메뉴 건너뛰기




Volumn 24, Issue 8, 2008, Pages 398-407

Iron-sulfur cluster biogenesis and human disease

Author keywords

[No Author keywords available]

Indexed keywords

ACONITATE HYDRATASE; CARRIER PROTEIN; FRATAXIN; GLUTAREDOXIN; IRON SULFUR PROTEIN; PROTEIN ABCB7;

EID: 47249142777     PISSN: 01689525     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tig.2008.05.008     Document Type: Review
Times cited : (329)

References (81)
  • 1
    • 20744446399 scopus 로고    scopus 로고
    • Structure, function, and formation of biological iron-sulfur clusters
    • Johnson D.C., et al. 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
  • 2
    • 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
  • 3
    • 33748428875 scopus 로고    scopus 로고
    • The DNA repair helicases XPD and FancJ have essential iron-sulfur domains
    • Rudolf J., et al. The DNA repair helicases XPD and FancJ have essential iron-sulfur domains. Mol. Cell 23 (2006) 801-808
    • (2006) Mol. Cell , vol.23 , pp. 801-808
    • Rudolf, J.1
  • 4
    • 33746864096 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron homeostasis by iron regulatory proteins
    • Wallander M.L., et al. Molecular control of vertebrate iron homeostasis by iron regulatory proteins. Biochim. Biophys. Acta 1763 (2006) 668-689
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 668-689
    • Wallander, M.L.1
  • 5
    • 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
  • 6
    • 38449094356 scopus 로고    scopus 로고
    • Iron-regulatory proteins: molecular biology and pathophysiological implications
    • Cairo G., and Recalcati S. Iron-regulatory proteins: molecular biology and pathophysiological implications. Expert Rev. Mol. Med. 9 (2007) 1-13
    • (2007) Expert Rev. Mol. Med. , vol.9 , pp. 1-13
    • Cairo, G.1    Recalcati, S.2
  • 7
    • 34548388956 scopus 로고    scopus 로고
    • Advancements in the pathophysiology of Friedreich's Ataxia and new prospects for treatments
    • Babady N.E., et al. Advancements in the pathophysiology of Friedreich's Ataxia and new prospects for treatments. Mol. Genet. Metab. 92 (2007) 23-35
    • (2007) Mol. Genet. Metab. , vol.92 , pp. 23-35
    • Babady, N.E.1
  • 8
    • 34548013116 scopus 로고    scopus 로고
    • The human counterpart of zebrafish shiraz shows sideroblastic-like microcytic anemia and iron overload
    • Camaschella C., et al. The human counterpart of zebrafish shiraz shows sideroblastic-like microcytic anemia and iron overload. Blood 110 (2007) 1353-1358
    • (2007) Blood , vol.110 , pp. 1353-1358
    • Camaschella, C.1
  • 9
    • 41149169596 scopus 로고    scopus 로고
    • Splice mutation in the iron-sulfur cluster scaffold protein ISCU causes myopathy with exercise intolerance
    • Mochel F., et al. Splice mutation in the iron-sulfur cluster scaffold protein ISCU causes myopathy with exercise intolerance. Am. J. Hum. Genet. 82 (2008) 652-660
    • (2008) Am. J. Hum. Genet. , vol.82 , pp. 652-660
    • Mochel, F.1
  • 10
    • 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., et al. 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 (2008) 1666-1672
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 1666-1672
    • Olsson, A.1
  • 11
    • 34249713769 scopus 로고    scopus 로고
    • On the chemistry and evolution of the pioneer organism
    • Wachtershauser G. On the chemistry and evolution of the pioneer organism. Chem. Biodivers. 4 (2007) 584-602
    • (2007) Chem. Biodivers. , vol.4 , pp. 584-602
    • Wachtershauser, G.1
  • 12
    • 17144378216 scopus 로고    scopus 로고
    • Opinion: Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis
    • Rouault T.A., and Tong W.H. Opinion: 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
    • 33747621648 scopus 로고    scopus 로고
    • The structure and function of frataxin
    • Bencze K.Z., et al. The structure and function of frataxin. Crit. Rev. Biochem. Mol. Biol. 41 (2006) 269-291
    • (2006) Crit. Rev. Biochem. Mol. Biol. , vol.41 , pp. 269-291
    • Bencze, K.Z.1
  • 14
    • 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., et al. 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 16 (2004) 993-1007
    • (2004) Plant Cell , vol.16 , pp. 993-1007
    • Yabe, T.1
  • 15
    • 34250192575 scopus 로고    scopus 로고
    • Formation and properties of [4Fe-4S] clusters on the IscU scaffold protein
    • Chandramouli K., et al. Formation and properties of [4Fe-4S] clusters on the IscU scaffold protein. Biochemistry 46 (2007) 6804-6811
    • (2007) Biochemistry , vol.46 , pp. 6804-6811
    • Chandramouli, K.1
  • 16
    • 30444433568 scopus 로고    scopus 로고
    • The Nfs1 interacting protein Isd11 has an essential role in Fe/S cluster biogenesis in mitochondria
    • Adam A.C., et al. 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
  • 17
    • 30444449009 scopus 로고    scopus 로고
    • Essential role of Isd11 in mitochondrial iron-sulfur cluster synthesis on Isu scaffold proteins
    • Wiedemann N., et al. Essential role of Isd11 in mitochondrial iron-sulfur cluster synthesis on Isu scaffold proteins. EMBO J. 25 (2006) 184-195
    • (2006) EMBO J. , vol.25 , pp. 184-195
    • Wiedemann, N.1
  • 18
    • 34447316711 scopus 로고    scopus 로고
    • Mitochondrial frataxin interacts with ISD11 of the NFS1/ISCU complex and multiple mitochondrial chaperones
    • Shan Y., et al. Mitochondrial frataxin interacts with ISD11 of the NFS1/ISCU complex and multiple mitochondrial chaperones. Hum. Mol. Genet. 16 (2007) 929-941
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 929-941
    • Shan, Y.1
  • 19
    • 0036226063 scopus 로고    scopus 로고
    • Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes
    • Rodriguez-Manzaneque M.T., et al. 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
  • 20
    • 23944500052 scopus 로고    scopus 로고
    • Deficiency of glutaredoxin 5 reveals Fe-S clusters are required for vertebrate haem synthesis
    • Wingert R.A., et al. Deficiency of glutaredoxin 5 reveals Fe-S clusters are required for vertebrate haem synthesis. Nature 436 (2005) 1035-1039
    • (2005) Nature , vol.436 , pp. 1035-1039
    • Wingert, R.A.1
  • 21
    • 44049094146 scopus 로고    scopus 로고
    • A Role for IOP1 in Mammalian Cytosolic Iron-Sulfur Protein Biogenesis
    • Song D., and Lee F.S. A Role for IOP1 in Mammalian Cytosolic Iron-Sulfur Protein Biogenesis. J. Biol. Chem. 283 (2008) 9231-9238
    • (2008) J. Biol. Chem. , vol.283 , pp. 9231-9238
    • Song, D.1    Lee, F.S.2
  • 22
    • 0034775927 scopus 로고    scopus 로고
    • Ferredoxin reductase affects p53-dependent, 5-fluorouracil-induced apoptosis in colorectal cancer cells
    • Hwang P.M., et al. Ferredoxin reductase affects p53-dependent, 5-fluorouracil-induced apoptosis in colorectal cancer cells. Nat. Med. 7 (2001) 1111-1117
    • (2001) Nat. Med. , vol.7 , pp. 1111-1117
    • Hwang, P.M.1
  • 23
    • 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
  • 24
    • 33748745666 scopus 로고    scopus 로고
    • RNA silencing of mitochondrial m-Nfs1 reduces Fe-S enzyme activity both in mitochondria and cytosol of mammalian cells
    • Fosset C., et al. RNA silencing of mitochondrial m-Nfs1 reduces Fe-S enzyme activity both in mitochondria and cytosol of mammalian cells. J. Biol. Chem. 281 (2006) 25398-25406
    • (2006) J. Biol. Chem. , vol.281 , pp. 25398-25406
    • Fosset, C.1
  • 25
    • 0032710401 scopus 로고    scopus 로고
    • Friedreich's ataxia: clinical aspects and pathogenesis
    • Pandolfo M. Friedreich's ataxia: clinical aspects and pathogenesis. Semin. Neurol. 19 (1999) 311-321
    • (1999) Semin. Neurol. , vol.19 , pp. 311-321
    • Pandolfo, M.1
  • 26
    • 13344270899 scopus 로고    scopus 로고
    • Friedreich's ataxia: autosomal recessive disease caused by an intronic GAA triplet repeat expansion
    • Campuzano V., et al. Friedreich's ataxia: autosomal recessive disease caused by an intronic GAA triplet repeat expansion. Science 271 (1996) 1423-1427
    • (1996) Science , vol.271 , pp. 1423-1427
    • Campuzano, V.1
  • 27
    • 33846815260 scopus 로고    scopus 로고
    • Progressive GAA expansions in dorsal root ganglia of Friedreich's ataxia patients
    • De Biase I., et al. Progressive GAA expansions in dorsal root ganglia of Friedreich's ataxia patients. Ann. Neurol. 61 (2007) 55-60
    • (2007) Ann. Neurol. , vol.61 , pp. 55-60
    • De Biase, I.1
  • 28
    • 33748778745 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors reverse gene silencing in Friedreich's ataxia
    • Herman D., et al. Histone deacetylase inhibitors reverse gene silencing in Friedreich's ataxia. Nat. Chem. Biol. 2 (2006) 551-558
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 551-558
    • Herman, D.1
  • 29
    • 0031253821 scopus 로고    scopus 로고
    • Aconitase and mitochondrial iron-sulphur protein deficiency in Friedreich ataxia
    • Rotig A., et al. Aconitase and mitochondrial iron-sulphur protein deficiency in Friedreich ataxia. Nat. Genet. 17 (1997) 215-217
    • (1997) Nat. Genet. , vol.17 , pp. 215-217
    • Rotig, A.1
  • 30
    • 14044273058 scopus 로고    scopus 로고
    • Friedreich ataxia: the oxidative stress paradox
    • Seznec H., et al. Friedreich ataxia: the oxidative stress paradox. Hum. Mol. Genet. 14 (2005) 463-474
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 463-474
    • Seznec, H.1
  • 31
    • 34547760795 scopus 로고    scopus 로고
    • Understanding the binding properties of an unusual metal-binding protein-a study of bacterial frataxin
    • Pastore C., et al. Understanding the binding properties of an unusual metal-binding protein-a study of bacterial frataxin. FEBS J. 274 (2007) 4199-4210
    • (2007) FEBS J. , vol.274 , pp. 4199-4210
    • Pastore, C.1
  • 32
    • 39149096860 scopus 로고    scopus 로고
    • The effects of frataxin silencing in HeLa cells are rescued by the expression of human mitochondrial ferritin
    • Zanella I., et al. The effects of frataxin silencing in HeLa cells are rescued by the expression of human mitochondrial ferritin. Biochim. Biophys. Acta 1782 (2008) 90-98
    • (2008) Biochim. Biophys. Acta , vol.1782 , pp. 90-98
    • Zanella, I.1
  • 33
    • 31544445770 scopus 로고    scopus 로고
    • Mitochondrial iron detoxification is a primary function of frataxin that limits oxidative damage and preserves cell longevity
    • Gakh O., et al. 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
  • 34
    • 45549107531 scopus 로고    scopus 로고
    • Binding of yeast frataxin to the scaffold for Fe-S cluster biogenesis, isu
    • Wang T., and Craig E.A. Binding of yeast frataxin to the scaffold for Fe-S cluster biogenesis, isu. J. Biol. Chem. 283 (2008) 12674-12679
    • (2008) J. Biol. Chem. , vol.283 , pp. 12674-12679
    • Wang, T.1    Craig, E.A.2
  • 35
    • 33845337036 scopus 로고    scopus 로고
    • Iron and iron-responsive proteins in the cardiomyopathy of Friedreich's ataxia
    • Michael S., et al. Iron and iron-responsive proteins in the cardiomyopathy of Friedreich's ataxia. Cerebellum 5 (2006) 257-267
    • (2006) Cerebellum , vol.5 , pp. 257-267
    • Michael, S.1
  • 36
    • 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., et al. 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
  • 37
    • 38649103446 scopus 로고    scopus 로고
    • Hydrogen peroxide scavenging rescues frataxin deficiency in a Drosophila model of Friedreich's ataxia
    • Anderson P.R., et al. 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
  • 38
    • 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. Mitochondrial control of iron homeostasis. A genome wide analysis of gene expression in a yeast frataxin-deficient strain. J. Biol. Chem. 276 (2001) 7762-7768
    • (2001) J. Biol. Chem. , vol.276 , pp. 7762-7768
    • Foury, F.1    Talibi, D.2
  • 39
    • 29644442275 scopus 로고    scopus 로고
    • Frataxin deficiency alters heme pathway transcripts and decreases mitochondrial heme metabolites in mammalian cells
    • Schoenfeld R.A., et al. Frataxin deficiency alters heme pathway transcripts and decreases mitochondrial heme metabolites in mammalian cells. Hum. Mol. Genet. 14 (2005) 3787-3799
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 3787-3799
    • Schoenfeld, R.A.1
  • 40
    • 47249127786 scopus 로고    scopus 로고
    • Iron-dependent regulation of frataxin expression: implications for treatment of Friedreich ataxia
    • 10.1093/hmg/ddn127
    • Li K., et al. Iron-dependent regulation of frataxin expression: implications for treatment of Friedreich ataxia. Hum. Mol. Genet. (2008) 10.1093/hmg/ddn127
    • (2008) Hum. Mol. Genet.
    • Li, K.1
  • 41
    • 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
  • 42
    • 34250731291 scopus 로고    scopus 로고
    • Monothiol glutaredoxins: a common domain for multiple functions
    • Herrero E., and de la Torre-Ruiz M.A. Monothiol glutaredoxins: a common domain for multiple functions. Cell. Mol. Life Sci. 64 (2007) 1518-1530
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 1518-1530
    • Herrero, E.1    de la Torre-Ruiz, M.A.2
  • 43
    • 41949108097 scopus 로고    scopus 로고
    • Chloroplast monothiol glutaredoxins as scaffold proteins for the assembly and delivery of [2Fe-2S] clusters
    • Bandyopadhyay S., et al. Chloroplast monothiol glutaredoxins as scaffold proteins for the assembly and delivery of [2Fe-2S] clusters. EMBO J. 27 (2008) 1122-1133
    • (2008) EMBO J. , vol.27 , pp. 1122-1133
    • Bandyopadhyay, S.1
  • 44
    • 33644804529 scopus 로고    scopus 로고
    • Crystal structure of human iron regulatory protein 1 as cytosolic aconitase
    • Dupuy J., et al. Crystal structure of human iron regulatory protein 1 as cytosolic aconitase. Structure 14 (2006) 129-139
    • (2006) Structure , vol.14 , pp. 129-139
    • Dupuy, J.1
  • 45
    • 33845865301 scopus 로고    scopus 로고
    • Structure of dual function iron regulatory protein 1 complexed with ferritin IRE-RNA
    • Walden W.E., et al. Structure of dual function iron regulatory protein 1 complexed with ferritin IRE-RNA. Science 314 (2006) 1903-1908
    • (2006) Science , vol.314 , pp. 1903-1908
    • Walden, W.E.1
  • 46
    • 23044503950 scopus 로고    scopus 로고
    • Microcytic anemia, erythropoietic protoporphyria, and neurodegeneration in mice with targeted deletion of iron-regulatory protein 2
    • Cooperman S.S., et al. Microcytic anemia, erythropoietic protoporphyria, and neurodegeneration in mice with targeted deletion of iron-regulatory protein 2. Blood 106 (2005) 1084-1091
    • (2005) Blood , vol.106 , pp. 1084-1091
    • Cooperman, S.S.1
  • 47
    • 27144467097 scopus 로고    scopus 로고
    • Altered body iron distribution and microcytosis in mice deficient in iron regulatory protein 2 (IRP2)
    • Galy B., et al. Altered body iron distribution and microcytosis in mice deficient in iron regulatory protein 2 (IRP2). Blood 106 (2005) 2580-2589
    • (2005) Blood , vol.106 , pp. 2580-2589
    • Galy, B.1
  • 48
    • 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. Targeting of a human iron-sulfur cluster assembly enzyme, nifs, to different subcellular compartments is regulated through alternative AUG utilization. Mol. Cell 2 (1998) 807-815
    • (1998) Mol. Cell , vol.2 , pp. 807-815
    • Land, T.1    Rouault, T.A.2
  • 49
    • 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., et al. 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 (2003) 9762-9767
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 9762-9767
    • Tong, W.H.1
  • 50
    • 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., et al. 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 (2005) 3917-3924
    • (2005) J. Cell Sci. , vol.118 , pp. 3917-3924
    • Acquaviva, F.1
  • 51
    • 33745222541 scopus 로고    scopus 로고
    • A pool of extramitochondrial frataxin that promotes cell survival
    • Condo I., et al. A pool of extramitochondrial frataxin that promotes cell survival. J. Biol. Chem. 281 (2006) 16750-16756
    • (2006) J. Biol. Chem. , vol.281 , pp. 16750-16756
    • Condo, I.1
  • 52
    • 41649116646 scopus 로고    scopus 로고
    • Localization and functionality of microsporidian iron-sulphur cluster assembly proteins
    • Goldberg A.V., et al. Localization and functionality of microsporidian iron-sulphur cluster assembly proteins. Nature 452 (2008) 624-628
    • (2008) Nature , vol.452 , pp. 624-628
    • Goldberg, A.V.1
  • 53
    • 0032540929 scopus 로고    scopus 로고
    • Mt-Hsp70 homolog, Ssc2p, required for maturation of yeast frataxin and mitochondrial iron homeostasis
    • Knight S.A., et al. Mt-Hsp70 homolog, Ssc2p, required for maturation of yeast frataxin and mitochondrial iron homeostasis. J. Biol. Chem. 273 (1998) 18389-18393
    • (1998) J. Biol. Chem. , vol.273 , pp. 18389-18393
    • Knight, S.A.1
  • 54
    • 0025951154 scopus 로고
    • Deficiency of skeletal muscle succinate dehydrogenase and aconitase. Pathophysiology of exercise in a novel human muscle oxidative defect
    • Haller R.G., et al. Deficiency of skeletal muscle succinate dehydrogenase and aconitase. Pathophysiology of exercise in a novel human muscle oxidative defect. J. Clin. Invest. 88 (1991) 1197-1206
    • (1991) J. Clin. Invest. , vol.88 , pp. 1197-1206
    • Haller, R.G.1
  • 55
    • 0001731713 scopus 로고
    • Hereditary metabolic myopathy with paroxysmal myoglobinuria due to abnormal glycolysis
    • Larsson L.E., et al. Hereditary metabolic myopathy with paroxysmal myoglobinuria due to abnormal glycolysis. J. Neurol. Neurosurg. Psychiatry 27 (1964) 361-380
    • (1964) J. Neurol. Neurosurg. Psychiatry , vol.27 , pp. 361-380
    • Larsson, L.E.1
  • 56
    • 0038161214 scopus 로고    scopus 로고
    • MDL1 is a high copy suppressor of ATM1: evidence for a role in resistance to oxidative stress
    • Chloupkova M., et al. MDL1 is a high copy suppressor of ATM1: evidence for a role in resistance to oxidative stress. J. Mol. Biol. 331 (2003) 155-165
    • (2003) J. Mol. Biol. , vol.331 , pp. 155-165
    • Chloupkova, M.1
  • 57
    • 0033565665 scopus 로고    scopus 로고
    • The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins
    • Kispal G., et al. 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
  • 58
    • 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., et al. 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
  • 59
    • 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., et al. The mitochondrial ATP-binding cassette transporter Abcb7 is essential in mice and participates in cytosolic iron-sulfur cluster biogenesis. Hum. Mol. Genet. 15 (2006) 953-964
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 953-964
    • Pondarre, C.1
  • 60
    • 23844558266 scopus 로고    scopus 로고
    • A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: a dawn for evolutionary medicine
    • Wallace D.C. A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: a dawn for evolutionary medicine. Annu. Rev. Genet. 39 (2005) 359-407
    • (2005) Annu. Rev. Genet. , vol.39 , pp. 359-407
    • Wallace, D.C.1
  • 61
    • 0035121867 scopus 로고    scopus 로고
    • A novel syndrome affecting multiple mitochondrial functions, located by microcell-mediated transfer to chromosome 2p14-2p13
    • Seyda A., et al. A novel syndrome affecting multiple mitochondrial functions, located by microcell-mediated transfer to chromosome 2p14-2p13. Am. J. Hum. Genet. 68 (2001) 386-396
    • (2001) Am. J. Hum. Genet. , vol.68 , pp. 386-396
    • Seyda, A.1
  • 62
    • 26244441704 scopus 로고    scopus 로고
    • A third locus for dominant optic atrophy on chromosome 22q
    • Barbet F., et al. A third locus for dominant optic atrophy on chromosome 22q. J. Med. Genet. 42 (2005) e1
    • (2005) J. Med. Genet. , vol.42
    • Barbet, F.1
  • 63
    • 33746930794 scopus 로고    scopus 로고
    • Succinate dehydrogenase and fumarate hydratase: linking mitochondrial dysfunction and cancer
    • King A., et al. Succinate dehydrogenase and fumarate hydratase: linking mitochondrial dysfunction and cancer. Oncogene 25 (2006) 4675-4682
    • (2006) Oncogene , vol.25 , pp. 4675-4682
    • King, A.1
  • 64
    • 1642498155 scopus 로고    scopus 로고
    • Ultrastructural features of bone marrow cells from patients with acquired sideroblastic anemia
    • Djaldetti M., et al. Ultrastructural features of bone marrow cells from patients with acquired sideroblastic anemia. Microsc. Res. Tech. 63 (2004) 155-158
    • (2004) Microsc. Res. Tech. , vol.63 , pp. 155-158
    • Djaldetti, M.1
  • 65
    • 0032722872 scopus 로고    scopus 로고
    • Yeast mitochondrial protein, Nfs1p, coordinately regulates iron-sulfur cluster proteins, cellular iron uptake, and iron distribution
    • Li J., et al. 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
  • 66
    • 0037173615 scopus 로고    scopus 로고
    • Functional profiling of the Saccharomyces cerevisiae genome
    • Giaever G., et al. Functional profiling of the Saccharomyces cerevisiae genome. Nature 418 (2002) 387-391
    • (2002) Nature , vol.418 , pp. 387-391
    • Giaever, G.1
  • 67
    • 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. Distinct iron-sulfur cluster assembly complexes exist in the cytosol and mitochondria of human cells. EMBO J. 19 (2000) 5692-5700
    • (2000) EMBO J. , vol.19 , pp. 5692-5700
    • Tong, W.H.1    Rouault, T.2
  • 68
    • 0033621156 scopus 로고    scopus 로고
    • Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae
    • Schilke B., et al. 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
  • 69
    • 30744458144 scopus 로고    scopus 로고
    • Reduction of Caenorhabditis elegans frataxin increases sensitivity to oxidative stress, reduces lifespan, and causes lethality in a mitochondrial complex II mutant
    • Vazquez-Manrique R.P., et al. Reduction of Caenorhabditis elegans frataxin increases sensitivity to oxidative stress, reduces lifespan, and causes lethality in a mitochondrial complex II mutant. FASEB J. 20 (2006) 172-174
    • (2006) FASEB J. , vol.20 , pp. 172-174
    • Vazquez-Manrique, R.P.1
  • 70
    • 0141737067 scopus 로고    scopus 로고
    • Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p
    • Muhlenhoff U., et al. Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p. EMBO J. 22 (2003) 4815-4825
    • (2003) EMBO J. , vol.22 , pp. 4815-4825
    • Muhlenhoff, U.1
  • 71
    • 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., et al. 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 (2003) 415-419
    • (2003) J. Hum. Genet. , vol.48 , pp. 415-419
    • Sun, G.1
  • 72
    • 44549087696 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis in bacteria: mechanisms of cluster assembly and transfer
    • 10.1016/j.abb.2007.12.014
    • Fontecave M., and Ollagnier-de-Choudens S. Iron-sulfur cluster biosynthesis in bacteria: mechanisms of cluster assembly and transfer. Arch. Biochem. Biophys. (2007) 10.1016/j.abb.2007.12.014
    • (2007) Arch. Biochem. Biophys.
    • Fontecave, M.1    Ollagnier-de-Choudens, S.2
  • 73
    • 33646241294 scopus 로고    scopus 로고
    • Regulatory roles for IscA and SufA in iron homeostasis and redox stress responses in the cyanobacterium Synechococcus sp. strain PCC 7002
    • Balasubramanian R., et al. Regulatory roles for IscA and SufA in iron homeostasis and redox stress responses in the cyanobacterium Synechococcus sp. strain PCC 7002. J. Bacteriol. 188 (2006) 3182-3191
    • (2006) J. Bacteriol. , vol.188 , pp. 3182-3191
    • Balasubramanian, R.1
  • 74
    • 34247247617 scopus 로고    scopus 로고
    • The Cfd1-Nbp35 complex acts as a scaffold for iron-sulfur protein assembly in the yeast cytosol
    • Netz D.J., et al. The Cfd1-Nbp35 complex acts as a scaffold for iron-sulfur protein assembly in the yeast cytosol. Nat. Chem. Biol. 3 (2007) 278-286
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 278-286
    • Netz, D.J.1
  • 75
    • 0141848663 scopus 로고    scopus 로고
    • A novel eukaryotic factor for cytosolic Fe-S cluster assembly
    • Roy A., et al. A novel eukaryotic factor for cytosolic Fe-S cluster assembly. EMBO J. 22 (2003) 4826-4835
    • (2003) EMBO J. , vol.22 , pp. 4826-4835
    • Roy, A.1
  • 76
    • 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., et al. 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
  • 77
    • 0030608375 scopus 로고    scopus 로고
    • NBP35 encodes an essential and evolutionary conserved protein in Saccharomyces cerevisiae with homology to a superfamily of bacterial ATPases
    • Vitale G., et al. NBP35 encodes an essential and evolutionary conserved protein in Saccharomyces cerevisiae with homology to a superfamily of bacterial ATPases. Gene 178 (1996) 97-106
    • (1996) Gene , vol.178 , pp. 97-106
    • Vitale, G.1
  • 78
    • 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., et al. 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
  • 79
    • 35148812715 scopus 로고    scopus 로고
    • Structure of the yeast WD40 domain protein Cia1, a component acting late in iron-sulfur protein biogenesis
    • Srinivasan V., et al. Structure of the yeast WD40 domain protein Cia1, a component acting late in iron-sulfur protein biogenesis. Structure 15 (2007) 1246-1257
    • (2007) Structure , vol.15 , pp. 1246-1257
    • Srinivasan, V.1
  • 80
    • 47249083098 scopus 로고    scopus 로고
    • The hydrogenase-like Nar1p is essential for maturation of cytosolic and nuclear iron-sulphur proteins
    • Balk J., et al. The hydrogenase-like Nar1p is essential for maturation of cytosolic and nuclear iron-sulphur proteins. EMBO J. 13 (2004) 773-780
    • (2004) EMBO J. , vol.13 , pp. 773-780
    • Balk, J.1
  • 81
    • 40749086415 scopus 로고    scopus 로고
    • Mitochondrial Iba57p is required for Fe/S cluster formation on aconitase and activation of radical SAM enzymes
    • Gelling C., et al. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.