메뉴 건너뛰기




Volumn 64, Issue 1, 2012, Pages 56-63

Exploring frataxin function

Author keywords

frataxin; iron homeostasis; mitochondria; respiration

Indexed keywords

FRATAXIN; HEME; IRON SULFUR PROTEIN;

EID: 84855442193     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.577     Document Type: Review
Times cited : (39)

References (65)
  • 1
    • 0030296878 scopus 로고    scopus 로고
    • Friedreich's ataxia protein: Phylogenetic evidence for mitochondrial dysfunction
    • DOI 10.1016/S0166-2236(96)20054-2, PII S0166223696200542
    • Gibson, T. J., Koonin, E. V., Musco, G., Pastore, A., and, Bork, P., (1996) Friedreich's ataxia protein: phylogenetic evidence for mitochondrial dysfunction. Trends Neurosci. 19, 465-468. (Pubitemid 26359860)
    • (1996) Trends in Neurosciences , vol.19 , Issue.11 , pp. 465-468
    • Gibson, T.J.1    Koonin, E.V.2    Musco, G.3    Pastore, A.4    Bork, P.5
  • 3
    • 0030813487 scopus 로고    scopus 로고
    • Studies of human, mouse and yeast homologues indicate a mitochondrial function for frataxin
    • DOI 10.1038/ng0897-345
    • Koutnikova, H., Campuzano, V., Foury, F., Dolle, P., Cazzalini, O., et al. (1997) Studies of human, mouse and yeast homologues indicate a mitochondrial function for frataxin. Nat. Genet. 16, 345-351. (Pubitemid 27323298)
    • (1997) Nature Genetics , vol.16 , Issue.4 , pp. 345-351
    • Koutnikova, H.1    Campuzano, V.2    Foury, F.3    Dolle, P.4    Cazzalini, O.5    Koenig, M.6
  • 6
    • 22144462536 scopus 로고    scopus 로고
    • Reduced expression of frataxin extends the lifespan of Caenorhabditis elegans
    • DOI 10.1111/j.1474-9726.2005.00149.x
    • Ventura, N., Rea, S., Henderson, S. T., Condo, I., Johnson, T. E., et al. (2005) Reduced expression of frataxin extends the lifespan of Caenorhabditis elegans. Aging Cell 4, 109-112. (Pubitemid 41632910)
    • (2005) Aging Cell , vol.4 , Issue.2 , pp. 109-112
    • Ventura, N.1    Rea, S.2    Henderson, S.T.3    Condo, I.4    Johnson, T.E.5    Testi, R.6
  • 7
    • 27944495710 scopus 로고    scopus 로고
    • RNAi-mediated suppression of the mitochondrial iron chaperone, frataxin, in Drosophila
    • DOI 10.1093/hmg/ddi367
    • Anderson, P. R., Kirby, K., Hilliker, A. J., and, Phillips, J. P., (2005) RNAi-mediated suppression of the mitochondrial iron chaperone, frataxin, in Drosophila. Hum. Mol. Genet. 14, 3397-3405. (Pubitemid 41672124)
    • (2005) Human Molecular Genetics , vol.14 , Issue.22 , pp. 3397-3405
    • Anderson, P.R.1    Kirby, K.2    Hilliker, A.J.3    Phillips, J.P.4
  • 8
    • 33845520813 scopus 로고    scopus 로고
    • Deficiency of Arabidopsis thaliana frataxin alters activity of mitochondrial Fe-S proteins and induces oxidative stress
    • DOI 10.1111/j.1365-313X.2006.02923.x
    • Busi, M. V., Maliandi, M. V., Valdez, H., Clemente, M., Zabaleta, E. J., et al. (2006) Deficiency of Arabidopsis thaliana frataxin alters activity of mitochondrial Fe-S proteins and induces oxidative stress. Plant J 48, 873-882. (Pubitemid 44924348)
    • (2006) Plant Journal , vol.48 , Issue.6 , pp. 873-882
    • Busi, M.V.1    Maliandi, M.V.2    Valdez, H.3    Clemente, M.4    Zabaleta, E.J.5    Araya, A.6    Gomez-Casati, D.F.7
  • 9
    • 78751663834 scopus 로고    scopus 로고
    • The mitochondrial protein frataxin is essential for heme biosynthesis in plants
    • Maliandi, M. V., Busi, M. V., Turowski, V. R., Leaden, L., Araya, A., et al. (2011) The mitochondrial protein frataxin is essential for heme biosynthesis in plants. FEBS J. 278, 470-481.
    • (2011) FEBS J. , vol.278 , pp. 470-481
    • Maliandi, M.V.1    Busi, M.V.2    Turowski, V.R.3    Leaden, L.4    Araya, A.5
  • 10
    • 4944240979 scopus 로고    scopus 로고
    • Functional and molecular characterization of the frataxin homolog from Arabidopsis thaliana
    • DOI 10.1016/j.febslet.2004.09.003, PII S0014579304011111
    • Busi, M. V., Zabaleta, E. J., Araya, A., and, Gomez-Casati, D. F., (2004) Functional and molecular characterization of the frataxin homolog from Arabidopsis thaliana. FEBS Lett. 576, 141-144. (Pubitemid 39330472)
    • (2004) FEBS Letters , vol.576 , Issue.1-2 , pp. 141-144
    • Busi, M.V.1    Zabaleta, E.J.2    Araya, A.3    Gomez-Casati, D.F.4
  • 11
    • 0343717915 scopus 로고    scopus 로고
    • Frataxin activates mitochondrial energy conversion and oxidative phosphorylation
    • Ristow, M., Pfister, M. F., Yee, A. J., Schubert, M., Michael, L., et al. (2000) Frataxin activates mitochondrial energy conversion and oxidative phosphorylation. Proc. Natl. Acad. Sci. USA 97, 12239-12243.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12239-12243
    • Ristow, M.1    Pfister, M.F.2    Yee, A.J.3    Schubert, M.4    Michael, L.5
  • 12
    • 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. USA 99, 12321-12326.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12321-12326
    • Chen, O.S.1    Hemenway, S.2    Kaplan, J.3
  • 13
    • 0037101845 scopus 로고    scopus 로고
    • The yeast frataxin homolog Yfh1p plays a specific role in the maturation of cellular Fe/S proteins
    • Muhlenhoff, U., Richhardt, N., Ristow, M., Kispal, G., and, Lill, R., (2002) The yeast frataxin homolog Yfh1p plays a specific role in the maturation of cellular Fe/S proteins. Hum. Mol. Genet. 11, 2025-2036. (Pubitemid 34919277)
    • (2002) Human Molecular Genetics , vol.11 , Issue.17 , pp. 2025-2036
    • Muhlenhoff, U.1    Richhardt, N.2    Ristow, M.3    Kispal, G.4    Lill, R.5
  • 14
    • 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. (Pubitemid 33069552)
    • (2001) Human Molecular Genetics , vol.10 , Issue.21 , pp. 2463-2468
    • Huynen, M.A.1    Snel, B.2    Bork, P.3    Gibson, T.J.4
  • 15
    • 0042232045 scopus 로고    scopus 로고
    • Yeast frataxin sequentially chaperones and stores iron by coupling protein assembly with iron oxidation
    • DOI 10.1074/jbc.M303158200
    • Park, S., Gakh, O., O'Neill, H. A., Mangravita, A., Nichol, H., et al. (2003) Yeast frataxin sequentially chaperones and stores iron by coupling protein assembly with iron oxidation. J. Biol. Chem. 278, 31340-31351. (Pubitemid 36994654)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.33 , pp. 31340-31351
    • Park, S.1    Gakh, O.2    O'Neill, H.A.3    Mangravita, A.4    Nichol, H.5    Ferreira, G.C.6    Isaya, G.7
  • 16
    • 3042763187 scopus 로고    scopus 로고
    • Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity
    • DOI 10.1126/science.1098991
    • Bulteau, A. L., O'Neill, H. A., Kennedy, M. C., Ikeda-Saito, M., Isaya, G., et al. (2004) Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity. Science 305, 242-245. (Pubitemid 38886737)
    • (2004) Science , vol.305 , Issue.5681 , 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
  • 17
  • 18
    • 31544445770 scopus 로고    scopus 로고
    • Mitochondrial iron detoxification is a primary function of frataxin that limits oxidative damage and preserves cell longevity
    • DOI 10.1093/hmg/ddi461
    • Gakh, O., Park, S., Liu, G., Macomber, L., Imlay, J. A., et al. (2006) Mitochondrial iron detoxification is a primary function of frataxin that limits oxidative damage and preserves cell longevity. Hum. Mol. Genet. 15, 467-479. (Pubitemid 43159898)
    • (2006) Human Molecular Genetics , vol.15 , Issue.3 , pp. 467-479
    • Gakh, O.1    Park, S.2    Liu, G.3    Macomber, L.4    Imlay, J.A.5    Ferreira, G.C.6    Isaya, G.7
  • 20
    • 0037064027 scopus 로고    scopus 로고
    • The ferroxidase activity of yeast frataxin
    • DOI 10.1074/jbc.M206711200
    • Park, S., Gakh, O., Mooney, S. M., and, Isaya, G., (2002) The ferroxidase activity of yeast frataxin. J. Biol. Chem. 277, 38589-38595. (Pubitemid 35154719)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.41 , pp. 38589-38595
    • Park, S.1    Gakh, O.2    Mooney, S.M.3    Isaya, G.4
  • 21
    • 58749093283 scopus 로고    scopus 로고
    • Nitric oxide accumulation is required to protect against iron-mediated oxidative stress in frataxin-deficient Arabidopsis plants
    • Martin, M., Colman, M. J., Gomez-Casati, D. F., Lamattina, L., and, Zabaleta, E. J., (2009) Nitric oxide accumulation is required to protect against iron-mediated oxidative stress in frataxin-deficient Arabidopsis plants. FEBS Lett. 583, 542-548.
    • (2009) FEBS Lett. , vol.583 , pp. 542-548
    • Martin, M.1    Colman, M.J.2    Gomez-Casati, D.F.3    Lamattina, L.4    Zabaleta, E.J.5
  • 22
    • 77951991939 scopus 로고    scopus 로고
    • Nitric oxide and frataxin: Two players contributing to maintain cellular iron homeostasis
    • Ramirez, L., Zabaleta, E. J., and, Lamattina, L., (2010) Nitric oxide and frataxin: two players contributing to maintain cellular iron homeostasis. Ann. Bot. 105, 801-810.
    • (2010) Ann. Bot. , vol.105 , pp. 801-810
    • Ramirez, L.1    Zabaleta, E.J.2    Lamattina, L.3
  • 25
    • 0034661480 scopus 로고    scopus 로고
    • Towards a structural understanding of Friedreich's ataxia: Solution structure of frataxin
    • DOI 10.1016/S0969-2126(00)00158-1
    • Musco, G., Stier, G., Kolmerer, B., Adinolfi, S., Martin, S., et al. (2000) Towards a structural understanding of Friedreich's ataxia: the solution structure of frataxin. Structure 8, 695-707. (Pubitemid 30469988)
    • (2000) Structure , vol.8 , Issue.7 , pp. 695-707
    • Musco, G.1    Stier, G.2    Kolmerer, B.3    Adinolfi, S.4    Martin, S.5    Frenkiel, T.6    Gibson, T.7    Pastore, A.8
  • 26
    • 11144265730 scopus 로고    scopus 로고
    • Yeast frataxin solution structure, iron binding, and ferrochelatase interaction
    • DOI 10.1021/bi0488193
    • He, Y., Alam, S. L., Proteasa, S. V., Zhang, Y., Lesuisse, E., et al. (2004) Yeast frataxin solution structure, iron binding, and ferrochelatase interaction. Biochemistry 43, 16254-16262. (Pubitemid 40041038)
    • (2004) Biochemistry , vol.43 , Issue.51 , pp. 16254-16262
    • He, Y.1    Alam, S.L.2    Proteasa, S.V.3    Zhang, Y.4    Lesuisse, E.5    Dancis, A.6    Stemmler, T.L.7
  • 27
    • 7944225865 scopus 로고    scopus 로고
    • Solution structure of the bacterial frataxin ortholog, CyaY: Mapping the iron binding sites
    • DOI 10.1016/j.str.2004.08.012, PII S0969212604003399
    • Nair, M., Adinolfi, S., Pastore, C., Kelly, G., Temussi, P., et al. (2004) Solution structure of the bacterial frataxin ortholog, CyaY: mapping the iron binding sites. Structure 12, 2037-2048. (Pubitemid 39469401)
    • (2004) Structure , vol.12 , Issue.11 , pp. 2037-2048
    • Nair, M.1    Adinolfi, S.2    Pastore, C.3    Kelly, G.4    Temussi, P.5    Pastore, A.6
  • 29
    • 0036472291 scopus 로고    scopus 로고
    • Assembly and iron-binding properties of human frataxin, the protein dificient in Friedreich ataxia
    • Cavadini, P., O'Neill, H. A., Benada, O., and, Isaya, G., (2002) Assembly and iron-binding properties of human frataxin, the protein deficient in Friedreich ataxia. Hum Mol Genet 11, 217-227. (Pubitemid 34173351)
    • (2002) Human Molecular Genetics , vol.11 , Issue.3 , pp. 217-227
    • Cavadini, P.1    O'Neill, H.A.2    Benada, O.3    Isaya, G.4
  • 30
    • 9644279682 scopus 로고    scopus 로고
    • Iron-induced oligomerization of yeast frataxin homologue Yfh1 is dispensable in vivo
    • DOI 10.1038/sj.embor.7400272
    • Aloria, K., Schilke, B., Andrew, A., and, Craig, E. A., (2004) Iron-induced oligomerization of yeast frataxin homologue Yfh1 is dispensable in vivo. EMBO Rep. 5, 1096-1101. (Pubitemid 39600210)
    • (2004) EMBO Reports , vol.5 , Issue.11 , pp. 1096-1101
    • Aloria, K.1    Schilke, B.2    Andrew, A.3    Craig, E.A.4
  • 31
    • 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
  • 32
    • 20744446399 scopus 로고    scopus 로고
    • Structure, function, and formation of biological iron-sulfur clusters
    • DOI 10.1146/annurev.biochem.74.082803.133518
    • 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. (Pubitemid 40995508)
    • (2005) Annual Review of Biochemistry , vol.74 , pp. 247-281
    • Johnson, D.C.1    Dean, D.R.2    Smith, A.D.3    Johnson, M.K.4
  • 33
    • 79954416607 scopus 로고    scopus 로고
    • Ancient and essential: The assembly of iron-sulfur clusters in plants
    • Balk, J., and, Pilon, M., (2011) Ancient and essential: the assembly of iron-sulfur clusters in plants. Trends Plant Sci. 16, 218-226.
    • (2011) Trends Plant Sci. , vol.16 , pp. 218-226
    • Balk, J.1    Pilon, M.2
  • 34
    • 1542304548 scopus 로고    scopus 로고
    • Formation and insertion of the nitrogenase iron-molybdenum cofactor
    • Dos Santos, P. C., Dean, D. R., Hu, Y., and, Ribbe, M. W., (2004) Formation and insertion of the nitrogenase iron-molybdenum cofactor. Chem. Rev. 104, 1159-1173.
    • (2004) Chem. Rev. , vol.104 , pp. 1159-1173
    • Dos Santos, P.C.1    Dean, D.R.2    Hu, Y.3    Ribbe, M.W.4
  • 35
    • 11844270546 scopus 로고    scopus 로고
    • Maturation of nitrogenase: A biochemical puzzle
    • DOI 10.1128/JB.187.2.405-414.2005
    • Rubio, L. M., and, Ludden, P. W., (2005) Maturation of nitrogenase: a biochemical puzzle. J. Bacteriol. 187, 405-414. (Pubitemid 40096228)
    • (2005) Journal of Bacteriology , vol.187 , Issue.2 , pp. 405-414
    • Rubio, L.M.1    Ludden, P.W.2
  • 36
    • 0032933919 scopus 로고    scopus 로고
    • Sufs is a nifs-like protein, and sufd is necessary for stability of the [2fe-2s] fhuf protein in escherichia coli
    • Patzer, S. I., and, Hantke, K., (1999) SufS is a NifS-like protein, and SufD is necessary for stability of the [2Fe-2S] FhuF protein in Escherichia coli. J. Bacteriol. 181, 3307-3309. (Pubitemid 29236944)
    • (1999) Journal of Bacteriology , vol.181 , Issue.10 , pp. 3307-3309
    • Patzer, S.I.1    Hantke, K.2
  • 37
    • 0037047411 scopus 로고    scopus 로고
    • A third bacterial system for the assembly of iron-sulfur clusters with homologs in Archaea and plastids
    • DOI 10.1074/jbc.C200365200
    • Takahashi, Y., and, Tokumoto, U., (2002) A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids. J. Biol. Chem. 277, 28380-28383. (Pubitemid 41079260)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.32 , pp. 28380-28383
    • Takahashi, Y.1    Tokumoto, U.2
  • 38
    • 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
    • DOI 10.1038/84818
    • Puccio, H., Simon, D., Cossee, M., Criqui-Filipe, P., Tiziano, F., et al. (2001) Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits. Nat. Genet. 27, 181-186. (Pubitemid 32157445)
    • (2001) Nature Genetics , vol.27 , Issue.2 , pp. 181-186
    • Puccio, H.1    Simon, D.2    Cossee, M.3    Criqui-Filipe, P.4    Tiziano, F.5    Melki, J.6    Hindelang, C.7    Matyas, R.8    Rustin, P.9    Koenig, M.10
  • 40
    • 2542556601 scopus 로고    scopus 로고
    • Idebenone delays the onset of cardiac functional alteration without correction of Fe-S enzymes deficit in a mouse model for Friedreich ataxia
    • DOI 10.1093/hmg/ddh114
    • Seznec, H., Simon, D., Monassier, L., Criqui-Filipe, P., Gansmuller, A., et al. (2004) Idebenone delays the onset of cardiac functional alteration without correction of Fe-S enzymes deficit in a mouse model for Friedreich ataxia. Hum. Mol. Genet. 13, 1017-1024. (Pubitemid 38702188)
    • (2004) Human Molecular Genetics , vol.13 , Issue.10 , pp. 1017-1024
    • Seznec, H.1    Simon, D.2    Monassier, L.3    Criqui-Filipe, P.4    Gansmuller, A.5    Rustin, P.6    Koening, M.7    Puccio, H.8
  • 41
    • 34447316711 scopus 로고    scopus 로고
    • Mitochondrial frataxin interacts with ISD11 of the NFS1/ISCU complex and multiple mitochondrial chaperones
    • DOI 10.1093/hmg/ddm038
    • Shan, Y., Napoli, E., and, Cortopassi, G., (2007) Mitochondrial frataxin interacts with ISD11 of the NFS1/ISCU complex and multiple mitochondrial chaperones. Hum. Mol. Genet. 16, 929-941. (Pubitemid 47062737)
    • (2007) Human Molecular Genetics , vol.16 , Issue.8 , pp. 929-941
    • Shan, Y.1    Napoli, E.2    Cortopassi, G.3
  • 42
    • 26444566405 scopus 로고    scopus 로고
    • Frataxin interacts functionally with mitochondrial electron transport chain proteins
    • DOI 10.1093/hmg/ddi214
    • Gonzalez-Cabo, P., Vazquez-Manrique, R. P., Garcia-Gimeno, M. A., Sanz, P., and, Palau, F., (2005) Frataxin interacts functionally with mitochondrial electron transport chain proteins. Hum. Mol. Genet. 14, 2091-2098. (Pubitemid 41418009)
    • (2005) Human Molecular Genetics , vol.14 , Issue.15 , pp. 2091-2098
    • Gonzalez-Cabo, P.1    Vazquez-Manrique, R.P.2    Garcia-Gimeno, M.A.3    Sanz, P.4    Palau, F.5
  • 43
    • 0141623560 scopus 로고    scopus 로고
    • An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1
    • DOI 10.1038/sj.embor.embor918
    • Gerber, J., Muhlenhoff, U., and, Lill, R., (2003) An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1. EMBO Rep. 4, 906-911. (Pubitemid 37304409)
    • (2003) EMBO Reports , vol.4 , Issue.9 , pp. 906-911
    • Gerber, J.1    Muhlenhoff, U.2    Lill, R.3
  • 44
    • 33745217828 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis: Characterization of Escherichia coli CYaY as an iron donor for the assembly of [2Fe-2S] clusters in the scaffold IscU
    • Layer, G., Ollagnier-de Choudens, S., Sanakis, Y., and, Fontecave, M., (2006) Iron-sulfur cluster biosynthesis: characterization of Escherichia coli CYaY as an iron donor for the assembly of [2Fe-2S] clusters in the scaffold IscU. J. Biol. Chem. 281, 16256-16263.
    • (2006) J. Biol. Chem. , vol.281 , pp. 16256-16263
    • Layer, G.1    Ollagnier-De Choudens, S.2    Sanakis, Y.3    Fontecave, M.4
  • 45
    • 33644872938 scopus 로고    scopus 로고
    • Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus
    • DOI 10.1126/science.1123809
    • Sazanov, L. A., and, Hinchliffe, P., (2006) Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus. Science 311, 1430-1436. (Pubitemid 43376691)
    • (2006) Science , vol.311 , Issue.5766 , pp. 1430-1436
    • Sazanov, L.A.1    Hinchliffe, P.2
  • 46
    • 70350351403 scopus 로고    scopus 로고
    • Structural basis for the mechanism of respiratory complex i
    • Berrisford, J. M., and, Sazanov, L. A., (2009) Structural basis for the mechanism of respiratory complex I. J. Biol. Chem. 284, 29773-29783.
    • (2009) J. Biol. Chem. , vol.284 , pp. 29773-29783
    • Berrisford, J.M.1    Sazanov, L.A.2
  • 47
    • 0036667986 scopus 로고    scopus 로고
    • A structural approach to understanding the iron-binding properties of phylogenetically different frataxins
    • Adinolfi, S., Trifuoggi, M., Politou, A. S., Martin, S., and, Pastore, A., (2002) A structural approach to understanding the iron-binding properties of phylogenetically different frataxins. Hum. Mol. Genet. 11, 1865-1877.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1865-1877
    • Adinolfi, S.1    Trifuoggi, M.2    Politou, A.S.3    Martin, S.4    Pastore, A.5
  • 48
    • 2942744572 scopus 로고    scopus 로고
    • Frataxin-mediated iron delivery to ferrochelatase in the final step of heme biosynthesis
    • DOI 10.1074/jbc.C400107200
    • 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. (Pubitemid 38798734)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.25 , pp. 25943-25946
    • Yoon, T.1    Cowan, J.A.2
  • 49
    • 6344272773 scopus 로고    scopus 로고
    • Candida albicans lacking the frataxin homologue: A relevant yeast model for studying the role of frataxin
    • DOI 10.1111/j.1365-2958.2004.04281.x
    • Santos, R., Buisson, N., Knight, S. A., Dancis, A., Camadro, J. M., et al. (2004) Candida albicans lacking the frataxin homologue: a relevant yeast model for studying the role of frataxin. Mol. Microbiol. 54, 507-519. (Pubitemid 39388292)
    • (2004) Molecular Microbiology , vol.54 , Issue.2 , pp. 507-519
    • Santos, R.1    Buisson, N.2    Knight, S.A.B.3    Dancis, A.4    Camadro, J.-M.5    Lesuisse, E.6
  • 50
    • 0041808717 scopus 로고    scopus 로고
    • Decreased expression of genes involved in sulfur amino acid metabolism in frataxin-deficient cells
    • DOI 10.1093/hmg/ddg187
    • Tan, G., Napoli, E., Taroni, F., and, Cortopassi, G., (2003) Decreased expression of genes involved in sulfur amino acid metabolism in frataxin-deficient cells. Hum. Mol. Genet. 12, 1699-1711. (Pubitemid 36896662)
    • (2003) Human Molecular Genetics , vol.12 , Issue.14 , pp. 1699-1711
    • Tan, G.1    Napoli, E.2    Taroni, F.3    Cortopassi, G.4
  • 51
    • 31344438920 scopus 로고    scopus 로고
    • Salmonella enterica strains lacking the frataxin homolog cyaY show defects in Fe-S cluster metabolism in vivo
    • DOI 10.1128/JB.188.3.1175-1179.2006
    • Vivas, E., Skovran, E., and, Downs, D. M., (2006) Salmonella enterica strains lacking the frataxin homolog CyaY show defects in Fe-S cluster metabolism in vivo. J. Bacteriol. 188, 1175-1179. (Pubitemid 43146435)
    • (2006) Journal of Bacteriology , vol.188 , Issue.3 , pp. 1175-1179
    • Vivas, E.1    Skovran, E.2    Downs, D.M.3
  • 52
    • 62549107492 scopus 로고    scopus 로고
    • Multicellular models of Friedreich ataxia
    • Puccio, H., (2009) Multicellular models of Friedreich ataxia. J. Neurol. 256 (Suppl 1), 18-24.
    • (2009) J. Neurol. , vol.256 , Issue.SUPPL. 1 , pp. 18-24
    • Puccio, H.1
  • 53
    • 33846782968 scopus 로고    scopus 로고
    • Knockout of frataxin gene causes embryo lethality in Arabidopsis
    • DOI 10.1016/j.febslet.2007.01.030, PII S0014579307000580
    • Vazzola, V., Losa, A., Soave, C., and, Murgia, I., (2007) Knockout of frataxin gene causes embryo lethality in Arabidopsis. FEBS Lett. 581, 667-672. (Pubitemid 46216291)
    • (2007) FEBS Letters , vol.581 , Issue.4 , pp. 667-672
    • Vazzola, V.1    Losa, A.2    Soave, C.3    Murgia, I.4
  • 54
    • 0037093206 scopus 로고    scopus 로고
    • Erythroid differentiation and protoporphyrin IX down-regulate frataxin expression in Friend cells: Characterization of frataxin expression compared to molecules involved in iron metabolism and hemoglobinization
    • DOI 10.1182/blood.V99.10.3813
    • Becker, E. M., Greer, J. M., Ponka, P., and, Richardson, D. R., (2002) Erythroid differentiation and protoporphyrin IX down-regulate frataxin expression in Friend cells: characterization of frataxin expression compared to molecules involved in iron metabolism and hemoglobinization. Blood 99, 3813-3822. (Pubitemid 34534556)
    • (2002) Blood , vol.99 , Issue.10 , pp. 3813-3822
    • Becker, E.M.1    Greer, J.M.2    Ponka, P.3    Richardson, D.R.4
  • 55
    • 0037025331 scopus 로고    scopus 로고
    • Deletion of the mitochondrial carrier genes MRS3 and MRS4 suppresses mitochondrial iron accumulation in a yeast frataxin-deficient strain
    • DOI 10.1074/jbc.M111789200
    • Foury, F., and, Roganti, T., (2002) Deletion of the mitochondrial carrier genes MRS3 and MRS4 suppresses mitochondrial iron accumulation in a yeast frataxin-deficient strain. J. Biol. Chem. 277, 24475-24483. (Pubitemid 34951972)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.27 , pp. 24475-24483
    • Foury, F.1    Roganti, T.2
  • 56
    • 21244448393 scopus 로고    scopus 로고
    • Frataxin and mitochondrial carrier proteins, Mrs3p and Mrs4p, cooperate in providing iron for heme synthesis
    • DOI 10.1074/jbc.M500397200
    • Zhang, Y., Lyver, E. R., Knight, S. A., Lesuisse, E., and, Dancis, A., (2005) Frataxin and mitochondrial carrier proteins, Mrs3p and Mrs4p, cooperate in providing iron for heme synthesis. J. Biol. Chem. 280, 19794-19807. (Pubitemid 41379505)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.20 , pp. 19794-19807
    • Zhang, Y.1    Lyver, E.K.2    Knight, S.A.B.3    Lesuisse, E.4    Dancis, A.5
  • 57
    • 33646696625 scopus 로고    scopus 로고
    • Frataxin, iron-sulfur clusters, heme, ROS, and aging
    • Napoli, E., Taroni, F., and, Cortopassi, G. A., (2006) Frataxin, iron-sulfur clusters, heme, ROS, and aging. Antioxid. Redox Signal. 8, 506-516.
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 506-516
    • Napoli, E.1    Taroni, F.2    Cortopassi, G.A.3
  • 58
    • 34250223092 scopus 로고    scopus 로고
    • Hemin rescues adrenodoxin, heme a and cytochrome oxidase activity in frataxin-deficient oligodendroglioma cells
    • DOI 10.1016/j.bbadis.2007.04.001, PII S0925443907000877
    • Napoli, E., Morin, D., Bernhardt, R., Buckpitt, A., and, Cortopassi, G., (2007) Hemin rescues adrenodoxin, heme a and cytochrome oxidase activity in frataxin-deficient oligodendroglioma cells. Biochim. Biophys. Acta 1772, 773-780. (Pubitemid 46900883)
    • (2007) Biochimica et Biophysica Acta - Molecular Basis of Disease , vol.1772 , Issue.7 , pp. 773-780
    • Napoli, E.1    Morin, D.2    Bernhardt, R.3    Buckpitt, A.4    Cortopassi, G.5
  • 59
    • 0027104253 scopus 로고
    • Biochemistry of nitric oxide and its redox-activated forms
    • Stamler, J. S., Singel, D. J., and, Loscalzo, J., (1992) Biochemistry of nitric oxide and its redox-activated forms. Science 258, 1898-1902. (Pubitemid 23026727)
    • (1992) Science , vol.258 , Issue.5090 , pp. 1898-1902
    • Stamler, J.S.1    Singel, D.J.2    Loscalzo, J.3
  • 61
    • 0141518650 scopus 로고    scopus 로고
    • Nitric Oxide: The Versatility of an Extensive Signal Molecule
    • DOI 10.1146/annurev.arplant.54.031902.134752
    • Lamattina, L., Garcia-Mata, C., Graziano, M., and, Pagnussat, G., (2003) Nitric oxide: the versatility of an extensive signal molecule. Annu. Rev. Plant. Biol. 54, 109-136. (Pubitemid 37399989)
    • (2003) Annual Review of Plant Biology , vol.54 , pp. 109-136
    • Lamattina, L.1    Garcia-Mata, C.2    Graziano, M.3    Pagnussat, G.4
  • 62
    • 11844296696 scopus 로고    scopus 로고
    • Nitric oxide and iron in plants: An emerging and converging story
    • DOI 10.1016/j.tplants.2004.12.004, PII S1360138504002754
    • Graziano, M., and, Lamattina, L., (2005) Nitric oxide and iron in plants: an emerging and converging story. Trends Plant. Sci. 10, 4-8. (Pubitemid 40084622)
    • (2005) Trends in Plant Science , vol.10 , Issue.1 , pp. 4-8
    • Graziano, M.1    Lamattina, L.2
  • 63
    • 33845337036 scopus 로고    scopus 로고
    • Iron and iron-responsive proteins in the cardiomyopathy of Friedreich's ataxia
    • DOI 10.1080/14734220600913246, PII P0X681011H30H2N6
    • Michael, S., Petrocine, S. V., Qian, J., Lamarche, J. B., Knutson, M. D., et al. (2006) Iron and iron-responsive proteins in the cardiomyopathy of Friedreich's ataxia. Cerebellum 5, 257-267. (Pubitemid 44875782)
    • (2006) Cerebellum , vol.5 , Issue.4 , pp. 257-267
    • Michael, S.1    Petrocine, S.V.2    Qian, J.3    Lamarche, J.B.4    Knutson, M.D.5    Garrick, M.D.6    Koeppen, A.H.7
  • 64
  • 65
    • 0037070223 scopus 로고    scopus 로고
    • Normoxic induction of the hypoxia-inducible factor 1α by insulin and interleukin-1β involves the phosphatidylinositol 3-kinase pathway
    • DOI 10.1016/S0014-5793(02)02247-0, PII S0014579302022470
    • Stiehl, D. P., Jelkmann, W., Wenger, R. H., and, Hellwig-Burgel, T., (2002) Normoxic induction of the hypoxia-inducible factor 1alpha by insulin and interleukin-1beta involves the phosphatidylinositol 3-kinase pathway. FEBS Lett. 512, 157-162. (Pubitemid 34164471)
    • (2002) FEBS Letters , vol.512 , Issue.1-3 , pp. 157-162
    • Stiehl, D.P.1    Jelkmann, W.2    Wenger, R.H.3    Hellwig-Burgel, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.