{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T05:40:41Z","timestamp":1791351641613,"version":"4.3.1"},"reference-count":142,"publisher":"MDPI AG","issue":"4","license":[{"start":{"date-parts":[[2015,3,31]],"date-time":"2015-03-31T00:00:00Z","timestamp":1427760000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Nutrients"],"abstract":"<jats:p>Iron and ascorbate are vital cellular constituents in mammalian systems.  The bulk-requirement for iron is during erythropoiesis leading to the generation of hemoglobin-containing erythrocytes. Additionally; both iron and ascorbate are required as co-factors in numerous metabolic reactions. Iron homeostasis is controlled at the level of uptake; rather than excretion. Accumulating evidence strongly suggests that in addition to the known ability of dietary ascorbate to enhance non-heme iron absorption in the gut; ascorbate regulates iron homeostasis. The involvement of ascorbate in dietary iron absorption extends beyond the direct chemical reduction of non-heme iron by dietary ascorbate. Among other activities; intra-enterocyte ascorbate appears to be involved in the provision of electrons to a family of trans-membrane redox enzymes; namely those of the cytochrome b561 class. These hemoproteins oxidize a pool of ascorbate on one side of the membrane in order to reduce an electron acceptor (e.g., non-heme iron) on the opposite side of the membrane. One member of this family; duodenal cytochrome b (DCYTB); may play an important role in ascorbate-dependent reduction of non-heme iron in the gut prior to uptake by ferrous-iron transporters. This review discusses the emerging relationship between cellular iron homeostasis; the emergent \u201cIRP1-HIF2\u03b1 axis\u201d; DCYTB and ascorbate in relation to  iron metabolism.<\/jats:p>","DOI":"10.3390\/nu7042274","type":"journal-article","created":{"date-parts":[[2015,4,7]],"date-time":"2015-04-07T03:47:46Z","timestamp":1428378466000},"page":"2274-2296","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":150,"title":["Duodenal Cytochrome b (DCYTB) in Iron Metabolism: An Update on Function and Regulation"],"prefix":"10.3390","volume":"7","author":[{"given":"Darius","family":"Lane","sequence":"first","affiliation":[{"name":"Molecular Pharmacology and Pathology Program, Department of Pathology and Bosch Institute, University of Sydney, Sydney, NSW 2006, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dong-Hun","family":"Bae","sequence":"additional","affiliation":[{"name":"Molecular Pharmacology and Pathology Program, Department of Pathology and Bosch Institute, University of Sydney, Sydney, NSW 2006, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Angelica","family":"Merlot","sequence":"additional","affiliation":[{"name":"Molecular Pharmacology and Pathology Program, Department of Pathology and Bosch Institute, University of Sydney, Sydney, NSW 2006, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sumit","family":"Sahni","sequence":"additional","affiliation":[{"name":"Molecular Pharmacology and Pathology Program, Department of Pathology and Bosch Institute, University of Sydney, Sydney, NSW 2006, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Des","family":"Richardson","sequence":"additional","affiliation":[{"name":"Molecular Pharmacology and Pathology Program, Department of Pathology and Bosch Institute, University of Sydney, Sydney, NSW 2006, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2015,3,31]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1146\/annurev.nutr.28.061807.155521","article-title":"Systemic iron homeostasis and the iron-responsive element\/iron-regulatory protein (IRE\/IRP) regulatory network","volume":"28","author":"Muckenthaler","year":"2008","journal-title":"Annu. Rev. Nutr."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/j.tcb.2006.12.003","article-title":"Iron uptake and metabolism in the new millennium","volume":"17","author":"Dunn","year":"2007","journal-title":"Trends Cell Biol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"2473","DOI":"10.1089\/ars.2011.4271","article-title":"Mammalian iron homeostasis in health and disease: Uptake, storage, transport, and molecular mechanisms of action","volume":"18","author":"Lawen","year":"2013","journal-title":"Antioxid. Redox Signal."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"3034","DOI":"10.3390\/nu5083034","article-title":"Out of balance\u2014Systemic iron homeostasis in iron-related disorders","volume":"5","author":"Steinbicker","year":"2013","journal-title":"Nutrients"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"783","DOI":"10.1016\/j.bbagen.2010.02.005","article-title":"Cytosolic and mitochondrial ferritins in the regulation of cellular iron homeostasis and oxidative damage","volume":"1800","author":"Arosio","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_6","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_7","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1242\/dmm.009019","article-title":"Biogenesis of iron-sulfur clusters in mammalian cells: New insights and relevance to human disease","volume":"5","author":"Rouault","year":"2012","journal-title":"Dis. Model. Mech."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"1130","DOI":"10.1016\/j.bbamcr.2015.01.021","article-title":"Cellular iron uptake, trafficking and metabolism: Key molecules and mechanisms and their roles in disease","volume":"1853","author":"Lane","year":"2015","journal-title":"Biochim. Biophys. Acta."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"173","DOI":"10.3389\/fphar.2014.00173","article-title":"Special delivery: Distributing iron in the cytosol of mammalian cells","volume":"5","author":"Philpott","year":"2014","journal-title":"Front. Pharmacol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"10775","DOI":"10.1073\/pnas.0912925107","article-title":"Mitochondrial iron trafficking and the integration of iron metabolism between the mitochondrion and cytosol","volume":"107","author":"Richardson","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_11","first-page":"166","article-title":"Expanding horizons in iron chelation and the treatment of cancer: Role of iron in the regulation of ER stress and the epithelial-mesenchymal transition","volume":"1845","author":"Lane","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"8175","DOI":"10.1073\/pnas.93.16.8175","article-title":"Molecular control of vertebrate iron metabolism: MRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress","volume":"93","author":"Hentze","year":"1996","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0304-4157(96)00014-7","article-title":"The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells","volume":"1331","author":"Richardson","year":"1997","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/j.cell.2010.06.028","article-title":"Two to tango: Regulation of mammalian iron metabolism","volume":"142","author":"Hentze","year":"2010","journal-title":"Cell"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1016\/j.freeradbiomed.2009.06.003","article-title":"Ascorbate and plasma membrane electron transport\u2014Enzymes vs. efflux","volume":"47","author":"Lane","year":"2009","journal-title":"Free Radic. Biol. Med."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1111\/j.1742-4658.2006.05607.x","article-title":"Vitamin C. Biosynthesis, recycling and degradation in mammals","volume":"274","author":"Linster","year":"2007","journal-title":"FEBS J."},{"key":"ref_17","first-page":"11","article-title":"Ascorbic acid-important for iron metabolism","volume":"50","author":"Atanassova","year":"2008","journal-title":"Folia Med. (Plovdiv)"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"2846","DOI":"10.1074\/jbc.270.6.2846","article-title":"Ascorbic acid enhances iron-induced ferritin translation in human leukemia and hepatoma cells","volume":"270","author":"Toth","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"14773","DOI":"10.1016\/S0021-9258(18)47862-3","article-title":"Ascorbic acid inhibits lysosomal autophagy of ferritin","volume":"262","author":"Bridges","year":"1987","journal-title":"J. Biol. Chem."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1188S","DOI":"10.1093\/ajcn\/54.6.1188s","article-title":"Ascorbic acid and iron metabolism: Alterations in lysosomal function","volume":"54","author":"Hoffman","year":"1991","journal-title":"Am. J. Clin. Nutr."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"454","DOI":"10.1016\/S0022-2143(99)90166-X","article-title":"Role of ceruloplasmin and ascorbate in cellular iron release","volume":"134","author":"Richardson","year":"1999","journal-title":"J. Lab. Clin. Med."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"12701","DOI":"10.1074\/jbc.M800713200","article-title":"Non-transferrin iron reduction and uptake are regulated by transmembrane ascorbate cycling in K562 cells","volume":"283","author":"Lane","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1042\/BJ20101317","article-title":"Two routes of iron accumulation in astrocytes: Ascorbate-dependent ferrous iron uptake via the divalent metal transporter (DMT1) plus an independent route for ferric iron","volume":"432","author":"Lane","year":"2010","journal-title":"Biochem. J."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1080\/10408360701428257","article-title":"The regulation of cellular iron metabolism","volume":"44","author":"Chua","year":"2007","journal-title":"Crit. Rev. Clin. Lab. Sci."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1016\/j.cmet.2005.01.003","article-title":"The iron exporter ferroportin\/Slc40a1 is essential for iron homeostasis","volume":"1","author":"Donovan","year":"2005","journal-title":"Cell Metab."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1426","DOI":"10.1016\/j.bbamcr.2012.03.004","article-title":"Ferroportin-mediated iron transport: Expression and regulation","volume":"1823","author":"Ward","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"2569","DOI":"10.1091\/mbc.e07-01-0060","article-title":"The molecular mechanism of hepcidin-mediated ferroportin down-regulation","volume":"18","author":"Ward","year":"2007","journal-title":"Mol. Biol. Cell"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"7806","DOI":"10.1074\/jbc.M008922200","article-title":"Hepcidin, a urinary antimicrobial peptide synthesized in the liver","volume":"276","author":"Park","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"2090","DOI":"10.1126\/science.1104742","article-title":"Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization","volume":"306","author":"Nemeth","year":"2004","journal-title":"Science"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"6225","DOI":"10.1182\/blood-2009-01-201590","article-title":"Hepcidin, the hormone of iron metabolism, is bound specifically to \u03b1-2-macroglobulin in blood","volume":"113","author":"Peslova","year":"2009","journal-title":"Blood"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"25450","DOI":"10.1074\/jbc.M113.471573","article-title":"Hepcidin bound to \u03b12-macroglobulin reduces ferroportin-1 expression and enhances its activity at reducing serum iron levels","volume":"288","author":"Huang","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"1434","DOI":"10.1016\/j.bbamcr.2012.01.014","article-title":"Hepcidin and iron homeostasis","volume":"1823","author":"Ganz","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1182\/blood-2014-05-516252","article-title":"Molecular liaisons between erythropoiesis and iron metabolism","volume":"124","author":"Kautz","year":"2014","journal-title":"Blood"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"G397","DOI":"10.1152\/ajpgi.00348.2013","article-title":"Mechanistic and regulatory aspects of intestinal iron absorption","volume":"307","author":"Gulec","year":"2014","journal-title":"Am. J. Physiol. Gastrointest. Liver Physiol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1007\/s10534-006-9030-2","article-title":"Regulation of systemic iron homeostasis: How the body responds to changes in iron demand","volume":"20","author":"Anderson","year":"2007","journal-title":"Biometals"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1024\/0300-9831\/a000029","article-title":"Intestinal iron absorption: Regulation by dietary & systemic factors","volume":"80","author":"Sharp","year":"2010","journal-title":"Int. J. Vitam. Nutr. Res."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1038\/199384a0","article-title":"Reducing agents and absorption of iron","volume":"199","author":"Pollack","year":"1963","journal-title":"Nature"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"1755","DOI":"10.1126\/science.1057206","article-title":"An iron-regulated ferric reductase associated with the absorption of dietary iron","volume":"291","author":"McKie","year":"2001","journal-title":"Science"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"1026","DOI":"10.1089\/ars.2012.5065","article-title":"Cytochromes b561: Ascorbate-mediated trans-membrane electron transport","volume":"19","author":"Asard","year":"2013","journal-title":"Antioxid. Redox Signal."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"1239","DOI":"10.1042\/BST0361239","article-title":"The role of Dcytb in iron metabolism: An update","volume":"36","author":"McKie","year":"2008","journal-title":"Biochem. Soc. Trans."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"1275","DOI":"10.1016\/S0006-2952(99)00040-4","article-title":"Role of ascorbic acid in transferrin-independent reduction and uptake of iron by U-937 cells","volume":"57","author":"May","year":"1999","journal-title":"Biochem. Pharmacol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"310","DOI":"10.1104\/pp.85.1.310","article-title":"Involvement of superoxide radical in extracellular ferric reduction by iron-deficient bean roots","volume":"85","author":"Cakmak","year":"1987","journal-title":"Plant Physiol."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1165\/rcmb.2003-0070OC","article-title":"Superoxide-dependent iron uptake: A new role for anion exchange protein 2","volume":"29","author":"Ghio","year":"2003","journal-title":"Am. J. Respir. Cell Mol. Biol."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1038\/ng0897-383","article-title":"Microcytic anaemia mice have a mutation in Nramp2, a candidate iron transporter gene","volume":"16","author":"Fleming","year":"1997","journal-title":"Nat. Genet."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"13612","DOI":"10.1073\/pnas.0606424103","article-title":"Zip14 (Slc39a14) mediates non-transferrin-bound iron uptake into cells","volume":"103","author":"Liuzzi","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1016\/S1097-2765(00)80425-6","article-title":"A novel duodenal iron-regulated transporter, IREG1, implicated in the basolateral transfer of iron to the circulation","volume":"5","author":"McKie","year":"2000","journal-title":"Mol. Cell"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1038\/5979","article-title":"Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse","volume":"21","author":"Vulpe","year":"1999","journal-title":"Nat. Genet."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"3933","DOI":"10.1182\/blood-2003-09-3139","article-title":"Hephaestin is a ferroxidase that maintains partial activity in sex-linked anemia mice","volume":"103","author":"Chen","year":"2004","journal-title":"Blood"},{"key":"ref_49","first-page":"69","article-title":"The active role of vitamin C in mammalian iron metabolism: Much more than just enhanced iron absorption!","volume":"75C","author":"Lane","year":"2014","journal-title":"Biol. Med."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"1527","DOI":"10.1016\/j.bbamcr.2013.02.010","article-title":"Transferrin iron uptake is stimulated by ascorbate via an intracellular reductive mechanism","volume":"1833","author":"Lane","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"19540","DOI":"10.1074\/jbc.270.33.19540","article-title":"Ascorbic acid enhances ferritin mRNA translation by an IRP\/aconitase switch","volume":"270","author":"Toth","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"249","DOI":"10.3390\/nu6010249","article-title":"Iron transport through ferroportin is induced by intracellular ascorbate and involves IRP2 and HIF2\u03b1","volume":"6","author":"Scheers","year":"2014","journal-title":"Nutrients"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"3722","DOI":"10.1111\/j.1742-4658.2006.05381.x","article-title":"Three mammalian cytochromes b561 are ascorbate-dependent ferrireductases","volume":"273","author":"Su","year":"2006","journal-title":"FEBS J."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"1173S","DOI":"10.1093\/ajcn\/54.6.1173s","article-title":"Cytochrome b561, ascorbic acid, and transmembrane electron transfer","volume":"54","author":"Fleming","year":"1991","journal-title":"Am. J. Clin. Nutr."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1016\/S0021-9258(18)64461-8","article-title":"Studies on the respiratory enzymes of the adrenal gland. I. The medulla","volume":"236","author":"Spiro","year":"1961","journal-title":"J. Biol. Chem."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1016\/0005-2728(71)90052-1","article-title":"Cytochrome b-561 of the bovine adrenal chromaffin granules. A high potential b-type cytochrome","volume":"253","author":"Flatmark","year":"1971","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1016\/0005-2736(80)90109-1","article-title":"Oxidoreductase activities of chromaffin granule ghosts isolated from the bovine adrenal medulla","volume":"597","author":"Terland","year":"1980","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1016\/0006-291X(65)90357-8","article-title":"Cytochrome 559 in the microsomes of the adrenal medulla","volume":"20","author":"Ichikawa","year":"1965","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/S0021-9258(18)33212-5","article-title":"Electron transfer across the chromaffin granule membrane","volume":"258","author":"Njus","year":"1983","journal-title":"J. Biol. Chem."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"6429","DOI":"10.1016\/S0021-9258(19)84579-9","article-title":"Cytochrome b561 spectral changes associated with electron transfer in chromaffin-vesicle ghosts","volume":"261","author":"Kelley","year":"1986","journal-title":"J. Biol. Chem."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"9746","DOI":"10.1016\/S0021-9258(18)67578-7","article-title":"Electron transfer across the chromaffin granule membrane. Use of EPR to demonstrate reduction of intravesicular ascorbate radical by the extravesicular mitochondrial NADH: Ascorbate radical oxidoreductase","volume":"261","author":"Wakefield","year":"1986","journal-title":"J. Biol. Chem."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1016\/0005-2728(93)90108-R","article-title":"The secretory-vesicle ascorbate-regenerating system: A chain of concerted H+\/e\u2212-transfer reactions","volume":"1144","author":"Njus","year":"1993","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"6878","DOI":"10.1016\/S0021-9258(20)89583-0","article-title":"Reaction of ascorbic acid with cytochrome b561. Concerted electron and proton transfer","volume":"266","author":"Jalukar","year":"1991","journal-title":"J. Biol. Chem."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1016\/j.bbapap.2005.08.015","article-title":"Cytochrome b561 protein family: Expanding roles and versatile transmembrane electron transfer abilities as predicted by a new classification system and protein sequence motif analyses","volume":"1753","author":"Tsubaki","year":"2005","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1093\/jb\/mvm181","article-title":"Histidine cycle mechanism for the concerted proton\/electron transfer from ascorbate to the cytosolic haem b centre of cytochrome b561: A unique machinery for the biological transmembrane electron transfer","volume":"142","author":"Nakanishi","year":"2007","journal-title":"J. Biochem."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"1813","DOI":"10.1073\/pnas.1323931111","article-title":"Structure and mechanism of a eukaryotic transmembrane ascorbate-dependent oxidoreductase","volume":"111","author":"Lu","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"1903","DOI":"10.1016\/j.bbagen.2006.07.019","article-title":"An ascorbate-reducible cytochrome b561 is localized in macrophage lysosomes","volume":"1760","author":"Zhang","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1016\/S1570-9639(03)00242-5","article-title":"Stromal cell-derived receptor 2 and cytochrome b561 are functional ferric reductases","volume":"1651","author":"Vargas","year":"2003","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1089\/ars.2013.5809","article-title":"How are cytochrome B561 electron currents controlled by membrane voltage and substrate availability?","volume":"21","author":"Picco","year":"2014","journal-title":"Antioxid. Redox Signal."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1093\/jb\/mvm185","article-title":"Involvement of 101F6, a homologue of cytochrome b561, in the reduction of ferric ions","volume":"142","author":"Mizutani","year":"2007","journal-title":"J. Biochem."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"3660","DOI":"10.1021\/bi301607s","article-title":"Electron transfer reactions of candidate tumor suppressor 101F6 protein, a cytochrome b561 homologue, with ascorbate and monodehydroascorbate radical","volume":"52","author":"Recuenco","year":"2013","journal-title":"Biochemistry"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"1901","DOI":"10.1016\/j.febslet.2008.05.010","article-title":"Dcytb (Cybrd1) functions as both a ferric and a cupric reductase in vitro","volume":"582","author":"Wyman","year":"2008","journal-title":"FEBS Lett."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"L272","DOI":"10.1152\/ajplung.00342.2005","article-title":"Duodenal cytochrome B: A novel ferrireductase in airway epithelial cells","volume":"291","author":"Turi","year":"2006","journal-title":"Am. J. Physiol. Lung Cell. Mol. Physiol."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1007\/s00249-012-0812-x","article-title":"Dihydrolipoic acid reduces cytochrome b561 proteins","volume":"42","author":"Berczi","year":"2013","journal-title":"Eur. Biophys. J."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"1135","DOI":"10.1016\/j.clinbiochem.2007.06.009","article-title":"Uptake and reduction of \u03b1-lipoic acid by human erythrocytes","volume":"40","author":"May","year":"2007","journal-title":"Clin. Biochem."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/S0891-5849(02)00862-6","article-title":"Uptake, recycling, and antioxidant actions of \u03b1-lipoic acid in endothelial cells","volume":"33","author":"Jones","year":"2002","journal-title":"Free Radic. Biol. Med."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1006\/bcmd.2002.0574","article-title":"Molecular and functional roles of duodenal cytochrome B (Dcytb) in iron metabolism","volume":"29","author":"Vulpe","year":"2002","journal-title":"Blood Cells Mol. Dis."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1016\/j.bbabio.2007.12.001","article-title":"Functional characterization of human duodenal cytochrome b (Cybrd1): Redox properties in relation to iron and ascorbate metabolism","volume":"1777","author":"Oakhill","year":"2008","journal-title":"Biochim. Biophys. Acta."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"991","DOI":"10.1093\/jn\/138.6.991","article-title":"Duodenal cytochrome b expression stimulates iron uptake by human intestinal epithelial cells","volume":"138","author":"Simpson","year":"2008","journal-title":"J. Nutr."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"1366","DOI":"10.1016\/j.freeradbiomed.2010.02.021","article-title":"Quercetin is a substrate for the transmembrane oxidoreductase Dcytb","volume":"48","author":"Vlachodimitropoulou","year":"2010","journal-title":"Free Radic. Biol. Med."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1080\/01635589309514267","article-title":"Intake of potentially anticarcinogenic flavonoids and their determinants in adults in The Netherlands","volume":"20","author":"Hertog","year":"1993","journal-title":"Nutr. Cancer"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1042\/BJ20040703","article-title":"Myricetin, quercetin and catechin-gallate inhibit glucose uptake in isolated rat adipocytes","volume":"386","author":"Strobel","year":"2005","journal-title":"Biochem. J."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"1297","DOI":"10.1093\/jn\/130.5.1297","article-title":"Intracellular accumulation of ascorbic acid is inhibited by flavonoids via blocking of dehydroascorbic acid and ascorbic acid uptakes in HL-60, U937 and Jurkat cells","volume":"130","author":"Park","year":"2000","journal-title":"J. Nutr."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"5797","DOI":"10.1074\/jbc.M509422200","article-title":"Docking studies show that l-glucose and quercetin slide through the transporter GLUT1","volume":"281","author":"Cunningham","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"934","DOI":"10.1016\/j.freeradbiomed.2011.01.005","article-title":"Quercetin-iron chelates are transported via glucose transporters","volume":"50","author":"Vlachodimitropoulou","year":"2011","journal-title":"Free Radic. Biol. Med."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"753","DOI":"10.1021\/bi701793a","article-title":"Recombinant expression and initial characterization of the putative human enteric ferric reductase Dcytb","volume":"47","author":"Ludwiczek","year":"2008","journal-title":"Biochemistry"},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1111\/j.1365-2141.2009.07843.x","article-title":"A novel association between a SNP in CYBRD1 and serum ferritin levels in a cohort study of HFE hereditary haemochromatosis","volume":"147","author":"Constantine","year":"2009","journal-title":"Br. J. Haematol."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"2879","DOI":"10.1182\/blood-2005-02-0716","article-title":"Cybrd1 (duodenal cytochrome b) is not necessary for dietary iron absorption in mice","volume":"106","author":"Gunshin","year":"2005","journal-title":"Blood"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1093\/jn\/134.3.501","article-title":"Duodenal ascorbate levels are changed in mice with altered iron metabolism","volume":"134","author":"Atanasova","year":"2004","journal-title":"J. Nutr."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1042\/cs0760237","article-title":"Ascorbic acid: A factor concentrated in human gastric juice","volume":"76","author":"Rathbone","year":"1989","journal-title":"Clin. Sci. (Lond.)"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1093\/ajcn\/81.1.130","article-title":"Duodenal ascorbate and ferric reductase in human iron deficiency","volume":"81","author":"Atanasova","year":"2005","journal-title":"Am. J. Clin. Nutr."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"4413","DOI":"10.1182\/blood-2005-07-2923","article-title":"The role of duodenal cytochrome b in intestinal iron absorption remains unclear","volume":"106","author":"Frazer","year":"2005","journal-title":"Blood"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"1929","DOI":"10.3945\/jn.112.160358","article-title":"Duodenal reductase activity and spleen iron stores are reduced and erythropoiesis is abnormal in Dcytb knockout mice exposed to hypoxic conditions","volume":"142","author":"Choi","year":"2012","journal-title":"J. Nutr."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"39852","DOI":"10.1074\/jbc.M606543200","article-title":"Human erythrocyte membranes contain a cytochrome b561 that may be involved in extracellular ascorbate recycling","volume":"281","author":"Su","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/j.bcmd.2006.06.004","article-title":"Stimulation of non-transferrin iron uptake by iron deprivation in K562 cells","volume":"37","author":"Kovar","year":"2006","journal-title":"Blood Cells Mol. Dis."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1007\/s11010-008-9926-y","article-title":"Differing expression of genes involved in non-transferrin iron transport across plasma membrane in various cell types under iron deficiency and excess","volume":"321","author":"Balusikova","year":"2009","journal-title":"Mol. Cell. Biochem."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1042\/BJ20100064","article-title":"A role for Na+\/H+ exchangers and intracellular pH in regulating vitamin C-driven electron transport across the plasma membrane","volume":"428","author":"Lane","year":"2010","journal-title":"Biochem. J."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"27144","DOI":"10.1074\/jbc.M301988200","article-title":"Glycosylphosphatidylinositol-anchored ceruloplasmin is required for iron efflux from cells in the central nervous system","volume":"278","author":"Jeong","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1002\/jnr.22217","article-title":"Uptake of ferrous iron by cultured rat astrocytes","volume":"88","author":"Tulpule","year":"2010","journal-title":"J. Neurosci. Res."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"220","DOI":"10.1006\/bbrc.2002.6423","article-title":"Characterization of a cytochrome b(558) ferric\/cupric reductase from rabbit duodenal brush border membranes","volume":"291","author":"Solioz","year":"2002","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1079\/PNS2004386","article-title":"The molecular basis of copper and iron interactions","volume":"63","author":"Sharp","year":"2004","journal-title":"Proc. Nutr. Soc."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"32385","DOI":"10.1074\/jbc.M110.143826","article-title":"Ctr1 is an apical copper transporter in mammalian intestinal epithelial cells in vivo that is controlled at the level of protein stability","volume":"285","author":"Nose","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1007\/s10534-013-9691-6","article-title":"Mouse divalent metal transporter 1 is a copper transporter in HEK293 cells","volume":"27","author":"Arredondo","year":"2014","journal-title":"Biometals"},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"1927","DOI":"10.3945\/jn.113.181867","article-title":"Divalent metal transporter 1 (Dmt1) mediates copper transport in the duodenum of iron-deficient rats and when overexpressed in iron-deprived HEK-293 cells","volume":"143","author":"Jiang","year":"2013","journal-title":"J. Nutr."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"e59538","DOI":"10.1371\/journal.pone.0059538","article-title":"Copper deficiency leads to anemia, duodenal hypoxia, upregulation of HIF-2\u03b1 and altered expression of iron absorption genes in mice","volume":"8","author":"Matak","year":"2013","journal-title":"PLoS ONE"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"23943","DOI":"10.1074\/jbc.M113.489500","article-title":"Transcription factors Sp1 and Hif2\u03b1 mediate induction of the copper-transporting ATPase (Atp7a) gene in intestinal epithelial cells during hypoxia","volume":"288","author":"Xie","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"C1298","DOI":"10.1152\/ajpcell.00023.2011","article-title":"Transcriptional regulation of the Menkes copper ATPase (Atp7a) gene by hypoxia-inducible factor (HIF2\u03b1) in intestinal epithelial cells","volume":"300","author":"Xie","year":"2011","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"ref_108","first-page":"35","article-title":"Function and regulation of transferrin and ferritin","volume":"35","author":"Ponka","year":"1998","journal-title":"Semin. Hematol."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"406","DOI":"10.1038\/nchembio807","article-title":"The role of iron regulatory proteins in mammalian iron homeostasis and disease","volume":"2","author":"Rouault","year":"2006","journal-title":"Nat. Chem. Biol."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/j.cmet.2013.06.015","article-title":"Human CIA2A-FAM96A and CIA2B-FAM96B integrate iron homeostasis and maturation of different subsets of cytosolic-nuclear iron-sulfur proteins","volume":"18","author":"Stehling","year":"2013","journal-title":"Cell Metab."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"21645","DOI":"10.1074\/jbc.270.37.21645","article-title":"Iron regulates the intracellular degradation of iron regulatory protein 2 by the proteasome","volume":"270","author":"Guo","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"722","DOI":"10.1126\/science.1176326","article-title":"An E3 ligase possessing an iron-responsive hemerythrin domain is a regulator of iron homeostasis","volume":"326","author":"Salahudeen","year":"2009","journal-title":"Science"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"718","DOI":"10.1126\/science.1176333","article-title":"Control of iron homeostasis by an iron-regulated ubiquitin ligase","volume":"326","author":"Vashisht","year":"2009","journal-title":"Science"},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"1468","DOI":"10.1016\/j.bbamcr.2012.05.010","article-title":"Mammalian iron metabolism and its control by iron regulatory proteins","volume":"1823","author":"Anderson","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"176","DOI":"10.3389\/fphar.2014.00176","article-title":"The IRP\/IRE system in vivo: Insights from mouse models","volume":"5","author":"Wilkinson","year":"2014","journal-title":"Front. Pharmacol."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"124","DOI":"10.3389\/fphar.2014.00124","article-title":"The physiological functions of iron regulatory proteins in iron homeostasis\u2014An update","volume":"5","author":"Zhang","year":"2014","journal-title":"Front. Pharmacol."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"386","DOI":"10.1038\/sj.emboj.7600041","article-title":"Genetic ablations of iron regulatory proteins 1 and 2 reveal why iron regulatory protein 2 dominates iron homeostasis","volume":"23","author":"Ghosh","year":"2004","journal-title":"EMBO J."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/j.cmet.2007.10.006","article-title":"Iron regulatory proteins are essential for intestinal function and control key iron absorption molecules in the duodenum","volume":"7","author":"Galy","year":"2008","journal-title":"Cell Metab."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1016\/j.cmet.2010.06.007","article-title":"Iron regulatory proteins secure mitochondrial iron sufficiency and function","volume":"12","author":"Galy","year":"2010","journal-title":"Cell Metab."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1038\/84859","article-title":"Targeted deletion of the gene encoding iron regulatory protein-2 causes misregulation of iron metabolism and neurodegenerative disease in mice","volume":"27","author":"LaVaute","year":"2001","journal-title":"Nat. Genet."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"1084","DOI":"10.1182\/blood-2004-12-4703","article-title":"Microcytic anemia, erythropoietic protoporphyria, and neurodegeneration in mice with targeted deletion of iron-regulatory protein 2","volume":"106","author":"Cooperman","year":"2005","journal-title":"Blood"},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"2580","DOI":"10.1182\/blood-2005-04-1365","article-title":"Altered body iron distribution and microcytosis in mice deficient in iron regulatory protein 2 (IRP2)","volume":"106","author":"Galy","year":"2005","journal-title":"Blood"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"1658","DOI":"10.1182\/blood-2013-03-492454","article-title":"IRP1 regulates erythropoiesis and systemic iron homeostasis by controlling HIF2\u03b1 mRNA translation","volume":"122","author":"Wilkinson","year":"2013","journal-title":"Blood"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1016\/j.cmet.2012.12.016","article-title":"Deletion of iron regulatory protein 1 causes polycythemia and pulmonary hypertension in mice through translational derepression of HIF2\u03b1","volume":"17","author":"Ghosh","year":"2013","journal-title":"Cell Metab."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"282","DOI":"10.1016\/j.cmet.2013.01.007","article-title":"The IRP1-HIF-2\u03b1 axis coordinates iron and oxygen sensing with erythropoiesis and iron absorption","volume":"17","author":"Anderson","year":"2013","journal-title":"Cell Metab."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1002\/jcb.22956","article-title":"Hypoxia-mediated biological control","volume":"112","author":"Cassavaugh","year":"2011","journal-title":"J. Cell Biochem."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1089\/ars.2009.2790","article-title":"Iron homeostasis and its interaction with prolyl hydroxylases","volume":"12","author":"Mole","year":"2010","journal-title":"Antioxid. Redox Signal."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"2092","DOI":"10.1128\/MCB.01514-06","article-title":"The hypoxia-inducible factor 2\u03b1 N-terminal and C-terminal transactivation domains cooperate to promote renal tumorigenesis in vivo","volume":"27","author":"Yan","year":"2007","journal-title":"Mol. Cell. Biol."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1016\/j.cell.2012.01.021","article-title":"Hypoxia-inducible factors in physiology and medicine","volume":"148","author":"Semenza","year":"2012","journal-title":"Cell"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"2015","DOI":"10.1182\/blood-2009-05-189985","article-title":"Involvement of oxygen-sensing pathways in physiologic and pathologic erythropoiesis","volume":"114","author":"Semenza","year":"2009","journal-title":"Blood"},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.blre.2012.12.003","article-title":"Regulation of erythropoiesis by hypoxia-inducible factors","volume":"27","author":"Haase","year":"2013","journal-title":"Blood Rev."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"838","DOI":"10.1016\/j.molcel.2008.12.004","article-title":"Small-molecule inhibitors of HIF-2\u03b1 translation link its 5\u02bcUTR iron-responsive element to oxygen sensing","volume":"32","author":"Zimmer","year":"2008","journal-title":"Mol. Cell"},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"420","DOI":"10.1038\/nsmb1222","article-title":"Iron-regulatory proteins limit hypoxia-inducible factor-2alpha expression in iron deficiency","volume":"14","author":"Sanchez","year":"2007","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1016\/j.cmet.2008.12.012","article-title":"Intestinal hypoxia-inducible transcription factors are essential for iron absorption following iron deficiency","volume":"9","author":"Shah","year":"2009","journal-title":"Cell Metab."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"1159","DOI":"10.1172\/JCI38499","article-title":"HIF-2\u03b1, but not HIF-1\u03b1, promotes iron absorption in mice","volume":"119","author":"Mastrogiannaki","year":"2009","journal-title":"J. Clin. Invest."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"2044","DOI":"10.1053\/j.gastro.2011.03.007","article-title":"Hypoxia-inducible factor-2\u03b1 mediates the adaptive increase of intestinal ferroportin during iron deficiency in mice","volume":"140","author":"Taylor","year":"2011","journal-title":"Gastroenterology"},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"340","DOI":"10.1136\/gut.52.3.340","article-title":"A rapid decrease in the expression of DMT1 and Dcytb but not Ireg1 or hephaestin explains the mucosal block phenomenon of iron absorption","volume":"52","author":"Frazer","year":"2003","journal-title":"Gut"},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1084\/jem.78.3.169","article-title":"Radioactive iron absorption by gastro-intestinal tract: Influence of Anemia, Anoxia, and Antecedent Feeding Distribution in Growing Dogs","volume":"78","author":"Hahn","year":"1943","journal-title":"J. Exp. Med."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1084\/jem.92.4.375","article-title":"Radioiron absorption in anemic dogs; fluctuations in the mucosal block and evidence for a gradient of absorption in the gastrointestinal tract","volume":"92","author":"Stewart","year":"1950","journal-title":"J. Exp. Med."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"885","DOI":"10.1182\/blood-2012-11-427765","article-title":"The gut in iron homeostasis: Role of HIF-2 under normal and pathological conditions","volume":"122","author":"Mastrogiannaki","year":"2013","journal-title":"Blood"},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1016\/j.cmet.2009.06.009","article-title":"Regulation of intestinal iron absorption: The mucosa takes control?","volume":"10","author":"Simpson","year":"2009","journal-title":"Cell Metab."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1007\/s00394-011-0175-6","article-title":"Duodenal cytochrome b (Cybrd 1) and HIF-2\u03b1 expression during acute hypoxic exposure in mice","volume":"50","author":"Xiang","year":"2011","journal-title":"Eur. J. Nutr."}],"container-title":["Nutrients"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2072-6643\/7\/4\/2274\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T20:44:10Z","timestamp":1760215450000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2072-6643\/7\/4\/2274"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,3,31]]},"references-count":142,"journal-issue":{"issue":"4","published-online":{"date-parts":[[2015,4]]}},"alternative-id":["nu7042274"],"URL":"https:\/\/doi.org\/10.3390\/nu7042274","relation":{},"ISSN":["2072-6643"],"issn-type":[{"value":"2072-6643","type":"electronic"}],"subject":[],"published":{"date-parts":[[2015,3,31]]}}}