-X","article-title":"Activation of cystathionine synthase by adenosylmethionine and adenosylethionine","volume":"66","author":"Finkelstein","year":"1975","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_344","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1002\/hep.22604","article-title":"Cystathionine \u03b2-synthase as a carbon monoxide-sensitive regulator of bile excretion","volume":"49","author":"Shintani","year":"2009","journal-title":"Hepatology"},{"key":"ref_345","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1007\/s00109-012-0875-2","article-title":"Carbon monoxide: Impact on remethylation\/transsulfuration metabolism and its pathophysiologic implications","volume":"90","author":"Hishiki","year":"2012","journal-title":"J. Mol. Med."},{"key":"ref_346","doi-asserted-by":"crossref","unstructured":"Takano, N., Yamamoto, T., Adachi, T., and Suematsu, M. (2010). Assessing a Shift of Glucose Biotransformation by LC-MS\/MS-Based Metabolome Analysis in Carbon Monoxide-Exposed Cells, Springer. Advances in Experimental Medicine and Biology.","DOI":"10.1007\/978-1-4419-1241-1_14"},{"key":"ref_347","doi-asserted-by":"crossref","first-page":"3480","DOI":"10.1038\/ncomms4480","article-title":"Reduced methylation of PFKFB3 in cancer cells shunts glucose towards the pentose phosphate pathway","volume":"5","author":"Yamamoto","year":"2014","journal-title":"Nat. Commun."},{"key":"ref_348","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1055\/s-2007-979127","article-title":"Orally given nicotinamide inhibits the decreasing of glutathione content in the pancreas of streptozotocin diabetic rats","volume":"28","author":"Kretowski","year":"1996","journal-title":"Horm. Metab. Res."},{"key":"ref_349","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1007\/BF01960237","article-title":"Effect of niacin\/nicotinamide deficiency on the diabetogenic effect of streptozotocin","volume":"44","author":"Wright","year":"1988","journal-title":"Experientia"},{"key":"ref_350","unstructured":"Orkin, S., Fisher, D.E., Look, T.A., Lux, S., Ginsburg, D., and Nathan, D.G. (2009). Glucose-6-Phosphate Dehydrogenase Deficiency. Nathan and Oski\u2019s Hematology of Infancy and Childhood, Elsevier."},{"key":"ref_351","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1186\/1475-2832-2-6","article-title":"Psychotic mania in glucose-6-phosphate-dehydrogenase-deficient subjects","volume":"2","author":"Bocchetta","year":"2003","journal-title":"Ann. Gen. Hosp. Psychiatry"},{"key":"ref_352","doi-asserted-by":"crossref","first-page":"1123","DOI":"10.1021\/cn400079y","article-title":"Brain glucose-6-phosphate dehydrogenase protects against endogenous oxidative DNA damage and neurodegeneration in aged mice","volume":"4","author":"Jeng","year":"2013","journal-title":"ACS Chem. Neurosci."},{"key":"ref_353","doi-asserted-by":"crossref","first-page":"5209","DOI":"10.1002\/j.1460-2075.1995.tb00205.x","article-title":"Targeted disruption of the housekeeping gene encoding glucose 6-phosphate dehydrogenase (G6PD): G6PD is dispensable for pentose synthesis but essential for defense against oxidative stress","volume":"14","author":"Pandolfi","year":"1995","journal-title":"EMBO J."},{"key":"ref_354","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1023\/A:1024497419821","article-title":"Classical homocystinuria: Vascular risk and its prevention","volume":"26","author":"Yap","year":"2003","journal-title":"J. Inherit. Metab. Dis."},{"key":"ref_355","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/j.psychres.2010.04.008","article-title":"Plasma homocysteine in schizophrenia: Determinants and clinical correlations in Tunisian patients free from antipsychotics","volume":"179","author":"Bouaziz","year":"2010","journal-title":"Psychiatry Res."},{"key":"ref_356","first-page":"373261","article-title":"Elevated serum levels of homocysteine as an early prognostic factor of psychiatric disorders in children and adolescents","volume":"2012","author":"Kevere","year":"2012","journal-title":"Schizophr. Res. Treat."},{"key":"ref_357","doi-asserted-by":"crossref","first-page":"308","DOI":"10.1016\/j.encep.2010.12.004","article-title":"Hyperhomocysteinemia and schizophrenia: Case control study","volume":"37","author":"Mabrouk","year":"2011","journal-title":"L\u2019encephale"},{"key":"ref_358","doi-asserted-by":"crossref","unstructured":"Mostaghel, E.A., Solomon, K.R., Pelton, K., Freeman, M.R., and Montgomery, R.B. (2012). Impact of circulating cholesterol levels on growth and intratumoral androgen concentration of prostate tumors. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0030062"},{"key":"ref_359","doi-asserted-by":"crossref","unstructured":"Gall, W.E., Beebe, K., Lawton, K.A., Adam, K.P., Mitchell, M.W., Nakhle, P.J., Ryals, J.A., Milburn, M.V., Nannipieri, M., and Camastra, S. (2010). \u03b1-hydroxybutyrate is an early biomarker of insulin resistance and glucose intolerance in a nondiabetic population. PLoS ONE, 5.","DOI":"10.1371\/journal.pone.0010883"},{"key":"ref_360","doi-asserted-by":"crossref","first-page":"636","DOI":"10.1093\/ajcn\/82.3.636","article-title":"Homocysteine and folate as risk factors for dementia and Alzheimer disease","volume":"82","author":"Ravaglia","year":"2005","journal-title":"Am. J. Clin. Nutr."},{"key":"ref_361","first-page":"57","article-title":"Serum Homocysteine, Dehydroepiandrosterone Sulphate and Lipoprotein (a) in Alzheimer\u2019s Disease and Vascular Dementia","volume":"4","author":"Ray","year":"2013","journal-title":"Aging Dis."},{"key":"ref_362","doi-asserted-by":"crossref","first-page":"476","DOI":"10.1056\/NEJMoa011613","article-title":"Plasma homocysteine as a risk factor for dementia and Alzheimer\u2019s disease","volume":"346","author":"Seshadri","year":"2002","journal-title":"N. Engl. J. Med."},{"key":"ref_363","doi-asserted-by":"crossref","first-page":"1809","DOI":"10.1016\/j.metabol.2010.05.016","article-title":"Preliminary report: Hyperhomocysteinemia in patients with acute intermittent porphyria","volume":"59","author":"Lopez","year":"2010","journal-title":"Metabolism"},{"key":"ref_364","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1186\/1475-2891-12-37","article-title":"Plasmatic higher levels of homocysteine in non-alcoholic fatty liver disease (NAFLD)","volume":"12","author":"Muniz","year":"2013","journal-title":"Nutr. J."},{"key":"ref_365","doi-asserted-by":"crossref","first-page":"31504","DOI":"10.1074\/jbc.M213036200","article-title":"Altered gene expression in liver from a murine model of hyperhomocysteinemia","volume":"278","author":"Robert","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_366","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/j.psychres.2015.11.045","article-title":"Serum folate levels in schizophrenia: A meta-analysis","volume":"235","author":"Wang","year":"2016","journal-title":"Psychiatry Res."},{"key":"ref_367","doi-asserted-by":"crossref","first-page":"134","DOI":"10.4306\/pi.2011.8.2.134","article-title":"Serum homocysteine and folate levels in korean schizophrenic patients","volume":"8","author":"Kim","year":"2011","journal-title":"Psychiatry Investig."},{"key":"ref_368","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.psychres.2009.01.013","article-title":"Reduced folic acid, vitamin B12 and docosahexaenoic acid and increased homocysteine and cortisol in never-medicated schizophrenia patients: Implications for altered one-carbon metabolism","volume":"175","author":"Kale","year":"2010","journal-title":"Psychiatry Res."},{"key":"ref_369","doi-asserted-by":"crossref","first-page":"410","DOI":"10.1301\/002966402320964089","article-title":"Homocysteine, folate deficiency, and Parkinson\u2019s disease","volume":"60","author":"Miller","year":"2002","journal-title":"Nutr. Rev."},{"key":"ref_370","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1159\/000054753","article-title":"Vitamin Intervention for Stroke Prevention (VISP) trial: Rationale and design","volume":"20","author":"Spence","year":"2001","journal-title":"Neuroepidemiology"},{"key":"ref_371","doi-asserted-by":"crossref","first-page":"9523","DOI":"10.1073\/pnas.1301816110","article-title":"Preventing Alzheimer\u2019s disease-related gray matter atrophy by B-vitamin treatment","volume":"110","author":"Douaud","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_372","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/j.biopsych.2005.10.009","article-title":"Homocysteine-reducing strategies improve symptoms in chronic schizophrenic patients with hyperhomocysteinemia","volume":"60","author":"Levine","year":"2006","journal-title":"Biol. Psychiatry"},{"key":"ref_373","first-page":"3069","article-title":"Aromatase in colon carcinoma","volume":"32","author":"Sato","year":"2012","journal-title":"Anticancer Res."},{"key":"ref_374","first-page":"204","article-title":"Oxidative state of glutathione in red blood cells and plasma of diabetic patients: In vivo and in vitro study","volume":"8","author":"Costagliola","year":"1990","journal-title":"Clin. Physiol. Biochem."},{"key":"ref_375","doi-asserted-by":"crossref","first-page":"2601","DOI":"10.1016\/j.lfs.2005.10.022","article-title":"Glucose-6-phosphate dehydrogenase activity and NADPH\/NADP+ ratio in liver and pancreas are dependent on the severity of hyperglycemia in rat","volume":"78","author":"Cruz","year":"2006","journal-title":"Life Sci."},{"key":"ref_376","doi-asserted-by":"crossref","unstructured":"Zhang, Z., Yang, Z., Zhu, B., Hu, J., Liew, C.W., Zhang, Y., Leopold, J.A., Handy, D.E., Loscalzo, J., and Stanton, R.C. (2012). Increasing glucose 6-phosphate dehydrogenase activity restores redox balance in vascular endothelial cells exposed to high glucose. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0049128"},{"key":"ref_377","doi-asserted-by":"crossref","unstructured":"Hashiba, M., Ono, M., Hyogo, H., Ikeda, Y., Masuda, K., Yoshioka, R., Ishikawa, Y., Nagata, Y., Munekage, K., and Ochi, T. (2013). Glycemic variability is an independent predictive factor for development of hepatic fibrosis in nonalcoholic Fatty liver disease. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0076161"},{"key":"ref_378","doi-asserted-by":"crossref","first-page":"1497","DOI":"10.1096\/fj.09-136572","article-title":"High glucose inhibits glucose-6-phosphate dehydrogenase, leading to increased oxidative stress and \u03b2-cell apoptosis","volume":"24","author":"Zhang","year":"2010","journal-title":"FASEB J."},{"key":"ref_379","doi-asserted-by":"crossref","first-page":"S108","DOI":"10.2337\/diabetes.54.suppl_2.S108","article-title":"Mechanisms of \u03b2-cell death in type 2 diabetes","volume":"54","author":"Donath","year":"2005","journal-title":"Diabetes"},{"key":"ref_380","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1007\/s00592-012-0435-9","article-title":"Increased prevalence of mood disorders and suicidal ideation in type 2 diabetic patients","volume":"49","author":"Ceretta","year":"2012","journal-title":"Acta Diabetol."},{"key":"ref_381","doi-asserted-by":"crossref","first-page":"F1040","DOI":"10.1152\/ajprenal.00076.2005","article-title":"Diabetes causes inhibition of glucose-6-phosphate dehydrogenase via activation of PKA, which contributes to oxidative stress in rat kidney cortex","volume":"289","author":"Xu","year":"2005","journal-title":"Am. J. Physiol.-Ren. Physiol."},{"key":"ref_382","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1096\/fj.09-135731","article-title":"Glucose-6-phosphate dehydrogenase-deficient mice have increased renal oxidative stress and increased albuminuria","volume":"24","author":"Xu","year":"2010","journal-title":"FASEB J."},{"key":"ref_383","doi-asserted-by":"crossref","first-page":"1234","DOI":"10.1007\/s00125-003-1174-9","article-title":"Haeme-oxygenase 1 expression in rat pancreatic beta cells is stimulated by supraphysiological glucose concentrations and by cyclic AMP","volume":"46","author":"Jonas","year":"2003","journal-title":"Diabetologia"},{"key":"ref_384","doi-asserted-by":"crossref","unstructured":"Bao, W., Rong, S., Zhang, M., Yu, X., Zhao, Y., Xiao, X., Yang, W., Wang, D., Yao, P., and Hu, F.B. (2012). Plasma heme oxygenase-1 concentration in relation to impaired glucose regulation in a non-diabetic Chinese population. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0032223"},{"key":"ref_385","doi-asserted-by":"crossref","first-page":"451","DOI":"10.3233\/JAD-140972","article-title":"Synergistic Exacerbation of Mitochondrial and Synaptic Dysfunction and Resultant Learning and Memory Deficit in a Mouse Model of Diabetic Alzheimer\u2019s Disease","volume":"43","author":"Wang","year":"2014","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_386","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1016\/j.canep.2012.04.002","article-title":"Androgen metabolism and JAK\/STAT pathway genes and prostate cancer risk","volume":"36","author":"Kwon","year":"2012","journal-title":"Cancer Epidemiol."},{"key":"ref_387","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1177\/1535370212473702","article-title":"Alterations of the redox state, pentose pathway and glutathione metabolism in an acute porphyria model. Their impact on heme pathway","volume":"238","author":"Faut","year":"2013","journal-title":"Exp. Biol. Med."},{"key":"ref_388","doi-asserted-by":"crossref","first-page":"1399","DOI":"10.3390\/nu4101399","article-title":"Dysregulation of glutathione homeostasis in neurodegenerative diseases","volume":"4","author":"Johnson","year":"2012","journal-title":"Nutrients"},{"key":"ref_389","doi-asserted-by":"crossref","first-page":"684","DOI":"10.1038\/sj.mp.4001511","article-title":"Mitochondrial dysfunction in schizophrenia: Evidence for compromised brain metabolism and oxidative stress","volume":"9","author":"Prabakaran","year":"2004","journal-title":"Mol. Psychiatry"},{"key":"ref_390","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1016\/j.pnpbp.2012.07.013","article-title":"Reduced antioxidant defense systems in schizophrenia and bipolar I disorder","volume":"39","author":"Raffa","year":"2012","journal-title":"Prog. Neuro-Psychopharmacol. Biol. Psychiatry"},{"key":"ref_391","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1155\/2006\/248387","article-title":"Altered glutathione redox state in schizophrenia","volume":"22","author":"Yao","year":"2006","journal-title":"Dis. Markers"},{"key":"ref_392","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1017\/S1461145710000805","article-title":"Decreased levels of glutathione, the major brain antioxidant, in post-mortem prefrontal cortex from patients with psychiatric disorders","volume":"14","author":"Gawryluk","year":"2011","journal-title":"Int. J. Neuropsychopharmacol."},{"key":"ref_393","doi-asserted-by":"crossref","first-page":"3721","DOI":"10.1046\/j.1460-9568.2000.00229.x","article-title":"Schizophrenia: Glutathione deficit in cerebrospinal fluid and prefrontal cortex in vivo","volume":"12","author":"Do","year":"2000","journal-title":"Eur. J. Neurosci."},{"key":"ref_394","doi-asserted-by":"crossref","first-page":"1178","DOI":"10.1016\/j.pnpbp.2009.06.018","article-title":"Decreased glutathione levels and antioxidant enzyme activities in untreated and treated schizophrenic patients","volume":"33","author":"Raffa","year":"2009","journal-title":"Prog. Neuro-Psychopharmacol. Biol. Psychiatry"},{"key":"ref_395","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/j.jtemb.2012.07.009","article-title":"Effect of S-allylcysteine, a sulphur containing amino acid on iron metabolism in streptozotocin induced diabetic rats","volume":"27","author":"Saravanan","year":"2013","journal-title":"J. Trace Elem. Med. Biol."},{"key":"ref_396","doi-asserted-by":"crossref","first-page":"993","DOI":"10.1016\/j.jhep.2008.02.011","article-title":"Fructose consumption as a risk factor for non-alcoholic fatty liver disease","volume":"48","author":"Ouyang","year":"2008","journal-title":"J. Hepatol."},{"key":"ref_397","doi-asserted-by":"crossref","first-page":"3633","DOI":"10.1210\/en.2012-1341","article-title":"Fructose-induced hypothalamic AMPK activation stimulates hepatic PEPCK and gluconeogenesis due to increased corticosterone levels","volume":"153","author":"Kinote","year":"2012","journal-title":"Endocrinology"},{"key":"ref_398","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1016\/j.metabol.2012.06.008","article-title":"High-fat, high-fructose diet induces hepatic iron overload via a hepcidin-independent mechanism prior to the onset of liver steatosis and insulin resistance in mice","volume":"62","author":"Tsuchiya","year":"2013","journal-title":"Metabolism"},{"key":"ref_399","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1093\/ajcn\/61.1.105","article-title":"Copper deficiency: Interaction with high-fructose and high-fat diets in rats","volume":"61","author":"Wapnir","year":"1995","journal-title":"Am. J. Clin. Nutr."},{"key":"ref_400","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1210\/en.2014-1454","article-title":"Restoration of autophagy alleviates hepatic ER stress and impaired insulin signalling transduction in high fructose-fed male mice","volume":"156","author":"Wang","year":"2015","journal-title":"Endocrinology"},{"key":"ref_401","doi-asserted-by":"crossref","first-page":"208","DOI":"10.4103\/1673-5374.152371","article-title":"Is glial heme oxygenase-1 suppression in neurodegenerative disorders permissive for neural repair?","volume":"10","author":"Schipper","year":"2015","journal-title":"Neural Regen. Res."},{"key":"ref_402","doi-asserted-by":"crossref","first-page":"776","DOI":"10.1111\/j.1471-4159.2009.06007.x","article-title":"HO-1-mediated macroautophagy: A mechanism for unregulated iron deposition in aging and degenerating neural tissues","volume":"109","author":"Zukor","year":"2009","journal-title":"J. Neurochem."},{"key":"ref_403","first-page":"57","article-title":"CYP2E1 overexpression up-regulates both non-specific \u03b4-aminolevulinate synthase and heme oxygenase-1 in the human hepatoma cell line HLE\/2E1","volume":"11","author":"Takahashi","year":"2003","journal-title":"Int. J. Mol. Med."},{"key":"ref_404","doi-asserted-by":"crossref","first-page":"1136","DOI":"10.1111\/j.1440-1746.2009.06196.x","article-title":"Oxidative stress and regulation of anti-oxidant enzymes in cytochrome P4502E1 transgenic mouse model of non-alcoholic fatty liver","volume":"25","author":"Kathirvel","year":"2010","journal-title":"J. Gastroenterol. Hepatol."},{"key":"ref_405","doi-asserted-by":"crossref","first-page":"1024","DOI":"10.1124\/mol.54.6.1024","article-title":"Oxidative stress and cytotoxicity induced by ferric-nitrilotriacetate in HepG2 cells that express cytochrome P450 2E1","volume":"54","author":"Sakurai","year":"1998","journal-title":"Mol. Pharmacol."},{"key":"ref_406","doi-asserted-by":"crossref","first-page":"5128","DOI":"10.1074\/jbc.M510484200","article-title":"Overexpression of CYP2E1 in mitochondria sensitizes HepG2 cells to the toxicity caused by depletion of glutathione","volume":"281","author":"Bai","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_407","doi-asserted-by":"crossref","first-page":"33698","DOI":"10.1074\/jbc.M805999200","article-title":"Structures of human cytochrome P-450 2E1: Insights into the binding of inhibitors and both small molecular weight and fatty acid substrates","volume":"283","author":"Porubsky","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_408","doi-asserted-by":"crossref","unstructured":"Huo, R., Tang, K., Wei, Z., Shen, L., Xiong, Y., Wu, X., Niu, J., Han, X., Tian, Z., and Yang, L. (2012). Genetic polymorphisms in CYP2E1: Association with schizophrenia susceptibility and risperidone response in the Chinese Han population. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0034809"},{"key":"ref_409","first-page":"4205","article-title":"Ferulic acid attenuated acetaminophen-induced hepatotoxicity though down-regulating the cytochrome P 2E1 and inhibiting toll-like receptor 4 signaling-mediated inflammation in mice","volume":"8","author":"Yuan","year":"2016","journal-title":"Am. J. Transl. Res."},{"key":"ref_410","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1006\/abbi.1997.9907","article-title":"Characterization of cytochrome P4502E1 turnover in transfected HepG2 cells expressing human CYP2E1","volume":"341","author":"Yang","year":"1997","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_411","doi-asserted-by":"crossref","first-page":"29632","DOI":"10.1074\/jbc.270.50.29632","article-title":"Ethanol induces CYP2E1 by protein stabilization: Role of ubiquitin conjugation in the rapid degradation of CYP2E1","volume":"270","author":"Roberts","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_412","first-page":"315","article-title":"Induction of heme oxygenase-1 in human hepatocytes to protect them from ethanol-induced cytotoxicity","volume":"17","author":"Liu","year":"2004","journal-title":"Biomed. Environ. Sci."},{"key":"ref_413","doi-asserted-by":"crossref","first-page":"S63","DOI":"10.1002\/hep.20957","article-title":"Alcohol and oxidative liver injury","volume":"43","author":"Dey","year":"2006","journal-title":"Hepatology"},{"key":"ref_414","doi-asserted-by":"crossref","first-page":"1406","DOI":"10.1016\/j.freeradbiomed.2010.07.026","article-title":"Chronic alcohol-induced liver injury and oxidant stress are decreased in cytochrome P4502E1 knockout mice and restored in humanized cytochrome P4502E1 knock-in mice","volume":"49","author":"Lu","year":"2010","journal-title":"Free Radic. Biol. Med."},{"key":"ref_415","doi-asserted-by":"crossref","first-page":"1352","DOI":"10.1111\/j.1530-0277.1996.tb01134.x","article-title":"Alcohol mediates increases in hepatic and serum nonheme iron stores in a rat model for alcohol-induced liver injury","volume":"20","author":"Valerio","year":"1996","journal-title":"Alcohol. Clin. Exp. Res."},{"key":"ref_416","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1111\/acer.12209","article-title":"MiR-214 promotes the alcohol-induced oxidative stress via down-regulation of glutathione reductase and cytochrome P450 oxidoreductase in liver cells","volume":"38","author":"Dong","year":"2014","journal-title":"Alcohol. Clin. Exp. Res."},{"key":"ref_417","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1097\/MEG.0b013e328328f461","article-title":"Overexpression of liver-specific cytochrome P4502E1 impairs hepatic insulin signaling in a transgenic mouse model of nonalcoholic fatty liver disease","volume":"21","author":"Kathirvel","year":"2009","journal-title":"Eur. J. Gastroenterol. Hepatol."},{"key":"ref_418","doi-asserted-by":"crossref","unstructured":"Zhao, Z., Li, S., Liu, G., Yan, F., Ma, X., Huang, Z., and Tian, H. (2012). Body iron stores and heme-iron intake in relation to risk of type 2 diabetes: A systematic review and meta-analysis. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0041641"},{"key":"ref_419","doi-asserted-by":"crossref","first-page":"308","DOI":"10.1002\/dmrr.2394","article-title":"Ferritin levels and risk of type 2 diabetes mellitus: An updated systematic review and meta-analysis of prospective evidence","volume":"29","author":"Kunutsor","year":"2013","journal-title":"Diabetes\/Metab. Res. Rev."},{"key":"ref_420","first-page":"336","article-title":"Hepatic porphyrias. Cytochemical and ultrastructural studies of liver in acute intermittent porphyria and porphyria cutanea tarda","volume":"98","author":"Biempica","year":"1974","journal-title":"Arch. Pathol."},{"key":"ref_421","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1016\/j.jhep.2004.11.040","article-title":"Heme oxygenase-1 levels and oxidative stress-related parameters in non-alcoholic fatty liver disease patients","volume":"42","author":"Malaguarnera","year":"2005","journal-title":"J. Hepatol."},{"key":"ref_422","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1007\/s10147-012-0430-8","article-title":"Genetic polymorphisms of CYP17A1 in steroidogenesis pathway are associated with risk of progression to castration-resistant prostate cancer in Japanese men receiving androgen deprivation therapy","volume":"18","author":"Yamada","year":"2013","journal-title":"Int. J. Clin. Oncol."},{"key":"ref_423","doi-asserted-by":"crossref","first-page":"6760","DOI":"10.1038\/ncomms7760","article-title":"Alzheimer\u2019s Disease Neuroimaging Initiative. Ferritin levels in the cerebrospinal fluid predict Alzheimer\u2019s disease outcomes and are regulated by APOE","volume":"6","author":"Ayton","year":"2015","journal-title":"Nat. Commun."},{"key":"ref_424","doi-asserted-by":"crossref","first-page":"1066","DOI":"10.1158\/1055-9965.EPI-07-2680","article-title":"Polymorphisms in steroid hormone biosynthesis genes and risk of breast cancer and fibrocystic breast conditions in Chinese women","volume":"17","author":"Sakoda","year":"2008","journal-title":"Cancer Epidemiol. Biomark. Prev."},{"key":"ref_425","doi-asserted-by":"crossref","first-page":"760","DOI":"10.1093\/brain\/awm337","article-title":"Recessive hereditary methaemoglobinaemia, type II: Delineation of the clinical spectrum","volume":"131","author":"Ewenczyk","year":"2008","journal-title":"Brain"},{"key":"ref_426","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1016\/j.psc.2007.07.006","article-title":"Hematologic problems in psychosomatic medicine","volume":"30","author":"Becker","year":"2007","journal-title":"Psychiatr. Clin. N. Am."},{"key":"ref_427","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/j.ijdevneu.2017.06.007","article-title":"Hemoglobins emerging roles in mental disorders. Metabolical, genetical and immunological aspects","volume":"61","author":"Altinoz","year":"2017","journal-title":"Int. J. Dev. Neurosci."},{"key":"ref_428","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1080\/17512433.2018.1473760","article-title":"Efficacy and safety of iron chelators in thalassemia and sickle cell disease: A multiple treatment comparison network meta-analysis and trial sequential analysis","volume":"11","author":"Sridharan","year":"2018","journal-title":"Expert Rev. Clin. Pharmacol."},{"key":"ref_429","first-page":"328","article-title":"Iron overload in Beta thalassaemia major and intermedia patients","volume":"8","author":"Mishra","year":"2013","journal-title":"Maedica"},{"key":"ref_430","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1016\/j.tox.2015.04.007","article-title":"Sodium nitrite potentiates renal oxidative stress and injury in hemoglobin exposed guinea pigs","volume":"333","author":"Baek","year":"2015","journal-title":"Toxicology"},{"key":"ref_431","doi-asserted-by":"crossref","first-page":"288","DOI":"10.1165\/rcmb.2015-0197OC","article-title":"Oxidized Ferric and Ferryl Forms of Hemoglobin Trigger Mitochondrial Dysfunction and Injury in Alveolar Type I Cells","volume":"55","author":"Chintagari","year":"2016","journal-title":"Am. J. Respir. Cell Mol. Biol."},{"key":"ref_432","doi-asserted-by":"crossref","unstructured":"Jana, S., Meng, F., Hirsch, R.E., Friedman, J.M., and Alayash, A.I. (2017). Oxidized Mutant Human Hemoglobins S and E Induce Oxidative Stress and Bioenergetic Dysfunction in Human Pulmonary Endothelial Cells. Front. Physiol., 8.","DOI":"10.3389\/fphys.2017.01082"},{"key":"ref_433","first-page":"250","article-title":"The transport of hemin and protoporphyrin across the plasma membrane of chick embryo liver cells in culture","volume":"8","author":"Sinclair","year":"1976","journal-title":"Ann. Clin. Res."},{"key":"ref_434","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1016\/S0021-9258(18)93628-8","article-title":"Exchange of heme among hemoglobins and between hemoglobin and albumin","volume":"243","author":"Bunn","year":"1968","journal-title":"J. Biol. Chem."},{"key":"ref_435","first-page":"648","article-title":"Exposure of endothelial cells to free heme potentiates damage mediated by granulocytes and toxic oxygen species","volume":"64","author":"Balla","year":"1991","journal-title":"Lab. Investig. J. Tech. Methods Pathol."},{"key":"ref_436","doi-asserted-by":"crossref","first-page":"9285","DOI":"10.1073\/pnas.90.20.9285","article-title":"Endothelial-cell heme uptake from heme proteins: Induction of sensitization and desensitization to oxidant damage","volume":"90","author":"Balla","year":"1993","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_437","doi-asserted-by":"crossref","first-page":"452","DOI":"10.1007\/s12975-012-0195-4","article-title":"Effect of iron chelators on methemoglobin and thrombin preconditioning","volume":"3","author":"Sinanan","year":"2012","journal-title":"Transl. Stroke Res."},{"key":"ref_438","doi-asserted-by":"crossref","first-page":"876","DOI":"10.1002\/2211-5463.12103","article-title":"Differential heme release from various hemoglobin redox states and the upregulation of cellular heme oxygenase-1","volume":"6","author":"Kassa","year":"2016","journal-title":"FEBS Open Bio"},{"key":"ref_439","doi-asserted-by":"crossref","first-page":"H2405","DOI":"10.1152\/ajpheart.2000.279.5.H2405","article-title":"Effects of hemoglobin on heme oxygenase gene expression and viability of cultured smooth muscle cells","volume":"279","author":"Marton","year":"2000","journal-title":"Am. J. Physiol.-Heart Circ. Physiol."},{"key":"ref_440","doi-asserted-by":"crossref","first-page":"27939","DOI":"10.1074\/jbc.M115.651257","article-title":"Sickle Cell Hemoglobin in the Ferryl State Promotes \u03b2Cys-93 Oxidation and Mitochondrial Dysfunction in Epithelial Lung Cells (E10)","volume":"290","author":"Kassa","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_441","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1016\/j.redox.2016.03.004","article-title":"Oxidative instability of hemoglobin E (\u03b226 Glu\u2192Lys) is increased in the presence of free \u03b1 subunits and reversed by \u03b1-hemoglobin stabilizing protein (AHSP): Relevance to HbE\/\u03b2-thalassemia","volume":"8","author":"Strader","year":"2016","journal-title":"Redox Biol."},{"key":"ref_442","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1016\/0891-5849(96)00035-4","article-title":"Correlation of membrane lipid peroxidation with oxidation of hemoglobin variants: Possibly related to the rates of hemin release","volume":"21","author":"Chiu","year":"1996","journal-title":"Free Radic. Biol. Med."},{"key":"ref_443","doi-asserted-by":"crossref","first-page":"14557","DOI":"10.1074\/jbc.M107658200","article-title":"Heme redox properties of S-nitrosated hemoglobin A0 and hemoglobin S: Implications for interactions of nitric oxide with normal and sickle red blood cells","volume":"277","author":"Bonaventura","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_444","doi-asserted-by":"crossref","first-page":"23452","DOI":"10.1074\/jbc.M110.183186","article-title":"Structural and functional studies indicating altered redox properties of hemoglobin E: Implications for production of bioactive nitric oxide","volume":"286","author":"Roche","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_445","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1182\/blood-2017-07-798728","article-title":"Inhibition of heme oxygenase ameliorates anemia and reduces iron overload in a \u03b2-thalassemia mouse model","volume":"131","author":"Hamdi","year":"2018","journal-title":"Blood"},{"key":"ref_446","doi-asserted-by":"crossref","first-page":"718","DOI":"10.1073\/pnas.70.3.718","article-title":"Structure of sickled erythrocytes and of sickle-cell hemoglobin fibers","volume":"70","author":"Finch","year":"1973","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_447","doi-asserted-by":"crossref","first-page":"1316","DOI":"10.1107\/S0907444910040370","article-title":"Structure of a crystal form of human methemoglobin indicative of fiber formation","volume":"D66","author":"Larson","year":"2010","journal-title":"Acta Crystallogr. Sect. D Struct. Biol."},{"key":"ref_448","doi-asserted-by":"crossref","first-page":"14","DOI":"10.3164\/jcbn.2008003","article-title":"Erythrocyte glutathione depletion impairs resistance to haemolysis in women consuming alcohol","volume":"42","author":"Padmini","year":"2008","journal-title":"J. Clin. Biochem. Nutr."},{"key":"ref_449","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1016\/j.bcmd.2011.07.003","article-title":"Development of a novel mouse model of severe glucose-6-phosphate dehydrogenase (G6PD)-deficiency for in vitro and in vivo assessment of hemolytic toxicity to red blood cells","volume":"47","author":"Ko","year":"2011","journal-title":"Blood Cells Mol. Dis."},{"key":"ref_450","doi-asserted-by":"crossref","first-page":"11153","DOI":"10.1073\/pnas.0404349101","article-title":"A role for heme in Alzheimer\u2019s disease: Heme binds amyloid \u03b2 and has altered metabolism","volume":"101","author":"Atamna","year":"2004","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_451","doi-asserted-by":"crossref","first-page":"817","DOI":"10.1016\/0092-8674(94)90131-7","article-title":"Hydrogen peroxide mediates amyloid \u03b2 protein toxicity","volume":"77","author":"Behl","year":"1994","journal-title":"Cell"},{"key":"ref_452","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1046\/j.1471-4159.2001.00379.x","article-title":"Induction of NADPH cytochrome P450 reductase by the Alzheimer \u03b2-protein. Amyloid as a \u2018foreign body\u2019","volume":"78","author":"Pappolla","year":"2001","journal-title":"J. Neurochem."},{"key":"ref_453","doi-asserted-by":"crossref","first-page":"1170","DOI":"10.4103\/1673-5374.235021","article-title":"Amyloid \u03b2 and free heme: Bloody new insights into the pathogenesis of Alzheimer\u2019s disease","volume":"13","author":"Flemmig","year":"2018","journal-title":"Neural Regen. Res."},{"key":"ref_454","doi-asserted-by":"crossref","first-page":"991","DOI":"10.1111\/jth.13277","article-title":"Alzheimer disease is in part a thrombohemorrhagic disorder","volume":"14","author":"Schmaier","year":"2016","journal-title":"J. Thromb. Haemost."},{"key":"ref_455","doi-asserted-by":"crossref","first-page":"38933","DOI":"10.1074\/jbc.M110.132860","article-title":"Inhibitors of catalase-amyloid interactions protect cells from \u03b2-amyloid-induced oxidative stress and toxicity","volume":"285","author":"Habib","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_456","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1038\/s41392-020-00428-9","article-title":"Ferroptosis: Mechanisms and links with diseases","volume":"6","author":"Yan","year":"2021","journal-title":"Signal Transduct. Target. Ther."},{"key":"ref_457","doi-asserted-by":"crossref","first-page":"e70769","DOI":"10.1096\/fj.202500415R","article-title":"Ferroptosis as an emerging target in diabetic Osteoporosis","volume":"39","author":"Li","year":"2025","journal-title":"FASEB J."},{"key":"ref_458","doi-asserted-by":"crossref","first-page":"925","DOI":"10.1111\/febs.70351","article-title":"Histone demethylases regulate ferroptosis in metabolic dysfunction-associated steatotic liver disease via epigenetic modification","volume":"293","author":"Huang","year":"2026","journal-title":"FEBS J."},{"key":"ref_459","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1124\/jpet.118.252759","article-title":"Ferroptosis as a Novel Therapeutic Target for Friedreich\u2019s Ataxia","volume":"369","author":"Cotticelli","year":"2019","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"ref_460","doi-asserted-by":"crossref","first-page":"e70916","DOI":"10.1096\/fj.202501371R","article-title":"Role of Ferroptosis in the Redox Biology of Mycotoxins","volume":"39","author":"Li","year":"2025","journal-title":"FASEB J."},{"key":"ref_461","doi-asserted-by":"crossref","unstructured":"Fei, Y., and Ding, Y. (2024). The role of ferroptosis in neurodegenerative diseases. Front. Cell. Neurosci., 18.","DOI":"10.3389\/fncel.2024.1475934"},{"key":"ref_462","doi-asserted-by":"crossref","first-page":"37","DOI":"10.3892\/mmr.2024.13402","article-title":"Ferroptosis in schizophrenia: Mechanisms and therapeutic potentials (Review)","volume":"31","author":"Lv","year":"2025","journal-title":"Mol. Med. Rep."},{"key":"ref_463","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1016\/j.cell.2017.09.021","article-title":"Ferroptosis: A Regulated Cell Death Nexus Linking Metabolism, Redox Biology, and Disease","volume":"171","author":"Stockwell","year":"2017","journal-title":"Cell"},{"key":"ref_464","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/j.tcb.2015.10.014","article-title":"Ferroptosis: Death by Lipid Peroxidation","volume":"26","author":"Yang","year":"2015","journal-title":"Trends Cell Biol."},{"key":"ref_465","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1016\/j.molcel.2020.11.024","article-title":"Membrane Damage during Ferroptosis Is Caused by Oxidation of Phospholipids Catalyzed by the Oxidoreductases POR and CYB5R1","volume":"81","author":"Yan","year":"2021","journal-title":"Mol. Cell"},{"key":"ref_466","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_467","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1038\/nchembio.2238","article-title":"Oxidized arachidonic and adrenic PEs navigate cells to ferroptosis","volume":"13","author":"Kagan","year":"2017","journal-title":"Nat. Chem. Biol."},{"key":"ref_468","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1038\/s41589-020-0472-6","article-title":"Cytochrome P450 oxidoreductase contributes to phospholipid peroxidation in ferroptosis","volume":"16","author":"Zou","year":"2020","journal-title":"Nat. Chem. Biol."},{"key":"ref_469","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":"ref_470","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1038\/s41418-024-01280-y","article-title":"Mitophagy mediated by BNIP3 and NIX protects against ferroptosis by downregulating mitochondrial reactive oxygen species","volume":"31","author":"Yamashita","year":"2024","journal-title":"Cell Death Differ."},{"key":"ref_471","doi-asserted-by":"crossref","first-page":"630","DOI":"10.1016\/j.ajhg.2017.09.007","article-title":"FDXR Mutations Cause Sensorial Neuropathies and Expand the Spectrum of Mitochondrial Fe-S-Synthesis Diseases","volume":"101","author":"Paul","year":"2017","journal-title":"Am. J. Hum. Genet."},{"key":"ref_472","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1038\/s41420-025-02840-y","article-title":"Ferroptosis is a novel pathogenic mechanism of FDXR-related disease via disruption of the NRF2 pathway","volume":"11","author":"Campbell","year":"2025","journal-title":"Cell Death Discov."},{"key":"ref_473","doi-asserted-by":"crossref","unstructured":"Xu, J., Chen, C., Yuan, H.-Y., Zhang, Y.-Y., Wang, C.-R., Xi, X., Pan, H., Li, D.-H., and Lu, Y. (2026). Reappraising heme oxygenase-1 as a ferroptosis modulator in atherosclerosis: A mechanism-focused review. Front. Immunol., 17.","DOI":"10.3389\/fimmu.2026.1737751"},{"key":"ref_474","doi-asserted-by":"crossref","unstructured":"Zou, X.-Y., Cai, L.-Y., Zhang, J., Yuan, Y., Song, J., Hu, Z.-D., Ruan, X.-F., Peng, R., and Zhang, X.-M. (2025). Mechanism of heme oxygenase-1 regulation of ferroptosis in vascular dementia. Front. Mol. Neurosci., 18.","DOI":"10.3389\/fnmol.2025.1585079"},{"key":"ref_475","doi-asserted-by":"crossref","first-page":"101971","DOI":"10.1016\/j.redox.2021.101971","article-title":"HO-1-mediated ferroptosis as a target for protection against retinal pigment epithelium degeneration","volume":"43","author":"Tang","year":"2021","journal-title":"Redox Biol."},{"key":"ref_476","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":"ref_477","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":"Cancer Lett."},{"key":"ref_478","doi-asserted-by":"crossref","first-page":"3341","DOI":"10.1172\/JCI99032","article-title":"Nano-targeted induction of dual ferroptotic mechanisms eradicates high-risk neuroblastoma","volume":"128","author":"Hassannia","year":"2018","journal-title":"J. Clin. Investig."},{"key":"ref_479","doi-asserted-by":"crossref","first-page":"1800","DOI":"10.1096\/fasebj.13.13.1800","article-title":"Reversal of HO-1 related cytoprotection with increased expression is due to reactive iron","volume":"13","author":"Suttner","year":"1999","journal-title":"FASEB J."},{"key":"ref_480","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1126\/science.aaw9872","article-title":"Cysteine depletion induces pancreatic tumor ferroptosis in mice","volume":"368","author":"Badgley","year":"2020","journal-title":"Science"},{"key":"ref_481","doi-asserted-by":"crossref","first-page":"1345","DOI":"10.3233\/JAD-170543","article-title":"Oxidative Stress, Amyloid-\u03b2 Peptide, and Altered Key Molecular Pathways in the Pathogenesis and Progression of Alzheimer\u2019s Disease","volume":"62","author":"Butterfield","year":"2018","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_482","doi-asserted-by":"crossref","first-page":"e35142","DOI":"10.1097\/MD.0000000000035142","article-title":"Research progress of ferroptosis in Alzheimer disease: A review","volume":"102","author":"Han","year":"2023","journal-title":"Medicine"},{"key":"ref_483","doi-asserted-by":"crossref","first-page":"782","DOI":"10.1038\/s41419-024-07152-0","article-title":"The link between amyloid \u03b2 and ferroptosis pathway in Alzheimer\u2019s disease progression","volume":"15","author":"Salinas","year":"2024","journal-title":"Cell Death Dis."},{"key":"ref_484","doi-asserted-by":"crossref","first-page":"1749","DOI":"10.1046\/j.1471-4159.2000.0741749.x","article-title":"Differential assembly of human tau isoforms in the presence of arachidonic acid","volume":"74","author":"King","year":"2000","journal-title":"J. Neurochem."},{"key":"ref_485","doi-asserted-by":"crossref","first-page":"562","DOI":"10.1016\/j.neurobiolaging.2012.05.009","article-title":"Intranasal deferoxamine reverses iron-induced memory deficits and inhibits amyloidogenic APP processing in a transgenic mouse model of Alzheimer\u2019s disease","volume":"34","author":"Guo","year":"2013","journal-title":"Neurobiol. Aging"},{"key":"ref_486","doi-asserted-by":"crossref","unstructured":"Guo, C., Zhang, Y.-X., Wang, T., Zhong, M.-L., Yang, Z.-H., Hao, L.-J., Chai, R., and Zhang, S. (2015). Intranasal deferoxamine attenuates synapse loss via up-regulating the P38\/HIF-1\u03b1 pathway on the brain of APP\/PS1 transgenic mice. Front. Aging Neurosci., 7.","DOI":"10.3389\/fnagi.2015.00104"},{"key":"ref_487","doi-asserted-by":"crossref","unstructured":"Harjum\u00e4ki, R., Pridgeon, C.S., and Ingelman-Sundberg, M. (2021). CYP2E1 in Alcoholic and Non-Alcoholic Liver Injury. Roles of ROS, Reactive Intermediates and Lipid Overload. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22158221"},{"key":"ref_488","doi-asserted-by":"crossref","first-page":"802","DOI":"10.1159\/000324289","article-title":"Role of CYP2E1 in ethanol-induced oxidant stress, fatty liver and hepatotoxicity","volume":"28","author":"Cederbaum","year":"2010","journal-title":"Dig. Dis."},{"key":"ref_489","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1016\/j.cotox.2020.07.001","article-title":"Molecular role of cytochrome P4501A enzymes inoxidative stress","volume":"20\u201321","author":"Stading","year":"2020","journal-title":"Curr. Opin. Toxicol."},{"key":"ref_490","doi-asserted-by":"crossref","first-page":"2833","DOI":"10.1021\/acs.molpharmaceut.6b00436","article-title":"Mechanism-Based Inhibition of CYP3A4 by Podophyllotoxin: Aging of an Intermediate Is Important for in Vitro\/in Vivo Correlations","volume":"13","author":"Barnaba","year":"2016","journal-title":"Mol. Pharm."},{"key":"ref_491","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1016\/j.bcp.2018.08.010","article-title":"Kinetic mechanism of time-dependent inhibition of CYP2D6 by 3,4-methylenedioxymethamphetamine (MDMA): Functional heterogeneity of the enzyme and the reversibility of its inactivation","volume":"156","author":"Rodgers","year":"2018","journal-title":"Biochem. Pharmacol."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/27\/15\/6971\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,8,6]],"date-time":"2026-08-06T04:29:12Z","timestamp":1785990552000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/27\/15\/6971"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,8,3]]},"references-count":491,"journal-issue":{"issue":"15","published-online":{"date-parts":[[2026,8]]}},"alternative-id":["ijms27156971"],"URL":"https:\/\/doi.org\/10.3390\/ijms27156971","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,8,3]]}}}