메뉴 건너뛰기




Volumn 101, Issue 9, 2003, Pages 3690-3698

Relationships and distinctions in iron-regulatory networks responding to interrelated signals

Author keywords

[No Author keywords available]

Indexed keywords

FERRIC AMMONIUM CITRATE; HEMIN; NITROPRUSSIDE SODIUM; COMPLEMENTARY DNA; DEFEROXAMINE; FERRIC ION; HFE PROTEIN, HUMAN; HLA ANTIGEN CLASS 1; HYBRID PROTEIN; HYDROGEN PEROXIDE; IRON; IRON CHELATING AGENT; MEMBRANE PROTEIN; QUATERNARY AMMONIUM DERIVATIVE;

EID: 0037939676     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood-2002-07-2140     Document Type: Article
Times cited : (58)

References (78)
  • 2
    • 0036525721 scopus 로고    scopus 로고
    • Metal transporters and disease
    • Andrews NC. Metal transporters and disease. Curr Opin Chem Biol. 2002;6:181-186.
    • (2002) Curr Opin Chem Biol , vol.6 , pp. 181-186
    • Andrews, N.C.1
  • 3
    • 0035006006 scopus 로고    scopus 로고
    • Ironing out disease: Inherited disorders of iron homeostasis
    • Anderson GJ. Ironing out disease: inherited disorders of iron homeostasis. IUBMB Life. 2001;51:11-17.
    • (2001) IUBMB Life , vol.51 , pp. 11-17
    • Anderson, G.J.1
  • 4
    • 0033599057 scopus 로고    scopus 로고
    • Disorders of iron metabolism
    • Andrews NC, Disorders of iron metabolism. N Engl J Med. 2000;341:1986-1995.
    • (2000) N Engl J Med , vol.341 , pp. 1986-1995
    • Andrews, N.C.1
  • 5
    • 0037096190 scopus 로고    scopus 로고
    • The iron regulatory proteins: Targets and modulators of free radical reactions and oxidative damage
    • Cairo G, Recalcati S, Pietrangelo A, Minotti G. The iron regulatory proteins: targets and modulators of free radical reactions and oxidative damage. Free Radic Biol Med. 2002;32:1237-1243.
    • (2002) Free Radic Biol Med , vol.32 , pp. 1237-1243
    • Cairo, G.1    Recalcati, S.2    Pietrangelo, A.3    Minotti, G.4
  • 6
    • 0029758487 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nithe oxide, and oxidative stress
    • Hentze MW, Kühn LC. Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nithe oxide, and oxidative stress. Proc Natl Acad Sci U S A. 1996;93:8175-8182.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 8175-8182
    • Hentze, M.W.1    Kühn, L.C.2
  • 7
    • 0025811624 scopus 로고
    • Human erythroid 5-aminolevulinate synthase: Promoter analysis and identification of an iron-responsive element in the mRNA
    • Cox TC, Bawden MJ, Martin A, May BK. Human erythroid 5-aminolevulinate synthase: promoter analysis and identification of an iron-responsive element in the mRNA. EMBO J. 1991;10:1891-1902.
    • (1991) EMBO J , vol.10 , pp. 1891-1902
    • Cox, T.C.1    Bawden, M.J.2    Martin, A.3    May, B.K.4
  • 8
    • 0025822118 scopus 로고
    • Identification of a novel iron-responsive element in murine and human erythroid delta-aminolevulinic acid synthase mRNA
    • Dandekar T, Stripecke R, Gray NK, et al. Identification of a novel iron-responsive element in murine and human erythroid delta-aminolevulinic acid synthase mRNA. EMBO J. 1991;10:1903-1909.
    • (1991) EMBO J , vol.10 , pp. 1903-1909
    • Dandekar, T.1    Stripecke, R.2    Gray, N.K.3
  • 9
    • 0029899154 scopus 로고    scopus 로고
    • Translational regulation of mammalian and Drosophila citric acid cycle enzymes via iron-responsive elements
    • Gray NK, Pantopoulos K, Dandekar T, Ackrell BA, Hentze MW. Translational regulation of mammalian and Drosophila citric acid cycle enzymes via iron-responsive elements. Proc Natl Acad Sci U S A. 1996;93:4925-4930.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 4925-4930
    • Gray, N.K.1    Pantopoulos, K.2    Dandekar, T.3    Ackrell, B.A.4    Hentze, M.W.5
  • 10
    • 0023612118 scopus 로고
    • Identification of the iron-responsive element for the translational regulation of human ferritin mRNA
    • Hentze MW, Caughman SW, Rouautt TA, et al. Identification of the iron-responsive element for the translational regulation of human ferritin mRNA. Science. 1987;238:1570-1573.
    • (1987) Science , vol.238 , pp. 1570-1573
    • Hentze, M.W.1    Caughman, S.W.2    Rouautt, T.A.3
  • 11
    • 0029793466 scopus 로고    scopus 로고
    • Identification of a conserved and functional iron-responsive element in the 5′-untranslated region of mammalian mitochondrial aconitase
    • Kim HY, LaVaute T, Iwai K, Klausner RD, Rouault TA. Identification of a conserved and functional iron-responsive element in the 5′-untranslated region of mammalian mitochondrial aconitase. J Biol Chem. 1996;271:24226-24230.
    • (1996) J Biol Chem , vol.271 , pp. 24226-24230
    • Kim, H.Y.1    LaVaute, T.2    Iwai, K.3    Klausner, R.D.4    Rouault, T.A.5
  • 12
    • 0029557688 scopus 로고
    • Succinate dehydrogenase b mRNA of Drosophila melanogaster has a functional iron-responsive element in its 5′-untranslated region
    • Kohler SA, Henderson BR, Kuhn LC. Succinate dehydrogenase b mRNA of Drosophila melanogaster has a functional iron-responsive element in its 5′-untranslated region. J Biol Chem. 1995;270:30781-30786.
    • (1995) J Biol Chem , vol.270 , pp. 30781-30786
    • Kohler, S.A.1    Henderson, B.R.2    Kuhn, L.C.3
  • 13
    • 0030638220 scopus 로고    scopus 로고
    • Mechanisms for posttranscriptional regulation by iron-responsive elements and iron regulatory proteins
    • Muckenthaler M, Hentze MW. Mechanisms for posttranscriptional regulation by iron-responsive elements and iron regulatory proteins. Prog Mol Subcell Biol. 1997;18:93-115.
    • (1997) Prog Mol Subcell Biol , vol.18 , pp. 93-115
    • Muckenthaler, M.1    Hentze, M.W.2
  • 14
    • 0034531651 scopus 로고    scopus 로고
    • Iron regulatory proteins in pathobiology
    • Cairo G, Pietrangelo A. Iron regulatory proteins in pathobiology. Biochem J. 2000;352:241-250.
    • (2000) Biochem J , vol.352 , pp. 241-250
    • Cairo, G.1    Pietrangelo, A.2
  • 15
    • 0033826764 scopus 로고    scopus 로고
    • Iron regulatory proteins and the molecular control of mammalian iron metabolism
    • Eisenstein RS. Iron regulatory proteins and the molecular control of mammalian iron metabolism. Annu Rev Nutr. 2000;20:627-662.
    • (2000) Annu Rev Nutr , vol.20 , pp. 627-662
    • Eisenstein, R.S.1
  • 16
    • 0028131454 scopus 로고
    • Iron regulates cytoplasmic levels of a novel iron-responsive element-binding protein without aconitase activity
    • Guo B, Yu Y, Leibold EA. Iron regulates cytoplasmic levels of a novel iron-responsive element-binding protein without aconitase activity. J Biol Chem. 1994;269:24252-24260.
    • (1994) J Biol Chem , vol.269 , pp. 24252-24260
    • Guo, B.1    Yu, Y.2    Leibold, E.A.3
  • 17
    • 0024471801 scopus 로고
    • Regulation of interaction of the iron-responsive element binding protein with iron-responsive RNA elements
    • Haile DJ, Hentze MW, Rouault TA, Harford JB, Klausner RD. Regulation of interaction of the iron-responsive element binding protein with iron-responsive RNA elements. Mol Cell Biol. 1989;9:5055-5061.
    • (1989) Mol Cell Biol , vol.9 , pp. 5055-5061
    • Haile, D.J.1    Hentze, M.W.2    Rouault, T.A.3    Harford, J.B.4    Klausner, R.D.5
  • 18
    • 0027717217 scopus 로고
    • Characterization of a second RNA-binding protein in rodents with specificity for iron-responsive elements
    • Henderson BR, Seiser C, Kühn LC. Characterization of a second RNA-binding protein in rodents with specificity for iron-responsive elements. J Biol Chem. 1993;268:27327-27334.
    • (1993) J Biol Chem , vol.268 , pp. 27327-27334
    • Henderson, B.R.1    Seiser, C.2    Kühn, L.C.3
  • 19
    • 0029281832 scopus 로고
    • Differential regulation of two related RNA-binding proteins, iron regulatory protein (IRP) and IRPB
    • Pantopoulos K, Gray NK, Hentze MW. Differential regulation of two related RNA-binding proteins, iron regulatory protein (IRP) and IRPB. RNA. 1995;1:155-163.
    • (1995) RNA , vol.1 , pp. 155-163
    • Pantopoulos, K.1    Gray, N.K.2    Hentze, M.W.3
  • 20
    • 0023713448 scopus 로고
    • Binding of a cytosolic protein to the iron-responsive element of human ferritin messenger RNA
    • Rouault TA, Hentze MW, Caughman SW, Harford JB, Klausner RD. Binding of a cytosolic protein to the iron-responsive element of human ferritin messenger RNA. Science. 1988;241:1207-1210.
    • (1988) Science , vol.241 , pp. 1207-1210
    • Rouault, T.A.1    Hentze, M.W.2    Caughman, S.W.3    Harford, J.B.4    Klausner, R.D.5
  • 21
    • 0028143071 scopus 로고
    • Molecular characterization of a second iron-responsive element binding protein, iron regulatory protein 2: Structure, function, and posttranslational regulation
    • Samaniego F, Chin J, Iwai K, Rouault TA, Klausner RD. Molecular characterization of a second iron-responsive element binding protein, iron regulatory protein 2: structure, function, and posttranslational regulation. J Biol Chem. 1994;269:30904-30910.
    • (1994) J Biol Chem , vol.269 , pp. 30904-30910
    • Samaniego, F.1    Chin, J.2    Iwai, K.3    Rouault, T.A.4    Klausner, R.D.5
  • 22
    • 0027301897 scopus 로고
    • Biosynthesis of nitric oxide activates iron regulatory factor in macrophages
    • Drapier JC, Hirling H, Wietzerbin J, Kaldy P, Kühn LC. Biosynthesis of nitric oxide activates iron regulatory factor in macrophages. EMBO J. 1993;12:3643-3649.
    • (1993) EMBO J , vol.12 , pp. 3643-3649
    • Drapier, J.C.1    Hirling, H.2    Wietzerbin, J.3    Kaldy, P.4    Kühn, L.C.5
  • 23
    • 0028799569 scopus 로고
    • Oxidative stress induces activation of a cytosolic protein responsible for control of iron uptake
    • Martins EA, Robalinho RL, Meneghini R. Oxidative stress induces activation of a cytosolic protein responsible for control of iron uptake. Arch Biochem Biophys. 1995;316:128-134.
    • (1995) Arch Biochem Biophys , vol.316 , pp. 128-134
    • Martins, E.A.1    Robalinho, R.L.2    Meneghini, R.3
  • 24
    • 0029054681 scopus 로고
    • Effect of nitric oxide on expression of transferrin receptor and ferritin and on cellular iron metabolism in K562 human erythroleukemia cells
    • Oria R, Sanchez L, Houston T, Hentze MW, Liew FY, Brock JH. Effect of nitric oxide on expression of transferrin receptor and ferritin and on cellular iron metabolism in K562 human erythroleukemia cells. Blood. 1995;85:2962-2966.
    • (1995) Blood , vol.85 , pp. 2962-2966
    • Oria, R.1    Sanchez, L.2    Houston, T.3    Hentze, M.W.4    Liew, F.Y.5    Brock, J.H.6
  • 25
    • 0028929741 scopus 로고
    • Nitric oxide signaling to iron-regulatory protein: Direct control of ferritin mRNA translation and transferrin receptor mRNA stability in transfected fibroblasts
    • Pantopoulos K, Hentze MW. Nitric oxide signaling to iron-regulatory protein: direct control of ferritin mRNA translation and transferrin receptor mRNA stability in transfected fibroblasts. Proc Natl Acad Sci U S A. 1995;92:1267-1271.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 1267-1271
    • Pantopoulos, K.1    Hentze, M.W.2
  • 26
    • 0032167632 scopus 로고    scopus 로고
    • Activation of iron regulatory protein-1 by oxidative stress in vitro
    • Pantopoulos K, Hentze MW. Activation of iron regulatory protein-1 by oxidative stress in vitro. Proc Natl Acad Sci U S A. 1998;95:10559-10563.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 10559-10563
    • Pantopoulos, K.1    Hentze, M.W.2
  • 27
  • 28
    • 0028784211 scopus 로고
    • The effect of redox-related species of nitrogen monoxide on transferrin and iron uptake and cellular proliferation of erythroleukemia (K562) cells
    • Richardson DR, Neumannova V, Nagy E, Ponka P. The effect of redox-related species of nitrogen monoxide on transferrin and iron uptake and cellular proliferation of erythroleukemia (K562) cells. Blood. 1995;86:3211-3219.
    • (1995) Blood , vol.86 , pp. 3211-3219
    • Richardson, D.R.1    Neumannova, V.2    Nagy, E.3    Ponka, P.4
  • 29
    • 0027184412 scopus 로고
    • Translational regulation via iron-responsive elements by the nitric oxide/NO-synthase pathway
    • Weiss G, Goossen B, Doppler W, et al. Translational regulation via iron-responsive elements by the nitric oxide/NO-synthase pathway. EMBO J. 1993;12:3651-3657.
    • (1993) EMBO J , vol.12 , pp. 3651-3657
    • Weiss, G.1    Goossen, B.2    Doppler, W.3
  • 30
    • 0033230181 scopus 로고    scopus 로고
    • HIF-1-mediated activation of transferrin receptor gene transcription by iron chelation
    • Bianchi L, Tacchini L, Cairo G. HIF-1-mediated activation of transferrin receptor gene transcription by iron chelation. Nucleic Acids Res. 1999;27:4223-4227.
    • (1999) Nucleic Acids Res , vol.27 , pp. 4223-4227
    • Bianchi, L.1    Tacchini, L.2    Cairo, G.3
  • 31
    • 0000655498 scopus 로고    scopus 로고
    • Identification of a hypoxia response element in the transferrin receptor gene
    • Lok CN, Ponka P. Identification of a hypoxia response element in the transferrin receptor gene. J Biol Chem. 1999;274:24147-24152.
    • (1999) J Biol Chem , vol.274 , pp. 24147-24152
    • Lok, C.N.1    Ponka, P.2
  • 32
    • 0033588021 scopus 로고    scopus 로고
    • Transferrin receptor induction by hypoxia: HIF-1-mediated transcriptional activation and cell-specific post-transcriptional regulation
    • Tacchini L, Bianchi L, Bernelli-Zazzera A, Cairo G. Transferrin receptor induction by hypoxia: HIF-1-mediated transcriptional activation and cell-specific post-transcriptional regulation. J Biol Chem. 1999;274:24142-24146.
    • (1999) J Biol Chem , vol.274 , pp. 24142-24146
    • Tacchini, L.1    Bianchi, L.2    Bernelli-Zazzera, A.3    Cairo, G.4
  • 33
    • 0032883958 scopus 로고    scopus 로고
    • Effects of TNF-alpha and IL-1beta on iron metabolism by A549 cells and influence on cytotoxicity
    • Smirnov IM, Bailey K, Flowers CH, Garrigues NW, Wesselius LJ. Effects of TNF-alpha and IL-1beta on iron metabolism by A549 cells and influence on cytotoxicity. Am J Physiol. 1999;277:L257-L263.
    • (1999) Am J Physiol , vol.277
    • Smirnov, I.M.1    Bailey, K.2    Flowers, C.H.3    Garrigues, N.W.4    Wesselius, L.J.5
  • 34
    • 0033568442 scopus 로고    scopus 로고
    • Induction of ferritin and heat shock proteins by prostaglandin A1 in human monocytes: Evidence for transcriptional and post-transcriptional regulation
    • Elia G, Polla B, Rossi A, Santoro MG. Induction of ferritin and heat shock proteins by prostaglandin A1 in human monocytes: evidence for transcriptional and post-transcriptional regulation. Eur J Biochem. 1999;264:736-745.
    • (1999) Eur J Biochem , vol.264 , pp. 736-745
    • Elia, G.1    Polla, B.2    Rossi, A.3    Santoro, M.G.4
  • 35
    • 0036535072 scopus 로고    scopus 로고
    • An alternative model of H ferritin promoter transactivation by c-Jun
    • Faniello MC, Chirico G, Quaresima B, et al. An alternative model of H ferritin promoter transactivation by c-Jun. Biochem J. 2002;363:53-58.
    • (2002) Biochem J , vol.363 , pp. 53-58
    • Faniello, M.C.1    Chirico, G.2    Quaresima, B.3
  • 36
    • 0033613854 scopus 로고    scopus 로고
    • Coordinated regulation of iron-controlling genes, H-ferritin and IRP2, by c-MYC
    • Wu KJ, Polack A, Dalla-Favera R. Coordinated regulation of iron-controlling genes, H-ferritin and IRP2, by c-MYC. Science. 1999;283:676-679.
    • (1999) Science , vol.283 , pp. 676-679
    • Wu, K.J.1    Polack, A.2    Dalla-Favera, R.3
  • 37
    • 9344224529 scopus 로고    scopus 로고
    • A novel MHC class I-like gene is mutated in patients with hereditary haemochromatosis
    • Feder JN, Gnirke A, Thomas W, et al. A novel MHC class I-like gene is mutated in patients with hereditary haemochromatosis. Nat Genet. 1996;13:399-408.
    • (1996) Nat Genet , vol.13 , pp. 399-408
    • Feder, J.N.1    Gnirke, A.2    Thomas, W.3
  • 38
    • 0034006860 scopus 로고    scopus 로고
    • Genetic disorders affecting proteins of iron metabolism: Clinical implications
    • Sheth S, Brittenham GM. Genetic disorders affecting proteins of iron metabolism: clinical implications. Annu Rev Med. 2000;51:443-464.
    • (2000) Annu Rev Med , vol.51 , pp. 443-464
    • Sheth, S.1    Brittenham, G.M.2
  • 39
    • 17644434333 scopus 로고    scopus 로고
    • The hemochromatosis founder mutation in HLA-H disrupts beta2-microglobutin interaction and cell surface expression
    • Feder JN, Tsuchihashi Z, Irrinki A, et al. The hemochromatosis founder mutation in HLA-H disrupts beta2-microglobutin interaction and cell surface expression. J Biol Chem. 1997;272:14025-14028.
    • (1997) J Biol Chem , vol.272 , pp. 14025-14028
    • Feder, J.N.1    Tsuchihashi, Z.2    Irrinki, A.3
  • 40
    • 0030732164 scopus 로고    scopus 로고
    • Hereditary hemochromatosis: Effects of C282Y and H63D mutations on association with beta2-microglobulin, intracellular processing, and cell surface expression of the HFE protein in COS-7 cells
    • Waheed A, Parkkila S, Zhou XY, et al. Hereditary hemochromatosis: effects of C282Y and H63D mutations on association with beta2-microglobulin, intracellular processing, and cell surface expression of the HFE protein in COS-7 cells. Proc Natl Acad Sci U S A. 1997;94:12384-12389.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 12384-12389
    • Waheed, A.1    Parkkila, S.2    Zhou, X.Y.3
  • 41
    • 0033628484 scopus 로고    scopus 로고
    • Two novel polymorphisms (E277K and V212V) in the haemochromatosis gene HFE
    • Bradbury R, Fagan E, Payne SJ. Two novel polymorphisms (E277K and V212V) in the haemochromatosis gene HFE. Hum Mutat. 2000;15:120-121.
    • (2000) Hum Mutat , vol.15 , pp. 120-121
    • Bradbury, R.1    Fagan, E.2    Payne, S.J.3
  • 43
    • 13144282684 scopus 로고    scopus 로고
    • The hemochromatosis gene product complexes with the transferrin receptor and lowers its affinity for ligand binding
    • Feder JN, Penny DM, Irrinki A, et al. The hemochromatosis gene product complexes with the transferrin receptor and lowers its affinity for ligand binding. Proc Natl Acad Sci U S A. 1998;95:1472-1477.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 1472-1477
    • Feder, J.N.1    Penny, D.M.2    Irrinki, A.3
  • 44
    • 0030712463 scopus 로고    scopus 로고
    • Association of the transferrin receptor in human placenta with HFE, the protein detective in hereditary hemochromatosis
    • Parkkila S, Waheed A, Britton RS, et al. Association of the transferrin receptor in human placenta with HFE, the protein detective in hereditary hemochromatosis. Proc Natl Acad Sci U S A. 1997;94:13198-13202.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 13198-13202
    • Parkkila, S.1    Waheed, A.2    Britton, R.S.3
  • 45
    • 0033020518 scopus 로고    scopus 로고
    • The transferrin receptor binding site on HFE, the class I MHC-related protein mutated in hereditary hemochromatosis
    • Lebron JA, Bjorkman PJ. The transferrin receptor binding site on HFE, the class I MHC-related protein mutated in hereditary hemochromatosis. J Mol Biol. 1999;289:1109-1118.
    • (1999) J Mol Biol , vol.289 , pp. 1109-1118
    • Lebron, J.A.1    Bjorkman, P.J.2
  • 46
    • 0033605595 scopus 로고    scopus 로고
    • The hereditary hemochromatosis protein, HFE, specifically regulates transterrin-mediated iron uptake in HeLa cells
    • Roy CN, Penny DM, Feder JN, Enns CA. The hereditary hemochromatosis protein, HFE, specifically regulates transterrin-mediated iron uptake in HeLa cells. J Biol Chem. 1999;274:9022-9028.
    • (1999) J Biol Chem , vol.274 , pp. 9022-9028
    • Roy, C.N.1    Penny, D.M.2    Feder, J.N.3    Enns, C.A.4
  • 47
    • 0033485885 scopus 로고    scopus 로고
    • HFE downregulates iron uptake from transferrin and induces iron-regulatory protein activity in stably transfected cells
    • Riedel HD, Muckenthaler MU, Gehrke SG, et al. HFE downregulates iron uptake from transferrin and induces iron-regulatory protein activity in stably transfected cells. Blood. 1999;94:3915-3921.
    • (1999) Blood , vol.94 , pp. 3915-3921
    • Riedel, H.D.1    Muckenthaler, M.U.2    Gehrke, S.G.3
  • 48
    • 0037022588 scopus 로고    scopus 로고
    • Regulation of transferrin-mediated iron uptake by HFE, the protein defective in hereditary hemochromatosis
    • Waheed A, Grubb JH, Zhou XY, et al. Regulation of transferrin-mediated iron uptake by HFE, the protein defective in hereditary hemochromatosis. Proc Natl Acad Sci U S A. 2002;99:3117-3122.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 3117-3122
    • Waheed, A.1    Grubb, J.H.2    Zhou, X.Y.3
  • 49
    • 0032555601 scopus 로고    scopus 로고
    • Co-trafficking of HFE, a nonclassical major histocompatibility complex class I protein, with the transferrin receptor implies a role in intracellular iron regulation
    • Gross CN, Irrinki A, Feder JN, Enns CA. Co-trafficking of HFE, a nonclassical major histocompatibility complex class I protein, with the transferrin receptor implies a role in intracellular iron regulation. J Biol Chem. 1998;273:22068-22074.
    • (1998) J Biol Chem , vol.273 , pp. 22068-22074
    • Gross, C.N.1    Irrinki, A.2    Feder, J.N.3    Enns, C.A.4
  • 50
    • 0035052391 scopus 로고    scopus 로고
    • Biochip technologies in cancer research
    • Kallioniemi OP. Biochip technologies in cancer research. Ann Med. 2001;33:142-147.
    • (2001) Ann Med , vol.33 , pp. 142-147
    • Kallioniemi, O.P.1
  • 51
    • 0034910345 scopus 로고    scopus 로고
    • Navigating gene expression using microarrays: A technology review
    • Schulze A, Downward J. Navigating gene expression using microarrays: a technology review. Nat Cell Biol. 2001;3:190-195.
    • (2001) Nat Cell Biol , vol.3 , pp. 190-195
    • Schulze, A.1    Downward, J.2
  • 52
    • 0034763772 scopus 로고    scopus 로고
    • Functional genomics and metal metabolism
    • Eide DJ. Functional genomics and metal metabolism. Genome Biol. 2001;2:1-3.
    • (2001) Genome Biol , vol.2 , pp. 1-3
    • Eide, D.J.1
  • 53
    • 0036752147 scopus 로고    scopus 로고
    • Comparison of fluorescent tag DNA labeling methods used for expression analysis by DNA microarrays
    • Richter A, Schwager C, Hentze S, Ansorge W, Hentze M, Muckenthaler M. Comparison of fluorescent tag DNA labeling methods used for expression analysis by DNA microarrays. Biotechniques. 2002;33:620-628,630.
    • (2002) Biotechniques , vol.33 , pp. 620-628
    • Richter, A.1    Schwager, C.2    Hentze, S.3    Ansorge, W.4    Hentze, M.5    Muckenthaler, M.6
  • 55
    • 0040126630 scopus 로고    scopus 로고
    • The deadenylating nuclease (DAN) is involved in poly(A) tail removal during the meiotic maturation of Xenopus oocytes
    • Körner CG, Wormington M, Muckenthaler M, Schneider S, Dehlin E, Wahle E. The deadenylating nuclease (DAN) is involved in poly(A) tail removal during the meiotic maturation of Xenopus oocytes. EMBO J. 1998;17:5427-5437.
    • (1998) EMBO J , vol.17 , pp. 5427-5437
    • Körner, C.G.1    Wormington, M.2    Muckenthaler, M.3    Schneider, S.4    Dehlin, E.5    Wahle, E.6
  • 56
    • 0023884191 scopus 로고
    • Induction of ferritin subunit synthesis by iron is regulated at both the transcriptional and translational levels
    • White K, Munro HN. Induction of ferritin subunit synthesis by iron is regulated at both the transcriptional and translational levels. J Biol Chem. 1988;263:8938-8942.
    • (1988) J Biol Chem , vol.263 , pp. 8938-8942
    • White, K.1    Munro, H.N.2
  • 57
    • 0024819020 scopus 로고
    • Iron regulation of transferrin receptor mRNA levels requires iron-responsive elements and a rapid turnover determinant in the 3′ untranslated region of the mRNA
    • Casey JL, Koeller DM, Ramin VC, Klausner RD, Harford JB. Iron regulation of transferrin receptor mRNA levels requires iron-responsive elements and a rapid turnover determinant in the 3′ untranslated region of the mRNA. EMBO J. 1989;8:3693-3699.
    • (1989) EMBO J , vol.8 , pp. 3693-3699
    • Casey, J.L.1    Koeller, D.M.2    Ramin, V.C.3    Klausner, R.D.4    Harford, J.B.5
  • 58
    • 0024365045 scopus 로고
    • A specific mRNA binding factor regulates the iron-dependent stability of cytoplasmic transferrin receptor mRNA
    • Müllner EW, Neupert B, Kühn LC. A specific mRNA binding factor regulates the iron-dependent stability of cytoplasmic transferrin receptor mRNA. Cell. 1989;58:373-382.
    • (1989) Cell , vol.58 , pp. 373-382
    • Müllner, E.W.1    Neupert, B.2    Kühn, L.C.3
  • 59
    • 18244389488 scopus 로고    scopus 로고
    • Iron-dependent regulation of the divalent metal ion transporter
    • Gunshin H, Allerson CR, Polycarpou-Schwarz M, et al. Iron-dependent regulation of the divalent metal ion transporter. FEBS Lett. 2001;509:309-316.
    • (2001) FEBS Lett , vol.509 , pp. 309-316
    • Gunshin, H.1    Allerson, C.R.2    Polycarpou-Schwarz, M.3
  • 60
    • 0014670945 scopus 로고
    • Microsomal heme oxygenase: Characterization of the enzyme
    • Tenhunen R, Marver HS, Schmid R. Microsomal heme oxygenase: characterization of the enzyme. J Biol Chem. 1969;244:6388-6394.
    • (1969) J Biol Chem , vol.244 , pp. 6388-6394
    • Tenhunen, R.1    Marver, H.S.2    Schmid, R.3
  • 61
  • 62
    • 0018104963 scopus 로고
    • Induction of heme oxygenase by hemin in cultured pig alveolar macrophages
    • Shibahara S, Yoshida T, Kikuchi G. Induction of heme oxygenase by hemin in cultured pig alveolar macrophages. Arch Biochem Biophys. 1978;188:243-250.
    • (1978) Arch Biochem Biophys , vol.188 , pp. 243-250
    • Shibahara, S.1    Yoshida, T.2    Kikuchi, G.3
  • 63
    • 0030886381 scopus 로고    scopus 로고
    • Heme oxygenase 1 is required for mammalian iron reutilization
    • Poss KD, Tonegawa S. Heme oxygenase 1 is required for mammalian iron reutilization. Proc Natl Acad Sci U S A. 1997;94:10919-10924.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 10919-10924
    • Poss, K.D.1    Tonegawa, S.2
  • 64
    • 0029055581 scopus 로고
    • Rapid responses to oxidative stress mediated by iron regulatory protein
    • Pantopoulos K, Hentze MW. Rapid responses to oxidative stress mediated by iron regulatory protein. EMBO J. 1995;14:2917-2924.
    • (1995) EMBO J , vol.14 , pp. 2917-2924
    • Pantopoulos, K.1    Hentze, M.W.2
  • 65
    • 0024497521 scopus 로고
    • Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite
    • Keyse SM, Tyrrell RM. Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite. Proc Natl Acad Sci U S A. 1989;86:99-103.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 99-103
    • Keyse, S.M.1    Tyrrell, R.M.2
  • 66
    • 0032746973 scopus 로고    scopus 로고
    • Control of transferrin receptor expression via nitric oxide-mediated modulation of iron-regulatory protein 2
    • Kim S, Ponka P. Control of transferrin receptor expression via nitric oxide-mediated modulation of iron-regulatory protein 2. J Biol Chem. 1999;274:33035-33042.
    • (1999) J Biol Chem , vol.274 , pp. 33035-33042
    • Kim, S.1    Ponka, P.2
  • 67
    • 0032866573 scopus 로고    scopus 로고
    • Overexpression of the hereditary hemochromatosis protein, HFE, in HeLa cells induces and iron-deficient phenotype
    • Corsi B, Levi S, Cozzi A, et al. Overexpression of the hereditary hemochromatosis protein, HFE, in HeLa cells induces and iron-deficient phenotype. FEBS Lett. 1999;460:149-152.
    • (1999) FEBS Lett , vol.460 , pp. 149-152
    • Corsi, B.1    Levi, S.2    Cozzi, A.3
  • 68
    • 0035938289 scopus 로고    scopus 로고
    • The effects of wild-type and mutant HFE expression upon cellular iron uptake in transfected human embryonic kidney cells
    • Feeney GP, Worwood M. The effects of wild-type and mutant HFE expression upon cellular iron uptake in transfected human embryonic kidney cells. Biochim Biophys Acta. 2001;1538:242-251.
    • (2001) Biochim Biophys Acta , vol.1538 , pp. 242-251
    • Feeney, G.P.1    Worwood, M.2
  • 69
    • 0036135887 scopus 로고    scopus 로고
    • Increased IRP1 and IRP2 RNA binding activity accompanies a reduction of the labile iron pool in HFE-expressing cells
    • Roy CN, Blemings KP, Deck KM, et al. Increased IRP1 and IRP2 RNA binding activity accompanies a reduction of the labile iron pool in HFE-expressing cells. J Cell Physiol. 2002;190:218-226.
    • (2002) J Cell Physiol , vol.190 , pp. 218-226
    • Roy, C.N.1    Blemings, K.P.2    Deck, K.M.3
  • 70
    • 0033545852 scopus 로고    scopus 로고
    • Transferrin receptor is negatively modulated by the hemochromatosis protein HFE: Implications for cellular iron homeostasis
    • Salter-Cid L, Brunmark A, Li Y, et al. Transferrin receptor is negatively modulated by the hemochromatosis protein HFE: implications for cellular iron homeostasis. Proc Natl Acad Sci U S A. 1999;96:5434-5439.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 5434-5439
    • Salter-Cid, L.1    Brunmark, A.2    Li, Y.3
  • 71
    • 0032160381 scopus 로고    scopus 로고
    • IRP-1 binding to ferritin mRNA prevents the recruitment of the small ribosomal subunit by the cap-binding complex elF4F
    • Muckenthaler M, Gray NK, Hentze MW. IRP-1 binding to ferritin mRNA prevents the recruitment of the small ribosomal subunit by the cap-binding complex elF4F. Mol Cell. 1998;2:383-388.
    • (1998) Mol Cell , vol.2 , pp. 383-388
    • Muckenthaler, M.1    Gray, N.K.2    Hentze, M.W.3
  • 72
    • 0034733635 scopus 로고    scopus 로고
    • A novel mammalian iron-regulated protein involved in intracellular iron metabolism
    • Abboud S, Haile DJ. A novel mammalian iron-regulated protein involved in intracellular iron metabolism. J Biol Chem. 2000;275:19906-19912.
    • (2000) J Biol Chem , vol.275 , pp. 19906-19912
    • Abboud, S.1    Haile, D.J.2
  • 73
    • 0034677467 scopus 로고    scopus 로고
    • Positional cloning of zebrafish ferroportin1 identifies a conserved vertebrate iron exporter
    • Donovan A, Brownlie A, Zhou Y, et al. Positional cloning of zebrafish ferroportin1 identifies a conserved vertebrate iron exporter. Nature. 2000;403:776-781.
    • (2000) Nature , vol.403 , pp. 776-781
    • Donovan, A.1    Brownlie, A.2    Zhou, Y.3
  • 74
    • 0033861745 scopus 로고    scopus 로고
    • A novel duodenal iron-regulated transporter, IREG1, implicated in the basolateral transfer of iron to the circulation
    • McKie AT, Marciani P, Rolts A, et al. A novel duodenal iron-regulated transporter, IREG1, implicated in the basolateral transfer of iron to the circulation. Mol Cell. 2000;5:299-309.
    • (2000) Mol Cell , vol.5 , pp. 299-309
    • McKie, A.T.1    Marciani, P.2    Rolts, A.3
  • 75
    • 0032540929 scopus 로고    scopus 로고
    • MtHsp70 homolog, Ssc2p, required for maturation of yeast frataxin and mitochondrial iron homeostasis
    • Knight SA, Sepuri NB, Pain D, Dancis A. MtHsp70 homolog, Ssc2p, required for maturation of yeast frataxin and mitochondrial iron homeostasis. J Biol Chem. 1998;273:18389-18393.
    • (1998) J Biol Chem , vol.273 , pp. 18389-18393
    • Knight, S.A.1    Sepuri, N.B.2    Pain, D.3    Dancis, A.4
  • 76
    • 0028834446 scopus 로고
    • Iron acquired from transferrin by K562 cells is delivered into a cytoplasmic pool of chelatable iron(II)
    • Breuer W, Epsztejn S, Cabantchik ZI. Iron acquired from transferrin by K562 cells is delivered into a cytoplasmic pool of chelatable iron(II). J Biol Chem. 1995;270:24209-24215.
    • (1995) J Biol Chem , vol.270 , pp. 24209-24215
    • Breuer, W.1    Epsztejn, S.2    Cabantchik, Z.I.3
  • 77
    • 0029266160 scopus 로고
    • Iron species in iron homeostasis and toxicity
    • Crichton RR, Ward RJ. Iron species in iron homeostasis and toxicity. Analyst. 1995;120:693-697.
    • (1995) Analyst , vol.120 , pp. 693-697
    • Crichton, R.R.1    Ward, R.J.2
  • 78
    • 0017700831 scopus 로고
    • Low molecular weight intracellular iron transport compounds
    • Jacobs A. Low molecular weight intracellular iron transport compounds. Blood. 1977;50:433-439.
    • (1977) Blood , vol.50 , pp. 433-439
    • Jacobs, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.