메뉴 건너뛰기




Volumn 41, Issue 2, 2009, Pages 82-99

The power plant of the cell is also a smithy: The emerging role of mitochondria in cellular iron homeostasis

Author keywords

Anemia; Ataxia; Hemochromatosis; Iron; Iron sulfur cluster; Mitochondria; Porphyria; Sideroblast

Indexed keywords

HEMOPROTEIN; IRON; IRON REGULATORY FACTOR; IRON SULFUR PROTEIN;

EID: 61349203895     PISSN: 07853890     EISSN: 16512219     Source Type: Journal    
DOI: 10.1080/07853890802322229     Document Type: Review
Times cited : (41)

References (155)
  • 1
    • 0000283394 scopus 로고
    • On a new reaction or tartaric acid
    • Fenton HJH. On a new reaction or tartaric acid. Chemical News 1876;33:190.
    • (1876) Chemical News , vol.33 , pp. 190
    • Fenton, H.J.H.1
  • 2
    • 0025126555 scopus 로고
    • Role of free radicals and catalytic metal ions in human disease: An overview
    • Halliwell B, Gutteridge JM. Role of free radicals and catalytic metal ions in human disease: an overview. Methods Enzymol. 1990;186:1-85.
    • (1990) Methods Enzymol , vol.186 , pp. 1-85
    • Halliwell, B.1    Gutteridge, J.M.2
  • 3
    • 0015980484 scopus 로고
    • The role of transferrin in iron transport
    • Aisen P. The role of transferrin in iron transport. Br J Haematol. 1974;26:159-63.
    • (1974) Br J Haematol , vol.26 , pp. 159-163
    • Aisen, P.1
  • 4
    • 0030885482 scopus 로고    scopus 로고
    • Iron accumulation in Alzheimer disease is a source of redox-generated free radicals
    • Smith MA, Harris PL, Sayre LM, Perry G. Iron accumulation in Alzheimer disease is a source of redox-generated free radicals. Proc Natl Acad Sci U S A. 1997;94:9866-8.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 9866-9868
    • Smith, M.A.1    Harris, P.L.2    Sayre, L.M.3    Perry, G.4
  • 6
    • 1842608738 scopus 로고    scopus 로고
    • Hereditary causes of disturbed iron homeostasis in the central nervous system
    • Ponka P. Hereditary causes of disturbed iron homeostasis in the central nervous system. Ann NY Acad Sci. 2004;1012:267-81.
    • (2004) Ann NY Acad Sci , vol.1012 , pp. 267-281
    • Ponka, P.1
  • 8
    • 0036809412 scopus 로고    scopus 로고
    • A specialized mitochondrial molecular chaperone system: A role in formation of Fe/S centers
    • Craig EA, Marszalek J. A specialized mitochondrial molecular chaperone system: a role in formation of Fe/S centers. Cell Mol Life Sci. 2002;59:1658-65.
    • (2002) Cell Mol Life Sci , vol.59 , pp. 1658-1665
    • Craig, E.A.1    Marszalek, J.2
  • 9
    • 17144378216 scopus 로고    scopus 로고
    • Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis
    • Rouault TA, Tong WH. Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis. Nat Rev Mol Cell Biol. 2005;6:345-51.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 345-351
    • Rouault, T.A.1    Tong, W.H.2
  • 11
    • 0031567095 scopus 로고    scopus 로고
    • The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells
    • Richardson DR, Ponka P. The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells. Biochim Biophys Acta. 1997;1331:1-40.
    • (1997) Biochim Biophys Acta , vol.1331 , pp. 1-40
    • Richardson, D.R.1    Ponka, P.2
  • 12
    • 27644455133 scopus 로고    scopus 로고
    • Identification of a ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells
    • Ohgami RS, Campagna DR, Greer EL, Antiochos B, McDonald A, Chen J, et al. Identification of a ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells. Nat Genet. 2005;37:1264-9.
    • (2005) Nat Genet , vol.37 , pp. 1264-1269
    • Ohgami, R.S.1    Campagna, D.R.2    Greer, E.L.3    Antiochos, B.4    McDonald, A.5    Chen, J.6
  • 13
    • 0030755366 scopus 로고    scopus 로고
    • Cloning and characterization of a mammalian proton-coupled metal-ion transporter
    • Gunshin H, Mackenzie B, Berger UV, Gunshin Y, Romero MF, Boron WF, et al. Cloning and characterization of a mammalian proton-coupled metal-ion transporter. Nature. 1997;388:482-8.
    • (1997) Nature , vol.388 , pp. 482-488
    • Gunshin, H.1    Mackenzie, B.2    Berger, U.V.3    Gunshin, Y.4    Romero, M.F.5    Boron, W.F.6
  • 14
    • 11144226961 scopus 로고    scopus 로고
    • Intracellular kinetics of iron in reticulocytes: Evidence for endosome involvement in iron targeting to mitochondria
    • Zhang AS, Sheftel AD, Ponka P. Intracellular kinetics of iron in reticulocytes: evidence for endosome involvement in iron targeting to mitochondria. Blood. 2005;105:368-75.
    • (2005) Blood , vol.105 , pp. 368-375
    • Zhang, A.S.1    Sheftel, A.D.2    Ponka, P.3
  • 15
    • 34347375300 scopus 로고    scopus 로고
    • Direct interorganellar transfer of iron from endosome to mitochondrion
    • Sheftel AD, Zhang AS, Brown C, Shirihai OS, Ponka P. Direct interorganellar transfer of iron from endosome to mitochondrion. Blood. 2007;110:125-32.
    • (2007) Blood , vol.110 , pp. 125-132
    • Sheftel, A.D.1    Zhang, A.S.2    Brown, C.3    Shirihai, O.S.4    Ponka, P.5
  • 16
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function and cellular regulation
    • Harrison PM, Arosio P. The ferritins: molecular properties, iron storage function and cellular regulation. Biochim Biophys Acta. 1996;1275:161-203.
    • (1996) Biochim Biophys Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 17
    • 0018236898 scopus 로고
    • Ferritin: Structure, biosynthesis, and role in iron metabolism
    • Munro HN, Linder MC. Ferritin: structure, biosynthesis, and role in iron metabolism. Physiol Rev. 1978;58:317-96.
    • (1978) Physiol Rev , vol.58 , pp. 317-396
    • Munro, H.N.1    Linder, M.C.2
  • 19
    • 0037151089 scopus 로고    scopus 로고
    • Human mitochondrial ferritin expressed in HeLa cells incorporates iron and affects cellular iron metabolism
    • Corsi B, Cozzi A, Arosio P, Drysdale J, Santambrogio P, Campanella A, et al. Human mitochondrial ferritin expressed in HeLa cells incorporates iron and affects cellular iron metabolism. J Biol Chem. 2002;277:22430-7.
    • (2002) J Biol Chem , vol.277 , pp. 22430-22437
    • Corsi, B.1    Cozzi, A.2    Arosio, P.3    Drysdale, J.4    Santambrogio, P.5    Campanella, A.6
  • 20
    • 0030060705 scopus 로고    scopus 로고
    • Overexpression of the ferritin H subunit in cultured erythroid cells changes the intracellular iron distribution
    • Picard V, Renaudie F, Porcher C, Hentze MW, Grandchamp B, Beaumont C. Overexpression of the ferritin H subunit in cultured erythroid cells changes the intracellular iron distribution. Blood. 1996;87:2057-64.
    • (1996) Blood , vol.87 , pp. 2057-2064
    • Picard, V.1    Renaudie, F.2    Porcher, C.3    Hentze, M.W.4    Grandchamp, B.5    Beaumont, C.6
  • 21
    • 0032546922 scopus 로고    scopus 로고
    • Role of ferritin in the control of the labile iron pool in murine erythroleukemia cells
    • Picard V, Epsztejn S, Santambrogio P, Cabantchik ZI, Beaumont C. Role of ferritin in the control of the labile iron pool in murine erythroleukemia cells. J Biol Chem. 1998;273:15382-6.
    • (1998) J Biol Chem , vol.273 , pp. 15382-15386
    • Picard, V.1    Epsztejn, S.2    Santambrogio, P.3    Cabantchik, Z.I.4    Beaumont, C.5
  • 22
    • 33646228833 scopus 로고    scopus 로고
    • Tissue-specific expression of ferritin H regulates cellular iron homoeostasis in vivo
    • Wilkinson J 4th, Di X, Schonig K, Buss JL, Kock ND, Cline JM, et al. Tissue-specific expression of ferritin H regulates cellular iron homoeostasis in vivo. Biochem J. 2006;395:501-7.
    • (2006) Biochem J , vol.395 , pp. 501-507
    • Wilkinson 4th, J.1    Di, X.2    Schonig, K.3    Buss, J.L.4    Kock, N.D.5    Cline, J.M.6
  • 23
    • 14944358625 scopus 로고    scopus 로고
    • Overexpression of mitochondrial ferritin causes cytosolic iron depletion and changes cellular iron homeostasis
    • Nie G, Sheftel AD, Kim SF, Ponka P. Overexpression of mitochondrial ferritin causes cytosolic iron depletion and changes cellular iron homeostasis. Blood. 2005;105:2161-7.
    • (2005) Blood , vol.105 , pp. 2161-2167
    • Nie, G.1    Sheftel, A.D.2    Kim, S.F.3    Ponka, P.4
  • 24
    • 0001189562 scopus 로고
    • Sur la cristallisation de la ferritine.
    • Laufberger V. Sur la cristallisation de la ferritine. Bull Soc Chim Biol. 1937;19:1575-82.
    • (1937) Bull Soc Chim Biol , vol.19 , pp. 1575-1582
    • Laufberger, V.1
  • 25
    • 0016287813 scopus 로고
    • Ferritin iron uptake and release. Structure-function relationships
    • Harrison PM, Hoy TG, Macara IG, Hoare RJ. Ferritin iron uptake and release. Structure-function relationships. Biochem J. 1974;143:445-51.
    • (1974) Biochem J , vol.143 , pp. 445-451
    • Harrison, P.M.1    Hoy, T.G.2    Macara, I.G.3    Hoare, R.J.4
  • 26
    • 0019797926 scopus 로고
    • Ferric ion sequestering agents: Kinetics of iron release from ferritin to catechoylamides
    • Tufano TP, Pecoraro VL, Raymond KN. Ferric ion sequestering agents: kinetics of iron release from ferritin to catechoylamides. Biochim Biophys Acta. 1981;668:420-8.
    • (1981) Biochim Biophys Acta , vol.668 , pp. 420-428
    • Tufano, T.P.1    Pecoraro, V.L.2    Raymond, K.N.3
  • 28
    • 33751103909 scopus 로고    scopus 로고
    • Ferroportin-mediated mobilization of ferritin iron precedes ferritin degradation by the proteasome
    • De Domenico I, Vaughn MB, Li L, Bagley D, Musci G, Ward DM, et al. Ferroportin-mediated mobilization of ferritin iron precedes ferritin degradation by the proteasome. EMBO J. 2006;25:5396-404.
    • (2006) EMBO J , vol.25 , pp. 5396-5404
    • De Domenico, I.1    Vaughn, M.B.2    Li, L.3    Bagley, D.4    Musci, G.5    Ward, D.M.6
  • 31
    • 33746872950 scopus 로고    scopus 로고
    • Iron uptake in fungi: A system for every source
    • Philpott CC. Iron uptake in fungi: a system for every source. Biochim Biophys Acta. 2006;1763:636-45.
    • (2006) Biochim Biophys Acta , vol.1763 , pp. 636-645
    • Philpott, C.C.1
  • 34
    • 17044451174 scopus 로고    scopus 로고
    • A specific role of the yeast mitochondrial carriers MRS3/4p in mitochondrial iron acquisition under iron-limiting conditions
    • Muhlenhoff U, Stadler JA, Richhardt N, Seubert A, Eickhorst T, Schweyen RJ, et al. A specific role of the yeast mitochondrial carriers MRS3/4p in mitochondrial iron acquisition under iron-limiting conditions. J Biol Chem. 2003;278:40612-20.
    • (2003) J Biol Chem , vol.278 , pp. 40612-40620
    • Muhlenhoff, U.1    Stadler, J.A.2    Richhardt, N.3    Seubert, A.4    Eickhorst, T.5    Schweyen, R.J.6
  • 35
    • 0035800856 scopus 로고    scopus 로고
    • CCC1 is a transporter that mediates vacuolar iron storage in yeast
    • Li L, Chen OS, McVey WD, Kaplan J. CCC1 is a transporter that mediates vacuolar iron storage in yeast. J Biol Chem. 2001;276:29515-9.
    • (2001) J Biol Chem , vol.276 , pp. 29515-29519
    • Li, L.1    Chen, O.S.2    McVey, W.D.3    Kaplan, J.4
  • 37
    • 0002698015 scopus 로고
    • Heme biosynthesis, the porphyrias, and the liver
    • Arias IM, Boyer JL, Fausto N, Jakoby WB, Schachter DA, Shafritz DA, editors, 3rd ed. New York: Raven Press Ltd
    • Wyckoff EE, Kushner JP. Heme biosynthesis, the porphyrias, and the liver. In: Arias IM, Boyer JL, Fausto N, Jakoby WB, Schachter DA, Shafritz DA, editors. The liver: biology and pathobiology, 3rd ed. New York: Raven Press Ltd, 1994. p. 505-27.
    • (1994) The liver: Biology and pathobiology , pp. 505-527
    • Wyckoff, E.E.1    Kushner, J.P.2
  • 40
    • 33749530252 scopus 로고    scopus 로고
    • Identification of a mammalian mitochondrial porphyrin transporter
    • Krishnamurthy PC, Du G, Fukuda Y, Sun D, Sampath J, Mercer KE, et al. Identification of a mammalian mitochondrial porphyrin transporter. Nature. 2006;443:586-9.
    • (2006) Nature , vol.443 , pp. 586-589
    • Krishnamurthy1    PC, D.G.2    Fukuda, Y.3    Sun, D.4    Sampath, J.5    Mercer, K.E.6
  • 42
    • 40849126574 scopus 로고    scopus 로고
    • Human ABC transporter isoform B6 (ABCB6) localizes primarily in the Golgi apparatus
    • Tsuchida M, Emi Y, Kida Y, Sakaguchi M. Human ABC transporter isoform B6 (ABCB6) localizes primarily in the Golgi apparatus. Biochem Biophys Res Commun. 2008;369:369-75.
    • (2008) Biochem Biophys Res Commun , vol.369 , pp. 369-375
    • Tsuchida, M.1    Emi, Y.2    Kida, Y.3    Sakaguchi, M.4
  • 44
    • 0034625457 scopus 로고    scopus 로고
    • MTABC3, a novel mitochondrial ATP-binding cassette protein involved in iron homeostasis
    • Mitsuhashi N, Miki T, Senbongi H, Yokoi N, Yano H, Miyazaki M, et al. MTABC3, a novel mitochondrial ATP-binding cassette protein involved in iron homeostasis. J Biol Chem. 2000;275:17536-40.
    • (2000) J Biol Chem , vol.275 , pp. 17536-17540
    • Mitsuhashi, N.1    Miki, T.2    Senbongi, H.3    Yokoi, N.4    Yano, H.5    Miyazaki, M.6
  • 45
    • 0032414310 scopus 로고    scopus 로고
    • Identification of a human mitochondrial ABC transporter, the functional orthologue of yeast Atm1p
    • Csere P, Lill R, Kispal G. Identification of a human mitochondrial ABC transporter, the functional orthologue of yeast Atm1p. FEBS Lett. 1998;441:266-70.
    • (1998) FEBS Lett , vol.441 , pp. 266-270
    • Csere, P.1    Lill, R.2    Kispal, G.3
  • 46
    • 33644772614 scopus 로고    scopus 로고
    • The mitochondrial ATP-binding cassette transporter Abcb7 is essential in mice and participates in cytosolic iron-sulfur cluster biogenesis
    • Pondarre C, Antiochos BB, Campagna DR, Clarke SL, Greer EL, Deck KM, et al. The mitochondrial ATP-binding cassette transporter Abcb7 is essential in mice and participates in cytosolic iron-sulfur cluster biogenesis. Hum Mol Genet. 2006;15:953-64.
    • (2006) Hum Mol Genet , vol.15 , pp. 953-964
    • Pondarre, C.1    Antiochos, B.B.2    Campagna, D.R.3    Clarke, S.L.4    Greer, E.L.5    Deck, K.M.6
  • 47
    • 34147158934 scopus 로고    scopus 로고
    • Abcb7, the gene responsible for X-linked sideroblastic anemia with ataxia, is essential for hematopoiesis
    • Pondarre C, Campagna DR, Antiochos B, Sikorski L, Mulhern H, Fleming MD. Abcb7, the gene responsible for X-linked sideroblastic anemia with ataxia, is essential for hematopoiesis. Blood. 2007;109:3567-9.
    • (2007) Blood , vol.109 , pp. 3567-3569
    • Pondarre, C.1    Campagna, D.R.2    Antiochos, B.3    Sikorski, L.4    Mulhern, H.5    Fleming, M.D.6
  • 48
    • 2442563409 scopus 로고    scopus 로고
    • Crystal structure of protoporphyrinogen IX oxidase: A key enzyme in haem and chlorophyll biosynthesis
    • Koch M, Breithaupt C, Kiefersauer R, Freigang J, Huber R, Messerschmidt A. Crystal structure of protoporphyrinogen IX oxidase: a key enzyme in haem and chlorophyll biosynthesis. EMBO J. 2004;23:1720-8.
    • (2004) EMBO J , vol.23 , pp. 1720-1728
    • Koch, M.1    Breithaupt, C.2    Kiefersauer, R.3    Freigang, J.4    Huber, R.5    Messerschmidt, A.6
  • 49
    • 0036670802 scopus 로고    scopus 로고
    • Terminal steps of haem biosynthesis
    • Dailey HA. Terminal steps of haem biosynthesis. Biochem Soc Trans. 2002;30:590-5.
    • (2002) Biochem Soc Trans , vol.30 , pp. 590-595
    • Dailey, H.A.1
  • 51
    • 0024332591 scopus 로고
    • Regulation of the stability of chicken embryo liver delta-aminolevulinate synthase mRNA by hemin
    • Drew PD, Ades IZ. Regulation of the stability of chicken embryo liver delta-aminolevulinate synthase mRNA by hemin. Biochem Biophys Res Commun. 1989;162:102-7.
    • (1989) Biochem Biophys Res Commun , vol.162 , pp. 102-107
    • Drew, P.D.1    Ades, I.Z.2
  • 52
    • 0026045762 scopus 로고
    • Heme regulates hepatic 5-aminolevulinate synthase mRNA expression by decreasing mRNA half-life and not by altering its rate of transcription
    • Hamilton JW, Bement WJ, Sinclair PR, Sinclair JF, Alcedo JA, Wetterhahn KE. Heme regulates hepatic 5-aminolevulinate synthase mRNA expression by decreasing mRNA half-life and not by altering its rate of transcription. Arch Biochem Biophys. 1991;289:387-92.
    • (1991) Arch Biochem Biophys , vol.289 , pp. 387-392
    • Hamilton, J.W.1    Bement, W.J.2    Sinclair, P.R.3    Sinclair, J.F.4    Alcedo, J.A.5    Wetterhahn, K.E.6
  • 53
    • 0019488137 scopus 로고
    • Regulation by heme of synthesis and intracellular translocation of delta-aminolevulinate synthase in the liver
    • Kikuchi G, Hayashi N. Regulation by heme of synthesis and intracellular translocation of delta-aminolevulinate synthase in the liver. Mol Cell Biochem. 1981;37:27-41.
    • (1981) Mol Cell Biochem , vol.37 , pp. 27-41
    • Kikuchi, G.1    Hayashi, N.2
  • 54
    • 0027405813 scopus 로고
    • Regulation by heme of mitochondrial protein transport through a conserved amino acid motif
    • Lathrop JT, Timko MP. Regulation by heme of mitochondrial protein transport through a conserved amino acid motif. Science. 1993;259:522-5.
    • (1993) Science , vol.259 , pp. 522-525
    • Lathrop, J.T.1    Timko, M.P.2
  • 55
    • 0002634758 scopus 로고
    • Tetrapyrrole and heme biosynthesis in the yeast Saccharomyces cerevisiae
    • Dailey HA, editor, New York: McGraw-Hill;
    • Labbe-Bois R, Labbe P. Tetrapyrrole and heme biosynthesis in the yeast Saccharomyces cerevisiae. In: Dailey HA, editor. Biosynthesis of heme and chlorophylls. New York: McGraw-Hill; 1990. p. 235-85.
    • (1990) Biosynthesis of heme and chlorophylls , pp. 235-285
    • Labbe-Bois, R.1    Labbe, P.2
  • 56
    • 0141996306 scopus 로고    scopus 로고
    • Identification of rate-limiting steps in yeast heme biosynthesis
    • Hoffman M, Gora M, Rytka J. Identification of rate-limiting steps in yeast heme biosynthesis. Biochem Biophys Res Commun. 2003;310:1247-53.
    • (2003) Biochem Biophys Res Commun , vol.310 , pp. 1247-1253
    • Hoffman, M.1    Gora, M.2    Rytka, J.3
  • 57
    • 0026559542 scopus 로고
    • Regulation of gene expression by oxygen in Saccharomyces cerevisiae
    • Zitomer RS, Lowry CV. Regulation of gene expression by oxygen in Saccharomyces cerevisiae. Microbiol Rev. 1992;56:1-11.
    • (1992) Microbiol Rev , vol.56 , pp. 1-11
    • Zitomer, R.S.1    Lowry, C.V.2
  • 58
    • 0032052761 scopus 로고    scopus 로고
    • Oxygen sensing and the transcriptional regulation of oxygen-responsive genes in yeast
    • Kwast KE, Burke PV, Poyton RO. Oxygen sensing and the transcriptional regulation of oxygen-responsive genes in yeast. J Exp Biol. 1998;201:1177-95.
    • (1998) J Exp Biol , vol.201 , pp. 1177-1195
    • Kwast, K.E.1    Burke, P.V.2    Poyton, R.O.3
  • 59
    • 0031028178 scopus 로고    scopus 로고
    • Tissue-specific regulation of iron metabolism and heme synthesis: Distinct control mechanisms in erythroid cells
    • Ponka P. Tissue-specific regulation of iron metabolism and heme synthesis: distinct control mechanisms in erythroid cells. Blood. 1997;89:1-25.
    • (1997) Blood , vol.89 , pp. 1-25
    • Ponka, P.1
  • 60
    • 47249094614 scopus 로고    scopus 로고
    • Maturation of iron-sulfur proteins in eukaryotes: Mechanisms, connected processes, and diseases
    • Lill R, Mühlenhoff U. Maturation of iron-sulfur proteins in eukaryotes: mechanisms, connected processes, and diseases. Annu Rev Biochem. 2008;77:669-700.
    • (2008) Annu Rev Biochem , vol.77 , pp. 669-700
    • Lill, R.1    Mühlenhoff, U.2
  • 61
    • 0034636795 scopus 로고    scopus 로고
    • IscU as a scaffold for iron-sulfur cluster biosynthesis: Sequential assembly of [2Fe-2S] and [4Fe-4S] clusters in IscU
    • Agar JN, Krebs C, Frazzon J, Huynh BH, Dean DR, Johnson MK. IscU as a scaffold for iron-sulfur cluster biosynthesis: sequential assembly of [2Fe-2S] and [4Fe-4S] clusters in IscU. Biochemistry. 2000;39:7856-62.
    • (2000) Biochemistry , vol.39 , pp. 7856-7862
    • Agar, J.N.1    Krebs, C.2    Frazzon, J.3    Huynh, B.H.4    Dean, D.R.5    Johnson, M.K.6
  • 62
    • 30444433568 scopus 로고    scopus 로고
    • The Nfs1 interacting protein Isd11 has an essential role in Fe/S cluster biogenesis in mitochondria
    • Adam AC, Bornhovd C, Prokisch H, Neupert W, Hell K. The Nfs1 interacting protein Isd11 has an essential role in Fe/S cluster biogenesis in mitochondria. EMBO J. 2006;25:174-83.
    • (2006) EMBO J , vol.25 , pp. 174-183
    • Adam, A.C.1    Bornhovd, C.2    Prokisch, H.3    Neupert, W.4    Hell, K.5
  • 63
    • 30444449009 scopus 로고    scopus 로고
    • Essential role of Isd11 in mitochondrial iron-sulfur cluster synthesis on Isu scaffold proteins
    • Wiedemann N, Urzica E, Guiard B, Müller H, Lohaus C, Meyer HE, et al. Essential role of Isd11 in mitochondrial iron-sulfur cluster synthesis on Isu scaffold proteins. EMBO J. 2006;25:184-95.
    • (2006) EMBO J , vol.25 , pp. 184-195
    • Wiedemann, N.1    Urzica, E.2    Guiard, B.3    Müller, H.4    Lohaus, C.5    Meyer, H.E.6
  • 64
    • 20744446399 scopus 로고    scopus 로고
    • Structure, function, and formation of biological iron-sulfur clusters
    • Johnson DC, Dean DR, Smith AD, Johnson MK. Structure, function, and formation of biological iron-sulfur clusters. Annu Rev Biochem. 2005;74:247-81.
    • (2005) Annu Rev Biochem , vol.74 , pp. 247-281
    • Johnson, D.C.1    Dean, D.R.2    Smith, A.D.3    Johnson, M.K.4
  • 65
    • 34247472498 scopus 로고    scopus 로고
    • Functional analysis of Arabidopsis genes involved in mitochondrial iron-sulfur cluster assembly
    • Frazzon AP, Ramirez MV, Warek U, Balk J, Frazzon J, Dean DR, et al. Functional analysis of Arabidopsis genes involved in mitochondrial iron-sulfur cluster assembly. Plant Mol Biol. 2007;64:225-40.
    • (2007) Plant Mol Biol , vol.64 , pp. 225-240
    • Frazzon, A.P.1    Ramirez, M.V.2    Warek, U.3    Balk, J.4    Frazzon, J.5    Dean, D.R.6
  • 66
    • 1842762970 scopus 로고    scopus 로고
    • The Arabidopsis chloroplastic NifU-like protein CnfU, which can act as an iron-sulfur cluster scaffold protein, is required for biogenesis of ferredoxin and photosystem I
    • Yabe T, Morimoto K, Kikuchi S, Nishio K, Terashima I, Nakai M. The Arabidopsis chloroplastic NifU-like protein CnfU, which can act as an iron-sulfur cluster scaffold protein, is required for biogenesis of ferredoxin and photosystem I. Plant Cell. 2004;16:993-1007.
    • (2004) Plant Cell , vol.16 , pp. 993-1007
    • Yabe, T.1    Morimoto, K.2    Kikuchi, S.3    Nishio, K.4    Terashima, I.5    Nakai, M.6
  • 67
    • 0141737067 scopus 로고    scopus 로고
    • Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p
    • Muhlenhoff U, Gerber J, Richhardt N, Lill R. Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p. EMBO J. 2003;22:4815-25.
    • (2003) EMBO J , vol.22 , pp. 4815-4825
    • Muhlenhoff, U.1    Gerber, J.2    Richhardt, N.3    Lill, R.4
  • 68
    • 2242453224 scopus 로고    scopus 로고
    • Characterization of iron-sulfur protein assembly in isolated mitochondria. A requirement for ATP, NADH, and reduced iron
    • Muhlenhoff U, Richhardt N, Gerber J, Lill R. Characterization of iron-sulfur protein assembly in isolated mitochondria. A requirement for ATP, NADH, and reduced iron. J Biol Chem. 2002;277:29810-6.
    • (2002) J Biol Chem , vol.277 , pp. 29810-29816
    • Muhlenhoff, U.1    Richhardt, N.2    Gerber, J.3    Lill, R.4
  • 69
    • 0141623560 scopus 로고    scopus 로고
    • An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1
    • 4:906-11
    • Gerber J, Muhlenhoff U, Lill R. An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1. EMBO Rep. 2003;4:906-11.
    • EMBO Rep. 2003
    • Gerber, J.1    Muhlenhoff, U.2    Lill, R.3
  • 70
    • 0037613459 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis. Characterization of frataxin as an iron donor for assembly of [2Fe-2S] clusters in ISU-type proteins
    • Yoon T, Cowan JA. Iron-sulfur cluster biosynthesis. Characterization of frataxin as an iron donor for assembly of [2Fe-2S] clusters in ISU-type proteins. J Am Chem Soc. 2003;125:6078-84.
    • (2003) J Am Chem Soc , vol.125 , pp. 6078-6084
    • Yoon, T.1    Cowan, J.A.2
  • 71
    • 0036226063 scopus 로고    scopus 로고
    • Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes
    • Rodriguez-Manzaneque MT, Tamarit J, Belli G, Ros J, Herrero E. Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes. Mol Biol Cell. 2002;13:1109-21.
    • (2002) Mol Biol Cell , vol.13 , pp. 1109-1121
    • Rodriguez-Manzaneque, M.T.1    Tamarit, J.2    Belli, G.3    Ros, J.4    Herrero, E.5
  • 72
    • 0033565665 scopus 로고    scopus 로고
    • The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins
    • Kispal G, Csere P, Prohl C, Lill R. The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins. EMBO J. 1999;18:3981-9.
    • (1999) EMBO J , vol.18 , pp. 3981-3989
    • Kispal, G.1    Csere, P.2    Prohl, C.3    Lill, R.4
  • 73
    • 2442707887 scopus 로고    scopus 로고
    • The yeast scaffold proteins Isu1p and Isu2p are required inside mitochondria for maturation of cytosolic Fe/S proteins
    • Gerber J, Neumann K, Prohl C, Muhlenhoff U, Lill R. The yeast scaffold proteins Isu1p and Isu2p are required inside mitochondria for maturation of cytosolic Fe/S proteins. Mol Cell Biol. 2004;24:4848-57.
    • (2004) Mol Cell Biol , vol.24 , pp. 4848-4857
    • Gerber, J.1    Neumann, K.2    Prohl, C.3    Muhlenhoff, U.4    Lill, R.5
  • 74
    • 0033953353 scopus 로고    scopus 로고
    • A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins
    • Lange H, Kaut A, Kispal G, Lill R. A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins. Proc Natl Acad Sci U S A. 2000;97:1050-5.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 1050-1055
    • Lange, H.1    Kaut, A.2    Kispal, G.3    Lill, R.4
  • 76
    • 0034255836 scopus 로고    scopus 로고
    • Maturation of cellular Fe-S proteins: An essential function of mitochondria
    • Lill R, Kispal G. Maturation of cellular Fe-S proteins: an essential function of mitochondria. Trends Biochem Sci. 2000;25:352-6.
    • (2000) Trends Biochem Sci , vol.25 , pp. 352-356
    • Lill, R.1    Kispal, G.2
  • 77
    • 15444371876 scopus 로고    scopus 로고
    • Activation of the iron regulon by the yeast Aft1/Aft2 transcription factors depends on mitochondrial but not cytosolic iron-sulfur protein biogenesis
    • Rutherford JC, Ojeda L, Balk J, Muhlenhoff U, Lill R, Winge DR. Activation of the iron regulon by the yeast Aft1/Aft2 transcription factors depends on mitochondrial but not cytosolic iron-sulfur protein biogenesis. J Biol Chem. 2005;280:10135-40.
    • (2005) J Biol Chem , vol.280 , pp. 10135-10140
    • Rutherford, J.C.1    Ojeda, L.2    Balk, J.3    Muhlenhoff, U.4    Lill, R.5    Winge, D.R.6
  • 78
    • 0034866458 scopus 로고    scopus 로고
    • An essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic Fe/S proteins
    • 2:715-20
    • Lange H, Lisowsky T, Gerber J, Muhlenhoff U, Kispal G, Lill R. An essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic Fe/S proteins. EMBO Rep. 2001;2:715-20.
    • EMBO Rep. 2001
    • Lange, H.1    Lisowsky, T.2    Gerber, J.3    Muhlenhoff, U.4    Kispal, G.5    Lill, R.6
  • 79
    • 0037178843 scopus 로고    scopus 로고
    • Maturation of cytosolic iron-sulfur proteins requires glutathione
    • Sipos K, Lange H, Fekete Z, Ullmann P, Lill R, Kispal G. Maturation of cytosolic iron-sulfur proteins requires glutathione. J Biol Chem. 2002;277:26944-9.
    • (2002) J Biol Chem , vol.277 , pp. 26944-26949
    • Sipos, K.1    Lange, H.2    Fekete, Z.3    Ullmann, P.4    Lill, R.5    Kispal, G.6
  • 81
    • 14744279245 scopus 로고    scopus 로고
    • The eukaryotic P loop NTPase Nbp35: An essential component of the cytosolic and nuclear iron-sulfur protein assembly machinery
    • Hausmann A, Aguilar Netz DJ, Balk J, Pierik AJ, Muhlenhoff U, Lill R. The eukaryotic P loop NTPase Nbp35: an essential component of the cytosolic and nuclear iron-sulfur protein assembly machinery. Proc Natl Acad Sci U S A. 2005;102:3266-71.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 3266-3271
    • Hausmann, A.1    Aguilar Netz, D.J.2    Balk, J.3    Pierik, A.J.4    Muhlenhoff, U.5    Lill, R.6
  • 82
    • 4544321137 scopus 로고    scopus 로고
    • The cell's cookbook for iron-sulfur clusters: Recipes for fool's gold?
    • Balk J, Lill R. The cell's cookbook for iron-sulfur clusters: recipes for fool's gold? Chembiochem. 2004;5:1044-9.
    • (2004) Chembiochem , vol.5 , pp. 1044-1049
    • Balk, J.1    Lill, R.2
  • 83
    • 2942565619 scopus 로고    scopus 로고
    • The hydrogenase-like Nar1p is essential for maturation of cytosolic and nuclear iron-sulphur proteins
    • Balk J, Pierik AJ, Netz DJ, Muhlenhoff U, Lill R. The hydrogenase-like Nar1p is essential for maturation of cytosolic and nuclear iron-sulphur proteins. EMBO J. 2004;23:2105-15.
    • (2004) EMBO J , vol.23 , pp. 2105-2115
    • Balk, J.1    Pierik, A.J.2    Netz, D.J.3    Muhlenhoff, U.4    Lill, R.5
  • 84
    • 28544450863 scopus 로고    scopus 로고
    • The essential WD40 protein Cia1 is involved in a late step of cytosolic and nuclear iron-sulfur protein assembly
    • Balk J, Aguilar Netz DJ, Tepper K, Pierik AJ, Lill R. The essential WD40 protein Cia1 is involved in a late step of cytosolic and nuclear iron-sulfur protein assembly. Mol Cell Biol. 2005;25:10833-41.
    • (2005) Mol Cell Biol , vol.25 , pp. 10833-10841
    • Balk, J.1    Aguilar Netz, D.J.2    Tepper, K.3    Pierik, A.J.4    Lill, R.5
  • 85
    • 34247247617 scopus 로고    scopus 로고
    • The Cfd1-Nbp35 complex acts as a scaffold for iron-sulfur protein assembly in the yeast cytosol
    • Netz DJ, Pierik AJ, Stumpfig M, Muhlenhoff U, Lill R. The Cfd1-Nbp35 complex acts as a scaffold for iron-sulfur protein assembly in the yeast cytosol. Nat Chem Biol. 2007;3:278-86.
    • (2007) Nat Chem Biol , vol.3 , pp. 278-286
    • Netz, D.J.1    Pierik, A.J.2    Stumpfig, M.3    Muhlenhoff, U.4    Lill, R.5
  • 86
    • 0035823615 scopus 로고    scopus 로고
    • Aft2p, a novel ironregulated transcription activator that modulates, with Aft1p, intracellular iron use and resistance to oxidative stress in yeast
    • Blaiseau PL, Lesuisse E, Camadro JM. Aft2p, a novel ironregulated transcription activator that modulates, with Aft1p, intracellular iron use and resistance to oxidative stress in yeast. J Biol Chem. 2001;276:34221-6.
    • (2001) J Biol Chem , vol.276 , pp. 34221-34226
    • Blaiseau, P.L.1    Lesuisse, E.2    Camadro, J.M.3
  • 87
    • 0028961739 scopus 로고
    • AFT1: A mediator of iron regulated transcriptional control in Saccharomyces cerevisiae
    • Yamaguchi-Iwai Y, Dancis A, Klausner RD. AFT1: a mediator of iron regulated transcriptional control in Saccharomyces cerevisiae. EMBO J. 1995;14:1231-9.
    • (1995) EMBO J , vol.14 , pp. 1231-1239
    • Yamaguchi-Iwai, Y.1    Dancis, A.2    Klausner, R.D.3
  • 89
    • 0037166279 scopus 로고    scopus 로고
    • Subcellular localization of Aft1 transcription factor responds to iron status in Saccharomyces cerevisiae
    • Yamaguchi-Iwai Y, Ueta R, Fukunaka A, Sasaki R. Subcellular localization of Aft1 transcription factor responds to iron status in Saccharomyces cerevisiae. J Biol Chem. 2002;277:18914-8.
    • (2002) J Biol Chem , vol.277 , pp. 18914-18918
    • Yamaguchi-Iwai, Y.1    Ueta, R.2    Fukunaka, A.3    Sasaki, R.4
  • 90
    • 3142667831 scopus 로고    scopus 로고
    • Transcription of the yeast iron regulon does not respond directly to iron but rather to iron-sulfur cluster biosynthesis
    • Chen OS, Crisp RJ, Valachovic M, Bard M, Winge DR, Kaplan J. Transcription of the yeast iron regulon does not respond directly to iron but rather to iron-sulfur cluster biosynthesis. J Biol Chem. 2004;279:29513-8.
    • (2004) J Biol Chem , vol.279 , pp. 29513-29518
    • Chen, O.S.1    Crisp, R.J.2    Valachovic, M.3    Bard, M.4    Winge, D.R.5    Kaplan, J.6
  • 91
    • 33745872884 scopus 로고    scopus 로고
    • Role of glutaredoxin-3 and glutaredoxin-4 in the iron regulation of the Aft1 transcriptional activator in Saccharomyces cerevisiae
    • Ojeda L, Keller G, Muhlenhoff U, Rutherford JC, Lill R, Winge DR. Role of glutaredoxin-3 and glutaredoxin-4 in the iron regulation of the Aft1 transcriptional activator in Saccharomyces cerevisiae. J Biol Chem. 2006;281:17661-9.
    • (2006) J Biol Chem , vol.281 , pp. 17661-17669
    • Ojeda, L.1    Keller, G.2    Muhlenhoff, U.3    Rutherford, J.C.4    Lill, R.5    Winge, D.R.6
  • 92
    • 33751529756 scopus 로고    scopus 로고
    • Glutaredoxins Grx3 and Grx4 regulate nuclear localisation of Aft1 and the oxidative stress response in Saccharomyces cerevisiae
    • Pujol-Carrion N, Belli G, Herrero E, Nogues A, de la Torre-Ruiz MA. Glutaredoxins Grx3 and Grx4 regulate nuclear localisation of Aft1 and the oxidative stress response in Saccharomyces cerevisiae. J Cell Sci. 2006;119:4554-64.
    • (2006) J Cell Sci , vol.119 , pp. 4554-4564
    • Pujol-Carrion, N.1    Belli, G.2    Herrero, E.3    Nogues, A.4    de la Torre-Ruiz, M.A.5
  • 93
    • 44849098197 scopus 로고    scopus 로고
    • Identification of FRA1 and FRA2 as genes involved in regulating the yeast iron regulon in response to decreased mitochondrial iron-sulfur cluster synthesis
    • Kumanovics A, Chen O, Li L, Bagley D, Adkins EM, Lin H, et al. Identification of FRA1 and FRA2 as genes involved in regulating the yeast iron regulon in response to decreased mitochondrial iron-sulfur cluster synthesis. J Biol Chem. 2008;283:10276-86.
    • (2008) J Biol Chem , vol.283 , pp. 10276-10286
    • Kumanovics, A.1    Chen, O.2    Li, L.3    Bagley, D.4    Adkins, E.M.5    Lin, H.6
  • 94
    • 43749114744 scopus 로고    scopus 로고
    • Cellular and mitochondrial remodeling upon defects in iron-sulfur protein biogenesis
    • Hausmann A, Samans B, Lill R, Muhlenhoff U. Cellular and mitochondrial remodeling upon defects in iron-sulfur protein biogenesis. J Biol Chem. 2008;283:8318-30.
    • (2008) J Biol Chem , vol.283 , pp. 8318-8330
    • Hausmann, A.1    Samans, B.2    Lill, R.3    Muhlenhoff, U.4
  • 95
  • 96
    • 2042546096 scopus 로고    scopus 로고
    • Balancing acts: Molecular control of mammalian iron metabolism
    • Hentze MW, Muckenthaler MU, Andrews NC. Balancing acts: molecular control of mammalian iron metabolism. Cell. 2004;117:285-97.
    • (2004) Cell , vol.117 , pp. 285-297
    • Hentze, M.W.1    Muckenthaler, M.U.2    Andrews, N.C.3
  • 97
    • 33746864096 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron homeostasis by iron regulatory proteins
    • Wallander ML, Leibold EA, Eisenstein RS. Molecular control of vertebrate iron homeostasis by iron regulatory proteins. Biochim Biophys Acta. 2006;1763:668-89.
    • (2006) Biochim Biophys Acta , vol.1763 , pp. 668-689
    • Wallander, M.L.1    Leibold, E.A.2    Eisenstein, R.S.3
  • 98
    • 33746361251 scopus 로고    scopus 로고
    • The role of iron regulatory proteins in mammalian iron homeostasis and disease
    • Rouault TA. The role of iron regulatory proteins in mammalian iron homeostasis and disease. Nat Chem Biol. 2006;2:406-14.
    • (2006) Nat Chem Biol , vol.2 , pp. 406-414
    • Rouault, T.A.1
  • 100
    • 39149112760 scopus 로고    scopus 로고
    • The functional duality of iron regulatory protein 1
    • Volz K. The functional duality of iron regulatory protein 1. Curr Opin Struct Biol. 2008;18:106-11.
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 106-111
    • Volz, K.1
  • 101
    • 33644623262 scopus 로고    scopus 로고
    • Functions of mitochondrial ISCU and cytosolic ISCU in mammalian iron-sulfur cluster biogenesis and iron homeostasis
    • Tong WH, Rouault TA. Functions of mitochondrial ISCU and cytosolic ISCU in mammalian iron-sulfur cluster biogenesis and iron homeostasis. Cell Metab. 2006;3:199-210.
    • (2006) Cell Metab , vol.3 , pp. 199-210
    • Tong, W.H.1    Rouault, T.A.2
  • 102
    • 33746509655 scopus 로고    scopus 로고
    • Role of human mitochondrial Nfs1 in cytosolic iron-sulfur protein biogenesis and iron regulation
    • Biederbick A, Stehling O, Rosser R, Niggemeyer B, Nakai Y, Elsässer HP, et al. Role of human mitochondrial Nfs1 in cytosolic iron-sulfur protein biogenesis and iron regulation. Mol Cell Biol. 2006;26:5675-87.
    • (2006) Mol Cell Biol , vol.26 , pp. 5675-5687
    • Biederbick, A.1    Stehling, O.2    Rosser, R.3    Niggemeyer, B.4    Nakai, Y.5    Elsässer, H.P.6
  • 103
    • 9744248303 scopus 로고    scopus 로고
    • Iron-sulfur protein maturation in human cells: Evidence for a function of frataxin
    • Stehling O, Elsasser HP, Bruckel B, Muhlenhoff U, Lill R. Iron-sulfur protein maturation in human cells: evidence for a function of frataxin. Hum Mol Genet. 2004;13:3007-15.
    • (2004) Hum Mol Genet , vol.13 , pp. 3007-3015
    • Stehling, O.1    Elsasser, H.P.2    Bruckel, B.3    Muhlenhoff, U.4    Lill, R.5
  • 104
    • 34147165135 scopus 로고    scopus 로고
    • RNA silencing of the mitochondrial ABCB7 transporter in HeLa cells causes an iron-deficient phenotype with mitochondrial iron overload
    • Cavadini P, Biasiotto G, Poli M, Levi S, Verardi R, Zanella I, et al. RNA silencing of the mitochondrial ABCB7 transporter in HeLa cells causes an iron-deficient phenotype with mitochondrial iron overload. Blood. 2007;109:3552-9.
    • (2007) Blood , vol.109 , pp. 3552-3559
    • Cavadini, P.1    Biasiotto, G.2    Poli, M.3    Levi, S.4    Verardi, R.5    Zanella, I.6
  • 105
    • 44049094146 scopus 로고    scopus 로고
    • A role for IOP1 in mammalian cytosolic iron-sulfur protein biogenesis
    • Song D, Lee FS. A role for IOP1 in mammalian cytosolic iron-sulfur protein biogenesis. J Biol Chem. 2008;283:9231-8.
    • (2008) J Biol Chem , vol.283 , pp. 9231-9238
    • Song, D.1    Lee, F.S.2
  • 106
    • 50249156530 scopus 로고    scopus 로고
    • The human CIA component huNbp35 is essential for both cytosolic iron-sulfur protein assembly and iron homeostasis
    • Jun 23 Epub ahead of print
    • Stehling O, Netz DJA, Niggemeyer B, Rösser R, Eisenstein RS, Puccio H, et al. The human CIA component huNbp35 is essential for both cytosolic iron-sulfur protein assembly and iron homeostasis. Moll Cell Biol. 2008 Jun 23 (Epub ahead of print).
    • (2008) Moll Cell Biol
    • Stehling, O.1    Netz, D.J.A.2    Niggemeyer, B.3    Rösser, R.4    Eisenstein, R.S.5    Puccio, H.6
  • 107
    • 0023942999 scopus 로고
    • Haem inhibits iron uptake subsequent to endocytosis of transferrin in reticulocytes
    • Ponka P, Schulman HM, Martinez-Medellin J. Haem inhibits iron uptake subsequent to endocytosis of transferrin in reticulocytes. Biochem J. 1988;251:105-9.
    • (1988) Biochem J , vol.251 , pp. 105-109
    • Ponka, P.1    Schulman, H.M.2    Martinez-Medellin, J.3
  • 108
    • 0032524657 scopus 로고    scopus 로고
    • Involvement of heme in the degradation of iron-regulatory protein 2
    • Goessling LS, Mascotti DP, Thach RE. Involvement of heme in the degradation of iron-regulatory protein 2. J Biol Chem. 1998;273:12555-7.
    • (1998) J Biol Chem , vol.273 , pp. 12555-12557
    • Goessling, L.S.1    Mascotti, D.P.2    Thach, R.E.3
  • 109
    • 8544244946 scopus 로고    scopus 로고
    • Identification of a heme-sensing domain in iron regulatory protein 2
    • Jeong J, Rouault TA, Levine RL. Identification of a heme-sensing domain in iron regulatory protein 2. J Biol Chem. 2004;279:45450-4.
    • (2004) J Biol Chem , vol.279 , pp. 45450-45454
    • Jeong, J.1    Rouault, T.A.2    Levine, R.L.3
  • 110
    • 4544220638 scopus 로고    scopus 로고
    • Why heme needs to be degraded to iron, biliverdin IXalpha, and carbon monoxide?
    • Sassa S. Why heme needs to be degraded to iron, biliverdin IXalpha, and carbon monoxide? Antioxid Redox Signal. 2004;6:819-24.
    • (2004) Antioxid Redox Signal , vol.6 , pp. 819-824
    • Sassa, S.1
  • 111
    • 23044503950 scopus 로고    scopus 로고
    • Microcytic anemia, erythropoietic protoporphyria, and neurodegeneration in mice with targeted deletion of iron-regulatory protein 2
    • Cooperman SS, Meyron-Holtz EG, Olivierre-Wilson H, Ghosh MC, McConnell JP, Rouault TA. Microcytic anemia, erythropoietic protoporphyria, and neurodegeneration in mice with targeted deletion of iron-regulatory protein 2. Blood. 2005;106:1084-91.
    • (2005) Blood , vol.106 , pp. 1084-1091
    • Cooperman, S.S.1    Meyron-Holtz, E.G.2    Olivierre-Wilson, H.3    Ghosh, M.C.4    McConnell, J.P.5    Rouault, T.A.6
  • 113
    • 0032722872 scopus 로고    scopus 로고
    • Yeast mitochondrial protein, Nfs1p, coordinately regulates iron-sulfur cluster proteins, cellular iron uptake, and iron distribution
    • Li J, Kogan M, Knight SA, Pain D, Dancis A. Yeast mitochondrial protein, Nfs1p, coordinately regulates iron-sulfur cluster proteins, cellular iron uptake, and iron distribution. J Biol Chem. 1999;274:33025-34.
    • (1999) J Biol Chem , vol.274 , pp. 33025-33034
    • Li, J.1    Kogan, M.2    Knight, S.A.3    Pain, D.4    Dancis, A.5
  • 114
    • 0035846961 scopus 로고    scopus 로고
    • Adrenodoxin reductase homolog (Arh1p) of yeast mitochondria required for iron homeostasis
    • Li J, Saxena S, Pain D, Dancis A. Adrenodoxin reductase homolog (Arh1p) of yeast mitochondria required for iron homeostasis. J Biol Chem. 2001;276:1503-9.
    • (2001) J Biol Chem , vol.276 , pp. 1503-1509
    • Li, J.1    Saxena, S.2    Pain, D.3    Dancis, A.4
  • 115
  • 116
    • 0032540929 scopus 로고    scopus 로고
    • Mt-Hsp70 homolog, Ssc2p, required for maturation of yeast frataxin and mitochondrial iron homeostasis
    • Knight SA, Sepuri NB, Pain D, Dancis A. Mt-Hsp70 homolog, Ssc2p, required for maturation of yeast frataxin and mitochondrial iron homeostasis. J Biol Chem. 1998;273:18389-93.
    • (1998) J Biol Chem , vol.273 , pp. 18389-18393
    • Knight, S.A.1    Sepuri, N.B.2    Pain, D.3    Dancis, A.4
  • 117
    • 0035907297 scopus 로고    scopus 로고
    • J-domain protein, Jac1p, of yeast mitochondria required for iron homeostasis and activity of Fe-S cluster proteins
    • Kim R, Saxena S, Gordon DM, Pain D, Dancis A. J-domain protein, Jac1p, of yeast mitochondria required for iron homeostasis and activity of Fe-S cluster proteins. J Biol Chem. 2001;276:17524-32.
    • (2001) J Biol Chem , vol.276 , pp. 17524-17532
    • Kim, R.1    Saxena, S.2    Gordon, D.M.3    Pain, D.4    Dancis, A.5
  • 118
    • 0030608677 scopus 로고    scopus 로고
    • The ABC transporter Atm1p is required for mitochondrial iron homeostasis
    • Kispal G, Csere P, Guiard B, Lill R. The ABC transporter Atm1p is required for mitochondrial iron homeostasis. FEBS Lett. 1997;418:346-50.
    • (1997) FEBS Lett , vol.418 , pp. 346-350
    • Kispal, G.1    Csere, P.2    Guiard, B.3    Lill, R.4
  • 119
    • 0015893042 scopus 로고
    • Study of intracellular iron distribution in rabbit reticulocytes with normal and inhibited heme synthesis
    • Borova J, Ponka P, Neuwirt J. Study of intracellular iron distribution in rabbit reticulocytes with normal and inhibited heme synthesis. Biochim Biophys Acta. 1973;320:143-56.
    • (1973) Biochim Biophys Acta , vol.320 , pp. 143-156
    • Borova, J.1    Ponka, P.2    Neuwirt, J.3
  • 120
    • 0020050144 scopus 로고
    • Iron utilization in rabbit reticulocytes. A study using succinylacetone as an inhibitor or heme synthesis
    • Ponka P, Wilczynska A, Schulman HM. Iron utilization in rabbit reticulocytes. A study using succinylacetone as an inhibitor or heme synthesis. Biochim Biophys Acta. 1982;720:96-105.
    • (1982) Biochim Biophys Acta , vol.720 , pp. 96-105
    • Ponka, P.1    Wilczynska, A.2    Schulman, H.M.3
  • 121
    • 0037372442 scopus 로고    scopus 로고
    • Mitochondrial ferritin expression in erythroid cells from patients with sideroblastic anemia
    • Cazzola M, Invernizzi R, Bergamaschi G, Levi S, Corsi B, Travaglino E, et al. Mitochondrial ferritin expression in erythroid cells from patients with sideroblastic anemia. Blood. 2003;101:1996-2000.
    • (2003) Blood , vol.101 , pp. 1996-2000
    • Cazzola, M.1    Invernizzi, R.2    Bergamaschi, G.3    Levi, S.4    Corsi, B.5    Travaglino, E.6
  • 122
    • 33749334487 scopus 로고    scopus 로고
    • In vivo tumor growth is inhibited by cytosolic iron deprivation caused by the expression of mitochondrial ferritin
    • Nie G, Chen G, Sheftel AD, Pantopoulos K, Ponka P. In vivo tumor growth is inhibited by cytosolic iron deprivation caused by the expression of mitochondrial ferritin. Blood. 2006;108:2428-34.
    • (2006) Blood , vol.108 , pp. 2428-2434
    • Nie, G.1    Chen, G.2    Sheftel, A.D.3    Pantopoulos, K.4    Ponka, P.5
  • 123
    • 0026603687 scopus 로고
    • Enzymatic defect in 'X-linked' sideroblastic anemia: Molecular evidence for erythroid delta-aminolevulinate synthase deficiency
    • Cotter PD, Baumann M, Bishop DF. Enzymatic defect in 'X-linked' sideroblastic anemia: molecular evidence for erythroid delta-aminolevulinate synthase deficiency. Proc Natl Acad Sci U S A. 1992;89:4028-32.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 4028-4032
    • Cotter, P.D.1    Baumann, M.2    Bishop, D.F.3
  • 124
    • 33748754872 scopus 로고    scopus 로고
    • Congenital sideroblastic anemias
    • Bottomley SS. Congenital sideroblastic anemias. Curr Hematol Rep. 2006;5:41-9.
    • (2006) Curr Hematol Rep , vol.5 , pp. 41-49
    • Bottomley, S.S.1
  • 126
    • 25144499698 scopus 로고    scopus 로고
    • Crystal structure of 5-aminolevulinate synthase, the first enzyme of heme biosynthesis, and its link to XLSA in humans
    • Astner I, Schulze JO, van den Heuvel J, Jahn D, Schubert WD, Heinz DW. Crystal structure of 5-aminolevulinate synthase, the first enzyme of heme biosynthesis, and its link to XLSA in humans. EMBO J. 2005;24:3166-77.
    • (2005) EMBO J , vol.24 , pp. 3166-3177
    • Astner, I.1    Schulze, J.O.2    van den Heuvel, J.3    Jahn, D.4    Schubert, W.D.5    Heinz, D.W.6
  • 127
    • 0031735118 scopus 로고    scopus 로고
    • Positional cloning of the zebrafish sauternes gene: A model for congenital sideroblastic anaemia
    • Brownlie A, Donovan A, Pratt SJ, Paw BH, Oates AC, Brugnara C, et al. Positional cloning of the zebrafish sauternes gene: a model for congenital sideroblastic anaemia. Nat Genet. 1998;20:244-50.
    • (1998) Nat Genet , vol.20 , pp. 244-250
    • Brownlie, A.1    Donovan, A.2    Pratt, S.J.3    Paw, B.H.4    Oates, A.C.5    Brugnara, C.6
  • 128
    • 0033571237 scopus 로고    scopus 로고
    • Heme deficiency in erythroid lineage causes differentiation arrest and cytoplasmic iron overload
    • Nakajima O, Takahashi S, Harigae H, Furuyama K, Hayashi N, Sassa S, et al. Heme deficiency in erythroid lineage causes differentiation arrest and cytoplasmic iron overload. EMBO J. 1999;18:6282-9.
    • (1999) EMBO J , vol.18 , pp. 6282-6289
    • Nakajima, O.1    Takahashi, S.2    Harigae, H.3    Furuyama, K.4    Hayashi, N.5    Sassa, S.6
  • 129
    • 33646754660 scopus 로고    scopus 로고
    • Transgenic rescue of erythroid 5-aminolevulinate synthase-deficient mice results in the formation of ring sideroblasts and siderocytes
    • Nakajima O, Okano S, Harada H, Kusaka T, Gao X, Hosoya T, et al. Transgenic rescue of erythroid 5-aminolevulinate synthase-deficient mice results in the formation of ring sideroblasts and siderocytes. Genes Cells. 2006;11:685-700.
    • (2006) Genes Cells , vol.11 , pp. 685-700
    • Nakajima, O.1    Okano, S.2    Harada, H.3    Kusaka, T.4    Gao, X.5    Hosoya, T.6
  • 130
    • 11144303634 scopus 로고    scopus 로고
    • Sideroblastic anemias
    • Greer JP, Joerster J, Lukens JN, Rodgers GM, Paraskevas F, Glader B, editors, 11th ed. Philadelphia: Lippincott Williams & Wilkins
    • Bottomley SS. Sideroblastic anemias. In: Greer JP, Joerster J, Lukens JN, Rodgers GM, Paraskevas F, Glader B, editors. Clinical hematology, 11th ed. Philadelphia: Lippincott Williams & Wilkins, 2004. p. 1101-33.
    • (2004) Clinical hematology , pp. 1101-1133
    • Bottomley, S.S.1
  • 131
    • 0032920837 scopus 로고    scopus 로고
    • Mutation of a putative mitochondrial iron transporter gene (ABC7) in X-linked sideroblastic anemia and ataxia (XLSA/A)
    • Allikmets R, Raskind WH, Hutchinson A, Schueck ND, Dean M, Koeller DM. Mutation of a putative mitochondrial iron transporter gene (ABC7) in X-linked sideroblastic anemia and ataxia (XLSA/A). Hum Mol Genet. 1999;8:743-9.
    • (1999) Hum Mol Genet , vol.8 , pp. 743-749
    • Allikmets, R.1    Raskind, W.H.2    Hutchinson, A.3    Schueck, N.D.4    Dean, M.5    Koeller, D.M.6
  • 132
    • 0034329310 scopus 로고    scopus 로고
    • Human ABC7 transporter: Gene structure and mutation causing X-linked sideroblastic anemia with ataxia with disruption of cytosolic iron-sulfur protein maturation
    • Bekri S, Kispal G, Lange H, Fitzsimons E, Tolmie J, Lill R, et al. Human ABC7 transporter: gene structure and mutation causing X-linked sideroblastic anemia with ataxia with disruption of cytosolic iron-sulfur protein maturation. Blood. 2000;96:3256-64.
    • (2000) Blood , vol.96 , pp. 3256-3264
    • Bekri, S.1    Kispal, G.2    Lange, H.3    Fitzsimons, E.4    Tolmie, J.5    Lill, R.6
  • 133
    • 3142722152 scopus 로고    scopus 로고
    • The heme synthesis defect of mutants impaired in mitochondrial iron-sulfur protein biogenesis is caused by reversible inhibition of ferrochelatase
    • Lange H, Muhlenhoff U, Denzel M, Kispal G, Lill R. The heme synthesis defect of mutants impaired in mitochondrial iron-sulfur protein biogenesis is caused by reversible inhibition of ferrochelatase. J Biol Chem. 2004;279:29101-8.
    • (2004) J Biol Chem , vol.279 , pp. 29101-29108
    • Lange, H.1    Muhlenhoff, U.2    Denzel, M.3    Kispal, G.4    Lill, R.5
  • 134
    • 0013813021 scopus 로고
    • Observations on free erythrocyte protoporphyrin in sideroachrestic anemia
    • Bottomley SS. Observations on free erythrocyte protoporphyrin in sideroachrestic anemia. Clinica Chimica Acta. 1965;12:542-5.
    • (1965) Clinica Chimica Acta , vol.12 , pp. 542-545
    • Bottomley, S.S.1
  • 135
    • 0015059672 scopus 로고
    • Idiopathic refractory sideroblastic anemia: Clinical and laboratory investigation of 17 patients and review of the literature
    • Kushner JP, Lee GR, Wintrobe MM, Cartwright GE. Idiopathic refractory sideroblastic anemia: clinical and laboratory investigation of 17 patients and review of the literature. Medicine (Baltimore). 1971;50:139-59.
    • (1971) Medicine (Baltimore) , vol.50 , pp. 139-159
    • Kushner, J.P.1    Lee, G.R.2    Wintrobe, M.M.3    Cartwright, G.E.4
  • 136
    • 44849143798 scopus 로고    scopus 로고
    • Boultwood J, Pellagatti A, Nikpour M, Pushkaran B, Fidler C, Cattan H, et al. The role of the iron transporter ABCB7 in refractory anemia with ring sideroblasts. PLoS ONE. 2008;3:e1970.
    • Boultwood J, Pellagatti A, Nikpour M, Pushkaran B, Fidler C, Cattan H, et al. The role of the iron transporter ABCB7 in refractory anemia with ring sideroblasts. PLoS ONE. 2008;3:e1970.
  • 137
    • 0037025331 scopus 로고    scopus 로고
    • Deletion of the mitochondrial carrier genes MRS3 and MRS4 suppresses mitochondrial iron accumulation in a yeast frataxin-deficient strain
    • Foury F, Roganti T. Deletion of the mitochondrial carrier genes MRS3 and MRS4 suppresses mitochondrial iron accumulation in a yeast frataxin-deficient strain. J Biol Chem. 2002;277:24475-83.
    • (2002) J Biol Chem , vol.277 , pp. 24475-24483
    • Foury, F.1    Roganti, T.2
  • 138
    • 0030662261 scopus 로고    scopus 로고
    • Characterization of two homologous yeast genes that encode mitochondrial iron transporters
    • Li L, Kaplan J. Characterization of two homologous yeast genes that encode mitochondrial iron transporters. J Biol Chem. 1997;272:28485-93.
    • (1997) J Biol Chem , vol.272 , pp. 28485-28493
    • Li, L.1    Kaplan, J.2
  • 139
    • 21244448393 scopus 로고    scopus 로고
    • Frataxin and mitochondrial carrier proteins, Mrs3p and Mrs4p, cooperate in providing iron for heme synthesis
    • Zhang Y, Lyver ER, Knight SA, Lesuisse E, Dancis A. Frataxin and mitochondrial carrier proteins, Mrs3p and Mrs4p, cooperate in providing iron for heme synthesis. J Biol Chem. 2005;280:19794-807.
    • (2005) J Biol Chem , vol.280 , pp. 19794-19807
    • Zhang, Y.1    Lyver, E.R.2    Knight, S.A.3    Lesuisse, E.4    Dancis, A.5
  • 140
    • 61349097350 scopus 로고    scopus 로고
    • Abnormal expression of human mitoferrin (SLC25A37) is associated with a variant of erythropoietic protoporphyria
    • Shaw GC, Longer NB, Wang YM, et al. Abnormal expression of human mitoferrin (SLC25A37) is associated with a variant of erythropoietic protoporphyria. Blood. 2006;108:6A.
    • (2006) Blood , vol.108
    • Shaw, G.C.1    Longer, N.B.2    Wang, Y.M.3
  • 141
    • 13344270899 scopus 로고    scopus 로고
    • Friedreich's ataxia: Autosomal recessive disease caused by an intronic GAA triplet repeat expansion
    • Campuzano V, Montermini L, Molto MD, Pianese L, Cossée M, Cavalcanti F, et al. Friedreich's ataxia: autosomal recessive disease caused by an intronic GAA triplet repeat expansion. Science. 1996;271:1423-7.
    • (1996) Science , vol.271 , pp. 1423-1427
    • Campuzano, V.1    Montermini, L.2    Molto, M.D.3    Pianese, L.4    Cossée, M.5    Cavalcanti, F.6
  • 142
    • 0031253821 scopus 로고    scopus 로고
    • Aconitase and mitochondrial iron-sulphur protein deficiency in Friedreich ataxia
    • Rotig A, de Lonlay P, Chretien D, Foury F, Koenig M, Sidi D, et al. Aconitase and mitochondrial iron-sulphur protein deficiency in Friedreich ataxia. Nat Genet. 1997;17:215-7.
    • (1997) Nat Genet , vol.17 , pp. 215-217
    • Rotig, A.1    de Lonlay, P.2    Chretien, D.3    Foury, F.4    Koenig, M.5    Sidi, D.6
  • 143
    • 0035138072 scopus 로고    scopus 로고
    • Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits
    • Puccio H, Simon D, Cossee M, Criqui-Filipe P, Tiziano F, Melki J, et al. Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits. Nat Genet. 2001;27:181-6.
    • (2001) Nat Genet , vol.27 , pp. 181-186
    • Puccio, H.1    Simon, D.2    Cossee, M.3    Criqui-Filipe, P.4    Tiziano, F.5    Melki, J.6
  • 144
    • 0017031971 scopus 로고
    • Pathology of the heart in Friedreich's ataxia: Review of the literature and report of one case
    • Sanchez-Casis G, Cote M, Barbeau A. Pathology of the heart in Friedreich's ataxia: review of the literature and report of one case. Can J Neurol Sci. 1976;3:349-54.
    • (1976) Can J Neurol Sci , vol.3 , pp. 349-354
    • Sanchez-Casis, G.1    Cote, M.2    Barbeau, A.3
  • 145
    • 34447316711 scopus 로고    scopus 로고
    • Mitochondrial frataxin interacts with ISD11 of the NFS1/ISCU complex and multiple mitochondrial chaperones
    • Shan Y, Napoli E, Cortopassi G. Mitochondrial frataxin interacts with ISD11 of the NFS1/ISCU complex and multiple mitochondrial chaperones. Hum Mol Genet. 2007;16:929-41.
    • (2007) Hum Mol Genet , vol.16 , pp. 929-941
    • Shan, Y.1    Napoli, E.2    Cortopassi, G.3
  • 146
    • 2942744572 scopus 로고    scopus 로고
    • Frataxin-mediated iron delivery to ferrochelatase in the final step of heme biosynthesis
    • Yoon T, Cowan JA. Frataxin-mediated iron delivery to ferrochelatase in the final step of heme biosynthesis. J Biol Chem. 2004;279:25943-6.
    • (2004) J Biol Chem , vol.279 , pp. 25943-25946
    • Yoon, T.1    Cowan, J.A.2
  • 147
    • 0037093206 scopus 로고    scopus 로고
    • Erythroid differentiation and protoporphyrin IX down-regulate frataxin expression in Friend cells: Characterization of frataxin expression compared to molecules involved in iron metabolism and hemoglobinization
    • Becker EM, Greer JM, Ponka P, Richardson DR. Erythroid differentiation and protoporphyrin IX down-regulate frataxin expression in Friend cells: characterization of frataxin expression compared to molecules involved in iron metabolism and hemoglobinization. Blood. 2002;99:3813-22.
    • (2002) Blood , vol.99 , pp. 3813-3822
    • Becker, E.M.1    Greer, J.M.2    Ponka, P.3    Richardson, D.R.4
  • 148
    • 0036472291 scopus 로고    scopus 로고
    • Assembly and iron-binding properties of human frataxin, the protein deficient in Friedreich ataxia
    • Cavadini P, O'Neill HA, Benada O, Isaya G. Assembly and iron-binding properties of human frataxin, the protein deficient in Friedreich ataxia. Hum Mol Genet. 2002;11:217-27.
    • (2002) Hum Mol Genet , vol.11 , pp. 217-227
    • Cavadini, P.1    O'Neill, H.A.2    Benada, O.3    Isaya, G.4
  • 149
    • 9644279682 scopus 로고    scopus 로고
    • Iron-induced oligomerization of yeast frataxin homologue Yfh1 is dispensable in vivo
    • 5:1096-101
    • Aloria K, Schilke B, Andrew A, Craig EA. Iron-induced oligomerization of yeast frataxin homologue Yfh1 is dispensable in vivo. EMBO Rep. 2004;5:1096-101.
    • EMBO Rep. 2004
    • Aloria, K.1    Schilke, B.2    Andrew, A.3    Craig, E.A.4
  • 150
    • 5444262935 scopus 로고    scopus 로고
    • The expression of human mitochondrial ferritin rescues respiratory function in frataxin-deficient yeast
    • Campanella A, Isaya G, O'Neill HA, Santambrogio P, Cozzi A, Arosio P, et al. The expression of human mitochondrial ferritin rescues respiratory function in frataxin-deficient yeast. Hum Mol Genet. 2004;13:2279-88.
    • (2004) Hum Mol Genet , vol.13 , pp. 2279-2288
    • Campanella, A.1    Isaya, G.2    O'Neill, H.A.3    Santambrogio, P.4    Cozzi, A.5    Arosio, P.6
  • 151
    • 39149096860 scopus 로고    scopus 로고
    • The effects of frataxin silencing in HeLa cells are rescued by the expression of human mitochondrial ferritin
    • Zanella I, Derosas M, Corrado M, Cocco E, Cavadini P, Biasiotto G, et al. The effects of frataxin silencing in HeLa cells are rescued by the expression of human mitochondrial ferritin. Biochim Biophys Acta. 2008;1782:90-8.
    • (2008) Biochim Biophys Acta , vol.1782 , pp. 90-98
    • Zanella, I.1    Derosas, M.2    Corrado, M.3    Cocco, E.4    Cavadini, P.5    Biasiotto, G.6
  • 152
    • 44349149346 scopus 로고    scopus 로고
    • Myopathy with lactic acidosis is linked to chromosome 12q23.3-24.11 and caused by an intron mutation in the ISCU gene resulting in a splicing defect
    • Olsson A, Lind L, Thornell LE, Holmberg M. Myopathy with lactic acidosis is linked to chromosome 12q23.3-24.11 and caused by an intron mutation in the ISCU gene resulting in a splicing defect. Hum Mol Genet. 2008;17:1666-72.
    • (2008) Hum Mol Genet , vol.17 , pp. 1666-1672
    • Olsson, A.1    Lind, L.2    Thornell, L.E.3    Holmberg, M.4
  • 153
    • 41149169596 scopus 로고    scopus 로고
    • Splice mutation in the iron-sulfur cluster scaffold protein ISCU causes myopathy with exercise intolerance
    • Mochel F, Knight MA, Tong WH, Hernandez D, Ayyad K, Taivassalo T, et al. Splice mutation in the iron-sulfur cluster scaffold protein ISCU causes myopathy with exercise intolerance. Am J Hum Genet. 2008;82:652-60.
    • (2008) Am J Hum Genet , vol.82 , pp. 652-660
    • Mochel, F.1    Knight, M.A.2    Tong, W.H.3    Hernandez, D.4    Ayyad, K.5    Taivassalo, T.6
  • 154
    • 23944500052 scopus 로고    scopus 로고
    • Deficiency of glutaredoxin 5 reveals Fe-S clusters are required for vertebrate haem synthesis
    • Wingert RA, Galloway JL, Barut B, Foott H, Fraenkel P, Axe JL, et al. Deficiency of glutaredoxin 5 reveals Fe-S clusters are required for vertebrate haem synthesis. Nature. 2005;436:1035-9.
    • (2005) Nature , vol.436 , pp. 1035-1039
    • Wingert, R.A.1    Galloway, J.L.2    Barut, B.3    Foott, H.4    Fraenkel, P.5    Axe, J.L.6
  • 155
    • 34548013116 scopus 로고    scopus 로고
    • The human counterpart of zebrafish shiraz shows sideroblastic-like microcytic anemia and iron overload
    • Camaschella C, Campanella A, De Falco L, Boschetto L, Merlini R, Silvestri L, et al. The human counterpart of zebrafish shiraz shows sideroblastic-like microcytic anemia and iron overload. Blood. 2007;110:1353-8.
    • (2007) Blood , vol.110 , pp. 1353-1358
    • Camaschella, C.1    Campanella, A.2    De Falco, L.3    Boschetto, L.4    Merlini, R.5    Silvestri, L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.