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Volumn 7, Issue 2, 2015, Pages 1184-1201

Plant ferritin—a source of iron to prevent its deficiency

Author keywords

Bioactive food; Biofortified plants; Ferritin; Iron

Indexed keywords

APOFERRITIN; BREAST CANCER RESISTANCE PROTEIN; DODECAMERIC MINIFERRITIN; FERRITIN; HEMOGLOBIN; LACTOFERRIN; MYOGLOBIN; NATURAL RESISTANCE ASSOCIATED MACROPHAGE PROTEIN 2; PHYTOFERRITIN; PLANT MEDICINAL PRODUCT; PROTON COUPLED FOLATE TRANSPORTER; TRACE ELEMENT; UNCLASSIFIED DRUG; IRON;

EID: 84922979227     PISSN: None     EISSN: 20726643     Source Type: Journal    
DOI: 10.3390/nu7021184     Document Type: Article
Times cited : (90)

References (129)
  • 3
    • 32944462943 scopus 로고    scopus 로고
    • Iron supplement use and iron status among US adults: Results from the third National Health and Nutrition Examination Survey
    • Blanck, H.M.; Cogswell, M.E.; Gillespie, C.; Reyes, M. Iron supplement use and iron status among US adults: Results from the third National Health and Nutrition Examination Survey. Am. J. Clin. Nutr. 2005, 82, 1024–1031.
    • (2005) Am. J. Clin. Nutr. , vol.82 , pp. 1024-1031
    • Blanck, H.M.1    Cogswell, M.E.2    Gillespie, C.3    Reyes, M.4
  • 4
    • 80155168960 scopus 로고    scopus 로고
    • Iron deficiency and iron-deficiency anemia in the first two years of life: Strategies to prevent loss of developmental potential
    • Black, M.M.; Quigg, A.M.; Hurley, K.M.; Pepper, M.R. Iron deficiency and iron-deficiency anemia in the first two years of life: Strategies to prevent loss of developmental potential. Nutr. Rev. 2011, 69, S64–S70.
    • (2011) Nutr. Rev. , vol.69 , pp. S64-S70
    • Black, M.M.1    Quigg, A.M.2    Hurley, K.M.3    Pepper, M.R.4
  • 5
    • 0034995398 scopus 로고    scopus 로고
    • Iron deficiency and cognitive achievement among school-aged children and adolescents in the United States
    • Halterman, J.S.; Kaczorowski, J.M.; Aligne, C.A.; Auinger, P.; Szilagyi, P.G. Iron deficiency and cognitive achievement among school-aged children and adolescents in the United States. Pediatrics 2001, 107, 1381–1386.
    • (2001) Pediatrics , vol.107 , pp. 1381-1386
    • Halterman, J.S.1    Kaczorowski, J.M.2    Aligne, C.A.3    Auinger, P.4    Szilagyi, P.G.5
  • 7
    • 34548399062 scopus 로고    scopus 로고
    • Iron deficiency in early childhood in the United States: Risk factors and racial/ethnic disparities
    • Brotanek, J.M.; Gosz, J.; Weitzman, M.; Flores, G. Iron deficiency in early childhood in the United States: Risk factors and racial/ethnic disparities. Pediatrics 2007, 120, 568–575.
    • (2007) Pediatrics , vol.120 , pp. 568-575
    • Brotanek, J.M.1    Gosz, J.2    Weitzman, M.3    Flores, G.4
  • 9
    • 84886974197 scopus 로고    scopus 로고
    • Iron
    • 10th ed.; Erdman, J.W., MacDonald I.A., Zeisel, S.H., Eds.; Wiley-Blackwell: Washington, DC, USA
    • Aggett, P.J. Iron. In Present Knowledge in Nutrition, 10th ed.; Erdman, J.W., MacDonald I.A., Zeisel, S.H., Eds.; Wiley-Blackwell: Washington, DC, USA, 2012; pp. 506–520.
    • (2012) Present Knowledge in Nutrition , pp. 506-520
    • Aggett, P.J.1
  • 10
    • 77951960886 scopus 로고    scopus 로고
    • Iron bioavailability and dietary reference values
    • Hurrell, R.; Egli, I. Iron bioavailability and dietary reference values. Am. J. Clin. Nutr. 2010, 91, 1461S–1467S.
    • (2010) Am. J. Clin. Nutr. , vol.91 , pp. 1461S-1467S
    • Hurrell, R.1    Egli, I.2
  • 11
    • 84922969180 scopus 로고    scopus 로고
    • Iron
    • USA Government, National Institutes of Health, Office of Dietary Supplements
    • National Institutes of Health. Iron. In Dietary Supplement Fact Sheet; USA Government, National Institutes of Health, Office of Dietary Supplements: 2014.
    • (2014) Dietary Supplement Fact Sheet
  • 12
    • 5144224375 scopus 로고    scopus 로고
    • Iron in ferritin or in salts (Ferrous sulfate) is equally bioavailable in nonanemic women
    • Davila-Hicks, P.; Theil, E.C.; Lönnerdal, B. Iron in ferritin or in salts (ferrous sulfate) is equally bioavailable in nonanemic women. Am. J. Clin. Nutr. 2004, 80, 936–940.
    • (2004) Am. J. Clin. Nutr. , vol.80 , pp. 936-940
    • Davila-Hicks, P.1    Theil, E.C.2    Lönnerdal, B.3
  • 14
    • 0036076469 scopus 로고    scopus 로고
    • Iron compounds for food fortification: Guidelines for Latin America and the Caribbean 2002
    • Dary, O.; Freire, W.; Kim, S. Iron compounds for food fortification: Guidelines for Latin America and the Caribbean 2002. Nutr. Rev. 2002, 60, S50–S61.
    • (2002) Nutr. Rev. , vol.60 , pp. S50-S61
    • Dary, O.1    Freire, W.2    Kim, S.3
  • 19
    • 41549147443 scopus 로고    scopus 로고
    • Caco-2 intestinal epithelial cells absorb soybean ferritin by Mu2 (AP2)-dependent endocytosis
    • San Martin, C.D.; Garri, C.; Pizarro, F.; Walter, T.; Theil, E.C.; Núñez, M.T. Caco-2 intestinal epithelial cells absorb soybean ferritin by Mu2 (AP2)-dependent endocytosis. J. Nutr. 2008, 138, 659–666.
    • (2008) J. Nutr. , vol.138 , pp. 659-666
    • San Martin, C.D.1    Garri, C.2    Pizarro, F.3    Walter, T.4    Theil, E.C.5    Núñez, M.T.6
  • 20
    • 0035951070 scopus 로고    scopus 로고
    • Molecular cloning and functional expression of a human intestinal lactoferrin receptor
    • Suzuki, Y.A.; Shin, K.; Lönnerdal, B. Molecular cloning and functional expression of a human intestinal lactoferrin receptor. Biochemistry 2001, 40, 15771–15770.
    • (2001) Biochemistry , vol.40 , pp. 15770-15771
    • Suzuki, Y.A.1    Shin, K.2    Lönnerdal, B.3
  • 21
    • 33746830877 scopus 로고    scopus 로고
    • Screening for hereditary hemochromatosis: A systematic review for the U.S. Preventive Services Task Force
    • Whitlock, E.P.; Garlitz, B.A.; Harris, E.L.; Beil, T.L.; Smith, P.R. Screening for hereditary hemochromatosis: A systematic review for the U.S. Preventive Services Task Force. Ann. Intern. Med. 2006, 145, 209–223.
    • (2006) Ann. Intern. Med. , vol.145 , pp. 209-223
    • Whitlock, E.P.1    Garlitz, B.A.2    Harris, E.L.3    Beil, T.L.4    Smith, P.R.5
  • 25
    • 84923012264 scopus 로고    scopus 로고
    • Iron
    • 2nd ed.; Coates, P.M., Betz, J.M., Blackman, M.R., Cragg, G.M., Levine, M., Moss, J., White J.D., Eds.; Informa Healthcare: London, UK; New York, NY, USA
    • Murray-Kolbe, L.E.; Beard, J. Iron. In Encyclopedia of Dietary Supplements, 2nd ed.; Coates, P.M., Betz, J.M., Blackman, M.R., Cragg, G.M., Levine, M., Moss, J., White J.D., Eds.; Informa Healthcare: London, UK; New York, NY, USA, 2010; pp. 432–438.
    • (2010) Encyclopedia of Dietary Supplements , pp. 432-438
    • Murray-Kolbe, L.E.1    Beard, J.2
  • 27
    • 0025790381 scopus 로고
    • Rossander-Hulthe’n, L. Iron requirements in menstruating women
    • Hallberg, L.; Rossander-Hulthe’n, L. Iron requirements in menstruating women. Am. J. Clin. Nutr. 1991, 54, 1047–1058.
    • (1991) Am. J. Clin. Nutr. , vol.54 , pp. 1047-1058
    • Hallberg, L.1
  • 28
    • 0036205164 scopus 로고    scopus 로고
    • Fortification: Overcoming technical and practical barriers
    • Hurrel, R.F. Fortification: Overcoming technical and practical barriers. J. Nutr. 2002, 132, 806–812.
    • (2002) J. Nutr. , vol.132 , pp. 806-812
    • Hurrel, R.F.1
  • 29
    • 0030738125 scopus 로고    scopus 로고
    • Oxidative stress and antioxidant status in mouse liver: Effects of dietary lipid, vitamin
    • Ibrahim, W.; Lee, U.S.; Yeh, C.C.; Szabo, J.; Bruckner, G.; Chow, C.K. Oxidative stress and antioxidant status in mouse liver: Effects of dietary lipid, vitamin E and iron. J. Nutr.1997, 127, 1401–1406.
    • (1997) E and Iron. J. Nutr. , vol.127 , pp. 1401-1406
    • Ibrahim, W.1    Lee, U.S.2    Yeh, C.C.3    Szabo, J.4    Bruckner, G.5    Chow, C.K.6
  • 31
    • 0023645647 scopus 로고
    • Isolation and characterization of ferritin from soybeans (Glycine max)
    • Sczekan, S.R.; Joshi, J.G. Isolation and characterization of ferritin from soybeans (Glycine max). J. Biol. Chem. 1987, 262, 13780–13788.
    • (1987) J. Biol. Chem. , vol.262 , pp. 13780-13788
    • Sczekan, S.R.1    Joshi, J.G.2
  • 32
    • 0029310487 scopus 로고
    • A novel stress-inducible metallothionein-like protein from rice
    • Hsieh, H.M.; Liu, W.K.; Huang, P.C. A novel stress-inducible metallothionein-like protein from rice. Plant Mol. Biol. 1995, 28, 381–389.
    • (1995) Plant Mol. Biol. , vol.28 , pp. 381-389
    • Hsieh, H.M.1    Liu, W.K.2    Huang, P.C.3
  • 33
    • 77951995410 scopus 로고    scopus 로고
    • New insights into ferritin synthesis and function highlight a link between iron homeostasis and oxidative stress in plants
    • Briat, J.-F.; Ravet, K.; Arnaud, N.; Duc, C.; Boucherez, J.; Touraine, B.; Cellier, F.; Gaymard, F. New insights into ferritin synthesis and function highlight a link between iron homeostasis and oxidative stress in plants. Ann. Bot. 2010, 105, 811–822.
    • (2010) Ann. Bot. , vol.105 , pp. 811-822
    • Briat, J.-F.1    Ravet, K.2    Arnaud, N.3    Duc, C.4    Boucherez, J.5    Touraine, B.6    Cellier, F.7    Gaymard, F.8
  • 34
    • 15244339209 scopus 로고    scopus 로고
    • Ferritins: Dynamic management of biological iron and oxygen chemistry
    • Liu, X.; Theil, E.C. Ferritins: Dynamic management of biological iron and oxygen chemistry. Acc. Chem. Res. 2005, 38, 167–175.
    • (2005) Acc. Chem. Res. , vol.38 , pp. 167-175
    • Liu, X.1    Theil, E.C.2
  • 35
    • 77953811022 scopus 로고    scopus 로고
    • Phytoferritin ant its implication for human health and nutrition
    • Zhao, G. Phytoferritin ant its implication for human health and nutrition. Biochim. Biophys. Acta 2010, 1800, 815–823.
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 815-823
    • Zhao, G.1
  • 36
    • 4344700535 scopus 로고    scopus 로고
    • The physiological role of ferritin-like compounds in bacteria
    • Smith, J.L. The physiological role of ferritin-like compounds in bacteria. Crit. Rev. Microbiol. 2004, 30, 173–185.
    • (2004) Crit. Rev. Microbiol. , vol.30 , pp. 173-185
    • Smith, J.L.1
  • 37
    • 0035379652 scopus 로고    scopus 로고
    • A novel plant ferritin subunit from soybean that is related to a mechanism in iron release
    • Masuda, T.; Goto, F.; Yoshihara, T. A novel plant ferritin subunit from soybean that is related to a mechanism in iron release. J. Biol. Chem. 2001, 276, 19575–19579.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19575-19579
    • Masuda, T.1    Goto, F.2    Yoshihara, T.3
  • 38
    • 0027056014 scopus 로고
    • Amino acid sequence and predicted three-dimensional structure of pea seed ferritin
    • Lobréaux, S.; Yewdall, S.; Briat, J.F.; Harrison, P.M. Amino acid sequence and predicted three-dimensional structure of pea seed ferritin. Biochem. J. 1992, 288, 931–939.
    • (1992) Biochem. J. , vol.288 , pp. 931-939
    • Lobréaux, S.1    Yewdall, S.2    Briat, J.F.3    Harrison, P.M.4
  • 39
    • 0025970277 scopus 로고
    • Ferritin accumulation and degradation in different organs of pea (Pisum sativum) during development
    • Lobreaux, S.; Briat, J.-F. Ferritin accumulation and degradation in different organs of pea (Pisum sativum) during development. Biochem. J. 1991, 274, 601–606.
    • (1991) Biochem. J. , vol.274 , pp. 601-606
    • Lobreaux, S.1    Briat, J.-F.2
  • 40
    • 35448945259 scopus 로고    scopus 로고
    • Construction of homo- and heteropolymers of plant ferritin subunits using an in vitro protein expression system
    • Masuda, T.; Goto, F.; Yoshihara, T.; Ezure, T.; Suzuki, T.; Kobayashi, S.; Shikata, M.; Utsumi, S. Construction of homo- and heteropolymers of plant ferritin subunits using an in vitro protein expression system. Protein Expr. Purif. 2007, 56, 237–246.
    • (2007) Protein Expr. Purif. , vol.56 , pp. 237-246
    • Masuda, T.1    Goto, F.2    Yoshihara, T.3    Ezure, T.4    Suzuki, T.5    Kobayashi, S.6    Shikata, M.7    Utsumi, S.8
  • 41
    • 36849007403 scopus 로고    scopus 로고
    • Novel ferritin gene, SferH-5, reveals heterogeneity of the 26.5-kDa subunit of soybean (Glycine max) seed ferritin
    • Dong, X.; Sun, Q.; Wei, D.; Li, J.; Tang, B.; Jia, Q.; Hu, W.; Zhao, Y.; Hua, Z.C. A novel ferritin gene, SferH-5, reveals heterogeneity of the 26.5-kDa subunit of soybean (Glycine max) seed ferritin. FEBS Lett. 2007, 581, 5796–5802.
    • (2007) FEBS Lett , vol.581 , pp. 5796-5802
    • Dong, X.1    Sun, Q.2    Wei, D.3    Li, J.4    Tang, B.5    Jia, Q.6    Hu, W.7    Zhao, Y.8    Hua, Z.9
  • 42
    • 3142781945 scopus 로고    scopus 로고
    • Iron, ferritin, and nutrition
    • Theil, E.C. Iron, ferritin, and nutrition. Annu. Rev. Nutr. 2004, 24, 327–343.
    • (2004) Annu. Rev. Nutr. , vol.24 , pp. 327-343
    • Theil, E.C.1
  • 43
    • 77952778704 scopus 로고    scopus 로고
    • A novel EP-involved pathway for iron release from soya bean seed ferritin
    • Fu, X.; Deng, J.; Yang, H.; Masuda, T.; Goto, F.; Yoshihara, T.; Zhao, G. A novel EP-involved pathway for iron release from soya bean seed ferritin. Biochem. J. 2010, 427, 313–321.
    • (2010) Biochem. J. , vol.427 , pp. 313-321
    • Fu, X.1    Deng, J.2    Yang, H.3    Masuda, T.4    Goto, F.5    Yoshihara, T.6    Zhao, G.7
  • 44
    • 0028938594 scopus 로고
    • Conformational changes and in vitro core formation modifications induced by site directed mutagenesis of the specific amino terminus (EP) of pea seed ferritin
    • Van Wuytswinkel, O.; Briat, J.F. Conformational changes and in vitro core formation modifications induced by site directed mutagenesis of the specific amino terminus (EP) of pea seed ferritin. Biochem. J. 1995, 305, 959–965.
    • (1995) Biochem. J. , vol.305 , pp. 959-965
    • Van Wuytswinkel, O.1    Briat, J.F.2
  • 45
    • 0028854811 scopus 로고
    • Purification and characterization of recombinant pea seed ferritins expressed in Escherichia coli: Influence of amino terminus deletions on protein solubility and in vitro core formation
    • Van Wuytswinkel, O.; Savino, G.; Briat, J.F. Purification and characterization of recombinant pea seed ferritins expressed in Escherichia coli: Influence of amino terminus deletions on protein solubility and in vitro core formation. Biochem. J. 1995, 305, 253–261.
    • (1995) Biochem. J. , vol.305 , pp. 253-261
    • Van Wuytswinkel, O.1    Savino, G.2    Briat, J.F.3
  • 46
    • 0025186372 scopus 로고
    • Evidence for conservation of ferritin sequences among plants and animals and for a transit peptide in soybean
    • Ragland, M.; Briat, J.F.; Gagnon, J.; Laulhere, J.P.; Massenet, O.; Theil, E.C. Evidence for conservation of ferritin sequences among plants and animals and for a transit peptide in soybean. J. Biol. Chem. 1990, 265, 18339–18344.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18339-18344
    • Ragland, M.1    Briat, J.F.2    Gagnon, J.3    Laulhere, J.P.4    Massenet, O.5    Theil, E.C.6
  • 47
    • 0000242126 scopus 로고
    • Iron induction of ferritin synthesis in soybean cell suspensions
    • Proudhon, D.; Briat, J.F.; Lescure, A.M. Iron induction of ferritin synthesis in soybean cell suspensions. Plant Physiol. 1989, 90, 586–590.
    • (1989) Plant Physiol , vol.90 , pp. 586-590
    • Proudhon, D.1    Briat, J.F.2    Lescure, A.M.3
  • 48
    • 0000171802 scopus 로고    scopus 로고
    • Ferritin
    • Messeschmidt, A., Huber, R., Poilos, T., Wieghardt, K., Eds.; John Wiley and Sons: Chichester, UK
    • Theil, E.C. Ferritin. In Handbook of Metaloproteins 1; Messeschmidt, A., Huber, R., Poilos, T., Wieghardt, K., Eds.; John Wiley and Sons: Chichester, UK, 2000; pp. 771–781.
    • (2000) Handbook of Metaloproteins 1 , pp. 771-781
    • Theil, E.C.1
  • 49
    • 38249040354 scopus 로고
    • The structure and function of ferritin
    • Harrison, P.M. The structure and function of ferritin. Biochem. Educ. 1986, 14, 154–162.
    • (1986) Biochem. Educ. , vol.14 , pp. 154-162
    • Harrison, P.M.1
  • 50
    • 0032743819 scopus 로고    scopus 로고
    • Ferritin induction by iron mediated oxidative stress and ABA in Vigna mungo (L.) Hepper seedlings: Role of antioxidants and free radical scavengers
    • Rama Kumar, T.; Prasad, M.N.V. Ferritin induction by iron mediated oxidative stress and ABA in Vigna mungo (L.) Hepper seedlings: Role of antioxidants and free radical scavengers. J. Plant Physiol. 1999, 155, 652–655.
    • (1999) J. Plant Physiol. , vol.155 , pp. 652-655
    • Rama Kumar, T.1    Prasad, M.2
  • 51
    • 27944458471 scopus 로고    scopus 로고
    • Endosperm-specific co-expression of recombinant soybean ferritin and Aspergillus phytase in maize results in significant increases in the levels of bioavailable iron
    • Drakakaki, G.; Marcel, S.; Glahn, R.P.; Lund, E.K.; Pariagh, S.; Fischer, R.; Christou, P.; Stoger, E. Endosperm-specific co-expression of recombinant soybean ferritin and Aspergillus phytase in maize results in significant increases in the levels of bioavailable iron. Plant Mol. Biol. 2005, 59, 869–880.
    • (2005) Plant Mol. Biol. , vol.59 , pp. 869-880
    • Drakakaki, G.1    Marcel, S.2    Glahn, R.P.3    Lund, E.K.4    Pariagh, S.5    Fischer, R.6    Christou, P.7    Stoger, E.8
  • 53
    • 18944406393 scopus 로고    scopus 로고
    • Nanophase iron phosphate, iron arsenate, iron vandate and iron molybdate minerals syntehesized within the protein cage of ferritin
    • Polanams, J.; Ray, A.D.; Watt, R.K. Nanophase iron phosphate, iron arsenate, iron vandate and iron molybdate minerals syntehesized within the protein cage of ferritin. Inorg. Chem. 2005, 44, 3203–3209.
    • (2005) Inorg. Chem. , vol.44 , pp. 3203-3209
    • Polanams, J.1    Ray, A.D.2    Watt, R.K.3
  • 54
    • 0032956115 scopus 로고    scopus 로고
    • Metal-binding properties of ferritin in Vigna mungo (L.) Hepper (Black gram): Possible role in heavy metal detoxification
    • Rama Kumar, T.; Prasad, M.N.V. Metal-binding properties of ferritin in Vigna mungo (L.) Hepper (Black gram): Possible role in heavy metal detoxification. Bull. Environ. Contam. Toxicol. 1999, 62, 502–507.
    • (1999) Bull. Environ. Contam. Toxicol. , vol.62 , pp. 502-507
    • Rama Kumar, T.1    Prasad, M.2
  • 55
    • 21744461905 scopus 로고    scopus 로고
    • Characterization of nuclear ferritin and mechanism of translocation
    • Surguladze, N.; Patton, S.; Cozzi, A.; Fried, M.G.; Connor, J.R. Characterization of nuclear ferritin and mechanism of translocation. Biochem. J. 2005, 388, 731–740.
    • (2005) Biochem. J. , vol.388 , pp. 731-740
    • Surguladze, N.1    Patton, S.2    Cozzi, A.3    Fried, M.G.4    Connor, J.R.5
  • 56
    • 84923649359 scopus 로고
    • Metal binding properties of phytoferritin and synthetic iron cores
    • Sczekan, S.R.; Joshi, J.G. Metal binding properties of phytoferritin and synthetic iron cores. Biochim. Biophys. Acta 1989, 990, 8–14.
    • (1989) Biochim. Biophys. Acta , vol.990 , pp. 8-14
    • Sczekan, S.R.1    Joshi, J.G.2
  • 57
    • 0344177528 scopus 로고    scopus 로고
    • Plants ectopically expressing the iron-binding protein, ferritin, are tolerant to oxidative damage and pathogens
    • Deak, M.; Horvarth, G.V.; Davletova, S.; Török, K.; Vass, I.; Barna, B.; Kiraly, Z; Dudits, D. Plants ectopically expressing the iron-binding protein, ferritin, are tolerant to oxidative damage and pathogens. Nat. Biotechnol. 1999, 17, 192–196.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 192-196
    • Deak, M.1    Horvarth, G.V.2    Davletova, S.3    Török, K.4    Vass, I.5    Barna, B.6    Kiraly, Z.7    Dudits, D.8
  • 59
    • 0034935874 scopus 로고    scopus 로고
    • Nuclear translocation of ferritin in corneal epithelial cells
    • Cai, C.X.; Linsenmayer, T.F. Nuclear translocation of ferritin in corneal epithelial cells. J. Cell Sci. 2001, 114, 2327–2334.
    • (2001) J. Cell Sci. , vol.114 , pp. 2327-2334
    • Cai, C.X.1    Linsenmayer, T.F.2
  • 60
    • 77953812085 scopus 로고    scopus 로고
    • Nuclear ferritin: A new role for ferritin in cell biology
    • Alkhateeb, A.A.; Connor, J.R. Nuclear ferritin: A new role for ferritin in cell biology. Biochim. Biophys. Acta 2010, 1800, 793–797.
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 793-797
    • Alkhateeb, A.A.1    Connor, J.R.2
  • 61
    • 0034887703 scopus 로고    scopus 로고
    • Involvement of iron and ferritin in the potato-Phytophthora infestans interaction
    • Mata, C.G.; Lamattina, L.; Cassia, R.O. Involvement of iron and ferritin in the potato-Phytophthora infestans interaction. Eur. J. Plant Pathol. 2001, 107, 557–562.
    • (2001) Eur. J. Plant Pathol. , vol.107 , pp. 557-562
    • Mata, C.G.1    Lamattina, L.2    Cassia, R.O.3
  • 62
    • 0029582837 scopus 로고
    • Cellular and molecular aspects of iron metabolism in plants
    • Briat, J.F.; Fobis-Loisy, I.; Grignon, N.; Vansuyt, G. Cellular and molecular aspects of iron metabolism in plants. Biol. Cell 1995, 84, 69–81.
    • (1995) Biol. Cell , vol.84 , pp. 69-81
    • Briat, J.F.1    Fobis-Loisy, I.2    Grignon, N.3    Vansuyt, G.4
  • 63
    • 0031774571 scopus 로고    scopus 로고
    • Puppo. A.; de Felipe, M.R. Immunolocalization of ferritin in determinate and indeterminate legume root nodules
    • Lucas, M.M.; van de Sype, G.; Hérouart, D.; Hernández, M.J.; Puppo. A.; de Felipe, M.R. Immunolocalization of ferritin in determinate and indeterminate legume root nodules. Protoplasma 1998, 204, 61–70.
    • (1998) Protoplasma , vol.204 , pp. 61-70
    • Lucas, M.M.1    Van De Sype, G.2    Hérouart, D.3    Hernández, M.J.4
  • 64
    • 0009740235 scopus 로고
    • Plant and microbial ferritins
    • Barton, L.L., Hemming, B.B., Eds.; Academic Press: San Diego, CA, USA
    • Theil, E.C.; Hase, T. Plant and microbial ferritins. In Iron Chelation in Plants and Soil Microorganism; Barton, L.L., Hemming, B.B., Eds.; Academic Press: San Diego, CA, USA, 1993; pp. 133–156.
    • (1993) Iron Chelation in Plants and Soil Microorganism , pp. 133-156
    • Theil, E.C.1    Hase, T.2
  • 66
    • 35348996059 scopus 로고    scopus 로고
    • Iron dynamics in plants
    • Briat, J.-F. Iron dynamics in plants. Adv. Bot. Res. 2008, 46, 138–180.
    • (2008) Adv. Bot. Res. , vol.46 , pp. 138-180
    • Briat, J.-F.1
  • 67
    • 0027975550 scopus 로고
    • Iron transport to developing ovules of Pisum sativum L. Seed import characteristics and phloem iron-loading capacity of source regions
    • Grusak, M.A. Iron transport to developing ovules of Pisum sativum L. Seed import characteristics and phloem iron-loading capacity of source regions. Plant Physiol. 1994, 104, 649–655.
    • (1994) Plant Physiol , vol.104 , pp. 649-655
    • Grusak, M.A.1
  • 68
    • 0000079961 scopus 로고
    • Mobilization of minerals to developing seeds of legumes
    • Hocking, P.J.; Pate, J.S. Mobilization of minerals to developing seeds of legumes. Ann. Bot. 1977, 41, 1259–1278.
    • (1977) Ann. Bot. , vol.41 , pp. 1259-1278
    • Hocking, P.J.1    Pate, J.S.2
  • 69
    • 0031959314 scopus 로고    scopus 로고
    • Evidence for reutilization of nodule iron in soybean seed development
    • Burton, J.W.; Harlow, C.; Theil, E.C. Evidence for reutilization of nodule iron in soybean seed development. J. Plant Nutr. 1998, 21, 913–927.
    • (1998) J. Plant Nutr. , vol.21 , pp. 913-927
    • Burton, J.W.1    Harlow, C.2    Theil, E.C.3
  • 70
    • 79952045559 scopus 로고    scopus 로고
    • The role of soy in vegetarian diets
    • Messina, M.; Messina, V. The role of soy in vegetarian diets. Nutrients 2010, 2, 855–888.
    • (2010) Nutrients , vol.2 , pp. 855-888
    • Messina, M.1    Messina, V.2
  • 71
    • 36749079917 scopus 로고    scopus 로고
    • Effect of dietary factors on iron uptake from ferritin by Caco-2 cells
    • Kalgaonkar, S.; Lönnerdal, B.Effect of dietary factors on iron uptake from ferritin by Caco-2 cells. J. Nutr. Biochem. 2008, 19, 33–39.
    • (2008) J. Nutr. Biochem. , vol.19 , pp. 33-39
    • Kalgaonkar, S.1    Lönnerdal, B.2
  • 75
    • 33644869600 scopus 로고    scopus 로고
    • Iron absorption from soybean ferritin in nonanemic women
    • Lönnerdal, B.; Bryant, A.; Liu, X.; Theil, E.C. Iron absorption from soybean ferritin in nonanemic women. Am. J. Clin. Nutr. 2006, 83, 103–107.
    • (2006) Am. J. Clin. Nutr. , vol.83 , pp. 103-107
    • Lönnerdal, B.1    Bryant, A.2    Liu, X.3    Theil, E.C.4
  • 76
    • 0030071285 scopus 로고    scopus 로고
    • Purified ferritin and soybean meal can be sources of iron for treating iron deficiency in rats
    • Beard, J.L.; Burton, J.W.; Theil, E.C. Purified ferritin and soybean meal can be sources of iron for treating iron deficiency in rats. J. Nutr. 1996, 126, 154–160.
    • (1996) J. Nutr. , vol.126 , pp. 154-160
    • Beard, J.L.1    Burton, J.W.2    Theil, E.C.3
  • 77
    • 84863229838 scopus 로고    scopus 로고
    • Absorption of iron from ferritin is independent of heme iron and ferrous salts in women and rat intestinal segments
    • Theil, E.C.; Chen, H.; Miranda, C.; Janser, H.; Elsenhans, B.; Núñez, M.T.; Pizarro, F.; Schümann, K. Absorption of iron from ferritin is independent of heme iron and ferrous salts in women and rat intestinal segments. J. Nutr. 2012, 142, 478–483.
    • (2012) J. Nutr. , vol.142 , pp. 478-483
    • Theil, E.C.1    Chen, H.2    Miranda, C.3    Janser, H.4    Elsenhans, B.5    Núñez, M.T.6    Pizarro, F.7    Schümann, K.8
  • 78
    • 42449088037 scopus 로고    scopus 로고
    • Ferritin-iron is released during boiling and in vitro gastric digestion
    • Hoppler, M.; Schonbachler, A.; Meile, L.; Hurrell, R.F.; Walczyk, T. Ferritin-iron is released during boiling and in vitro gastric digestion. J. Nutr. 2008, 138, 878–884.
    • (2008) J. Nutr. , vol.138 , pp. 878-884
    • Hoppler, M.1    Schonbachler, A.2    Meile, L.3    Hurrell, R.F.4    Walczyk, T.5
  • 79
    • 34249021014 scopus 로고    scopus 로고
    • Gastric digestion of pea ferritin and modulation of its iron bioavailability by ascorbic and phytic acids in Caco-2 cells
    • Bejjani, S.; Pullakhandam, R.; Punjal, R.; Nair, K.M. Gastric digestion of pea ferritin and modulation of its iron bioavailability by ascorbic and phytic acids in Caco-2 cells. World J. Gastroenterol. 2007, 13, 2083–2088.
    • (2007) World J. Gastroenterol. , vol.13 , pp. 2083-2088
    • Bejjani, S.1    Pullakhandam, R.2    Punjal, R.3    Nair, K.M.4
  • 80
    • 84887587465 scopus 로고    scopus 로고
    • Encapsulation of β-carotene within ferritin nanocages greatly increases its water-solubility and thermal stability
    • Chen, L.; Bai, G.; Yang, R.; Zang, J.; Zhou, T.; Zhao, G. Encapsulation of β-carotene within ferritin nanocages greatly increases its water-solubility and thermal stability. Food Chem. 2014, 15, 307–312.
    • (2014) Food Chem , vol.15 , pp. 307-312
    • Chen, L.1    Bai, G.2    Yang, R.3    Zang, J.4    Zhou, T.5    Zhao, G.6
  • 81
    • 65549136658 scopus 로고    scopus 로고
    • Soybean ferritin: Implications for iron status of vegetarians
    • Lönnerdal, B. Soybean ferritin: Implications for iron status of vegetarians. Am. J. Clin. Nutr. 2009, 89, 1680S–1685S.
    • (2009) Am. J. Clin. Nutr. , vol.89 , pp. 1680S-1685S
    • Lönnerdal, B.1
  • 82
    • 0033058390 scopus 로고    scopus 로고
    • Iron fortification of rice seed by the soybean ferritin gene
    • Goto, F.; Yoshihara, T.; Toki, S.; Takaiwa, F. Iron fortification of rice seed by the soybean ferritin gene. Nat. Biotechnol. 1999, 17, 282–286.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 282-286
    • Goto, F.1    Yoshihara, T.2    Toki, S.3    Takaiwa, F.4
  • 83
    • 0034947473 scopus 로고    scopus 로고
    • Approaches to improving the bioavailability and level of iron in rice seeds
    • Lucca, P.; Hurrell, R.; Potrykus, I. Approaches to improving the bioavailability and level of iron in rice seeds. J. Sci. Food Agric. 2001, 81, 828–834.
    • (2001) J. Sci. Food Agric. , vol.81 , pp. 828-834
    • Lucca, P.1    Hurrell, R.2    Potrykus, I.3
  • 84
    • 84878190494 scopus 로고    scopus 로고
    • Molecular breeding of Osfer2 gene to increase iron nutrition in rice grain
    • Paul, S.; Ali, N.; Gayen, D.; Datta, S.K.; Datta, K. Molecular breeding of Osfer2 gene to increase iron nutrition in rice grain. GM Crops Food 2012, 3, 310–316.
    • (2012) GM Crops Food , vol.3 , pp. 310-316
    • Paul, S.1    Ali, N.2    Gayen, D.3    Datta, S.K.4    Datta, K.5
  • 85
    • 26444525370 scopus 로고    scopus 로고
    • Iron accumulation does not parallel the high expression level of ferritin in transgenic rice seeds
    • Qu, Q.; Yoshihara, T.; Ooyama, A.; Goto, F.; Takaiwa, F. Iron accumulation does not parallel the high expression level of ferritin in transgenic rice seeds. Planta 2005, 222, 225–233.
    • (2005) Planta , vol.222 , pp. 225-233
    • Qu, Q.1    Yoshihara, T.2    Ooyama, A.3    Goto, F.4    Takaiwa, F.5
  • 86
    • 0036806486 scopus 로고    scopus 로고
    • Expression of human lactoferrin in transgenic rice grains for the application in infant formula
    • Nandi, S.; Suzuki, Y.; Huang, J.; Yalda, D.; Pham, P.; Wu, L.; Bartley, G.; Huang, N.; Lönnerdal, B. Expression of human lactoferrin in transgenic rice grains for the application in infant formula. Plant Sci. 2002, 163, 713–722.
    • (2002) Plant Sci , vol.163 , pp. 713-722
    • Nandi, S.1    Suzuki, Y.2    Huang, J.3    Yalda, D.4    Pham, P.5    Wu, L.6    Bartley, G.7    Huang, N.8    Lönnerdal, B.9
  • 87
    • 84863011637 scopus 로고    scopus 로고
    • Increase in iron and zinc concentrations in rice grains via the introduction of barley genes involved in phytosiderophore synthesis
    • Masuda, H.; Suzuki, M.; Morikawa, K.C.; Kobayashi, T.; Nakanishi, H.; Takahashi, M.; Saigusa, M.; Mori, S.; Nishizawa, N.K. Increase in iron and zinc concentrations in rice grains via the introduction of barley genes involved in phytosiderophore synthesis. Rice 2008, 6, 100–108.
    • (2008) Rice , vol.6 , pp. 100-108
    • Masuda, H.1    Suzuki, M.2    Morikawa, K.C.3    Kobayashi, T.4    Nakanishi, H.5    Takahashi, M.6    Saigusa, M.7    Mori, S.8    Nishizawa, N.K.9
  • 89
    • 38049077826 scopus 로고    scopus 로고
    • Transgenic rice lines that include barley genes have increased tolerance to low iron availability in a calcareous paddy soil
    • Suzuki, M.; Morikawa, K.C.; Nakanishi, H.; Takahashi, M.; Saigusa, M.; Mori, S.; Nishizawa, N.K. Transgenic rice lines that include barley genes have increased tolerance to low iron availability in a calcareous paddy soil. Soil Sci. Plant Nutr. 2008, 6, 77–85.
    • (2008) Soil Sci. Plant Nutr. , vol.6 , pp. 77-85
    • Suzuki, M.1    Morikawa, K.C.2    Nakanishi, H.3    Takahashi, M.4    Saigusa, M.5    Mori, S.6    Nishizawa, N.K.7
  • 90
    • 52449108403 scopus 로고    scopus 로고
    • Ectopic expression of soybean leghemoglobin in chloroplasts impairs gibberellin biosynthesis and induces dwarfism in transgenic potato plants
    • Bonna, A.L.; Chaparro-Giraldo, A.; Appezzato-da-Gloria, B.; Hedden P.; Silva-Filho, M.C. Ectopic expression of soybean leghemoglobin in chloroplasts impairs gibberellin biosynthesis and induces dwarfism in transgenic potato plants. Mol. Breed. 2008, 22, 613–618.
    • (2008) Mol. Breed. , vol.22 , pp. 613-618
    • Bonna, A.L.1    Chaparro-Giraldo, A.2    Appezzato-Da-Gloria, B.3    Hedden, P.4    Silva-Filho, M.C.5
  • 92
    • 84863791372 scopus 로고    scopus 로고
    • OsNRAMP5, a major player for constitutive iron and manganese uptake in rice
    • Ishimaru, Y.; Bashir, K.; Nakanishi, H.; Nishizawa, N.K. OsNRAMP5, a major player for constitutive iron and manganese uptake in rice. Plant Signal. Behav. 2012, 7, 763–766.
    • (2012) Plant Signal. Behav. , vol.7 , pp. 763-766
    • Ishimaru, Y.1    Bashir, K.2    Nakanishi, H.3    Nishizawa, N.K.4
  • 95
    • 0031787424 scopus 로고    scopus 로고
    • Effect of genetically modified, low-phytic acid maize on absorption of iron from tortillas
    • Mendoza, C.; Viteri, F.E.; Lönnerdal, B.; Young, K.A.; Raboy, V.; Brown, K.H. Effect of genetically modified, low-phytic acid maize on absorption of iron from tortillas. Am. J. Clin. Nutr. 1998, 68, 1123–1127.
    • (1998) Am. J. Clin. Nutr. , vol.68 , pp. 1123-1127
    • Mendoza, C.1    Viteri, F.E.2    Lönnerdal, B.3    Young, K.A.4    Raboy, V.5    Brown, K.H.6
  • 96
    • 0036195965 scopus 로고    scopus 로고
    • Progress in breeding low phytate crops
    • Raboy, V. Progress in breeding low phytate crops. J. Nutr. 2002, 132, 503S–505S.
    • (2002) J. Nutr. , vol.132 , pp. 503S-505S
    • Raboy, V.1
  • 97
    • 0035092567 scopus 로고    scopus 로고
    • Genetic engineering approaches to improve the bioavailability and the level of iron in rice grains
    • Lucca, P.; Hurrell, R.; Potrykus, I. Genetic engineering approaches to improve the bioavailability and the level of iron in rice grains. Theor. Appl. Genet. 2001, 102, 392–397.
    • (2001) Theor. Appl. Genet. , vol.102 , pp. 392-397
    • Lucca, P.1    Hurrell, R.2    Potrykus, I.3
  • 98
    • 0036016073 scopus 로고    scopus 로고
    • Fighting iron deficiency anemia with iron-rich rice
    • Lucca, P.; Hurrell, R.; Potrykus, I. Fighting iron deficiency anemia with iron-rich rice. J. Am. Coll. Nutr. 2002, 21, 184S–190S.
    • (2002) J. Am. Coll. Nutr. , vol.21 , pp. 184S-190S
    • Lucca, P.1    Hurrell, R.2    Potrykus, I.3
  • 102
    • 80052449864 scopus 로고    scopus 로고
    • Constitutive overexpression of the OsNAS gene family reveals single gene strategies for effective iron- and zinc-biofortification of rice endosperm
    • Johnson, A.A.T.; Kyriacou, B.; Callahan, D.L.; Carruthers, L.; Stangoulis, J.; Lombi, E.; Tester, M. Constitutive overexpression of the OsNAS gene family reveals single gene strategies for effective iron- and zinc-biofortification of rice endosperm. PLoS One 2011, 6, e24476, doi:10.1371/journal.pone.0024476.
    • (2011) Plos One , vol.6
    • Johnson, A.1    Kyriacou, B.2    Callahan, D.L.3    Carruthers, L.4    Stangoulis, J.5    Lombi, E.6    Tester, M.7
  • 103
    • 79953674494 scopus 로고    scopus 로고
    • Metallothioneins, a diverse protein family
    • Grennan, A.K. Metallothioneins, a diverse protein family. Plant. Physiol. 2011, 155, 1750–1751.
    • (2011) Plant. Physiol. , vol.155 , pp. 1750-1751
    • Grennan, A.K.1
  • 104
    • 34547098821 scopus 로고    scopus 로고
    • The rice bHLH protein OsIRO2 is an essential regulator of the genes involved in Fe uptake under Fe deficient conditions
    • Ogo, Y.; Itai, R.N.; Nakanishi, H.; Kobayashi, T.; Takahashi, M.; Mori, S.; Nishizawa, N.K. The rice bHLH protein OsIRO2 is an essential regulator of the genes involved in Fe uptake under Fe deficient conditions. Plant J. 2007, 51, 366–377.
    • (2007) Plant J , vol.51 , pp. 366-377
    • Ogo, Y.1    Itai, R.N.2    Nakanishi, H.3    Kobayashi, T.4    Takahashi, M.5    Mori, S.6    Nishizawa, N.K.7
  • 105
    • 79952703526 scopus 로고    scopus 로고
    • OsIRO2 is responsible for iron utilization in rice and improves growth and yield in calcareous soil
    • Ogo, Y.; Itai, R.N.; Kobayashi, T.; Aung, M.S.; Nakanishi, H.; Nishizawa, N.K. OsIRO2 is responsible for iron utilization in rice and improves growth and yield in calcareous soil. Plant Mol. Biol. 2011, 75, 593–605.
    • (2011) Plant Mol. Biol. , vol.75 , pp. 593-605
    • Ogo, Y.1    Itai, R.N.2    Kobayashi, T.3    Aung, M.S.4    Nakanishi, H.5    Nishizawa, N.K.6
  • 106
    • 84887863313 scopus 로고    scopus 로고
    • Iron-biofortification in rice by the introduction of three barley genes participated in mugineic acid biosynthesis with soybean ferritin gene
    • Masuda, H.; Kobayashi, T.; Ishimaru, Y.; Takahashi, M.; Aung, M.S.; Nakanishi, H.; Mori, S.; Nishizawa, N.K. Iron-biofortification in rice by the introduction of three barley genes participated in mugineic acid biosynthesis with soybean ferritin gene. Front. Plant Sci. 2013, 6, 132, doi:10.3389/fpls.2013.00132.
    • (2013) Front. Plant Sci. , vol.6
    • Masuda, H.1    Kobayashi, T.2    Ishimaru, Y.3    Takahashi, M.4    Aung, M.S.5    Nakanishi, H.6    Mori, S.7    Nishizawa, N.K.8
  • 111
    • 84900842827 scopus 로고    scopus 로고
    • Changes in endogenous gene transcript and protein levels in maize plants expressing the soybean ferritin transgene
    • Kanobe, M.N.; Rodermel, S.R.; Bailey, T.; Scott, M.P. Changes in endogenous gene transcript and protein levels in maize plants expressing the soybean ferritin transgene. Front. Plant Sci. 2013, 4, 196, doi:10.3389/fpls.2013.00196.
    • (2013) Front. Plant Sci. , vol.4
    • Kanobe, M.N.1    Rodermel, S.R.2    Bailey, T.3    Scott, M.P.4
  • 113
    • 84900986658 scopus 로고    scopus 로고
    • Improvement Fe content of wheat (Triticum aestivum) grain by soybeanferritin expression cassette without vector backbone sequence
    • Sui, X.; Zhao, Y.; Wang, S.; Duan, X.; Xu, L.; Liang, R.; Li, B.-Y. Improvement Fe content of wheat (Triticum aestivum) grain by soybeanferritin expression cassette without vector backbone sequence. J. Agric. Biotechnol. 2012, 20, 766–773.
    • (2012) J. Agric. Biotechnol. , vol.20 , pp. 766-773
    • Sui, X.1    Zhao, Y.2    Wang, S.3    Duan, X.4    Xu, L.5    Liang, R.6    Li, B.-Y.7
  • 114
    • 0034007455 scopus 로고    scopus 로고
    • Iron acumulation and enhanced growth in transgenic lettuce plants expressing the iron binding protein ferritin
    • Goto, F.; Yoshihara, T.; Saiki, H. Iron acumulation and enhanced growth in transgenic lettuce plants expressing the iron binding protein ferritin. Theor. Appl. Genet. 2000, 100, 658–664.
    • (2000) Theor. Appl. Genet. , vol.100 , pp. 658-664
    • Goto, F.1    Yoshihara, T.2    Saiki, H.3
  • 115
    • 84874564524 scopus 로고    scopus 로고
    • Lentil (Lens culinaris L.) as a candidate crop for iron biofortification: Is there genetic potential for iron bioavailability? Field Crop
    • DellaValle, D.M.; Thavarajah, D.; Thavarajah, P.; Vandenberg, A.; Glahn, R.P. Lentil (Lens culinaris L.) as a candidate crop for iron biofortification: Is there genetic potential for iron bioavailability? Field Crop. Res. 2013, 144, 119–125.
    • (2013) Res , vol.144 , pp. 119-125
    • Dellavalle, D.M.1    Thavarajah, D.2    Thavarajah, P.3    Vandenberg, A.4    Glahn, R.P.5
  • 116
    • 84883735500 scopus 로고    scopus 로고
    • The example of common bean
    • Mineral biofortification strategies for food staples
    • Blair, M.W. Mineral biofortification strategies for food staples: The example of common bean. J. Agric. Food Chem. 2013, 61, 8287–8294.
    • (2013) J. Agric. Food Chem. , vol.61 , pp. 8287-8294
    • Blair, M.W.1
  • 117
    • 0038332165 scopus 로고    scopus 로고
    • Genetically modified plants for improved trace element nutrition
    • Lönnerdal, B. Genetically modified plants for improved trace element nutrition. J. Nutr. 2003, 133, 1490–1493.
    • (2003) J. Nutr. , vol.133 , pp. 1490-1493
    • Lönnerdal, B.1
  • 118
    • 0034497919 scopus 로고    scopus 로고
    • Constitutive expression of soybean cDNA in transgenic wheat and rice results in increased iron levels in vegetative tissues but not in seeds
    • Drakakaki, G.; Christou, P.; Stoger, E. Constitutive expression of soybean cDNA in transgenic wheat and rice results in increased iron levels in vegetative tissues but not in seeds. Transgenic Res. 2000, 9, 445–452.
    • (2000) Transgenic Res , vol.9 , pp. 445-452
    • Drakakaki, G.1    Christou, P.2    Stoger, E.3
  • 119
    • 84861231493 scopus 로고    scopus 로고
    • Effect of elevated accumulation of iron in ferritin on the antioxidants content in soybean sprouts
    • Zielińska-Dawidziak, M.; Siger, A. Effect of elevated accumulation of iron in ferritin on the antioxidants content in soybean sprouts. Eur. Food Res. Technol. 2012, 234, 1005–1012
    • (2012) Eur. Food Res. Technol , vol.234 , pp. 1005-1012
    • Zielińska-Dawidziak, M.1    Siger, A.2
  • 121
    • 23644441493 scopus 로고    scopus 로고
    • Soybean genotypic difference in growth, nutrient accumulation and ultrastructure in response to manganese and iron supply in solution culture
    • Izaguirre-Mayoral, M.L.; Sinclair, T.R. Soybean genotypic difference in growth, nutrient accumulation and ultrastructure in response to manganese and iron supply in solution culture. Ann. Bot. (Lond.) 2005, 96, 149–158.
    • (2005) Ann. Bot. (Lond.) , vol.96 , pp. 149-158
    • Izaguirre-Mayoral, M.L.1    Sinclair, T.R.2
  • 122
    • 67650355074 scopus 로고    scopus 로고
    • Intestinal epithelial cell proteome from wild-type and TNFDeltaARE/WT mice: Effect of iron on the development of chronic ileitis
    • Werner, T.; Hoermannsperger, G.; Schuemann, K.; Hoelzlwimmer, G.; Tsuji, S.; Haller, D. Intestinal epithelial cell proteome from wild-type and TNFDeltaARE/WT mice: Effect of iron on the development of chronic ileitis. J. Proteome Res. 2009, 8, 3252–3264.
    • (2009) J. Proteome Res. , vol.8 , pp. 3252-3264
    • Werner, T.1    Hoermannsperger, G.2    Schuemann, K.3    Hoelzlwimmer, G.4    Tsuji, S.5    Haller, D.6
  • 123
    • 77952656662 scopus 로고    scopus 로고
    • Antioxidant-rich oral supplements attenuate the effects of oral iron on in situ oxidation susceptibility of human feces
    • Orozco, M.N.; Solomons, N.W.; Schumann, K.; Friel, J.K.; de Montenegro, A.L. Antioxidant-rich oral supplements attenuate the effects of oral iron on in situ oxidation susceptibility of human feces. J. Nutr. 2010, 140, 1105–1110.
    • (2010) J. Nutr. , vol.140 , pp. 1105-1110
    • Orozco, M.N.1    Solomons, N.W.2    Schumann, K.3    Friel, J.K.4    De Montenegro, A.L.5
  • 124
    • 33745838898 scopus 로고    scopus 로고
    • Iron at the center of ferritin, metal/oxygen homeostasis and novel dietary strategies
    • Liu, X.; Hintze, K.B.; Lonnerdal, B.; Theil, E.C. Iron at the center of ferritin, metal/oxygen homeostasis and novel dietary strategies. Biol. Res. 2006, 39, 167–171.
    • (2006) Biol. Res. , vol.39 , pp. 167-171
    • Liu, X.1    Hintze, K.B.2    Lonnerdal, B.3    Theil, E.C.4
  • 125
    • 0343659409 scopus 로고
    • Lupin ferritin: Purification and characterization, biosynthesis and regulation of in vitro synthesis in plant system
    • Korcz, A.; Twardowski, T. Lupin ferritin: Purification and characterization, biosynthesis and regulation of in vitro synthesis in plant system. J. Plant Physiol. 1992, 141, 75–81.
    • (1992) J. Plant Physiol. , vol.141 , pp. 75-81
    • Korcz, A.1    Twardowski, T.2
  • 126
    • 37549050569 scopus 로고    scopus 로고
    • Biosynthesis, isolation and characterization of 57Fe enriched Phaseolus vulgaris ferritin after heterologous expression in Escherichia coli
    • Hoppler, M.; Meile, L.; Walczyk, T. Biosynthesis, isolation and characterization of 57Fe enriched Phaseolus vulgaris ferritin after heterologous expression in Escherichia coli. Anal. Bioanal. Chem. 2008, 390, 53–59.
    • (2008) Anal. Bioanal. Chem. , vol.390 , pp. 53-59
    • Hoppler, M.1    Meile, L.2    Walczyk, T.3
  • 127
    • 69749099455 scopus 로고    scopus 로고
    • Quantification of ferritin-bound iron in plant samples by isotope tagging and species-specific isotope dilution mass spectrometry
    • Hoppler, M.; Zeder, C.; Walczyk, T. Quantification of ferritin-bound iron in plant samples by isotope tagging and species-specific isotope dilution mass spectrometry. Anal. Chem. 2009, 81, 7368–7372.
    • (2009) Anal. Chem. , vol.81 , pp. 7368-7372
    • Hoppler, M.1    Zeder, C.2    Walczyk, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.