메뉴 건너뛰기




Volumn 53, Issue , 2002, Pages 147-173

Friedreich's ataxia

Author keywords

[No Author keywords available]

Indexed keywords

ANTIOXIDANT; IRON CHELATING AGENT;

EID: 0036985830     PISSN: 00747742     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s0074-7742(02)53006-3     Document Type: Review
Times cited : (7)

References (120)
  • 2
    • 0034112046 scopus 로고    scopus 로고
    • Modular organization and identification of a mononuclear iron-binding site within the NifU protein
    • J.N. Agar P. Yuvaniyama R.F. Jack V.L. Cash A.D. Smith D.R. Dean Modular organization and identification of a mononuclear iron-binding site within the NifU protein J. Biol. Inorg. Chem. 5 2000 167 177
    • (2000) J. Biol. Inorg. Chem. , vol.5 , pp. 167-177
    • Agar, J.N.1    Yuvaniyama, P.2    Jack, R.F.3    Cash, V.L.4    Smith, A.D.5    Dean, D.R.6
  • 3
    • 0032920837 scopus 로고    scopus 로고
    • Mutation of a putative mitochondrial iron transporter gene (ABC7) in X-linked sideroblastic anemia and ataxia (XLSA/A)
    • R. Allikmets W.H. Raskind A. Hutchinson N.D. Schueck M. Dean D.M. Koeller 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
  • 5
    • 0032511744 scopus 로고    scopus 로고
    • Identification of a missense mutation in a Friedreich's ataxia patient: Implications for diagnosis and carrier studies
    • C. Bartolo J.R. Mendell T.W. Prior Identification of a missense mutation in a Friedreich's ataxia patient: Implications for diagnosis and carrier studies Am. J. Med. Genet. 79 1998 396 399
    • (1998) Am. J. Med. Genet. , vol.79 , pp. 396-399
    • Bartolo, C.1    Mendell, J.R.2    Prior, T.W.3
  • 6
    • 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
    • S. Bekri G. Kispal H. Lange E. Fitzsimons J. Tolmie R. Lill 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
  • 7
    • 0031154432 scopus 로고    scopus 로고
    • Intronic GAA triplet repeat expansion in Friedreich's ataxia presenting with pure sensory ataxia
    • J. Berciano O. Combarros M. De Castro F. Palau Intronic GAA triplet repeat expansion in Friedreich's ataxia presenting with pure sensory ataxia J. Neurol. 244 1997 390 391
    • (1997) J. Neurol. , vol.244 , pp. 390-391
    • Berciano, J.1    Combarros, O.2    De Castro, M.3    Palau, F.4
  • 8
    • 0030895266 scopus 로고    scopus 로고
    • Atypical Friedreich ataxia caused by compound heterozygosity for a novel missense mutation and the GAA triplet repeat expansion
    • S.I. Bidichandani T. Ashizawa P.I. Patel Atypical Friedreich ataxia caused by compound heterozygosity for a novel missense mutation and the GAA triplet repeat expansion Am. J. Hum. Genet. 60 1997 1251 1256
    • (1997) Am. J. Hum. Genet. , vol.60 , pp. 1251-1256
    • Bidichandani, S.I.1    Ashizawa, T.2    Patel, P.I.3
  • 9
    • 0031941447 scopus 로고    scopus 로고
    • The GAA triplet-repeat expansion Friedreich's ataxia interferes with transcription and may be associated with an unusual DNA structure
    • S.I. Bidichandani T. Ashizawa P.I. Patel The GAA triplet-repeat expansion Friedreich's ataxia interferes with transcription and may be associated with an unusual DNA structure Am. J. Hum. Genet. 62 1998 111 121
    • (1998) Am. J. Hum. Genet. , vol.62 , pp. 111-121
    • Bidichandani, S.I.1    Ashizawa, T.2    Patel, P.I.3
  • 10
    • 0032739342 scopus 로고    scopus 로고
    • Somatic sequence variation and the Friedreich's ataxia locus includes complete contraction of the expanded GAA triplet repeat, significant length variation in serially passaged lymphoblasts and enhanced mutagenesis in the flanking sequence
    • S.I. Bidichandani S.M. Purandare E.E. Taylor G. Gumin H. Machkhas Y. Harati Somatic sequence variation and the Friedreich's ataxia locus includes complete contraction of the expanded GAA triplet repeat, significant length variation in serially passaged lymphoblasts and enhanced mutagenesis in the flanking sequence Hum. Mol. Genet. 8 1999 2425 2436
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 2425-2436
    • Bidichandani, S.I.1    Purandare, S.M.2    Taylor, E.E.3    Gumin, G.4    Machkhas, H.5    Harati, Y.6
  • 11
    • 0033951420 scopus 로고    scopus 로고
    • Very late onset Friedreich's ataxia despite large GAA triplet repeat expansions
    • S.I. Bidichandani C.A. Garcia P.I. Patel M.M. Dimachkie Very late onset Friedreich's ataxia despite large GAA triplet repeat expansions Arch. Neurol. 57 2000 246 251
    • (2000) Arch. Neurol. , vol.57 , pp. 246-251
    • Bidichandani, S.I.1    Garcia, C.A.2    Patel, P.I.3    Dimachkie, M.M.4
  • 14
    • 0033529554 scopus 로고    scopus 로고
    • Yeast and human frataxin are processed to the mature form in two sequential steps by the mitochondrial processing peptidase
    • S.S. Branda P. Cavadini J. Adamec F. Kalousek F. Taroni G. Isaya Yeast and human frataxin are processed to the mature form in two sequential steps by the mitochondrial processing peptidase J. Biol. Chem. 274 1999 22763 22769
    • (1999) J. Biol. Chem. , vol.274 , pp. 22763-22769
    • Branda, S.S.1    Cavadini, P.2    Adamec, J.3    Kalousek, F.4    Taroni, F.5    Isaya, G.6
  • 15
    • 0033618254 scopus 로고    scopus 로고
    • Human cytoplasmic aconitase (Iron regulatory protein 1) is converted into its [3Fe-4S] form by hydrogen peroxide in vitro but is not activated for iron-responsive element binding
    • X. Brazzolotto J. Gaillard K. Pantopoulos M.W. Hentze Human cytoplasmic aconitase (Iron regulatory protein 1) is converted into its [3Fe-4S] form by hydrogen peroxide in vitro but is not activated for iron-responsive element binding J. Biol. Chem. 274 1999 21625 21630
    • (1999) J. Biol. Chem. , vol.274 , pp. 21625-21630
    • Brazzolotto, X.1    Gaillard, J.2    Pantopoulos, K.3    Hentze, M.W.4
  • 16
    • 0023709438 scopus 로고
    • The alpha-tocopherol and phospholipid fatty acid content of rat liver subcellular membranes in vitamin E and selenium deficiency
    • J.L. Buttriss A.T. Diplock The alpha-tocopherol and phospholipid fatty acid content of rat liver subcellular membranes in vitamin E and selenium deficiency Biochim. Biophys. Acta. 963 1988 61 69
    • (1988) Biochim. Biophys. Acta. , vol.963 , pp. 61-69
    • Buttriss, J.L.1    Diplock, A.T.2
  • 17
    • 13344270899 scopus 로고    scopus 로고
    • Friedreich's ataxia: Autosomal recessive disease caused by an intronic GAA triplet repeat expansion
    • V. Campuzano L. Montermini M.D. Molto L. Pianese M. Cossee F. Cavalcanti 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    Montermini, L.2    Molto, M.D.3    Pianese, L.4    Cossee, M.5    Cavalcanti, F.6
  • 18
  • 19
    • 0034731447 scopus 로고    scopus 로고
    • Two-step processing of human frataxin by mitochondrial processing peptidase. Precursor and intermediate forms are cleaved at different rates
    • P. Cavadini J. Adamec F. Taroni O. Gakh G. Isaya Two-step processing of human frataxin by mitochondrial processing peptidase. Precursor and intermediate forms are cleaved at different rates J. Biol. Chem. 275 2000 41469 41475
    • (2000) J. Biol. Chem. , vol.275 , pp. 41469-41475
    • Cavadini, P.1    Adamec, J.2    Taroni, F.3    Gakh, O.4    Isaya, G.5
  • 20
    • 0036472291 scopus 로고    scopus 로고
    • Assembly and iron-binding properties of human frataxin, the protein deficient in Friedreich ataxia
    • P. Cavadini H.A. O'Neill O. Benada G. Isaya Assembly and iron-binding properties of human frataxin, the protein deficient in Friedreich ataxia Hum. Mol. Genet. 11 2002 217 227
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 217-227
    • Cavadini, P.1    O'Neill, H.A.2    Benada, O.3    Isaya, G.4
  • 21
    • 0031889483 scopus 로고    scopus 로고
    • Ataxia with isolated vitamin E deficiency: Heterogeneity of mutations and phenotypic variability in a large number of families
    • L. Cavalier K. Ouahchi H.J. Kayden S. Di Donato L. Reutenauer J.L. Mandel Ataxia with isolated vitamin E deficiency: Heterogeneity of mutations and phenotypic variability in a large number of families Am. J. Hum. Genet. 62 1998 301 310
    • (1998) Am. J. Hum. Genet. , vol.62 , pp. 301-310
    • Cavalier, L.1    Ouahchi, K.2    Kayden, H.J.3    Di Donato, S.4    Reutenauer, L.5    Mandel, J.L.6
  • 22
    • 0030739437 scopus 로고    scopus 로고
    • Evolution of the Friedreich's ataxia trinucleotide repeat expansion: Founder effect and premutations
    • M. Cossee M. Schmitt V. Campuzano L. Reutenauer C. Moutou J.L. Mandel Evolution of the Friedreich's ataxia trinucleotide repeat expansion: Founder effect and premutations Proc. Natl. Acad. Sci. USA 94 1997 7452 7457
    • (1997) , pp. 7452-7457
    • Cossee, M.1    Schmitt, M.2    Campuzano, V.3    Reutenauer, L.4    Moutou, C.5    Mandel, J.L.6
  • 23
    • 0344820730 scopus 로고    scopus 로고
    • Friedreich's ataxia: Point mutations and clinical presentation of compound heterozygotes
    • M. Cossee A. Durr M. Schmitt N. Dahl P. Trouillas P. Allinson Friedreich's ataxia: Point mutations and clinical presentation of compound heterozygotes Ann. Neurol. 45 1999 200 206
    • (1999) Ann. Neurol. , vol.45 , pp. 200-206
    • Cossee, M.1    Durr, A.2    Schmitt, M.3    Dahl, N.4    Trouillas, P.5    Allinson, P.6
  • 24
    • 0034192352 scopus 로고    scopus 로고
    • Inactivation of the Friedreich's ataxia mouse gene leads to early embryonic lethality without iron accumulation
    • M. Cossee H. Puccio A. Gansmuller H. Koutnikova A. Dierich M. LeMeur Inactivation of the Friedreich's ataxia mouse gene leads to early embryonic lethality without iron accumulation Hum. Mol. Genet. 9 2000 1219 1226
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 1219-1226
    • Cossee, M.1    Puccio, H.2    Gansmuller, A.3    Koutnikova, H.4    Dierich, A.5    LeMeur, M.6
  • 25
    • 0027976808 scopus 로고
    • X-linked pyridoxine-responsive sideroblastic anemia due to a Thr388-to-Ser substitution in erythroid 5-aminolevulinate synthase
    • T.C. Cox S.S. Bottomley J.S. Wiley M.J. Bawden C.S. Matthews B.K. May X-linked pyridoxine-responsive sideroblastic anemia due to a Thr388-to-Ser substitution in erythroid 5-aminolevulinate synthase N. Engl. J. Med. 330 1994 675 679
    • (1994) N. Engl. J. Med. , vol.330 , pp. 675-679
    • Cox, T.C.1    Bottomley, S.S.2    Wiley, J.S.3    Bawden, M.J.4    Matthews, C.S.5    May, B.K.6
  • 26
    • 0031739916 scopus 로고    scopus 로고
    • Parental gender, age at birth and expansion length influence GAA repeat intergenerational instability in the X25 gene: Pedigree studies and analysis of sperm from patients with Friedreich's ataxia
    • G. De Michele F. Cavalcanti C. Criscuolo L. Pianese A. Monticelli A. Filla Parental gender, age at birth and expansion length influence GAA repeat intergenerational instability in the X25 gene: Pedigree studies and analysis of sperm from patients with Friedreich's ataxia Hum. Mol. Genet. 7 1998 1901 1906
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 1901-1906
    • De Michele, G.1    Cavalcanti, F.2    Criscuolo, C.3    Pianese, L.4    Monticelli, A.5    Filla, A.6
  • 27
    • 17344377955 scopus 로고    scopus 로고
    • Atypical Friedreich ataxia phenotype associated with a novel missense mutation in the X25 gene
    • G. De Michele A. Filla F. Cavalcanti A. Tammaro A. Monticelli L. Pianese Atypical Friedreich ataxia phenotype associated with a novel missense mutation in the X25 gene Neurology 54 2000 496 499
    • (2000) Neurology , vol.54 , pp. 496-499
    • De Michele, G.1    Filla, A.2    Cavalcanti, F.3    Tammaro, A.4    Monticelli, A.5    Pianese, L.6
  • 31
    • 0034642214 scopus 로고    scopus 로고
    • Increased levels of plasma malondialdehyde in Friedreich's ataxia
    • M. Emond G. Lepage M. Vanasse M. Pandolfo Increased levels of plasma malondialdehyde in Friedreich's ataxia Neurology 55 2000 1752 1753
    • (2000) Neurology , vol.55 , pp. 1752-1753
    • Emond, M.1    Lepage, G.2    Vanasse, M.3    Pandolfo, M.4
  • 32
    • 0029042393 scopus 로고
    • Biochemical, physiological and medical aspects of ubiquinone function
    • L. Ernster G. Dallner Biochemical, physiological and medical aspects of ubiquinone function Biochim. Biophys. Acta 1271 1995 195 204
    • (1995) Biochim. Biophys. Acta , vol.1271 , pp. 195-204
    • Ernster, L.1    Dallner, G.2
  • 34
    • 0028609515 scopus 로고
    • A one year bioavailability study of coenzyme Q10 with 3 months withdrawal period
    • K. Folkers S. Moesgaard M. Morita A one year bioavailability study of coenzyme Q10 with 3 months withdrawal period Mol. Aspects Med. 15 1994 s281 s285 (Suppl)
    • (1994) Mol. Aspects Med. , vol.15 , pp. s281-s285
    • Folkers, K.1    Moesgaard, S.2    Morita, M.3
  • 35
    • 0032129416 scopus 로고    scopus 로고
    • The correlation of clinical phenotype in Friedreich ataxia with the site of point mutations in the FRDA gene
    • S.M. Forrest M. Knight M.B. Delatycki D. Paris R. Williamson J. King The correlation of clinical phenotype in Friedreich ataxia with the site of point mutations in the FRDA gene Neurogenetics 1 1998 253 257
    • (1998) Neurogenetics , vol.1 , pp. 253-257
    • Forrest, S.M.1    Knight, M.2    Delatycki, M.B.3    Paris, D.4    Williamson, R.5    King, J.6
  • 36
    • 0032800601 scopus 로고    scopus 로고
    • Low iron concentration and aconitase deficiency in a yeast frataxin homologue deficient strain
    • F. Foury Low iron concentration and aconitase deficiency in a yeast frataxin homologue deficient strain FEBS Lett. 456 1999 281 284
    • (1999) FEBS Lett. , vol.456 , pp. 281-284
    • Foury, F.1
  • 37
    • 0031567601 scopus 로고    scopus 로고
    • Deletion of the yeast homologue of the human gene associated with Friedreich's ataxia elicits iron accumulation in mitochondria
    • F. Foury O. Cazzalini Deletion of the yeast homologue of the human gene associated with Friedreich's ataxia elicits iron accumulation in mitochondria FEBS Lett. 411 1997 373 377
    • (1997) FEBS Lett. , vol.411 , pp. 373-377
    • Foury, F.1    Cazzalini, O.2
  • 38
    • 34447604868 scopus 로고
    • Uber degenerative atrophie der spinalen hinterstrange
    • N. Friedreich Uber degenerative atrophie der spinalen hinterstrange Virchows Arch. Pathol. Anat. 26 1863 391 419
    • (1863) Virchows Arch. Pathol. Anat. , vol.26 , pp. 391-419
    • Friedreich, N.1
  • 39
    • 0035726073 scopus 로고    scopus 로고
    • Effect of vitamin E supplementation in patients with ataxia with vitamin E deficiency
    • S. Gabsi N. Gouider-Khouja S. Belal M. Fki M. Kefi I. Turki Effect of vitamin E supplementation in patients with ataxia with vitamin E deficiency Eur. J. Neurol. 8 2001 477 481
    • (2001) Eur. J. Neurol. , vol.8 , pp. 477-481
    • Gabsi, S.1    Gouider-Khouja, N.2    Belal, S.3    Fki, M.4    Kefi, M.5    Turki, I.6
  • 41
    • 0034660695 scopus 로고    scopus 로고
    • The GAATCC triplet repeat expanded in Friedreich's ataxia impedes transcription elongation by T7 RNA polymerase in a length and supercoil dependent manner
    • E. Grabczyk K. Usdin The GAATCC triplet repeat expanded in Friedreich's ataxia impedes transcription elongation by T7 RNA polymerase in a length and supercoil dependent manner Nucleic acids Res. 28 2000 2815 2822
    • (2000) Nucleic acids Res. , vol.28 , pp. 2815-2822
    • Grabczyk, E.1    Usdin, K.2
  • 42
    • 0031593616 scopus 로고    scopus 로고
    • Sustained efficacy and safety of idebenone in the treatment of Alzheimer's disease: Update on a 2-year double-blind multicentre study
    • H. Gutzmann D. Hadler Sustained efficacy and safety of idebenone in the treatment of Alzheimer's disease: Update on a 2-year double-blind multicentre study J. Neural. Transm. Suppl. 54 1998 301 310
    • (1998) J. Neural. Transm. Suppl. , vol.54 , pp. 301-310
    • Gutzmann, H.1    Hadler, D.2
  • 43
    • 0031883441 scopus 로고    scopus 로고
    • Generalized chorea in two patients harboring the Friedreich's ataxia gene trinucleotide repeat expansion
    • M.G. Hanna M.B. Davis M.G. Sweeney M. Noursadeghi C.J. Ellis P. Elliot Generalized chorea in two patients harboring the Friedreich's ataxia gene trinucleotide repeat expansion Mov. Disord. 13 1998 339 340
    • (1998) Mov. Disord. , vol.13 , pp. 339-340
    • Hanna, M.G.1    Davis, M.B.2    Sweeney, M.G.3    Noursadeghi, M.4    Ellis, C.J.5    Elliot, P.6
  • 44
    • 0019782799 scopus 로고
    • Friedreich's ataxia: A clinical and genetic study of 90 families with an analysis of early diagnosis criteria and intrafamilial clustering of clinical features
    • A.E. Harding Friedreich's ataxia: A clinical and genetic study of 90 families with an analysis of early diagnosis criteria and intrafamilial clustering of clinical features Brain 104 1981 589 620
    • (1981) Brain , vol.104 , pp. 589-620
    • Harding, A.E.1
  • 45
    • 0024997609 scopus 로고
    • 1-Methyl-4-phenylpyridinium (MPP+) induces NADH-dependent superoxide formation and enhances NADH-dependent lipid peroxidation in bovine heart submitochondrial particles
    • E. Hasegawa K. Takeshige T. Oishi Y. Murai S. Minakami 1-Methyl-4-phenylpyridinium (MPP+) induces NADH-dependent superoxide formation and enhances NADH-dependent lipid peroxidation in bovine heart submitochondrial particles Biochem. Biophys. Res. Commun. 170 1990 1049 1055
    • (1990) Biochem. Biophys. Res. Commun. , vol.170 , pp. 1049-1055
    • Hasegawa, E.1    Takeshige, K.2    Oishi, T.3    Murai, Y.4    Minakami, S.5
  • 46
    • 0027960215 scopus 로고
    • Superoxide and peroxynitrite inactivate aconitase, but nitric oxide does not
    • A. Hausalden I. Fridovich Superoxide and peroxynitrite inactivate aconitase, but nitric oxide does not J. Biol. Chem. 269 1994 29405 29408
    • (1994) J. Biol. Chem. , vol.269 , pp. 29405-29408
    • Hausalden, A.1    Fridovich, I.2
  • 47
  • 48
    • 0029758487 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress
    • M.W. Hentze L.C. Kuhn Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress Proc. Natl. Acad. Sci. 93 1996 8175 8182
    • (1996) , pp. 8175-8182
    • Hentze, M.W.1    Kuhn, L.C.2
  • 49
    • 0014379575 scopus 로고
    • The peripheral sensory pathway in friedreich's ataxia. An examination by light and electron microscopy of the posterior nerve roots, posterior root ganglia, and peripheral sensory nerves in cases of friedreich's ataxia
    • J.I. Hughes B. Brownell R.L. Hewer The peripheral sensory pathway in friedreich's ataxia. An examination by light and electron microscopy of the posterior nerve roots, posterior root ganglia, and peripheral sensory nerves in cases of friedreich's ataxia Brain 91 1968 803 818
    • (1968) Brain , vol.91 , pp. 803-818
    • Hughes, J.I.1    Brownell, B.2    Hewer, R.L.3
  • 50
    • 0033832615 scopus 로고    scopus 로고
    • Predicting protein function by genomic context: Quantitative evaluation and qualitative inferences
    • M. Huynen B. Snel W. Lathe 3rd P. Bork Predicting protein function by genomic context: Quantitative evaluation and qualitative inferences Genome Res. 10 2000 1204 1210
    • (2000) Genome Res. , vol.10 , pp. 1204-1210
    • Huynen, M.1    Snel, B.2    Lathe, W.3    Bork, P.4
  • 51
    • 0035504444 scopus 로고    scopus 로고
    • The phylogenetic distribution of frataxin indicates a role in iron-sulphur cluster protein assembly
    • M.A. Huynen B. Snel P. Bork T.J. Gibson The phylogenetic distribution of frataxin indicates a role in iron-sulphur cluster protein assembly Hum. Mol. Genet. 10 2001 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
  • 53
    • 0034107324 scopus 로고    scopus 로고
    • Role of Saccharomyces cerevisiae ISAI and ISA2 in iron homeostasis
    • L.T. Jensen V.C. Culotta Role of Saccharomyces cerevisiae ISAI 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
  • 54
    • 0024439014 scopus 로고
    • Desferrithiocin and desferrioxamine B. Cellular pharmacology and storage iron mobilization
    • Y. Jin A. Baquet A. Florence R.R. Crichton Y.J. Schneider Desferrithiocin and desferrioxamine B. Cellular pharmacology and storage iron mobilization Biochem. Pharmacol. 38 1989 3233 3240
    • (1989) Biochem. Pharmacol. , vol.38 , pp. 3233-3240
    • Jin, Y.1    Baquet, A.2    Florence, A.3    Crichton, R.R.4    Schneider, Y.J.5
  • 55
    • 0030826433 scopus 로고    scopus 로고
    • Frataxin shows developmentally regulated tissue-specific expression in the mouse embryo
    • S. Jiralerspong Y. Liu L. Montermini S. Stifani M. Pandolfo Frataxin shows developmentally regulated tissue-specific expression in the mouse embryo Neurobiol. Dis. 4 1997 103 113
    • (1997) Neurobiol. Dis. , vol.4 , pp. 103-113
    • Jiralerspong, S.1    Liu, Y.2    Montermini, L.3    Stifani, S.4    Pandolfo, M.5
  • 56
    • 0035976855 scopus 로고    scopus 로고
    • Manganese superoxide dismutase induction by iron is impaired in Friedreich's ataxia cells
    • S. Jiralerspong B. Ge T.J. Hudson M. Pandolfo Manganese superoxide dismutase induction by iron is impaired in Friedreich's ataxia cells FEBS Lett. 509 2001 101 105
    • (2001) FEBS Lett. , vol.509 , pp. 101-105
    • Jiralerspong, S.1    Ge, B.2    Hudson, T.J.3    Pandolfo, M.4
  • 57
    • 0034717132 scopus 로고    scopus 로고
    • Isalp is a component of the mitochondrial machinery for maturation of cellular iron-sulfur proteins and requires conserved cysteine residues for function
    • A. Kaut H. Lange K. Diekert G. Kispal R. Lill Isalp is a component of the mitochondrial machinery for maturation of cellular iron-sulfur proteins and requires conserved cysteine residues for function J. Biol. Chem. 275 2000 15955 15961
    • (2000) J. Biol. Chem. , vol.275 , pp. 15955-15961
    • Kaut, A.1    Lange, H.2    Diekert, K.3    Kispal, G.4    Lill, R.5
  • 58
    • 0027654218 scopus 로고
    • Quantitative analysis by 31P magnetic resonance spectroscopy of abnormal mitochondrial oxidation in skeletal muscle during recovery from exercise
    • G.J. Kemp D.J. Taylor C.H. Thompson L.J. Hands B. Rajagopalan P. Styles Quantitative analysis by 31P magnetic resonance spectroscopy of abnormal mitochondrial oxidation in skeletal muscle during recovery from exercise NMR Biomed. 6 1993 302 310
    • (1993) NMR Biomed. , vol.6 , pp. 302-310
    • Kemp, G.J.1    Taylor, D.J.2    Thompson, C.H.3    Hands, L.J.4    Rajagopalan, B.5    Styles, P.6
  • 59
    • 0027081042 scopus 로고
    • Purification and characterisation of cytosolic aconitase from beef liver and its relationship to the ironresponsive element binding protein
    • M.C. Kennedy L. Mende-Mueller G.A. Blondin H. Beinert Purification and characterisation of cytosolic aconitase from beef liver and its relationship to the ironresponsive element binding protein Proc. Natl. Acad. Sci. USA 89 1992 11730 11734
    • (1992) , pp. 11730-11734
    • Kennedy, M.C.1    Mende-Mueller, L.2    Blondin, G.A.3    Beinert, H.4
  • 60
    • 0030608677 scopus 로고    scopus 로고
    • The ABC transporter Atm1p is required for mitochondrial iron homeostasis
    • G. Kispal P. Csere B. Guiard R. Lill The ABC transporter Atm1p is required for mitochondrial iron homeostasis FEBS Lett. 418 1997 346 350
    • (1997) FEBS Lett. , vol.418 , pp. 346-350
    • Kispal, G.1    Csere, P.2    Guiard, B.3    Lill, R.4
  • 61
    • 0033565665 scopus 로고    scopus 로고
    • The mitochondrial proteins Atmlp and Nfs1p are essential for biogenesis of cytosolic FeS proteins
    • G. Kispal P. Csere I.C. Proh R. Lill The mitochondrial proteins Atmlp 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    Proh, I.C.3    Lill, R.4
  • 62
    • 0029990713 scopus 로고    scopus 로고
    • Friedreich's ataxia with retained tendon reflexes: Molecular genetics, clinical neurophysiology, and magnetic resonance imaging
    • T. Klockgether C. Zuhlke J.B. Schulz K. Burk M. Fetter H. Dittmann Friedreich's ataxia with retained tendon reflexes: Molecular genetics, clinical neurophysiology, and magnetic resonance imaging Neurology 46 1996 118 121
    • (1996) Neurology , vol.46 , pp. 118-121
    • Klockgether, T.1    Zuhlke, C.2    Schulz, J.B.3    Burk, K.4    Fetter, M.5    Dittmann, H.6
  • 63
    • 0032540929 scopus 로고    scopus 로고
    • Mt-Hsp70 homolog, Ssc2p, required for maturation of yeast frataxin and mitochondrial iron homeostasis
    • S.A.B. Knight N.B.V. Sepuri D. Pain A. Dancis 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.B.1    Sepuri, N.B.V.2    Pain, D.3    Dancis, A.4
  • 65
    • 0030813487 scopus 로고    scopus 로고
    • Studies of human mouse and yeast homologues indicate a mitochondrial function for frataxin
    • H. Koutnikova V. Campuzano F. Foury P. Dollé O. Cazzalini M. Koenig Studies of human mouse and yeast homologues indicate a mitochondrial function for frataxin Nat. Genet. 16 1997 345 351
    • (1997) Nat. Genet. , vol.16 , pp. 345-351
    • Koutnikova, H.1    Campuzano, V.2    Foury, F.3    Dollé, P.4    Cazzalini, O.5    Koenig, M.6
  • 66
    • 0031656903 scopus 로고    scopus 로고
    • Maturation of wild type and mutated frataxin by the mitochondrial processing peptide
    • H. Kourtnikova V. Campuzano M. Koenig Maturation of wild type and mutated frataxin by the mitochondrial processing peptide Hum. Mol. Genet. 7 1998 1485 1489
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 1485-1489
    • Kourtnikova, H.1    Campuzano, V.2    Koenig, M.3
  • 67
    • 0001787556 scopus 로고
    • Cardiac iron deposits in Friedreich's ataxia
    • J.B. Lamarche D. Shapcott M. Cote B. Lemieux Cardiac iron deposits in Friedreich's ataxia R. Lechtenberg Handbook of cerebellar diseases 1993 Marcel Dekker New York 453 456
    • (1993) , pp. 453-456
    • Lamarche, J.B.1    Shapcott, D.2    Cote, M.3    Lemieux, B.4
  • 68
    • 0033516467 scopus 로고    scopus 로고
    • Mechanism of iron transport to the site of heme synthesis inside yeast mitochondria
    • H. Lange G. Kispal R. Lill 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
  • 69
    • 0033953353 scopus 로고    scopus 로고
    • A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins
    • H. Lange A. Kaut G. Kispal R. Lill A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins Proc. Natl. Acad. Sci. USA 97 2000 1050 1055
    • (2000) , pp. 1050-1055
    • Lange, H.1    Kaut, A.2    Kispal, G.3    Lill, R.4
  • 71
    • 0032797179 scopus 로고    scopus 로고
    • Knockout of the cyaY gene in Escherichia coli does not affect cellular iron content and sensitivity to oxidants
    • D.S. Li K. Ohshima S. Jiralerspong M.W. Bojanowski M Pandolfo Knockout of the cyaY gene in Escherichia coli does not affect cellular iron content and sensitivity to oxidants FEBS Lett. 456 1999 13 16
    • (1999) FEBS Lett. , vol.456 , pp. 13-16
    • Li, D.S.1    Ohshima, K.2    Jiralerspong, S.3    Bojanowski, M.W.4    Pandolfo, M5
  • 72
    • 0032722872 scopus 로고    scopus 로고
    • Yeast mitochondrial protein, Nfs1p, coordinately regulates iron-sulfur cluster proteins, cellular iron uptake, and iron distribution
    • J. Li M. Kogan S.A. Knight D. Pain A. Dancis 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
  • 73
    • 0032746009 scopus 로고    scopus 로고
    • The essential role of mitochondria in the biogenesis of cellular iron-sulfur proteins
    • R. Lill K. Diekert A. Kaut H. Lange W. Pelzer C. Prohl The essential role of mitochondria in the biogenesis of cellular iron-sulfur proteins Biol. Chem. 380 1999 1157 1166
    • (1999) Biol. Chem. , vol.380 , pp. 1157-1166
    • Lill, R.1    Diekert, K.2    Kaut, A.3    Lange, H.4    Pelzer, W.5    Prohl, C.6
  • 74
    • 0034255836 scopus 로고    scopus 로고
    • Maturation of cellular FeS proteins: an essential function of mitochondria
    • R. Lill G. Kispal Maturation of cellular FeS proteins: an essential function of mitochondria Trends Biol. Sci. 25 2000 352 356
    • (2000) Trends Biol. Sci. , vol.25 , pp. 352-356
    • Lill, R.1    Kispal, G.2
  • 75
    • 0034734011 scopus 로고    scopus 로고
    • Targeting of proteins to mitochondria
    • T. Lithgow Targeting of proteins to mitochondria FEBS Lett. 476 2000 22 26
    • (2000) FEBS Lett. , vol.476 , pp. 22-26
    • Lithgow, T.1
  • 76
    • 0033613262 scopus 로고    scopus 로고
    • Deficit of in vivo mitochondrial ATP production in patients with Friedreich's ataxia
    • R. Lodi J.M. Cooper J.L. Bradley D. Manners P. Styles D.J. Taylor Deficit of in vivo mitochondrial ATP production in patients with Friedreich's ataxia Proc. Natl. Acad. Sci. USA 96 1999 11492 11495
    • (1999) , pp. 11492-11495
    • Lodi, R.1    Cooper, J.M.2    Bradley, J.L.3    Manners, D.4    Styles, P.5    Taylor, D.J.6
  • 77
    • 0035020940 scopus 로고    scopus 로고
    • Antioxidant treatment improves in vivo cardiac and skeletal muscle bioenergetics in patients with Friedreich's Ataxia
    • R. Lodi B. Rajagopalan P.E. Hart A.M. Blamire J.G. Crilley J.L. Bradley Antioxidant treatment improves in vivo cardiac and skeletal muscle bioenergetics in patients with Friedreich's Ataxia Ann. Neurol. 49 2001 590 596
    • (2001) Ann. Neurol. , vol.49 , pp. 590-596
    • Lodi, R.1    Rajagopalan, B.2    Hart, P.E.3    Blamire, A.M.4    Crilley, J.G.5    Bradley, J.L.6
  • 78
    • 0034839688 scopus 로고    scopus 로고
    • Cardiac energetics are abnormal in Friedreich's ataxia patients in the absence of cardiac dysfunction and hypertrophy. An in vivo 31p magnetic resonance spectroscopy study is abnormal
    • R. Lodi B. Rajagopalan A.M. Blamire J.M. Cooper C.H. Davies J.L. Bradley Cardiac energetics are abnormal in Friedreich's ataxia patients in the absence of cardiac dysfunction and hypertrophy. An in vivo 31p magnetic resonance spectroscopy study is abnormal Cardiovasc. Res. 52 2001 111 119
    • (2001) Cardiovasc. Res. , vol.52 , pp. 111-119
    • Lodi, R.1    Rajagopalan, B.2    Blamire, A.M.3    Cooper, J.M.4    Davies, C.H.5    Bradley, J.L.6
  • 79
    • 0032581215 scopus 로고    scopus 로고
    • ARHI of Saccharomyces cerevisiae: A new essential gene that codes for a protein homologous to the human adrenodoxin reductase
    • L. Manzella M.H. Barros F.G. Nobrega ARHI of Saccharomyces cerevisiae: A new essential gene that codes for a protein homologous to the human adrenodoxin reductase Yeast 14 1998 839 846
    • (1998) Yeast , vol.14 , pp. 839-846
    • Manzella, L.1    Barros, M.H.2    Nobrega, F.G.3
  • 81
    • 0032555066 scopus 로고    scopus 로고
    • Coenzyme Q10 administration increases brain mitochondrial concentrations and exerts neuroprotective effects
    • R.T. Matthews L. Yang S. Browne M. Baik M.F. Beal Coenzyme Q10 administration increases brain mitochondrial concentrations and exerts neuroprotective effects Proc. Natl. Acad. Sci. USA 95 1998 8892 8897
    • (1998) , pp. 8892-8897
    • Matthews, R.T.1    Yang, L.2    Browne, S.3    Baik, M.4    Beal, M.F.5
  • 82
    • 13044285432 scopus 로고    scopus 로고
    • Mitochondrial disease in superoxide dismutase 2 mutant mice
    • S. Melov P. Coskun M. Patel R. Tuinstra B. Cottrell A.S. Jun Mitochondrial disease in superoxide dismutase 2 mutant mice Proc. Natl. Acad. Sci. USA 96 1999 846 851
    • (1999) , pp. 846-851
    • Melov, S.1    Coskun, P.2    Patel, M.3    Tuinstra, R.4    Cottrell, B.5    Jun, A.S.6
  • 85
    • 0031885039 scopus 로고    scopus 로고
    • Antioxidant properties of 2,3-dimethoxy-5-methyl-6-(10-hydroxydecyl)-1,4-benzoquinone (idebenone)
    • A. Mordente G.E. Martorana G. Minotti B. Giardina Antioxidant properties of 2,3-dimethoxy-5-methyl-6-(10-hydroxydecyl)-1,4-benzoquinone (idebenone) Chem. Res. Toxicol. 11 1998 54 63
    • (1998) Chem. Res. Toxicol. , vol.11 , pp. 54-63
    • Mordente, A.1    Martorana, G.E.2    Minotti, G.3    Giardina, B.4
  • 86
    • 0024501895 scopus 로고
    • Brain distribution of idebenone and its effect on local cerebral glucose utilization in rats
    • Y. Nagai K. Yoshida S. Narumi S. Tanayama A. Nagaoka Brain distribution of idebenone and its effect on local cerebral glucose utilization in rats Arch. Gerontol. Geriatr. 8 1989 257 272
    • (1989) Arch. Gerontol. Geriatr. , vol.8 , pp. 257-272
    • Nagai, Y.1    Yoshida, K.2    Narumi, S.3    Tanayama, S.4    Nagaoka, A.5
  • 87
    • 0032486276 scopus 로고    scopus 로고
    • Inhibitory effects of expanded GAA. TTC triplet repeats from intron I of the Friedreich ataxia gene on transcription and replication in vivo
    • K. Ohshima L. Montermini R.D. Wells M. Pandolfo Inhibitory effects of expanded GAA. TTC triplet repeats from intron I of the Friedreich ataxia gene on transcription and replication in vivo J. Biol. Chem. 273 1998 14588 14595
    • (1998) J. Biol. Chem. , vol.273 , pp. 14588-14595
    • Ohshima, K.1    Montermini, L.2    Wells, R.D.3    Pandolfo, M.4
  • 88
    • 0034969491 scopus 로고    scopus 로고
    • Friedreich's ataxia: From GAA triplet-repeat expansion to frataxin deficiency
    • P.I. Patel G. Isaya Friedreich's ataxia: From GAA triplet-repeat expansion to frataxin deficiency Am. J. Hum. Genet. 69 2001 15 24
    • (2001) Am. J. Hum. Genet. , vol.69 , pp. 15-24
    • Patel, P.I.1    Isaya, G.2
  • 89
    • 0343628833 scopus 로고    scopus 로고
    • Mitochondrial Isa2p plays a crucial role in the maturation of cellular iron-sulfur proteins
    • W. Pelzer U. Muhlenhoff K. Diekert K. Siegmund G. Kispal R. Lill Mitochondrial Isa2p plays a crucial role in the maturation of cellular iron-sulfur proteins FEBS Lett. 476 2000 134 139
    • (2000) FEBS Lett. , vol.476 , pp. 134-139
    • Pelzer, W.1    Muhlenhoff, U.2    Diekert, K.3    Siegmund, K.4    Kispal, G.5    Lill, R.6
  • 93
    • 0035138072 scopus 로고    scopus 로고
    • Mouse models for Friedreich's ataxia exhibit cardiomyopathy, sensory nerve defect and FeS enzyme deficiency followed by intramitochondrial iron deposits
    • H. Puccio D. Simon M. Cossee P. Criqui-Filipe F. Tiziano J. Melki Mouse models for Friedreich's 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
  • 94
    • 0033582421 scopus 로고    scopus 로고
    • The yeast frataxin homologue mediates mitochondrial iron efflux. Evidence for a mitochondrial iron cycle
    • D. Radisky M.C. Babcock J. Kaplan The yeast frataxin homologue mediates mitochondrial iron efflux. Evidence for a mitochondrial iron cycle J. Biol. Chem. 274 1999 4497 4499
    • (1999) J. Biol. Chem. , vol.274 , pp. 4497-4499
    • Radisky, D.1    Babcock, M.C.2    Kaplan, J.3
  • 96
    • 0026666969 scopus 로고
    • Tissue concentrations of coenzyme Q10 in the rat following its oral and intraperitoneal administration
    • S. Reahal J. Wrigglesworth Tissue concentrations of coenzyme Q10 in the rat following its oral and intraperitoneal administration Drug. Metab. Dispos. 20 1992 423 427
    • (1992) Drug. Metab. Dispos. , vol.20 , pp. 423-427
    • Reahal, S.1    Wrigglesworth, J.2
  • 97
    • 0035978474 scopus 로고    scopus 로고
    • Development of potential iron chelators for the treatment of Friedreich's ataxia: Ligands that mobilise mitochondrial iron
    • D.R. Richardson C. Mouralian P. Ponka E. Becker Development of potential iron chelators for the treatment of Friedreich's ataxia: Ligands that mobilise mitochondrial iron Biochim. Biophys. Acta 1536 2001 133 140
    • (2001) Biochim. Biophys. Acta , vol.1536 , pp. 133-140
    • Richardson, D.R.1    Mouralian, C.2    Ponka, P.3    Becker, E.4
  • 98
    • 0031567095 scopus 로고    scopus 로고
    • The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells
    • D.R. Richardson P. Ponka The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells Biochim. Biophys. Acta 1331 1997 1 40
    • (1997) Biochim. Biophys. Acta , vol.1331 , pp. 1-40
    • Richardson, D.R.1    Ponka, P.2
  • 99
    • 1842327122 scopus 로고
    • Iron uptake by mitochondria
    • I. Romslo Iron uptake by mitochondria I. Urushizaki P. Aisen I. Listowski J.W. Drysdale Structure and function of iron storage and transport proteins 1983 Elsevier Amsterdam 493
    • (1983) , pp. 493
    • Romslo, I.1
  • 100
    • 0031253821 scopus 로고    scopus 로고
    • Aconitase and mitochondrial iron-sulphur protein deficiency in Friedreich's ataxia
    • A. Rotig P. de Lonlay D. Chretien F. Foury M. Koenig D. Sidi Aconitase and mitochondrial iron-sulphur protein deficiency in Friedreich's ataxia Nat. Genet. 17 1997 215 217
    • (1997) Nat. Genet. , vol.17 , pp. 215-217
    • Rotig, A.1    de Lonlay, P.2    Chretien, D.3    Foury, F.4    Koenig, M.5    Sidi, D.6
  • 101
    • 0033621156 scopus 로고    scopus 로고
    • Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae
    • B. Schilke C. Voisine H. Beinert E. Craig Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae Proc. Natl. Acad. Sci. USA 96 1999 10206 10211
    • (1999) , pp. 10206-10211
    • Schilke, B.1    Voisine, C.2    Beinert, H.3    Craig, E.4
  • 104
    • 0031711714 scopus 로고    scopus 로고
    • DATATOP: A decade of neuroprotective inquiry. Parkinson Study Group. Deprenyl And Tocopherol Antioxidative Therapy of Parkinsonism
    • I. Shoulson DATATOP: A decade of neuroprotective inquiry. Parkinson Study Group. Deprenyl And Tocopherol Antioxidative Therapy of Parkinsonism Ann. Neurol. 44 1998 S160 5166
    • (1998) Ann. Neurol. , vol.44 , pp. S160-5166
    • Shoulson, I.1
  • 106
    • 0029925181 scopus 로고    scopus 로고
    • Randomised controlled trial of vitamin E in patients with coronary disease: Cambridge Heart Antioxidant Study (CHAOS)
    • N.G. Stephens A. Parsons P.M. Schofield F. Kelly K. Cheeseman M.J. Mitchinson Randomised controlled trial of vitamin E in patients with coronary disease: Cambridge Heart Antioxidant Study (CHAOS) Lancet 347 1996 781 786
    • (1996) Lancet , vol.347 , pp. 781-786
    • Stephens, N.G.1    Parsons, A.2    Schofield, P.M.3    Kelly, F.4    Cheeseman, K.5    Mitchinson, M.J.6
  • 107
    • 0032553445 scopus 로고    scopus 로고
    • Suppressors of superoxide dismutase (SODI) deficiency in Saccharomyces cerevisiae
    • J. Strain C.R. Lorenz J. Bode S. Garland G.A. Smolen D.T. Ta Suppressors of superoxide dismutase (SODI) deficiency in Saccharomyces cerevisiae J. Biol. Chem. 273 1998 31138 31144
    • (1998) J. Biol. Chem. , vol.273 , pp. 31138-31144
    • Strain, J.1    Lorenz, C.R.2    Bode, J.3    Garland, S.4    Smolen, G.A.5    Ta, D.T.6
  • 108
    • 0033982887 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and free radical damage in the Huntington R6/2 transgenic mouse
    • S.J. Tabrizi J. Workman P.E. Hart L. Mangiarini A. Mahal G. Bates Mitochondrial dysfunction and free radical damage in the Huntington R6/2 transgenic mouse Ann. Neurol. 47 2000 80 86
    • (2000) Ann. Neurol. , vol.47 , pp. 80-86
    • Tabrizi, S.J.1    Workman, J.2    Hart, P.E.3    Mangiarini, L.4    Mahal, A.5    Bates, G.6
  • 110
    • 0022521936 scopus 로고
    • Effect of decreased ferrochelatase activity on iron and porphyrin content in mitochondria of mice with porphyria induced by griseofulvin
    • A. Tangeras Effect of decreased ferrochelatase activity on iron and porphyrin content in mitochondria of mice with porphyria induced by griseofulvin Biochim. Biophys. Acta 882 1986 77 84
    • (1986) Biochim. Biophys. Acta , vol.882 , pp. 77-84
    • Tangeras, A.1
  • 111
    • 0027739829 scopus 로고
    • Myopathy in vitamin E deficient rats: Muscle fibre necrosis associated with disturbances of mitochondrial function
    • P.K. Thomas J.M. Cooper K.H. King J.M. Workman A.H. Schapira M.A. Goss-Sampson Myopathy in vitamin E deficient rats: Muscle fibre necrosis associated with disturbances of mitochondrial function J. Anat. 183 1993 451 461
    • (1993) J. Anat. , vol.183 , pp. 451-461
    • Thomas, P.K.1    Cooper, J.M.2    King, K.H.3    Workman, J.M.4    Schapira, A.H.5    Goss-Sampson, M.A.6
  • 113
    • 0030939011 scopus 로고    scopus 로고
    • International cooperative ataxia rating scale for pharmacological assessment of the cerebellar syndrome
    • P. Trouillas T. Takayanagi M. Hallett R.D. Currier S.H. Subramony K. Wessel International cooperative ataxia rating scale for pharmacological assessment of the cerebellar syndrome J. Neurol. Sci. 145 1997 205 211
    • (1997) J. Neurol. Sci. , vol.145 , pp. 205-211
    • Trouillas, P.1    Takayanagi, T.2    Hallett, M.3    Currier, R.D.4    Subramony, S.H.5    Wessel, K.6
  • 114
    • 0032971328 scopus 로고    scopus 로고
    • Increased iron in the dentate nucleus of patients with Friedrich's ataxia
    • D. Waldvogel P. van Gelderen M. Hallett Increased iron in the dentate nucleus of patients with Friedrich's ataxia Ann. Neurol. 46 1999 123 125
    • (1999) Ann. Neurol. , vol.46 , pp. 123-125
    • Waldvogel, D.1    van Gelderen, P.2    Hallett, M.3
  • 115
    • 0031903392 scopus 로고    scopus 로고
    • Normal serum iron and ferritin concentrations in patients with Friedreich's ataxia
    • R.B. Wilson D.R. Lynch K.H. Fischbeck Normal serum iron and ferritin concentrations in patients with Friedreich's ataxia Ann. Neurol. 44 1998 132 134
    • (1998) Ann. Neurol. , vol.44 , pp. 132-134
    • Wilson, R.B.1    Lynch, D.R.2    Fischbeck, K.H.3
  • 116
    • 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
    • A. Wong J. Yang P. Cavadini C. Gellera B. Lonnerdal F. Taroni 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
  • 117
    • 0034681155 scopus 로고    scopus 로고
    • NifS-directed assembly of a transient [2Fe-2S] cluster within the NifU protein
    • P. Yuvaniyama J.N. Agar V.L. Cash M.K. Johnson D.R. Dean NifS-directed assembly of a transient [2Fe-2S] cluster within the NifU protein Proc. Natl. Acad. Sci. USA 97 2000 599 604
    • (2000) , pp. 599-604
    • Yuvaniyama, P.1    Agar, J.N.2    Cash, V.L.3    Johnson, M.K.4    Dean, D.R.5
  • 119
    • 0028265941 scopus 로고
    • Mechanism for the desulfurization of L-cysteine catalyzed by the nifS gene product
    • L. Zheng R.H. White V.L. Cash D.R. Dean Mechanism for the desulfurization of L-cysteine catalyzed by the nifS gene product Biochemistry 33 1994 4714 4720
    • (1994) Biochemistry , vol.33 , pp. 4714-4720
    • Zheng, L.1    White, R.H.2    Cash, V.L.3    Dean, D.R.4
  • 120
    • 0032557666 scopus 로고    scopus 로고
    • Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA fdx gene cluster from Azotobacter vinelandii
    • L. Zheng V.L. Cash D.H. Flint D.R. Dean Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA fdx gene cluster from Azotobacter vinelandii J. Biol. Chem. 273 1998 13264 13272
    • (1998) J. Biol. Chem. , vol.273 , pp. 13264-13272
    • Zheng, L.1    Cash, V.L.2    Flint, D.H.3    Dean, D.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.