메뉴 건너뛰기




Volumn 1790, Issue 7, 2009, Pages 629-636

The role of iron in mitochondrial function

Author keywords

Heme; Iron; Iron sulfur cluster; Mitochondria; Mitochondria iron overload diseases

Indexed keywords

ACONITATE HYDRATASE; FERROCHELATASE; FRATAXIN; HEME; IRON; IRON REGULATORY PROTEIN 1; IRON SULFUR PROTEIN; MITOCHONDRIAL PROTEIN; PROTOPORPHYRIN; REACTIVE OXYGEN METABOLITE; SUCCINATE DEHYDROGENASE;

EID: 67349165712     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2008.09.008     Document Type: Review
Times cited : (163)

References (128)
  • 1
    • 34248199153 scopus 로고    scopus 로고
    • Healthy aging: regulation of the metabolome by cellular redox modulation and prooxidant signaling systems: the essential roles of superoxide anion and hydrogen peroxide
    • Linnane A.W., Kios M., and Vitetta L. Healthy aging: regulation of the metabolome by cellular redox modulation and prooxidant signaling systems: the essential roles of superoxide anion and hydrogen peroxide. Biogerontology 8 (2007) 445-467
    • (2007) Biogerontology , vol.8 , pp. 445-467
    • Linnane, A.W.1    Kios, M.2    Vitetta, L.3
  • 3
    • 3042613609 scopus 로고    scopus 로고
    • Heme, iron, and the mitochondrial decay of ageing
    • Atamna H. Heme, iron, and the mitochondrial decay of ageing. Ageing Res. Rev. 3 (2004) 303-318
    • (2004) Ageing Res. Rev. , vol.3 , pp. 303-318
    • Atamna, H.1
  • 4
    • 47249094614 scopus 로고    scopus 로고
    • Maturation of iron-sulfur proteins in Eukaryotes: mechanisms, connected processes, and diseases
    • Lill R., and Muhlenhoff U. Maturation of iron-sulfur proteins in Eukaryotes: mechanisms, connected processes, and diseases. Annu. Rev. Biochem. 77 (2008) 669-700
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 669-700
    • Lill, R.1    Muhlenhoff, U.2
  • 5
    • 0028283948 scopus 로고
    • Molecular and cellular physiology of intracellular calcium stores
    • Pozzan T., Rizzuto R., Volpe P., and Meldolesi J. Molecular and cellular physiology of intracellular calcium stores. Physiol. Rev. 74 (1994) 595-636
    • (1994) Physiol. Rev. , vol.74 , pp. 595-636
    • Pozzan, T.1    Rizzuto, R.2    Volpe, P.3    Meldolesi, J.4
  • 6
    • 34248640533 scopus 로고    scopus 로고
    • Metal Ion availability in mitochondria
    • Pierrel F., Cobine P.A., and Winge D.R. Metal Ion availability in mitochondria. Biometals 20 (2007) 675-682
    • (2007) Biometals , vol.20 , pp. 675-682
    • Pierrel, F.1    Cobine, P.A.2    Winge, D.R.3
  • 7
    • 33751177803 scopus 로고    scopus 로고
    • Iron-sulfur protein biogenesis in eukaryotes: components and mechanisms
    • Lill R., and Muhlenhoff U. Iron-sulfur protein biogenesis in eukaryotes: components and mechanisms. Annu. Rev. Cell Dev. Biol. 22 (2006) 457-486
    • (2006) Annu. Rev. Cell Dev. Biol. , vol.22 , pp. 457-486
    • Lill, R.1    Muhlenhoff, U.2
  • 8
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: nature's modular, multipurpose structures
    • Beinert H., Holm R.H., and Munck E. Iron-sulfur clusters: nature's modular, multipurpose structures. Science 277 (1997) 653-659
    • (1997) Science , vol.277 , pp. 653-659
    • Beinert, H.1    Holm, R.H.2    Munck, E.3
  • 10
    • 0034003112 scopus 로고    scopus 로고
    • Iron-sulfur proteins: ancient structures, still full of surprises
    • Beinert H. Iron-sulfur proteins: ancient structures, still full of surprises. J. Biol. Inorg. Chem. 5 (2000) 2-15
    • (2000) J. Biol. Inorg. Chem. , vol.5 , pp. 2-15
    • Beinert, H.1
  • 11
    • 14944387002 scopus 로고    scopus 로고
    • Iron trafficking in the mitochondrion: novel pathways revealed by disease
    • Napier I., Ponka P., and Richardson D.R. Iron trafficking in the mitochondrion: novel pathways revealed by disease. Blood 105 (2005) 1867-1874
    • (2005) Blood , vol.105 , pp. 1867-1874
    • Napier, I.1    Ponka, P.2    Richardson, D.R.3
  • 12
    • 17144378216 scopus 로고    scopus 로고
    • Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis
    • Rouault T.A., and Tong W.H. Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis. Nat. Rev. Mol. Cell Biol. 6 (2005) 345-351
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 345-351
    • Rouault, T.A.1    Tong, W.H.2
  • 13
    • 0033516467 scopus 로고    scopus 로고
    • Mechanism of iron transport to the site of heme synthesis inside yeast mitochondria
    • Lange H., Kispal G., and Lill R. Mechanism of iron transport to the site of heme synthesis inside yeast mitochondria. J. Biol. Chem. 274 (1999) 18989-18996
    • (1999) J. Biol. Chem. , vol.274 , pp. 18989-18996
    • Lange, H.1    Kispal, G.2    Lill, R.3
  • 14
    • 35048833703 scopus 로고    scopus 로고
    • Non-transferrin-bound iron reaches mitochondria by a chelator-inaccessible mechanism: biological and clinical implications
    • Shvartsman M., Kikkeri R., Shanzer A., and Cabantchik Z.I. Non-transferrin-bound iron reaches mitochondria by a chelator-inaccessible mechanism: biological and clinical implications. Am. J. Physiol. Cell Physiol. 293 (2007) C1383-C1394
    • (2007) Am. J. Physiol. Cell Physiol. , vol.293
    • Shvartsman, M.1    Kikkeri, R.2    Shanzer, A.3    Cabantchik, Z.I.4
  • 15
    • 34347375300 scopus 로고    scopus 로고
    • Direct interorganellar transfer of iron from endosome to mitochondrion
    • Sheftel A.D., Zhang A.S., Brown C., Shirihai O.S., and Ponka P. Direct interorganellar transfer of iron from endosome to mitochondrion. Blood 110 (2007) 125-132
    • (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
    • 0029856099 scopus 로고    scopus 로고
    • Intermediate steps in cellular iron uptake from transferrin. II. A cytoplasmic pool of iron is released from cultured cells via temperature-dependent mechanical wounding
    • Richardson D.R., Dickson L., and Baker E. Intermediate steps in cellular iron uptake from transferrin. II. A cytoplasmic pool of iron is released from cultured cells via temperature-dependent mechanical wounding. In Vitro Cell Dev. Biol. Anim. 32 (1996) 486-495
    • (1996) In Vitro Cell Dev. Biol. Anim. , vol.32 , pp. 486-495
    • Richardson, D.R.1    Dickson, L.2    Baker, E.3
  • 17
    • 0029865751 scopus 로고    scopus 로고
    • Distribution of iron in reticulocytes after inhibition of heme synthesis with succinylacetone: examination of the intermediates involved in iron metabolism
    • Richardson D.R., Ponka P., and Vyoral D. Distribution of iron in reticulocytes after inhibition of heme synthesis with succinylacetone: examination of the intermediates involved in iron metabolism. Blood 87 (1996) 3477-3488
    • (1996) Blood , vol.87 , pp. 3477-3488
    • Richardson, D.R.1    Ponka, P.2    Vyoral, D.3
  • 18
    • 11144226961 scopus 로고    scopus 로고
    • Intracellular kinetics of iron in reticulocytes: evidence for endosome involvement in iron targeting to mitochondria
    • Zhang A.S., Sheftel A.D., and Ponka P. Intracellular kinetics of iron in reticulocytes: evidence for endosome involvement in iron targeting to mitochondria. Blood 105 (2005) 368-375
    • (2005) Blood , vol.105 , pp. 368-375
    • Zhang, A.S.1    Sheftel, A.D.2    Ponka, P.3
  • 19
    • 0031967829 scopus 로고    scopus 로고
    • ATP transport through a single mitochondrial channel, VDAC, studied by current fluctuation analysis
    • Rostovtseva T.K., and Bezrukov S.M. ATP transport through a single mitochondrial channel, VDAC, studied by current fluctuation analysis. Biophys. J. 74 (1998) 2365-2373
    • (1998) Biophys. J. , vol.74 , pp. 2365-2373
    • Rostovtseva, T.K.1    Bezrukov, S.M.2
  • 20
    • 0020485742 scopus 로고
    • Pore protein and the hexokinase-binding protein from the outer membrane of rat liver mitochondria are identical
    • Linden M., Gellerfors P., and Nelson B.D. Pore protein and the hexokinase-binding protein from the outer membrane of rat liver mitochondria are identical. FEBS Lett. 141 (1982) 189-192
    • (1982) FEBS Lett. , vol.141 , pp. 189-192
    • Linden, M.1    Gellerfors, P.2    Nelson, B.D.3
  • 22
    • 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., and Roganti T. Deletion of the mitochondrial carrier genes MRS3 and MRS4 suppresses mitochondrial iron accumulation in a yeast frataxin-deficient strain. J. Biol. Chem. 277 (2002) 24475-24483
    • (2002) J. Biol. Chem. , vol.277 , pp. 24475-24483
    • Foury, F.1    Roganti, T.2
  • 25
    • 21244448393 scopus 로고    scopus 로고
    • Frataxin and mitochondrial carrier proteins, Mrs3p and Mrs4p, cooperate in providing iron for heme synthesis
    • Zhang Y., Lyver E.R., Knight S.A., Lesuisse E., and Dancis A. Frataxin and mitochondrial carrier proteins, Mrs3p and Mrs4p, cooperate in providing iron for heme synthesis. J. Biol. Chem. 280 (2005) 19794-19807
    • (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
  • 27
    • 1242317666 scopus 로고    scopus 로고
    • The mitochondrial transporter family (SLC25): physiological and pathological implications
    • Palmieri F. The mitochondrial transporter family (SLC25): physiological and pathological implications. Pflugers Arch. 447 (2004) 689-709
    • (2004) Pflugers Arch. , vol.447 , pp. 689-709
    • Palmieri, F.1
  • 28
    • 34547845251 scopus 로고    scopus 로고
    • Mitochondrial carrier family: repertoire and peculiarities of the cellular slime mould Dictyostelium discoideum
    • Satre M., Mattei S., Aubry L., Gaudet P., Pelosi L., Brandolin G., and Klein G. Mitochondrial carrier family: repertoire and peculiarities of the cellular slime mould Dictyostelium discoideum. Biochimie 89 (2007) 1058-1069
    • (2007) Biochimie , vol.89 , pp. 1058-1069
    • Satre, M.1    Mattei, S.2    Aubry, L.3    Gaudet, P.4    Pelosi, L.5    Brandolin, G.6    Klein, G.7
  • 29
    • 0036134621 scopus 로고    scopus 로고
    • Characterization of a putative murine mitochondrial transporter homology of hMRS3/4
    • Li F.Y., Leibiger B., Leibiger I., and Larsson C. Characterization of a putative murine mitochondrial transporter homology of hMRS3/4. Mamm. Genome 13 (2002) 20-23
    • (2002) Mamm. Genome , vol.13 , pp. 20-23
    • Li, F.Y.1    Leibiger, B.2    Leibiger, I.3    Larsson, C.4
  • 30
    • 0035815443 scopus 로고    scopus 로고
    • Characterization of a novel human putative mitochondrial transporter homologous to the yeast mitochondrial RNA splicing proteins 3 and 4
    • Li F.Y., Nikali K., Gregan J., Leibiger I., Leibiger B., Schweyen R., Larsson C., and Suomalainen A. Characterization of a novel human putative mitochondrial transporter homologous to the yeast mitochondrial RNA splicing proteins 3 and 4. FEBS Lett. 494 (2001) 79-84
    • (2001) FEBS Lett. , vol.494 , pp. 79-84
    • Li, F.Y.1    Nikali, K.2    Gregan, J.3    Leibiger, I.4    Leibiger, B.5    Schweyen, R.6    Larsson, C.7    Suomalainen, A.8
  • 31
    • 34547602992 scopus 로고    scopus 로고
    • Assessment of chelatable mitochondrial iron by using mitochondrion-selective fluorescent iron indicators with different iron-binding affinities
    • Rauen U., Springer A., Weisheit D., Petrat F., Korth H.G., de Groot H., and Sustmann R. Assessment of chelatable mitochondrial iron by using mitochondrion-selective fluorescent iron indicators with different iron-binding affinities. Chembiochem 8 (2007) 341-352
    • (2007) Chembiochem , vol.8 , pp. 341-352
    • Rauen, U.1    Springer, A.2    Weisheit, D.3    Petrat, F.4    Korth, H.G.5    de Groot, H.6    Sustmann, R.7
  • 32
    • 0037083893 scopus 로고    scopus 로고
    • Selective determination of mitochondrial chelatable iron in viable cells with a new fluorescent sensor
    • Petrat F., Weisheit D., Lensen M., de Groot H., Sustmann R., and Rauen U. Selective determination of mitochondrial chelatable iron in viable cells with a new fluorescent sensor. Biochem. J. 362 (2002) 137-147
    • (2002) Biochem. J. , vol.362 , pp. 137-147
    • Petrat, F.1    Weisheit, D.2    Lensen, M.3    de Groot, H.4    Sustmann, R.5    Rauen, U.6
  • 34
    • 0037064027 scopus 로고    scopus 로고
    • The ferroxidase activity of yeast frataxin
    • Park S., Gakh O., Mooney S.M., and Isaya G. The ferroxidase activity of yeast frataxin. J. Biol. Chem. 277 (2002) 38589-38595
    • (2002) J. Biol. Chem. , vol.277 , pp. 38589-38595
    • Park, S.1    Gakh, O.2    Mooney, S.M.3    Isaya, G.4
  • 35
    • 0042232045 scopus 로고    scopus 로고
    • Yeast frataxin sequentially chaperones and stores iron by coupling protein assembly with iron oxidation
    • Park S., Gakh O., O'Neill H.A., Mangravita A., Nichol H., Ferreira G.C., and Isaya G. Yeast frataxin sequentially chaperones and stores iron by coupling protein assembly with iron oxidation. J. Biol. Chem. 278 (2003) 31340-31351
    • (2003) J. Biol. Chem. , vol.278 , pp. 31340-31351
    • Park, S.1    Gakh, O.2    O'Neill, H.A.3    Mangravita, A.4    Nichol, H.5    Ferreira, G.C.6    Isaya, G.7
  • 37
    • 31544445770 scopus 로고    scopus 로고
    • Mitochondrial iron detoxification is a primary function of frataxin that limits oxidative damage and preserves cell longevity
    • Gakh O., Park S., Liu G., Macomber L., Imlay J.A., Ferreira G.C., and Isaya G. Mitochondrial iron detoxification is a primary function of frataxin that limits oxidative damage and preserves cell longevity. Hum. Mol. Genet. 15 (2006) 467-479
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 467-479
    • Gakh, O.1    Park, S.2    Liu, G.3    Macomber, L.4    Imlay, J.A.5    Ferreira, G.C.6    Isaya, G.7
  • 39
    • 3042763187 scopus 로고    scopus 로고
    • Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity
    • Bulteau A.L., O'Neill H.A., Kennedy M.C., Ikeda-Saito M., Isaya G., and Szweda L.I. Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity. Science 305 (2004) 242-245
    • (2004) Science , vol.305 , pp. 242-245
    • Bulteau, A.L.1    O'Neill, H.A.2    Kennedy, M.C.3    Ikeda-Saito, M.4    Isaya, G.5    Szweda, L.I.6
  • 41
    • 0141623560 scopus 로고    scopus 로고
    • An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1
    • Gerber J., Muhlenhoff U., and Lill R. An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1. EMBO Rep. 4 (2003) 906-911
    • (2003) EMBO Rep. , vol.4 , pp. 906-911
    • Gerber, J.1    Muhlenhoff, U.2    Lill, R.3
  • 42
    • 0037101845 scopus 로고    scopus 로고
    • The yeast frataxin homolog Yfh1p plays a specific role in the maturation of cellular Fe/S proteins
    • Muhlenhoff U., Richhardt N., Ristow M., Kispal G., and Lill R. The yeast frataxin homolog Yfh1p plays a specific role in the maturation of cellular Fe/S proteins. Hum. Mol. Genet. 11 (2002) 2025-2036
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2025-2036
    • Muhlenhoff, U.1    Richhardt, N.2    Ristow, M.3    Kispal, G.4    Lill, R.5
  • 43
    • 0037126057 scopus 로고    scopus 로고
    • Inhibition of Fe-S cluster biosynthesis decreases mitochondrial iron export: evidence that Yfh1p affects Fe-S cluster synthesis
    • Chen O.S., Hemenway S., and Kaplan J. Inhibition of Fe-S cluster biosynthesis decreases mitochondrial iron export: evidence that Yfh1p affects Fe-S cluster synthesis. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 12321-12326
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 12321-12326
    • Chen, O.S.1    Hemenway, S.2    Kaplan, J.3
  • 44
    • 33644872938 scopus 로고    scopus 로고
    • Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus
    • Sazanov L.A., and Hinchliffe P. Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus. Science 311 (2006) 1430-1436
    • (2006) Science , vol.311 , pp. 1430-1436
    • Sazanov, L.A.1    Hinchliffe, P.2
  • 46
    • 33747330134 scopus 로고    scopus 로고
    • Mrs3p, Mrs4p, and frataxin provide iron for Fe-S cluster synthesis in mitochondria
    • Zhang Y., Lyver E.R., Knight S.A., Pain D., Lesuisse E., and Dancis A. Mrs3p, Mrs4p, and frataxin provide iron for Fe-S cluster synthesis in mitochondria. J. Biol. Chem. 281 (2006) 22493-22502
    • (2006) J. Biol. Chem. , vol.281 , pp. 22493-22502
    • Zhang, Y.1    Lyver, E.R.2    Knight, S.A.3    Pain, D.4    Lesuisse, E.5    Dancis, A.6
  • 50
    • 5444262935 scopus 로고    scopus 로고
    • The expression of human mitochondrial ferritin rescues respiratory function in frataxin-deficient yeast
    • Campanella A., Isaya G., O'Neill H.A., Santambrogio P., Cozzi A., Arosio P., and Levi S. The expression of human mitochondrial ferritin rescues respiratory function in frataxin-deficient yeast. Hum. Mol. Genet. 13 (2004) 2279-2288
    • (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    Levi, S.7
  • 52
    • 67349121459 scopus 로고    scopus 로고
    • A. Campanella, E. Rovelli, P. Santambrogio, A. Cozzi, F. Taroni, S. Levi, Mitochondrial ferritin regulates iron availability for mitochondria functionality: implication for Friedreich ataxia, Human molecular genetics, Hum. Mol. Genet. 17 (in press) [Electronic publication ahead of print].
    • A. Campanella, E. Rovelli, P. Santambrogio, A. Cozzi, F. Taroni, S. Levi, Mitochondrial ferritin regulates iron availability for mitochondria functionality: implication for Friedreich ataxia, Human molecular genetics, Hum. Mol. Genet. 17 (in press) [Electronic publication ahead of print].
  • 53
    • 0035997354 scopus 로고    scopus 로고
    • Great metalloclusters in enzymology
    • Rees D.C. Great metalloclusters in enzymology. Annu. Rev. Biochem. 71 (2002) 221-246
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 221-246
    • Rees, D.C.1
  • 54
    • 20744446399 scopus 로고    scopus 로고
    • Structure, function, and formation of biological iron-sulfur clusters
    • Johnson D.C., Dean D.R., Smith A.D., and Johnson M.K. Structure, function, and formation of biological iron-sulfur clusters. Annu. Rev. Biochem. 74 (2005) 247-281
    • (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
  • 55
    • 26444455549 scopus 로고    scopus 로고
    • How Escherichia coli and Saccharomyces cerevisiae build Fe/S proteins
    • Barras F., Loiseau L., and Py B. How Escherichia coli and Saccharomyces cerevisiae build Fe/S proteins. Adv. Microb. Physiol. 50 (2005) 41-101
    • (2005) Adv. Microb. Physiol. , vol.50 , pp. 41-101
    • Barras, F.1    Loiseau, L.2    Py, B.3
  • 56
    • 14744294785 scopus 로고    scopus 로고
    • Iron-sulfur-protein biogenesis in eukaryotes
    • Lill R., and Muhlenhoff U. Iron-sulfur-protein biogenesis in eukaryotes. Trends Biochem. Sci. 30 (2005) 133-141
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 133-141
    • Lill, R.1    Muhlenhoff, U.2
  • 57
    • 9744248303 scopus 로고    scopus 로고
    • Iron-sulfur protein maturation in human cells: evidence for a function of frataxin
    • Stehling O., Elsasser H.P., Bruckel B., Muhlenhoff U., and Lill R. Iron-sulfur protein maturation in human cells: evidence for a function of frataxin. Hum. Mol. Genet. 13 (2004) 3007-3015
    • (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
  • 58
    • 33644623262 scopus 로고    scopus 로고
    • Functions of mitochondrial ISCU and cytosolic ISCU in mammalian iron-sulfur cluster biogenesis and iron homeostasis
    • Tong W.H., and Rouault T.A. Functions of mitochondrial ISCU and cytosolic ISCU in mammalian iron-sulfur cluster biogenesis and iron homeostasis. Cell. Metab. 3 (2006) 199-210
    • (2006) Cell. Metab. , vol.3 , pp. 199-210
    • Tong, W.H.1    Rouault, T.A.2
  • 59
    • 0033621156 scopus 로고    scopus 로고
    • Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae
    • Schilke B., Voisine C., Beinert H., and Craig E. Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 10206-10211
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 10206-10211
    • Schilke, B.1    Voisine, C.2    Beinert, H.3    Craig, E.4
  • 60
    • 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 S.A., Pain D., and Dancis A. Yeast mitochondrial protein, Nfs1p, coordinately regulates iron-sulfur cluster proteins, cellular iron uptake, and iron distribution. J Biol. Chem. 274 (1999) 33025-33034
    • (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
  • 61
    • 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., and Lill R. The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins. EMBO J. 18 (1999) 3981-3989
    • (1999) EMBO J. , vol.18 , pp. 3981-3989
    • Kispal, G.1    Csere, P.2    Prohl, C.3    Lill, R.4
  • 63
    • 0036809412 scopus 로고    scopus 로고
    • A specialized mitochondrial molecular chaperone system: a role in formation of Fe/S centers
    • Craig E.A., and Marszalek J. A specialized mitochondrial molecular chaperone system: a role in formation of Fe/S centers. Cell. Mol. Life Sci. 59 (2002) 1658-1665
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1658-1665
    • Craig, E.A.1    Marszalek, J.2
  • 64
    • 43749114744 scopus 로고    scopus 로고
    • Cellular and mitochondrial remodeling upon defects in iron-sulfur protein biogenesis
    • Hausmann A., Samans B., Lill R., and Muhlenhoff U. Cellular and mitochondrial remodeling upon defects in iron-sulfur protein biogenesis. J. Biol. Chem. 283 (2008) 8318-8330
    • (2008) J. Biol. Chem. , vol.283 , pp. 8318-8330
    • Hausmann, A.1    Samans, B.2    Lill, R.3    Muhlenhoff, U.4
  • 65
    • 30444433568 scopus 로고    scopus 로고
    • The Nfs1 interacting protein Isd11 has an essential role in Fe/S cluster biogenesis in mitochondria
    • Adam A.C., Bornhovd C., Prokisch H., Neupert W., and Hell K. The Nfs1 interacting protein Isd11 has an essential role in Fe/S cluster biogenesis in mitochondria. EMBO J. 25 (2006) 174-183
    • (2006) EMBO J. , vol.25 , pp. 174-183
    • Adam, A.C.1    Bornhovd, C.2    Prokisch, H.3    Neupert, W.4    Hell, K.5
  • 66
    • 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., and Lill R. The yeast scaffold proteins Isu1p and Isu2p are required inside mitochondria for maturation of cytosolic Fe/S proteins. Mol. Cell. Biol. 24 (2004) 4848-4857
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4848-4857
    • Gerber, J.1    Neumann, K.2    Prohl, C.3    Muhlenhoff, U.4    Lill, R.5
  • 67
    • 0033953353 scopus 로고    scopus 로고
    • A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins
    • Lange H., Kaut A., Kispal G., and Lill R. A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 1050-1055
    • (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
  • 68
    • 0035846961 scopus 로고    scopus 로고
    • Adrenodoxin reductase homolog (Arh1p) of yeast mitochondria required for iron homeostasis
    • Li J., Saxena S., Pain D., and Dancis A. Adrenodoxin reductase homolog (Arh1p) of yeast mitochondria required for iron homeostasis. J. Biol. Chem. 276 (2001) 1503-1509
    • (2001) J. Biol. Chem. , vol.276 , pp. 1503-1509
    • Li, J.1    Saxena, S.2    Pain, D.3    Dancis, A.4
  • 69
    • 3142716203 scopus 로고    scopus 로고
    • Sequence-specific interaction between mitochondrial Fe-S scaffold protein Isu and Hsp70 Ssq1 is essential for their in vivo function
    • Dutkiewicz R., Schilke B., Cheng S., Knieszner H., Craig E.A., and Marszalek J. Sequence-specific interaction between mitochondrial Fe-S scaffold protein Isu and Hsp70 Ssq1 is essential for their in vivo function. J. Biol. Chem. 279 (2004) 29167-29174
    • (2004) J. Biol. Chem. , vol.279 , pp. 29167-29174
    • Dutkiewicz, R.1    Schilke, B.2    Cheng, S.3    Knieszner, H.4    Craig, E.A.5    Marszalek, J.6
  • 70
    • 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 D.M., Pain D., and Dancis A. J-domain protein, Jac1p, of yeast mitochondria required for iron homeostasis and activity of Fe-S cluster proteins. J. Biol. Chem. 276 (2001) 17524-17532
    • (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
  • 71
    • 34248653740 scopus 로고    scopus 로고
    • Metabolic regulation of citrate and iron by aconitases: role of iron-sulfur cluster biogenesis
    • Tong W.H., and Rouault T.A. Metabolic regulation of citrate and iron by aconitases: role of iron-sulfur cluster biogenesis. Biometals 20 (2007) 549-564
    • (2007) Biometals , vol.20 , pp. 549-564
    • Tong, W.H.1    Rouault, T.A.2
  • 72
    • 0034866458 scopus 로고    scopus 로고
    • An essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic Fe/S proteins
    • Lange H., Lisowsky T., Gerber J., Muhlenhoff U., Kispal G., and Lill R. An essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic Fe/S proteins. EMBO Rep. 2 (2001) 715-720
    • (2001) EMBO Rep. , vol.2 , pp. 715-720
    • Lange, H.1    Lisowsky, T.2    Gerber, J.3    Muhlenhoff, U.4    Kispal, G.5    Lill, R.6
  • 73
    • 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 D.J., Balk J., Pierik A.J., Muhlenhoff U., and 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. 102 (2005) 3266-3271
    • (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
  • 74
    • 2942565619 scopus 로고    scopus 로고
    • The hydrogenase-like Nar1p is essential for maturation of cytosolic and nuclear iron-sulphur proteins
    • Balk J., Pierik A.J., Netz D.J., Muhlenhoff U., and Lill R. The hydrogenase-like Nar1p is essential for maturation of cytosolic and nuclear iron-sulphur proteins. EMBO J. 23 (2004) 2105-2115
    • (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
  • 75
    • 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 D.J., Tepper K., Pierik A.J., and Lill R. The essential WD40 protein Cia1 is involved in a late step of cytosolic and nuclear iron-sulfur protein assembly. Mol. Cell. Biol. 25 (2005) 10833-10841
    • (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
  • 76
    • 1242277806 scopus 로고    scopus 로고
    • Metal-responsive transcription factors that regulate iron, zinc, and copper homeostasis in eukaryotic cells
    • Rutherford J.C., and Bird A.J. Metal-responsive transcription factors that regulate iron, zinc, and copper homeostasis in eukaryotic cells. Eukaryot. Cell 3 (2004) 1-13
    • (2004) Eukaryot. Cell , vol.3 , pp. 1-13
    • Rutherford, J.C.1    Bird, A.J.2
  • 77
    • 0033511832 scopus 로고    scopus 로고
    • Cell biology of heme
    • Ponka P. Cell biology of heme. Am. J. Med. Sci. 318 (1999) 241-256
    • (1999) Am. J. Med. Sci. , vol.318 , pp. 241-256
    • Ponka, P.1
  • 78
    • 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 89 (1997) 1-25
    • (1997) Blood , vol.89 , pp. 1-25
    • Ponka, P.1
  • 79
    • 0029027246 scopus 로고
    • 5-Aminolevulinate synthase and the first step of heme biosynthesis
    • Ferreira G.C., and Gong J. 5-Aminolevulinate synthase and the first step of heme biosynthesis. J. Bioenerg. Biomembr. 27 (1995) 151-159
    • (1995) J. Bioenerg. Biomembr. , vol.27 , pp. 151-159
    • Ferreira, G.C.1    Gong, J.2
  • 82
    • 34249740700 scopus 로고    scopus 로고
    • The role of transporters in cellular heme and porphyrin homeostasis
    • Krishnamurthy P., Xie T., and Schuetz J.D. The role of transporters in cellular heme and porphyrin homeostasis. Pharmacol. Ther. 114 (2007) 345-358
    • (2007) Pharmacol. Ther. , vol.114 , pp. 345-358
    • Krishnamurthy, P.1    Xie, T.2    Schuetz, J.D.3
  • 83
    • 0034213588 scopus 로고    scopus 로고
    • ABC-me: a novel mitochondrial transporter induced by GATA-1 during erythroid differentiation
    • Shirihai O.S., Gregory T., Yu C., Orkin S.H., and Weiss M.J. ABC-me: a novel mitochondrial transporter induced by GATA-1 during erythroid differentiation. EMBO J. 19 (2000) 2492-2502
    • (2000) EMBO J. , vol.19 , pp. 2492-2502
    • Shirihai, O.S.1    Gregory, T.2    Yu, C.3    Orkin, S.H.4    Weiss, M.J.5
  • 84
    • 33947154878 scopus 로고    scopus 로고
    • Structure of an ABC transporter in complex with its binding protein
    • Hollenstein K., Frei D.C., and Locher K.P. Structure of an ABC transporter in complex with its binding protein. Nature 446 (2007) 213-216
    • (2007) Nature , vol.446 , pp. 213-216
    • Hollenstein, K.1    Frei, D.C.2    Locher, K.P.3
  • 86
    • 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 W.H., Hutchinson A., Schueck N.D., Dean M., and Koeller D.M. Mutation of a putative mitochondrial iron transporter gene (ABC7) in X-linked sideroblastic anemia and ataxia (XLSA/A). Hum. Mol. Genet. 8 (1999) 743-749
    • (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
  • 87
    • 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., Derosas M., Ingrassia R., Corrado M., and Arosio P. RNA silencing of the mitochondrial ABCB7 transporter in HeLa cells causes an iron-deficient phenotype with mitochondrial iron overload. Blood 109 (2007) 3552-3559
    • (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    Derosas, M.7    Ingrassia, R.8    Corrado, M.9    Arosio, P.10
  • 88
    • 33745410626 scopus 로고    scopus 로고
    • Mitochondrial disease
    • Schapira A.H. Mitochondrial disease. Lancet 368 (2006) 70-82
    • (2006) Lancet , vol.368 , pp. 70-82
    • Schapira, A.H.1
  • 89
    • 1542573338 scopus 로고    scopus 로고
    • Mitochondrial encephalomyopathies: gene mutation
    • Servidei S. Mitochondrial encephalomyopathies: gene mutation. Neuromuscul. Disord. 14 (2004) 107-116
    • (2004) Neuromuscul. Disord. , vol.14 , pp. 107-116
    • Servidei, S.1
  • 93
    • 33750301410 scopus 로고    scopus 로고
    • Iron and Friedreich ataxia
    • Pandolfo M. Iron and Friedreich ataxia. J. Neural Transm. Suppl. (2006) 143-146
    • (2006) J. Neural Transm. , Issue.SUPPL , pp. 143-146
    • Pandolfo, M.1
  • 94
    • 33846782071 scopus 로고    scopus 로고
    • Friedreich ataxia: detection of GAA repeat expansions and frataxin point mutations
    • Pandolfo M. Friedreich ataxia: detection of GAA repeat expansions and frataxin point mutations. Methods Mol. Med. 126 (2006) 197-216
    • (2006) Methods Mol. Med. , vol.126 , pp. 197-216
    • Pandolfo, M.1
  • 99
    • 0030825723 scopus 로고    scopus 로고
    • Respiratory deficiency due to loss of mitochondrial DNA in yeast lacking the frataxin homologue
    • Wilson R.B., and Roof D.M. Respiratory deficiency due to loss of mitochondrial DNA in yeast lacking the frataxin homologue. Nat. Genet. 16 (1997) 352-357
    • (1997) Nat. Genet. , vol.16 , pp. 352-357
    • Wilson, R.B.1    Roof, D.M.2
  • 100
    • 0036603021 scopus 로고    scopus 로고
    • Friedreich ataxia: a paradigm for mitochondrial diseases
    • Puccio H., and Koenig M. Friedreich ataxia: a paradigm for mitochondrial diseases. Curr. Opin. Genet. Dev. 12 (2002) 272-277
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 272-277
    • Puccio, H.1    Koenig, M.2
  • 101
    • 33750706562 scopus 로고    scopus 로고
    • Iron dysregulation in Friedreich ataxia
    • Wilson R.B. Iron dysregulation in Friedreich ataxia. Semin. Pediatr. Neurol. 13 (2006) 166-175
    • (2006) Semin. Pediatr. Neurol. , vol.13 , pp. 166-175
    • Wilson, R.B.1
  • 102
    • 38949197818 scopus 로고    scopus 로고
    • Redistribution of accumulated cell iron: a modality of chelation with therapeutic implications
    • Sohn Y.S., Breuer W., Munnich A., and Cabantchik Z.I. Redistribution of accumulated cell iron: a modality of chelation with therapeutic implications. Blood 111 (2008) 1690-1699
    • (2008) Blood , vol.111 , pp. 1690-1699
    • Sohn, Y.S.1    Breuer, W.2    Munnich, A.3    Cabantchik, Z.I.4
  • 106
    • 0033054177 scopus 로고    scopus 로고
    • The Friedreich's ataxia mutation confers cellular sensitivity to oxidant stress which is rescued by chelators of iron and calcium and inhibitors of apoptosis
    • Wong A., Yang J., Cavadini P., Gellera C., Lonnerdal B., Taroni F., and Cortopassi G. The Friedreich's ataxia mutation confers cellular sensitivity to oxidant stress which is rescued by chelators of iron and calcium and inhibitors of apoptosis. Hum. Mol. Genet. 8 (1999) 425-430
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 425-430
    • Wong, A.1    Yang, J.2    Cavadini, P.3    Gellera, C.4    Lonnerdal, B.5    Taroni, F.6    Cortopassi, G.7
  • 107
    • 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., Hindelang C., Matyas R., Rustin P., and Koenig M. Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits. Nat. Genet. 27 (2001) 181-186
    • (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    Hindelang, C.7    Matyas, R.8    Rustin, P.9    Koenig, M.10
  • 108
    • 38649103446 scopus 로고    scopus 로고
    • Hydrogen peroxide scavenging rescues frataxin deficiency in a Drosophila model of Friedreich's ataxia
    • Anderson P.R., Kirby K., Orr W.C., Hilliker A.J., and Phillips J.P. Hydrogen peroxide scavenging rescues frataxin deficiency in a Drosophila model of Friedreich's ataxia. Proc. Natl. Acad. Sci. U. S. A. 105 (2008) 611-616
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 611-616
    • Anderson, P.R.1    Kirby, K.2    Orr, W.C.3    Hilliker, A.J.4    Phillips, J.P.5
  • 110
    • 5044229348 scopus 로고    scopus 로고
    • Molecular mechanisms of translational control
    • Gebauer F., and Hentze M.W. Molecular mechanisms of translational control. Nat. Rev. Mol. Cell Biol. 5 (2004) 827-835
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 827-835
    • Gebauer, F.1    Hentze, M.W.2
  • 111
    • 33746361251 scopus 로고    scopus 로고
    • The role of iron regulatory proteins in mammalian iron homeostasis and disease
    • Rouault T.A. The role of iron regulatory proteins in mammalian iron homeostasis and disease. Nat. Chem. Biol. 2 (2006) 406-414
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 406-414
    • Rouault, T.A.1
  • 112
    • 0038491193 scopus 로고    scopus 로고
    • Biochemical characterization of yeast mitochondrial Grx5 monothiol glutaredoxin
    • Tamarit J., Belli G., Cabiscol E., Herrero E., and Ros J. Biochemical characterization of yeast mitochondrial Grx5 monothiol glutaredoxin. J. Biol. Chem. 278 (2003) 25745-25751
    • (2003) J. Biol. Chem. , vol.278 , pp. 25745-25751
    • Tamarit, J.1    Belli, G.2    Cabiscol, E.3    Herrero, E.4    Ros, J.5
  • 113
    • 0036226063 scopus 로고    scopus 로고
    • Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes
    • Rodriguez-Manzaneque M.T., Tamarit J., Belli G., Ros J., and Herrero E. Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes. Mol. Biol. Cell 13 (2002) 1109-1121
    • (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
  • 117
    • 0027145130 scopus 로고
    • Mitochondrial myopathy with succinate dehydrogenase and aconitase deficiency. Abnormalities of several iron-sulfur proteins
    • Hall R.E., Henriksson K.G., Lewis S.F., Haller R.G., and Kennaway N.G. Mitochondrial myopathy with succinate dehydrogenase and aconitase deficiency. Abnormalities of several iron-sulfur proteins. J. Clin. Invest. 92 (1993) 2660-2666
    • (1993) J. Clin. Invest. , vol.92 , pp. 2660-2666
    • Hall, R.E.1    Henriksson, K.G.2    Lewis, S.F.3    Haller, R.G.4    Kennaway, N.G.5
  • 118
    • 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., and Bishop D.F. Human ABC7 transporter: gene structure and mutation causing X-linked sideroblastic anemia with ataxia with disruption of cytosolic iron-sulfur protein maturation. Blood 96 (2000) 3256-3264
    • (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    Bishop, D.F.7
  • 119
    • 0035672913 scopus 로고    scopus 로고
    • X-linked cerebellar ataxia and sideroblastic anaemia associated with a missense mutation in the ABC7 gene predicting V411L
    • Maguire A., Hellier K., Hammans S., and May A. X-linked cerebellar ataxia and sideroblastic anaemia associated with a missense mutation in the ABC7 gene predicting V411L. Br. J. Haematol. 115 (2001) 910-917
    • (2001) Br. J. Haematol. , vol.115 , pp. 910-917
    • Maguire, A.1    Hellier, K.2    Hammans, S.3    May, A.4
  • 121
    • 0036799489 scopus 로고    scopus 로고
    • The genetics of inherited sideroblastic anemias
    • Fleming M.D. The genetics of inherited sideroblastic anemias. Semin. Hematol. 39 (2002) 270-281
    • (2002) Semin. Hematol. , vol.39 , pp. 270-281
    • Fleming, M.D.1
  • 122
    • 33748754872 scopus 로고    scopus 로고
    • Congenital sideroblastic anemias
    • Bottomley S.S. Congenital sideroblastic anemias. Curr. Hematol. Rep. 5 (2006) 41-49
    • (2006) Curr. Hematol. Rep. , vol.5 , pp. 41-49
    • Bottomley, S.S.1
  • 123
    • 34147158934 scopus 로고    scopus 로고
    • Abcb7, the gene responsible for X-linked sideroblastic anemia with ataxia, is essential for hematopoiesis
    • Pondarre C., Campagna D.R., Antiochos B., Sikorski L., Mulhern H., and Fleming M.D. Abcb7, the gene responsible for X-linked sideroblastic anemia with ataxia, is essential for hematopoiesis. Blood 109 (2007) 3567-3569
    • (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
  • 127
    • 0034107324 scopus 로고    scopus 로고
    • Role of Saccharomyces cerevisiae ISA1 and ISA2 in iron homeostasis
    • Jensen L.T., and Culotta V.C. Role of Saccharomyces cerevisiae ISA1 and ISA2 in iron homeostasis. Mol. Cell. Biol. 20 (2000) 3918-3927
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3918-3927
    • Jensen, L.T.1    Culotta, V.C.2
  • 128
    • 40749086415 scopus 로고    scopus 로고
    • Mitochondrial Iba57p is required for Fe/S cluster formation on aconitase and activation of radical SAM enzymes
    • Gelling C., Dawes I.W., Richhardt N., Lill R., and Muhlenhoff U. Mitochondrial Iba57p is required for Fe/S cluster formation on aconitase and activation of radical SAM enzymes. Mol. Cell. Biol. 28 (2008) 1851-1861
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 1851-1861
    • Gelling, C.1    Dawes, I.W.2    Richhardt, N.3    Lill, R.4    Muhlenhoff, U.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.