메뉴 건너뛰기




Volumn 49, Issue 24, 2010, Pages 4945-4956

Human iron-sulfur cluster assembly, cellular iron homeostasis, and disease

Author keywords

[No Author keywords available]

Indexed keywords

ACONITASE; CLUSTER SYNTHESIS; CYTOSOLIC; ENZYMATIC FUNCTIONS; FRATAXIN; HUMAN DISEASE; IRON ATOMS; IRON DEFICIENCY; IRON HOMEOSTASIS; IRON-SULFUR CLUSTERS; MULTIPLE FUNCTION; PATHOPHYSIOLOGY; PROSTHETIC GROUPS; REDOX ACTIVITY; SIDEROBLASTIC ANEMIAS; SUCCINATE DEHYDROGENASE; SULFUR LIGANDS;

EID: 77953669993     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi1004798     Document Type: Review
Times cited : (216)

References (109)
  • 3
    • 2042546096 scopus 로고    scopus 로고
    • Balancing acts: Molecular control of mammalian iron metabolism
    • Hentze, M. W., Muckenthaler, M. U., and Andrews, N. C. (2004) Balancing acts: Molecular control of mammalian iron metabolism Cell 117, 285-297
    • (2004) Cell , vol.117 , pp. 285-297
    • Hentze, M.W.1    Muckenthaler, M.U.2    Andrews, N.C.3
  • 4
    • 37549059612 scopus 로고    scopus 로고
    • Regulation of iron acquisition and storage: Consequences for iron-linked disorders
    • De Domenico, I., McVey Ward, D., and Kaplan, J. (2008) Regulation of iron acquisition and storage: Consequences for iron-linked disorders Nat. Rev. Mol. Cell Biol. 9, 72-81
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 72-81
    • De Domenico, I.1    McVey Ward, D.2    Kaplan, J.3
  • 5
    • 41549127253 scopus 로고    scopus 로고
    • Iron homeostasis: Fitting the puzzle pieces together
    • Ganz, T. (2008) Iron homeostasis: Fitting the puzzle pieces together Cell Metab. 7, 288-290
    • (2008) Cell Metab. , vol.7 , pp. 288-290
    • Ganz, T.1
  • 6
    • 54049156405 scopus 로고    scopus 로고
    • The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel
    • Dong, X. P., Cheng, X., Mills, E., Delling, M., Wang, F., Kurz, T., and Xu, H. (2008) The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel Nature 455, 992-996
    • (2008) Nature , vol.455 , pp. 992-996
    • Dong, X.P.1    Cheng, X.2    Mills, E.3    Delling, M.4    Wang, F.5    Kurz, T.6    Xu, H.7
  • 7
    • 17144378216 scopus 로고    scopus 로고
    • Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis
    • Rouault, T. A. and Tong, W. H. (2005) Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis Nat. Rev. Mol. Cell Biol. 6, 345-351
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 345-351
    • Rouault, T.A.1    Tong, W.H.2
  • 8
    • 0342657758 scopus 로고    scopus 로고
    • + clusters with endogenous iron and sulfide in anaerobic ribonucleotide reductase activase in vitro
    • + clusters with endogenous iron and sulfide in anaerobic ribonucleotide reductase activase in vitro J. Biol. Chem. 275, 12367-12373
    • (2000) J. Biol. Chem. , vol.275 , pp. 12367-12373
    • Liu, A.1    Graslund, A.2
  • 9
    • 45849123222 scopus 로고    scopus 로고
    • A cytosolic iron chaperone that delivers iron to ferritin
    • Shi, H., Bencze, K. Z., Stemmler, T. L., and Philpott, C. C. (2008) A cytosolic iron chaperone that delivers iron to ferritin Science 320, 1207-1210
    • (2008) Science , vol.320 , pp. 1207-1210
    • Shi, H.1    Bencze, K.Z.2    Stemmler, T.L.3    Philpott, C.C.4
  • 11
    • 47249142777 scopus 로고    scopus 로고
    • Iron-sulfur cluster biogenesis and human disease
    • Rouault, T. A. and Tong, W. H. (2008) Iron-sulfur cluster biogenesis and human disease Trends Genet. 24, 398-407
    • (2008) Trends Genet. , vol.24 , pp. 398-407
    • Rouault, T.A.1    Tong, W.H.2
  • 12
    • 47249094614 scopus 로고    scopus 로고
    • Maturation of iron-sulfur proteins in eukaryotes: Mechanisms, connected processes, and diseases
    • Lill, R. and Muhlenhoff, U. (2008) Maturation of iron-sulfur proteins in eukaryotes: Mechanisms, connected processes, and diseases Annu. Rev. Biochem. 77, 669-700
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 669-700
    • Lill, R.1    Muhlenhoff, U.2
  • 15
    • 33746361251 scopus 로고    scopus 로고
    • The role of iron regulatory proteins in mammalian iron homeostasis and disease
    • Rouault, T. A. (2006) The role of iron regulatory proteins in mammalian iron homeostasis and disease Nat. Chem. Biol. 2, 406-414
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 406-414
    • Rouault, T.A.1
  • 16
    • 33746864096 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron homeostasis by iron regulatory proteins
    • Wallander, M. L., Leibold, E. A., and Eisenstein, R. S. (2006) Molecular control of vertebrate iron homeostasis by iron regulatory proteins Biochim. Biophys. Acta 1763, 668-689
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 668-689
    • Wallander, M.L.1    Leibold, E.A.2    Eisenstein, R.S.3
  • 17
    • 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. (2005) Structure, function, and formation of biological iron-sulfur clusters Annu. Rev. Biochem. 74, 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
  • 18
    • 14744294785 scopus 로고    scopus 로고
    • Iron-sulfur-protein biogenesis in eukaryotes
    • Lill, R. and Muhlenhoff, U. (2005) Iron-sulfur-protein biogenesis in eukaryotes Trends Biochem. Sci. 30, 133-141
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 133-141
    • Lill, R.1    Muhlenhoff, U.2
  • 19
    • 62549093116 scopus 로고    scopus 로고
    • The pathogenesis of Friedreich ataxia and the structure and function of frataxin
    • Pandolfo, M. and Pastore, A. (2009) The pathogenesis of Friedreich ataxia and the structure and function of frataxin J. Neurol. 256 (Suppl. 1) 9-17
    • (2009) J. Neurol. , vol.256 , Issue.SUPPL. 1 , pp. 9-17
    • Pandolfo, M.1    Pastore, A.2
  • 20
    • 34247124148 scopus 로고    scopus 로고
    • Molecular chaperones HscA/Ssq1 and HscB/Jac1 and their roles in iron-sulfur protein maturation
    • Vickery, L. E. and Cupp-Vickery, J. R. (2007) Molecular chaperones HscA/Ssq1 and HscB/Jac1 and their roles in iron-sulfur protein maturation Crit. Rev. Biochem. Mol. Biol. 42, 95-111
    • (2007) Crit. Rev. Biochem. Mol. Biol. , vol.42 , pp. 95-111
    • Vickery, L.E.1    Cupp-Vickery, J.R.2
  • 21
    • 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. (2008) Mitochondrial Iba57p is required for Fe/S cluster formation on aconitase and activation of radical SAM enzymes Mol. Cell. Biol. 28, 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
  • 22
    • 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. (2004) The hydrogenase-like Nar1p is essential for maturation of cytosolic and nuclear iron-sulphur proteins EMBO J. 23, 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
  • 24
    • 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. (2007) Metabolic regulation of citrate and iron by aconitases: Role of iron-sulfur cluster biogenesis BioMetals 20, 549-564
    • (2007) BioMetals , vol.20 , pp. 549-564
    • Tong, W.H.1    Rouault, T.A.2
  • 25
    • 0032245425 scopus 로고    scopus 로고
    • Targeting of a human iron-sulfur cluster assembly enzyme, nifs, to different subcellular compartments is regulated through alternative AUG utilization
    • Land, T. and Rouault, T. A. (1998) Targeting of a human iron-sulfur cluster assembly enzyme, nifs, to different subcellular compartments is regulated through alternative AUG utilization Mol. Cell 2, 807-815
    • (1998) Mol. Cell , vol.2 , pp. 807-815
    • Land, T.1    Rouault, T.A.2
  • 26
    • 68049086933 scopus 로고    scopus 로고
    • Human ISD11 is essential for both iron-sulfur cluster assembly and maintenance of normal cellular iron homeostasis
    • Shi, Y., Ghosh, M. C., Tong, W. H., and Rouault, T. A. (2009) Human ISD11 is essential for both iron-sulfur cluster assembly and maintenance of normal cellular iron homeostasis Hum. Mol. Genet. 18, 3014-3025
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 3014-3025
    • Shi, Y.1    Ghosh, M.C.2    Tong, W.H.3    Rouault, T.A.4
  • 27
    • 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. and Cowan, J. A. (2003) 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. 125, 6078-6084
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6078-6084
    • Yoon, T.1    Cowan, J.A.2
  • 28
    • 0034331239 scopus 로고    scopus 로고
    • Distinct iron-sulfur cluster assembly complexes exist in the cytosol and mitochondria of human cells
    • Tong, W. H. and Rouault, T. (2000) Distinct iron-sulfur cluster assembly complexes exist in the cytosol and mitochondria of human cells EMBO J. 19, 5692-5700
    • (2000) EMBO J. , vol.19 , pp. 5692-5700
    • Tong, W.H.1    Rouault, T.2
  • 29
    • 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. (2006) Functions of mitochondrial ISCU and cytosolic ISCU in mammalian iron-sulfur cluster biogenesis and iron homeostasis Cell Metab. 3, 199-210
    • (2006) Cell Metab. , vol.3 , pp. 199-210
    • Tong, W.H.1    Rouault, T.A.2
  • 30
    • 0041691163 scopus 로고    scopus 로고
    • Subcellular compartmentalization of human Nfu, an iron-sulfur cluster scaffold protein, and its ability to assemble a [4Fe-4S] cluster
    • Tong, W. H., Jameson, G. N., Huynh, B. H., and Rouault, T. A. (2003) Subcellular compartmentalization of human Nfu, an iron-sulfur cluster scaffold protein, and its ability to assemble a [4Fe-4S] cluster Proc. Natl. Acad. Sci. U.S.A. 100, 9762-9767
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 9762-9767
    • Tong, W.H.1    Jameson, G.N.2    Huynh, B.H.3    Rouault, T.A.4
  • 32
    • 77951843593 scopus 로고    scopus 로고
    • Glutaredoxin 5 deficiency causes sideroblastic anemia by specifically impairing heme biosynthesis and depleting cytosolic iron in human erythroblasts
    • Ye, H., Jeong, S. Y., Ghosh, M. C., Kovtunovych, G., Silvestri, L., Ortillo, D., Uchida, N., Tisdale, J., Camaschella, C., and Rouault, T. A. (2010) Glutaredoxin 5 deficiency causes sideroblastic anemia by specifically impairing heme biosynthesis and depleting cytosolic iron in human erythroblasts J. Clin. Invest. 120, 1749-1761
    • (2010) J. Clin. Invest. , vol.120 , pp. 1749-1761
    • Ye, H.1    Jeong, S.Y.2    Ghosh, M.C.3    Kovtunovych, G.4    Silvestri, L.5    Ortillo, D.6    Uchida, N.7    Tisdale, J.8    Camaschella, C.9    Rouault, T.A.10
  • 33
    • 44049094146 scopus 로고    scopus 로고
    • A role for IOP1 in mammalian cytosolic iron-sulfur protein biogenesis
    • Song, D. and Lee, F. S. (2008) A role for IOP1 in mammalian cytosolic iron-sulfur protein biogenesis J. Biol. Chem. 283, 9231-9238
    • (2008) J. Biol. Chem. , vol.283 , pp. 9231-9238
    • Song, D.1    Lee, F.S.2
  • 34
    • 33846298869 scopus 로고    scopus 로고
    • IOP1, a novel hydrogenase-like protein that modulates hypoxia-inducible factor-1α activity
    • Huang, J., Song, D., Flores, A., Zhao, Q., Mooney, S. M., Shaw, L. M., and Lee, F. S. (2007) IOP1, a novel hydrogenase-like protein that modulates hypoxia-inducible factor-1α activity Biochem. J. 401, 341-352
    • (2007) Biochem. J. , vol.401 , pp. 341-352
    • Huang, J.1    Song, D.2    Flores, A.3    Zhao, Q.4    Mooney, S.M.5    Shaw, L.M.6    Lee, F.S.7
  • 36
    • 26244448912 scopus 로고    scopus 로고
    • Extra-mitochondrial localisation of frataxin and its association with IscU1 during enterocyte-like differentiation of the human colon adenocarcinoma cell line Caco-2
    • Acquaviva, F., De Biase, I., Nezi, L., Ruggiero, G., Tatangelo, F., Pisano, C., Monticelli, A., Garbi, C., Acquaviva, A. M., and Cocozza, S. (2005) Extra-mitochondrial localisation of frataxin and its association with IscU1 during enterocyte-like differentiation of the human colon adenocarcinoma cell line Caco-2 J. Cell Sci. 118, 3917-3924
    • (2005) J. Cell Sci. , vol.118 , pp. 3917-3924
    • Acquaviva, F.1    De Biase, I.2    Nezi, L.3    Ruggiero, G.4    Tatangelo, F.5    Pisano, C.6    Monticelli, A.7    Garbi, C.8    Acquaviva, A.M.9    Cocozza, S.10
  • 37
    • 33745222541 scopus 로고    scopus 로고
    • A pool of extramitochondrial frataxin that promotes cell survival
    • Condo, I., Ventura, N., Malisan, F., Tomassini, B., and Testi, R. (2006) A pool of extramitochondrial frataxin that promotes cell survival J. Biol. Chem. 281, 16750-16756
    • (2006) J. Biol. Chem. , vol.281 , pp. 16750-16756
    • Condo, I.1    Ventura, N.2    Malisan, F.3    Tomassini, B.4    Testi, R.5
  • 38
    • 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, J. C., Lill, R., and Winge, D. R. (2006) Role of glutaredoxin-3 and glutaredoxin-4 in the iron regulation of the Aft1 transcriptional activator in Saccharomyces cerevisiae J. Biol. Chem. 281, 17661-17669
    • (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
  • 39
    • 70350070125 scopus 로고    scopus 로고
    • The yeast iron regulatory proteins Grx3/4 and Fra2 form heterodimeric complexes containing a [2Fe-2S] cluster with cysteinyl and histidyl ligation
    • Li, H., Mapolelo, D. T., Dingra, N. N., Naik, S. G., Lees, N. S., Hoffman, B. M., Riggs-Gelasco, P. J., Huynh, B. H., Johnson, M. K., and Outten, C. E. (2009) The yeast iron regulatory proteins Grx3/4 and Fra2 form heterodimeric complexes containing a [2Fe-2S] cluster with cysteinyl and histidyl ligation Biochemistry 48, 9569-9581
    • (2009) Biochemistry , vol.48 , pp. 9569-9581
    • Li, H.1    Mapolelo, D.T.2    Dingra, N.N.3    Naik, S.G.4    Lees, N.S.5    Hoffman, B.M.6    Riggs-Gelasco, P.J.7    Huynh, B.H.8    Johnson, M.K.9    Outten, C.E.10
  • 40
    • 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. S., Li, L., Bagley, D., Adkins, E. M., Lin, H., Dingra, N. N., Outten, C. E., Keller, G., Winge, D., Ward, D. M., and Kaplan, J. (2008) 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. 283, 10276-10286
    • (2008) J. Biol. Chem. , vol.283 , pp. 10276-10286
    • Kumanovics, A.1    Chen, O.S.2    Li, L.3    Bagley, D.4    Adkins, E.M.5    Lin, H.6    Dingra, N.N.7    Outten, C.E.8    Keller, G.9    Winge, D.10    Ward, D.M.11    Kaplan, J.12
  • 44
    • 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. (2004) Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity Science 305, 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
  • 45
    • 0037188390 scopus 로고    scopus 로고
    • Physical evidence that yeast frataxin is an iron storage protein
    • Gakh, O., Adamec, J., Gacy, A. M., Twesten, R. D., Owen, W. G., and Isaya, G. (2002) Physical evidence that yeast frataxin is an iron storage protein Biochemistry 41, 6798-6804
    • (2002) Biochemistry , vol.41 , pp. 6798-6804
    • Gakh, O.1    Adamec, J.2    Gacy, A.M.3    Twesten, R.D.4    Owen, W.G.5    Isaya, G.6
  • 46
    • 2942744572 scopus 로고    scopus 로고
    • Frataxin-mediated iron delivery to ferrochelatase in the final step of heme biosynthesis
    • Yoon, T. and Cowan, J. A. (2004) Frataxin-mediated iron delivery to ferrochelatase in the final step of heme biosynthesis J. Biol. Chem. 279, 25943-25946
    • (2004) J. Biol. Chem. , vol.279 , pp. 25943-25946
    • Yoon, T.1    Cowan, J.A.2
  • 47
    • 0033582421 scopus 로고    scopus 로고
    • The yeast frataxin homologue mediates mitochondrial iron efflux. Evidence for a mitochondrial iron cycle
    • Radisky, D. C., Babcock, M. C., and Kaplan, J. (1999) The yeast frataxin homologue mediates mitochondrial iron efflux. Evidence for a mitochondrial iron cycle J. Biol. Chem. 274, 4497-4499
    • (1999) J. Biol. Chem. , vol.274 , pp. 4497-4499
    • Radisky, D.C.1    Babcock, M.C.2    Kaplan, J.3
  • 51
    • 0036603021 scopus 로고    scopus 로고
    • Friedreich ataxia: A paradigm for mitochondrial diseases
    • Puccio, H. and Koenig, M. (2002) Friedreich ataxia: A paradigm for mitochondrial diseases Curr. Opin. Genet. Dev. 12, 272-277
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 272-277
    • Puccio, H.1    Koenig, M.2
  • 52
    • 0036252812 scopus 로고    scopus 로고
    • Molecular insights into Friedreich's ataxia and antioxidant-based therapies
    • Rotig, A., Sidi, D., Munnich, A., and Rustin, P. (2002) Molecular insights into Friedreich's ataxia and antioxidant-based therapies Trends Mol. Med. 8, 221-224
    • (2002) Trends Mol. Med. , vol.8 , pp. 221-224
    • Rotig, A.1    Sidi, D.2    Munnich, A.3    Rustin, P.4
  • 53
    • 47249127786 scopus 로고    scopus 로고
    • Iron-dependent regulation of frataxin expression: Implications for treatment of Friedreich ataxia
    • Li, K., Besse, E. K., Ha, D., Kovtunovych, G., and Rouault, T. A. (2008) Iron-dependent regulation of frataxin expression: Implications for treatment of Friedreich ataxia Hum. Mol. Genet. 17, 2265-2273
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 2265-2273
    • Li, K.1    Besse, E.K.2    Ha, D.3    Kovtunovych, G.4    Rouault, T.A.5
  • 54
    • 70349504414 scopus 로고    scopus 로고
    • Elucidation of the mechanism of mitochondrial iron loading in Friedreich's ataxia by analysis of a mouse mutant
    • Huang, M. L., Becker, E. M., Whitnall, M., Rahmanto, Y. S., Ponka, P., and Richardson, D. R. (2009) Elucidation of the mechanism of mitochondrial iron loading in Friedreich's ataxia by analysis of a mouse mutant Proc. Natl. Acad. Sci. U.S.A. 106, 16381-16386
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 16381-16386
    • Huang, M.L.1    Becker, E.M.2    Whitnall, M.3    Rahmanto, Y.S.4    Ponka, P.5    Richardson, D.R.6
  • 55
    • 44949208513 scopus 로고    scopus 로고
    • DNA triplexes and Friedreich ataxia
    • Wells, R. D. (2008) DNA triplexes and Friedreich ataxia FASEB J. 22, 1625-1634
    • (2008) FASEB J. , vol.22 , pp. 1625-1634
    • Wells, R.D.1
  • 57
    • 0036554660 scopus 로고    scopus 로고
    • Heart hypertrophy and function are improved by idebenone in Friedreich's ataxia
    • DOI 10.1080/10715760290021333
    • Rustin, P., Rotig, A., Munnich, A., and Sidi, D. (2002) Heart hypertrophy and function are improved by idebenone in Friedreich's ataxia Free Radical Res. 36, 467-469 (Pubitemid 35154096)
    • (2002) Free Radical Research , vol.36 , Issue.4 , pp. 467-469
    • Rustin, P.1    Rotig, A.2    Munnich, A.3    Sidi, D.4
  • 59
    • 34250731291 scopus 로고    scopus 로고
    • Monothiol glutaredoxins: A common domain for multiple functions
    • Herrero, E. and de la Torre-Ruiz, M. A. (2007) Monothiol glutaredoxins: A common domain for multiple functions Cell. Mol. Life Sci. 64, 1518-1530
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 1518-1530
    • Herrero, E.1    De La Torre-Ruiz, M.A.2
  • 60
    • 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. (2002) Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes Mol. Biol. Cell 13, 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
  • 63
    • 10644242480 scopus 로고    scopus 로고
    • Nuclear monothiol glutaredoxins of Saccharomyces cerevisiae can function as mitochondrial glutaredoxins
    • Molina, M. M., Belli, G., de la Torre, M. A., Rodriguez-Manzaneque, M. T., and Herrero, E. (2004) Nuclear monothiol glutaredoxins of Saccharomyces cerevisiae can function as mitochondrial glutaredoxins J. Biol. Chem. 279, 51923-51930
    • (2004) J. Biol. Chem. , vol.279 , pp. 51923-51930
    • Molina, M.M.1    Belli, G.2    De La Torre, M.A.3    Rodriguez-Manzaneque, M.T.4    Herrero, E.5
  • 65
    • 65349126484 scopus 로고    scopus 로고
    • A ferroportin transcript that lacks an iron-responsive element enables duodenal and erythroid precursor cells to evade translational repression
    • Zhang, D. L., Hughes, R. M., Ollivierre-Wilson, H., Ghosh, M. C., and Rouault, T. A. (2009) A ferroportin transcript that lacks an iron-responsive element enables duodenal and erythroid precursor cells to evade translational repression Cell Metab. 9, 461-473
    • (2009) Cell Metab. , vol.9 , pp. 461-473
    • Zhang, D.L.1    Hughes, R.M.2    Ollivierre-Wilson, H.3    Ghosh, M.C.4    Rouault, T.A.5
  • 66
    • 33744956665 scopus 로고    scopus 로고
    • Roles of the mammalian cytosolic cysteine desulfurase, ISCS, and scaffold protein, ISCU, in iron-sulfur cluster assembly
    • Li, K., Tong, W. H., Hughes, R. M., and Rouault, T. A. (2006) Roles of the mammalian cytosolic cysteine desulfurase, ISCS, and scaffold protein, ISCU, in iron-sulfur cluster assembly J. Biol. Chem. 281, 12344-12351
    • (2006) J. Biol. Chem. , vol.281 , pp. 12344-12351
    • Li, K.1    Tong, W.H.2    Hughes, R.M.3    Rouault, T.A.4
  • 68
    • 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, L. E., and Holmberg, M. (2008) 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. 17, 1666-1672
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 1666-1672
    • Olsson, A.1    Lind, L.2    Thornell, L.E.3    Holmberg, M.4
  • 69
    • 77949328686 scopus 로고    scopus 로고
    • Post-translational stability of the heme biosynthetic enzyme ferrochelatase is dependent on iron availability and intact iron-sulfur cluster assembly machinery
    • Crooks, D. R., Ghosh, M. C., Haller, R. G., Tong, W. H., and Rouault, T. A. (2010) Post-translational stability of the heme biosynthetic enzyme ferrochelatase is dependent on iron availability and intact iron-sulfur cluster assembly machinery Blood 115, 860-869
    • (2010) Blood , vol.115 , pp. 860-869
    • Crooks, D.R.1    Ghosh, M.C.2    Haller, R.G.3    Tong, W.H.4    Rouault, T.A.5
  • 70
  • 71
    • 70449536411 scopus 로고    scopus 로고
    • Antisense oligonucleotide therapeutics for iron-sulphur cluster deficiency myopathy
    • Kollberg, G. and Holme, E. (2009) Antisense oligonucleotide therapeutics for iron-sulphur cluster deficiency myopathy Neuromuscular Disord. 19, 833-836
    • (2009) Neuromuscular Disord. , vol.19 , pp. 833-836
    • Kollberg, G.1    Holme, E.2
  • 72
    • 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. (2000) Human ABC7 transporter: Gene structure and mutation causing X-linked sideroblastic anemia with ataxia with disruption of cytosolic iron-sulfur protein maturation Blood 96, 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
  • 73
    • 0035002973 scopus 로고    scopus 로고
    • Mitochondrial ABC transporters
    • Lill, R. and Kispal, G. (2001) Mitochondrial ABC transporters Res. Microbiol. 152, 331-340
    • (2001) Res. Microbiol. , vol.152 , pp. 331-340
    • Lill, R.1    Kispal, G.2
  • 74
    • 0032414310 scopus 로고    scopus 로고
    • Identification of a human mitochondrial ABC transporter, the functional orthologue of yeast Atm1p
    • Csere, P., Lill, R., and Kispal, G. (1998) Identification of a human mitochondrial ABC transporter, the functional orthologue of yeast Atm1p FEBS Lett. 441, 266-270
    • (1998) FEBS Lett. , vol.441 , pp. 266-270
    • Csere, P.1    Lill, R.2    Kispal, G.3
  • 75
    • 0031569858 scopus 로고    scopus 로고
    • Isolation and chromosomal mapping of a novel ATP-binding cassette transporter conserved in mouse and human
    • Savary, S., Allikmets, R., Denizot, F., Luciani, M. F., Mattei, M. G., Dean, M., and Chimini, G. (1997) Isolation and chromosomal mapping of a novel ATP-binding cassette transporter conserved in mouse and human Genomics 41, 275-278
    • (1997) Genomics , vol.41 , pp. 275-278
    • Savary, S.1    Allikmets, R.2    Denizot, F.3    Luciani, M.F.4    Mattei, M.G.5    Dean, M.6    Chimini, G.7
  • 78
    • 70349649362 scopus 로고    scopus 로고
    • An allelic mutant series of ATM3 reveals its key role in the biogenesis of cytosolic iron-sulfur proteins in Arabidopsis
    • Bernard, D. G., Cheng, Y., Zhao, Y., and Balk, J. (2009) An allelic mutant series of ATM3 reveals its key role in the biogenesis of cytosolic iron-sulfur proteins in Arabidopsis Plant Physiol. 151, 590-602
    • (2009) Plant Physiol. , vol.151 , pp. 590-602
    • Bernard, D.G.1    Cheng, Y.2    Zhao, Y.3    Balk, J.4
  • 80
    • 74849109450 scopus 로고    scopus 로고
    • Systematic molecular genetic analysis of congenital sideroblastic anemia: Evidence for genetic heterogeneity and identification of novel mutations
    • Bergmann, A. K., Campagna, D. R., McLoughlin, E. M., Agarwal, S., Fleming, M. D., Bottomley, S. S., and Neufeld, E. J. (2010) Systematic molecular genetic analysis of congenital sideroblastic anemia: Evidence for genetic heterogeneity and identification of novel mutations Pediatr. Blood Cancer 54, 273-278
    • (2010) Pediatr. Blood Cancer , vol.54 , pp. 273-278
    • Bergmann, A.K.1    Campagna, D.R.2    McLoughlin, E.M.3    Agarwal, S.4    Fleming, M.D.5    Bottomley, S.S.6    Neufeld, E.J.7
  • 82
    • 0022387391 scopus 로고
    • Diabetes mellitus, thiamine-dependent megaloblastic anemia, and sensorineural deafness associated with deficient α-ketoglutarate dehydrogenase activity
    • Abboud, M. R., Alexander, D., and Najjar, S. S. (1985) Diabetes mellitus, thiamine-dependent megaloblastic anemia, and sensorineural deafness associated with deficient α-ketoglutarate dehydrogenase activity J. Pediatr. 107, 537-541
    • (1985) J. Pediatr. , vol.107 , pp. 537-541
    • Abboud, M.R.1    Alexander, D.2    Najjar, S.S.3
  • 83
    • 0037944100 scopus 로고    scopus 로고
    • Involvement of ABC7 in the biosynthesis of heme in erythroid cells: Interaction of ABC7 with ferrochelatase
    • Taketani, S., Kakimoto, K., Ueta, H., Masaki, R., and Furukawa, T. (2003) Involvement of ABC7 in the biosynthesis of heme in erythroid cells: Interaction of ABC7 with ferrochelatase Blood 101, 3274-3280
    • (2003) Blood , vol.101 , pp. 3274-3280
    • Taketani, S.1    Kakimoto, K.2    Ueta, H.3    Masaki, R.4    Furukawa, T.5
  • 84
    • 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. (2007) Abcb7, the gene responsible for X-linked sideroblastic anemia with ataxia, is essential for hematopoiesis Blood 109, 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
  • 85
    • 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. (1999) Mutation of a putative mitochondrial iron transporter gene (ABC7) in X-linked sideroblastic anemia and ataxia (XLSA/A) Hum. Mol. Genet. 8, 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
  • 86
    • 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. (2001) X-linked cerebellar ataxia and sideroblastic anaemia associated with a missense mutation in the ABC7 gene predicting V411L Br. J. Haematol. 115, 910-917
    • (2001) Br. J. Haematol. , vol.115 , pp. 910-917
    • Maguire, A.1    Hellier, K.2    Hammans, S.3    May, A.4
  • 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. (2007) RNA silencing of the mitochondrial ABCB7 transporter in HeLa cells causes an iron-deficient phenotype with mitochondrial iron overload Blood 109, 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
    • 33947624626 scopus 로고    scopus 로고
    • The iron-sulfur cluster proteins Isa1 and Isa2 are required for the function but not for the de novo synthesis of the Fe/S clusters of biotin synthase in Saccharomyces cerevisiae
    • DOI 10.1128/EC.00191-06
    • Muhlenhoff, U., Gerl, M. J., Flauger, B., Pirner, H. M., Balser, S., Richhardt, N., Lill, R., and Stolz, J. (2007) The ISC [corrected] proteins Isa1 and Isa2 are required for the function but not for the de novo synthesis of the Fe/S clusters of biotin synthase in Saccharomyces cerevisiae Eukaryotic Cell 6, 495-504 (Pubitemid 46492337)
    • (2007) Eukaryotic Cell , vol.6 , Issue.3 , pp. 495-504
    • Muhlenhoff, U.1    Gerl, M.J.2    Flauger, B.3    Pirner, H.M.4    Baiser, S.5    Richhardt, N.6    Lill, R.7    Stolz, J.8
  • 89
    • 0035504444 scopus 로고    scopus 로고
    • The phylogenetic distribution of frataxin indicates a role in iron-sulfur cluster protein assembly
    • Huynen, M. A., Snel, B., Bork, P., and Gibson, T. J. (2001) The phylogenetic distribution of frataxin indicates a role in iron-sulfur cluster protein assembly Hum. Mol. Genet. 10, 2463-2468
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 2463-2468
    • Huynen, M.A.1    Snel, B.2    Bork, P.3    Gibson, T.J.4
  • 90
    • 0141533145 scopus 로고    scopus 로고
    • Identification of a novel candidate gene in the iron-sulfur pathway implicated in ataxia-susceptibility: Human gene encoding HscB, a J-type co-chaperone
    • Sun, G., Gargus, J. J., Ta, D. T., and Vickery, L. E. (2003) Identification of a novel candidate gene in the iron-sulfur pathway implicated in ataxia-susceptibility: Human gene encoding HscB, a J-type co-chaperone J. Hum. Genet. 48, 415-419
    • (2003) J. Hum. Genet. , vol.48 , pp. 415-419
    • Sun, G.1    Gargus, J.J.2    Ta, D.T.3    Vickery, L.E.4
  • 91
    • 0034671178 scopus 로고    scopus 로고
    • Crystal structure of Hsc20, a J-type Co-chaperone from Escherichia coli
    • Cupp-Vickery, J. R. and Vickery, L. E. (2000) Crystal structure of Hsc20, a J-type Co-chaperone from Escherichia coli J. Mol. Biol. 304, 835-845
    • (2000) J. Mol. Biol. , vol.304 , pp. 835-845
    • Cupp-Vickery, J.R.1    Vickery, L.E.2
  • 92
    • 0028149374 scopus 로고
    • Erythropoietic protoporphyria
    • Todd, D. J. (1994) Erythropoietic protoporphyria Br. J. Dermatol. 131, 751-766
    • (1994) Br. J. Dermatol. , vol.131 , pp. 751-766
    • Todd, D.J.1
  • 94
    • 54349118938 scopus 로고    scopus 로고
    • Iron-sulfur cluster biogenesis systems and their crosstalk
    • Xu, X. M. and Moller, S. G. (2008) Iron-sulfur cluster biogenesis systems and their crosstalk ChemBioChem 9, 2355-2362
    • (2008) ChemBioChem , vol.9 , pp. 2355-2362
    • Xu, X.M.1    Moller, S.G.2
  • 95
    • 33745213111 scopus 로고    scopus 로고
    • CpNifS-dependent iron-sulfur cluster biogenesis in chloroplasts
    • Ye, H., Pilon, M., and Pilon-Smits, E. A. (2006) CpNifS-dependent iron-sulfur cluster biogenesis in chloroplasts New Phytol. 171, 285-292
    • (2006) New Phytol. , vol.171 , pp. 285-292
    • Ye, H.1    Pilon, M.2    Pilon-Smits, E.A.3
  • 96
    • 21444455377 scopus 로고    scopus 로고
    • Biogenesis of iron-sulfur proteins in plants
    • Balk, J. and Lobreaux, S. (2005) Biogenesis of iron-sulfur proteins in plants Trends Plant Sci. 10, 324-331
    • (2005) Trends Plant Sci. , vol.10 , pp. 324-331
    • Balk, J.1    Lobreaux, S.2
  • 97
    • 52049116969 scopus 로고    scopus 로고
    • Genome analysis of Chlamydomonas reinhardtii reveals the existence of multiple, compartmentalized iron-sulfur protein assembly machineries of different evolutionary origins
    • Godman, J. and Balk, J. (2008) Genome analysis of Chlamydomonas reinhardtii reveals the existence of multiple, compartmentalized iron-sulfur protein assembly machineries of different evolutionary origins Genetics 179, 59-68
    • (2008) Genetics , vol.179 , pp. 59-68
    • Godman, J.1    Balk, J.2
  • 98
    • 58149092094 scopus 로고    scopus 로고
    • The essential cytosolic iron-sulfur protein Nbp35 acts without Cfd1 partner in the green lineage
    • Bych, K., Netz, D. J., Vigani, G., Bill, E., Lill, R., Pierik, A. J., and Balk, J. (2008) The essential cytosolic iron-sulfur protein Nbp35 acts without Cfd1 partner in the green lineage J. Biol. Chem. 283, 35797-35804
    • (2008) J. Biol. Chem. , vol.283 , pp. 35797-35804
    • Bych, K.1    Netz, D.J.2    Vigani, G.3    Bill, E.4    Lill, R.5    Pierik, A.J.6    Balk, J.7
  • 99
    • 70350576223 scopus 로고    scopus 로고
    • An E3 ligase possessing an iron-responsive hemerythrin domain is a regulator of iron homeostasis
    • Salahudeen, A. A., Thompson, J. W., Ruiz, J. C., Ma, H. W., Kinch, L. N., Li, Q., Grishin, N. V., and Bruick, R. K. (2009) An E3 ligase possessing an iron-responsive hemerythrin domain is a regulator of iron homeostasis Science 326, 722-726
    • (2009) Science , vol.326 , pp. 722-726
    • Salahudeen, A.A.1    Thompson, J.W.2    Ruiz, J.C.3    Ma, H.W.4    Kinch, L.N.5    Li, Q.6    Grishin, N.V.7    Bruick, R.K.8
  • 101
    • 70350588653 scopus 로고    scopus 로고
    • Cell biology. An ancient gauge for iron
    • Rouault, T. A. (2009) Cell biology. An ancient gauge for iron Science 326, 676-677
    • (2009) Science , vol.326 , pp. 676-677
    • Rouault, T.A.1
  • 102
    • 67549136242 scopus 로고    scopus 로고
    • Mitochondrial dysfunction leads to nuclear genome instability via an iron-sulfur cluster defect
    • Veatch, J. R., McMurray, M. A., Nelson, Z. W., and Gottschling, D. E. (2009) Mitochondrial dysfunction leads to nuclear genome instability via an iron-sulfur cluster defect Cell 137, 1247-1258
    • (2009) Cell , vol.137 , pp. 1247-1258
    • Veatch, J.R.1    McMurray, M.A.2    Nelson, Z.W.3    Gottschling, D.E.4
  • 103
    • 0030608677 scopus 로고    scopus 로고
    • The ABC transporter Atm1p is required for mitochondrial iron homeostasis
    • Kispal, G., Csere, P., Guiard, B., and Lill, R. (1997) The ABC transporter Atm1p is required for mitochondrial iron homeostasis FEBS Lett. 418, 346-350
    • (1997) FEBS Lett. , vol.418 , pp. 346-350
    • Kispal, G.1    Csere, P.2    Guiard, B.3    Lill, R.4
  • 104
    • 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. (1999) The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins EMBO J. 18, 3981-3989
    • (1999) EMBO J. , vol.18 , pp. 3981-3989
    • Kispal, G.1    Csere, P.2    Prohl, C.3    Lill, R.4
  • 105
    • 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. (2002) 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, 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
  • 106
    • 33748428875 scopus 로고    scopus 로고
    • The DNA repair helicases XPD and FancJ have essential iron-sulfur domains
    • Rudolf, J., Makrantoni, V., Ingledew, W. J., Stark, M. J., and White, M. F. (2006) The DNA repair helicases XPD and FancJ have essential iron-sulfur domains Mol. Cell 23, 801-808
    • (2006) Mol. Cell , vol.23 , pp. 801-808
    • Rudolf, J.1    Makrantoni, V.2    Ingledew, W.J.3    Stark, M.J.4    White, M.F.5
  • 107
    • 34548492954 scopus 로고    scopus 로고
    • An iron-sulfur domain of the eukaryotic primase is essential for RNA primer synthesis
    • Klinge, S., Hirst, J., Maman, J. D., Krude, T., and Pellegrini, L. (2007) An iron-sulfur domain of the eukaryotic primase is essential for RNA primer synthesis Nat. Struct. Mol. Biol. 14, 875-877
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 875-877
    • Klinge, S.1    Hirst, J.2    Maman, J.D.3    Krude, T.4    Pellegrini, L.5
  • 108
    • 0035896520 scopus 로고    scopus 로고
    • Mitochondrial control of iron homeostasis. A genome wide analysis of gene expression in a yeast frataxin-deficient strain
    • Foury, F. and Talibi, D. (2001) Mitochondrial control of iron homeostasis. A genome wide analysis of gene expression in a yeast frataxin-deficient strain J. Biol. Chem. 276, 7762-7768
    • (2001) J. Biol. Chem. , vol.276 , pp. 7762-7768
    • Foury, F.1    Talibi, D.2
  • 109
    • 0035896587 scopus 로고    scopus 로고
    • Nuclear localization of yeast Nfs1p is required for cell survival
    • Nakai, Y., Nakai, M., Hayashi, H., and Kagamiyama, H. (2001) Nuclear localization of yeast Nfs1p is required for cell survival J. Biol. Chem. 276, 8314-8320
    • (2001) J. Biol. Chem. , vol.276 , pp. 8314-8320
    • Nakai, Y.1    Nakai, M.2    Hayashi, H.3    Kagamiyama, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.