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Volumn 39, Issue 1, 2006, Pages 167-171

Iron at the center of ferritin, metal/oxygen homeostasis and novel dietary strategies

Author keywords

[No Author keywords available]

Indexed keywords

DNA; FERRITIN; FERROPORTIN 1; HEME; IRON; MESSENGER RNA; METAL; OXYGEN;

EID: 33745838898     PISSN: 07169760     EISSN: 07176287     Source Type: Journal    
DOI: 10.4067/S0716-97602006000100018     Document Type: Conference Paper
Times cited : (12)

References (26)
  • 1
    • 0030071285 scopus 로고    scopus 로고
    • Ferritin and soybean meal can be sources of iron for treating iron deficiency in rats
    • BEARD JL, BURTON, JOSEPH W, THEIL EC (1996) Ferritin and soybean meal can be sources of iron for treating iron deficiency in rats. J Nutr 126: 154-160
    • (1996) J Nutr , vol.126 , pp. 154-160
    • Beard, J.L.1    Burton, J.W.2    Theil, E.C.3
  • 2
    • 0031605218 scopus 로고    scopus 로고
    • Iron storage and ferritin in plants
    • BRIAT JF, LOBREAUX S (1998) Iron storage and ferritin in plants. Met Ions Biol Syst 35: 563-584
    • (1998) Met Ions Biol Syst , vol.35 , pp. 563-584
    • Briat, J.F.1    Lobreaux, S.2
  • 3
    • 0034531651 scopus 로고    scopus 로고
    • Iron regulatory proteins in pathobiology
    • CAIRO G, PIETRANGELO A (2000) Iron regulatory proteins in pathobiology. Biochemical Journal 352: 241-250
    • (2000) Biochemical Journal , vol.352 , pp. 241-250
    • Cairo, G.1    Pietrangelo, A.2
  • 4
    • 0033617958 scopus 로고    scopus 로고
    • Mineralization in ferritin: An efficient means of iron storage
    • CHASTEEN ND, HARRISON PM (1999) Mineralization in ferritin: An efficient means of iron storage. J Struct Biol 126: 182-194
    • (1999) J Struct Biol , vol.126 , pp. 182-194
    • Chasteen, N.D.1    Harrison, P.M.2
  • 6
    • 5144224375 scopus 로고    scopus 로고
    • Iron in ferritin or in salts (ferrous sulfate) is equally bioavailable in nonanemic women
    • DÁVILA-HICKS P, THEIL EC, LONNERDAL B (2004) Iron in ferritin or in salts (ferrous sulfate) is equally bioavailable in nonanemic women. Am J Clin Nutr 80: 936-940
    • (2004) Am J Clin Nutr , vol.80 , pp. 936-940
    • Dávila-Hicks, P.1    Theil, E.C.2    Lonnerdal, B.3
  • 7
    • 0036206393 scopus 로고    scopus 로고
    • Redox control of iron regulatory proteins
    • FILLEBEEN C, PANTOPOULOS K (2002) Redox control of iron regulatory proteins. Redox Rep 7: 15-22
    • (2002) Redox Rep , vol.7 , pp. 15-22
    • Fillebeen, C.1    Pantopoulos, K.2
  • 9
    • 0032793828 scopus 로고    scopus 로고
    • Crystal structure of bullfrog M ferritin at 2.8 A resolution: Analysis of subunit interactions and the binuclear metal center
    • HA Y, SHI D, SMALL GW, THEIL EC, ALLEWELL NM (1999) Crystal structure of bullfrog M ferritin at 2.8 A resolution: Analysis of subunit interactions and the binuclear metal center. J Biol Inorg Chem 4: 243-256
    • (1999) J Biol Inorg Chem , vol.4 , pp. 243-256
    • Ha, Y.1    Shi, D.2    Small, G.W.3    Theil, E.C.4    Allewell, N.M.5
  • 10
    • 0141890273 scopus 로고    scopus 로고
    • Oxygen and iron regulation of iron regulatory protein 2
    • HANSON ES, RAWLINS ML, LEIBOLD EA (2003) Oxygen and iron regulation of iron regulatory protein 2. J Biol Chem 278: 40337-40342
    • (2003) J Biol Chem , vol.278 , pp. 40337-40342
    • Hanson, E.S.1    Rawlins, M.L.2    Leibold, E.A.3
  • 11
    • 2042546096 scopus 로고    scopus 로고
    • Balancing acts: Molecular control of mammalian iron metabolism
    • HENTZE MW, MUCKENTHALER MU, ANDREWS NC (2004) Balancing acts: Molecular control of mammalian iron metabolism. Cell 117: 285-297
    • (2004) Cell , vol.117 , pp. 285-297
    • Hentze, M.W.1    Muckenthaler, M.U.2    Andrews, N.C.3
  • 12
    • 27244457379 scopus 로고    scopus 로고
    • DNA and mRNA elements with complementary responses to hemin, antioxidant inducers, and iron control ferritin-L expression
    • HINTZE KJ, THEIL EC (2005) DNA and mRNA elements with complementary responses to hemin, antioxidant inducers, and iron control ferritin-L expression. Proc Nat'l Sci 102: 15048-15052
    • (2005) Proc Nat'l Sci , vol.102 , pp. 15048-15052
    • Hintze, K.J.1    Theil, E.C.2
  • 14
    • 2942558543 scopus 로고    scopus 로고
    • Ferritin reactions: Direct identification of the site for the diferric peroxide reaction intermediate
    • LIU X, THEIL EC (2004) Ferritin reactions: Direct identification of the site for the diferric peroxide reaction intermediate. Proc Nat'l Acad Sci USA 101
    • (2004) Proc Nat'l Acad Sci USA , vol.101
    • Liu, X.1    Theil, E.C.2
  • 15
    • 15244339209 scopus 로고    scopus 로고
    • Ferritin: Dynamic management of biological iron and oxygen chemistry
    • LIU X, THEIL EC (2005) Ferritin: Dynamic management of biological iron and oxygen chemistry. Accounts of Chemical Research 38: 161-175
    • (2005) Accounts of Chemical Research , vol.38 , pp. 161-175
    • Liu, X.1    Theil, E.C.2
  • 16
    • 10844282789 scopus 로고    scopus 로고
    • Mammalian tissue oxygen levels modulate iron-regulatory protein activities in vivo
    • MEYRON-HOLTZ EG, GHOSH MC, ROUAULT TA (2004) Mammalian tissue oxygen levels modulate iron-regulatory protein activities in vivo. Science 306: 2087-2090
    • (2004) Science , vol.306 , pp. 2087-2090
    • Meyron-Holtz, E.G.1    Ghosh, M.C.2    Rouault, T.A.3
  • 18
    • 0029944620 scopus 로고    scopus 로고
    • Ferritin gene organization: Differences between plants and animals suggest possible kingdom-specific selective constraints
    • PROUDHON D, WEI J, BRIAT J, THEIL EC (1996) Ferritin gene organization: Differences between plants and animals suggest possible kingdom-specific selective constraints. Molecular Evolution 42: 325-336
    • (1996) Molecular Evolution , vol.42 , pp. 325-336
    • Proudhon, D.1    Wei, J.2    Briat, J.3    Theil, E.C.4
  • 19
    • 0000171802 scopus 로고    scopus 로고
    • Ferritin
    • Messerschmidt A, Huber R, Poulos T, Wieghardt K (eds) Chichester: John Wiley & Sons
    • THEIL EC (2001) Ferritin. In: MESSERSCHMIDT A, HUBER R, POULOS T, WIEGHARDT K (eds) Handbook of Metalloproteins. Chichester: John Wiley & Sons. pp: 771-781
    • (2001) Handbook of Metalloproteins , pp. 771-781
    • Theil, E.C.1
  • 20
    • 3142781945 scopus 로고    scopus 로고
    • Iron, ferritin, and nutrition
    • THEIL EC (2004) Iron, ferritin, and nutrition. Annu Rev Nutr 24: 327-343
    • (2004) Annu Rev Nutr , vol.24 , pp. 327-343
    • Theil, E.C.1
  • 21
    • 0034731457 scopus 로고    scopus 로고
    • Combinatorial mRNA regulation: Iron regulatory proteins and iso-iron responsive elements (iso-IREs)
    • THEIL EC, EISENSTEIN RS (2000) Combinatorial mRNA regulation: iron regulatory proteins and iso-iron responsive elements (iso-IREs). J Biol Chem 275: 40659-40662
    • (2000) J Biol Chem , vol.275 , pp. 40659-40662
    • Theil, E.C.1    Eisenstein, R.S.2
  • 22
    • 0037093202 scopus 로고    scopus 로고
    • Regulation of ferritin genes and protein
    • TORTI FM, TORTI SV (2002) Regulation of ferritin genes and protein. Blood 99: 3505-3516
    • (2002) Blood , vol.99 , pp. 3505-3516
    • Torti, F.M.1    Torti, S.V.2
  • 24
    • 0032579380 scopus 로고    scopus 로고
    • Activation of the ferritin H enhancer, FER-1, by the cooperative action of members of the AP1 and Sp1 transcription factor families
    • TSUJI Y, TORTI SV, TORTI FM (1998) Activation of the ferritin H enhancer, FER-1, by the cooperative action of members of the AP1 and Sp1 transcription factor families. J Biol Chem 273: 2984-2992
    • (1998) J Biol Chem , vol.273 , pp. 2984-2992
    • Tsuji, Y.1    Torti, S.V.2    Torti, F.M.3
  • 25
    • 0029781087 scopus 로고    scopus 로고
    • Molecular diffusion into horse spleen ferritin: A nitroxide radical spin probe study
    • YANG X, CHASTEEN ND (1996) Molecular diffusion into horse spleen ferritin: A nitroxide radical spin probe study. Biophys J 71: 1587-1595
    • (1996) Biophys J , vol.71 , pp. 1587-1595
    • Yang, X.1    Chasteen, N.D.2
  • 26
    • 0037008743 scopus 로고    scopus 로고
    • Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells. A ferritin-like DNA-binding protein of Escherichia coli
    • ZHAO G, CECI P, ILARI A, GIANGIACOMO L, LAUE TM, CHIANCONE E, CHASTEEN N D(2002) Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells. A ferritin-like DNA-binding protein of Escherichia coli. J Biol Chem 277: 27689-27696
    • (2002) J Biol Chem , vol.277 , pp. 27689-27696
    • Zhao, G.1    Ceci, P.2    Ilari, A.3    Giangiacomo, L.4    Laue, T.M.5    Chiancone, E.6    Chasteen, N.D.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.