메뉴 건너뛰기




Volumn 460, Issue 7257, 2009, Pages 831-838

Function and biogenesis of iron-sulphur proteins

Author keywords

[No Author keywords available]

Indexed keywords

APOPROTEIN; IRON; IRON SULFUR PROTEIN; NUCLEAR PROTEIN; SCAFFOLD PROTEIN; SULFUR;

EID: 68949128587     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature08301     Document Type: Review
Times cited : (912)

References (100)
  • 1
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: Nature's modular, multipurpose structures
    • Beinert, H., Holm, R. H. & Münck, E. Iron-sulfur clusters: nature's modular, multipurpose structures. Science 277, 653-659 (1997).
    • (1997) Science , vol.277 , pp. 653-659
    • Beinert, H.1    Holm, R.H.2    Münck, E.3
  • 2
    • 38649087966 scopus 로고    scopus 로고
    • Iron-sulfur protein folds, iron-sulfur chemistry, and evolution
    • Meyer, J. Iron-sulfur protein folds, iron-sulfur chemistry, and evolution. J. Biol. Inorg. Chem. 13, 157-170 (2008).
    • (2008) J. Biol. Inorg. Chem , vol.13 , pp. 157-170
    • Meyer, J.1
  • 4
    • 20744446399 scopus 로고    scopus 로고
    • Structure, function and formation of biological iron-sulfur clusters
    • Johnson, D. C., Dean, D. R., Smith, A. D. & Johnson, M. K. Structure, function and formation of biological iron-sulfur clusters. Annu. Rev. Biochem. 74, 247-281 (2005).
    • (2005) Annu. Rev. Biochem , vol.74 , pp. 247-281
    • Johnson, D.C.1    Dean, D.R.2    Smith, A.D.3    Johnson, M.K.4
  • 5
    • 21444455377 scopus 로고    scopus 로고
    • Biogenesis of iron-sulfur proteins in plants
    • Balk, J. & Lobreaux, S. Biogenesis of iron-sulfur proteins in plants. Trends Plant Sci. 10, 324-331 (2005).
    • (2005) Trends Plant Sci , vol.10 , pp. 324-331
    • Balk, J.1    Lobreaux, S.2
  • 6
    • 33751177803 scopus 로고    scopus 로고
    • Iron-sulfur protein biogenesis in eukaryotes: Components and mechanisms
    • Lill, R. & Mühlenhoff, U. Iron-sulfur protein biogenesis in eukaryotes: components and mechanisms. Annu. Rev. Cell Dev. Biol. 22, 457-486 (2006).
    • (2006) Annu. Rev. Cell Dev. Biol , vol.22 , pp. 457-486
    • Lill, R.1    Mühlenhoff, U.2
  • 7
    • 34247124148 scopus 로고    scopus 로고
    • Molecular chaperones HscA/Ssq1 and HscB/Jac1 and their roles in iron-sulfur protein maturation
    • Vickery, L. E. & Cupp-Vickery, J. R. Molecular chaperones HscA/Ssq1 and HscB/Jac1 and their roles in iron-sulfur protein maturation. Crit. Rev. Biochem. Mol. Biol. 42, 95-111 (2007).
    • (2007) Crit. Rev. Biochem. Mol. Biol , vol.42 , pp. 95-111
    • Vickery, L.E.1    Cupp-Vickery, J.R.2
  • 8
    • 47249094614 scopus 로고    scopus 로고
    • Maturation of iron-sulfur proteins in eukaryotes: Mechanisms, connected processes, and diseases
    • Lill, R. & Mühlenhoff, U. Maturation of iron-sulfur proteins in eukaryotes: mechanisms, connected processes, and diseases. Annu. Rev. Biochem. 77, 669-700 (2008).
    • (2008) Annu. Rev. Biochem , vol.77 , pp. 669-700
    • Lill, R.1    Mühlenhoff, U.2
  • 10
    • 47249142777 scopus 로고    scopus 로고
    • Iron-sulfur cluster biogenesis and human disease
    • Rouault, T. A. & Tong, W. H. Iron-sulfur cluster biogenesis and human disease. Trends Genet. 24, 398-407 (2008).
    • (2008) Trends Genet , vol.24 , pp. 398-407
    • Rouault, T.A.1    Tong, W.H.2
  • 11
    • 54349118938 scopus 로고    scopus 로고
    • Iron-sulfur cluster biogenesis systems and their crosstalk
    • Xu, X. M. & Moller, S. G. Iron-sulfur cluster biogenesis systems and their crosstalk. ChemBioChem 9, 2355-2362 (2008).
    • (2008) ChemBioChem , vol.9 , pp. 2355-2362
    • Xu, X.M.1    Moller, S.G.2
  • 12
    • 44549087696 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis in bacteria: Mechanisms of cluster assembly and transfer
    • Fontecave, M. & Ollagnier-de-Choudens, S. Iron-sulfur cluster biosynthesis in bacteria: mechanisms of cluster assembly and transfer. Arch. Biochem. Biophys. 474, 226-237 (2008).
    • (2008) Arch. Biochem. Biophys , vol.474 , pp. 226-237
    • Fontecave, M.1    Ollagnier-de-Choudens, S.2
  • 14
    • 35348854977 scopus 로고    scopus 로고
    • Self-sacrifice in radical S-adenosylmethionine proteins
    • Booker, S. J., Cicchillo, R. M. & Grove, T. L. Self-sacrifice in radical S-adenosylmethionine proteins. Curr. Opin. Chem. Biol. 11, 543-552 (2007).
    • (2007) Curr. Opin. Chem. Biol , vol.11 , pp. 543-552
    • Booker, S.J.1    Cicchillo, R.M.2    Grove, T.L.3
  • 15
    • 33748428875 scopus 로고    scopus 로고
    • The DNA repair helicases XPD and FancJ have essential iron-sulfur domains
    • Rudolf, J., Makrantoni, V., Ingledew, W. J., Stark, M. J. & White, M. F. The DNA repair helicases XPD and FancJ have essential iron-sulfur domains. Mol. Cell 23, 801-808 (2006).
    • (2006) Mol. Cell , vol.23 , pp. 801-808
    • Rudolf, J.1    Makrantoni, V.2    Ingledew, W.J.3    Stark, M.J.4    White, M.F.5
  • 16
    • 20044391418 scopus 로고    scopus 로고
    • Biogenesis of cytosolic ribosomes requires the essential iron-sulphur protein Rli1p and mitochondria
    • Kispal, G. et al. Biogenesis of cytosolic ribosomes requires the essential iron-sulphur protein Rli1p and mitochondria. EMBO J. 24, 589-598 (2005).
    • (2005) EMBO J , vol.24 , pp. 589-598
    • Kispal, G.1
  • 17
    • 43149119755 scopus 로고    scopus 로고
    • X-ray structure of the complete ABC enzyme ABCE1 from Pyrococcus abyssi
    • Karcher, A., Schele, A. & Hopfner, K. P. X-ray structure of the complete ABC enzyme ABCE1 from Pyrococcus abyssi. J. Biol. Chem. 283, 7962-7971 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 7962-7971
    • Karcher, A.1    Schele, A.2    Hopfner, K.P.3
  • 18
    • 50649117912 scopus 로고    scopus 로고
    • Cellular defenses against superoxide and hydrogen peroxide
    • Imlay, J. A. Cellular defenses against superoxide and hydrogen peroxide. Annu. Rev. Biochem. 77, 755-776 (2008).
    • (2008) Annu. Rev. Biochem , vol.77 , pp. 755-776
    • Imlay, J.A.1
  • 19
    • 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, 1903-1908 (2006).
    • (2006) Science , vol.314 , pp. 1903-1908
    • Walden, W.E.1
  • 20
    • 33746361251 scopus 로고    scopus 로고
    • Rouault, T. A. The role of iron regulatory proteins in mammalian iron homeostasis and disease. Nature Chem. Biol. 2, 406-414 (2006).
    • Rouault, T. A. The role of iron regulatory proteins in mammalian iron homeostasis and disease. Nature Chem. Biol. 2, 406-414 (2006).
  • 21
    • 33746864096 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron homeostasis by iron regulatory proteins
    • Wallander, M. L., Leibold, E. A. & Eisenstein, R. S. Molecular control of vertebrate iron homeostasis by iron regulatory proteins. Biochim. Biophys. Acta 1763, 668-689 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 668-689
    • Wallander, M.L.1    Leibold, E.A.2    Eisenstein, R.S.3
  • 22
    • 39149112760 scopus 로고    scopus 로고
    • The functional duality of iron regulatory protein 1
    • Volz, K. The functional duality of iron regulatory protein 1. Curr. Opin. Struct. Biol. 18, 106-111 (2008).
    • (2008) Curr. Opin. Struct. Biol , vol.18 , pp. 106-111
    • Volz, K.1
  • 23
    • 0033565665 scopus 로고    scopus 로고
    • The mitochondrial proteins Atm1p and Nfs1p are required for biogenesis of cytosolic Fe/S proteins
    • This paper and reference 28 functionally characterize the first components of the mitochondrial ISC assembly machinery and show the role of mitochondria for both cytosolic Fe-S-protein biogenesis and iron homeostasis
    • Kispal, G., Csere, P., Prohl, C. & Lill, R. The mitochondrial proteins Atm1p and Nfs1p are required for biogenesis of cytosolic Fe/S proteins. EMBO J. 18, 3981-3989 (1999). This paper and reference 28 functionally characterize the first components of the mitochondrial ISC assembly machinery and show the role of mitochondria for both cytosolic Fe-S-protein biogenesis and iron homeostasis.
    • (1999) EMBO J , vol.18 , pp. 3981-3989
    • Kispal, G.1    Csere, P.2    Prohl, C.3    Lill, R.4
  • 24
    • 50149115452 scopus 로고    scopus 로고
    • Biosynthesis of the iron-molybdenum cofactor of nitrogenase
    • Rubio, L. M. & Ludden, P. W. Biosynthesis of the iron-molybdenum cofactor of nitrogenase. Annu. Rev. Microbiol. 62, 93-111 (2008).
    • (2008) Annu. Rev. Microbiol , vol.62 , pp. 93-111
    • Rubio, L.M.1    Ludden, P.W.2
  • 26
    • 34047134687 scopus 로고    scopus 로고
    • Metallocenter assembly of the hydrogenase enzymes
    • Leach, M. R. & Zamble, D. B. Metallocenter assembly of the hydrogenase enzymes. Curr. Opin. Chem. Biol. 11, 159-165 (2007).
    • (2007) Curr. Opin. Chem. Biol , vol.11 , pp. 159-165
    • Leach, M.R.1    Zamble, D.B.2
  • 27
    • 0032557666 scopus 로고    scopus 로고
    • Zheng, L., Cash, V. L., Flint, D. H. & Dean, D. R. Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii. J. Biol. Chem. 273, 13264-13272 (1998). This paper describes the isc operon encoding components of the bacterial ISC assembly machinery.
    • Zheng, L., Cash, V. L., Flint, D. H. & Dean, D. R. Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii. J. Biol. Chem. 273, 13264-13272 (1998). This paper describes the isc operon encoding components of the bacterial ISC assembly machinery.
  • 28
    • 0033621156 scopus 로고    scopus 로고
    • Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae
    • Schilke, B., Voisine, C., Beinert, H. & Craig, E. Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae. Proc. Natl Acad. Sci. USA 96, 10206-10211 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 10206-10211
    • Schilke, B.1    Voisine, C.2    Beinert, H.3    Craig, E.4
  • 29
    • 0034681155 scopus 로고    scopus 로고
    • NifS-directed assembly of a transient [2Fe-2S] cluster within the NifU protein
    • This paper introduces the concept of de novo Fe-S-cluster assembly on a scaffold protein
    • Yuvaniyama, P., Agar, J. N., Cash, V. L., Johnson, M. K. & Dean, D. R. NifS-directed assembly of a transient [2Fe-2S] cluster within the NifU protein. Proc. Natl Acad. Sci. USA 97, 599-604 (2000). This paper introduces the concept of de novo Fe-S-cluster assembly on a scaffold protein.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 599-604
    • Yuvaniyama, P.1    Agar, J.N.2    Cash, V.L.3    Johnson, M.K.4    Dean, D.R.5
  • 30
    • 0141737067 scopus 로고    scopus 로고
    • Mühlenhoff, U., Gerber, J., Richhardt, N. & Lill, R. Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p. EMBO J. 22, 4815-4825 (2003). This paper defines various stages of mitochondrial Fe-S-protein assembly and verifies the scaffold concept in vivo.
    • Mühlenhoff, U., Gerber, J., Richhardt, N. & Lill, R. Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p. EMBO J. 22, 4815-4825 (2003). This paper defines various stages of mitochondrial Fe-S-protein assembly and verifies the scaffold concept in vivo.
  • 32
    • 34250187112 scopus 로고    scopus 로고
    • In vitro activation of apo-aconitase using a [4Fe-4S] clusterloaded form of the IscU [Fe-S] cluster scaffolding protein
    • Unciuleac, M. C. et al. In vitro activation of apo-aconitase using a [4Fe-4S] clusterloaded form of the IscU [Fe-S] cluster scaffolding protein. Biochemistry 46, 6812-6821 (2007).
    • (2007) Biochemistry , vol.46 , pp. 6812-6821
    • Unciuleac, M.C.1
  • 33
    • 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, 6804-6811 (2007).
    • (2007) Biochemistry , vol.46 , pp. 6804-6811
    • Chandramouli, K.1
  • 34
    • 0027450059 scopus 로고
    • Cysteine desulfurase activity indicates a role for NifS in metallocluster biosynthesis
    • This paper identifies and characterizes the founding member of cysteine desulphurases
    • Zheng, L., White, R. H., Cash, V. L., Jack, R. F. & Dean, D. R. Cysteine desulfurase activity indicates a role for NifS in metallocluster biosynthesis. Proc. Natl Acad. Sci. USA 90, 2754-2758 (1993). This paper identifies and characterizes the founding member of cysteine desulphurases.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 2754-2758
    • Zheng, L.1    White, R.H.2    Cash, V.L.3    Jack, R.F.4    Dean, D.R.5
  • 35
    • 0034708346 scopus 로고    scopus 로고
    • Crystal structure of a NifS-like protein from Thermotoga maritima: Implications for iron-sulfur cluster assembly
    • Kaiser, J. T. et al. Crystal structure of a NifS-like protein from Thermotoga maritima: implications for iron-sulfur cluster assembly. J. Mol. Biol. 297, 451-464 (2000).
    • (2000) J. Mol. Biol , vol.297 , pp. 451-464
    • Kaiser, J.T.1
  • 36
    • 0038351831 scopus 로고    scopus 로고
    • Crystal structure of IscS, a cysteine desulfurase from Escherichia coli
    • Cupp-Vickery, J. R., Urbina, H. & Vickery, L. E. Crystal structure of IscS, a cysteine desulfurase from Escherichia coli. J. Mol. Biol. 330, 1049-1059 (2003).
    • (2003) J. Mol. Biol , vol.330 , pp. 1049-1059
    • Cupp-Vickery, J.R.1    Urbina, H.2    Vickery, L.E.3
  • 37
    • 30444449009 scopus 로고    scopus 로고
    • Essential role of Isd11 in iron-sulfur cluster synthesis on Isu scaffold proteins
    • Wiedemann, N. et al. Essential role of Isd11 in iron-sulfur cluster synthesis on Isu scaffold proteins. EMBO J. 25, 184-195 (2006).
    • (2006) EMBO J , vol.25 , pp. 184-195
    • Wiedemann, N.1
  • 38
    • 30444433568 scopus 로고    scopus 로고
    • The Nfs1 interacting protein Isd11 has an essential role in Fe/S cluster biogenesis in mitochondria
    • Adam, A. C., Bornhövd, C., Prokisch, H., Neupert, W. & Hell, K. The Nfs1 interacting protein Isd11 has an essential role in Fe/S cluster biogenesis in mitochondria. EMBO J. 25, 174-183 (2006).
    • (2006) EMBO J , vol.25 , pp. 174-183
    • Adam, A.C.1    Bornhövd, C.2    Prokisch, H.3    Neupert, W.4    Hell, K.5
  • 39
    • 0141623560 scopus 로고    scopus 로고
    • An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1
    • 906-911
    • Gerber, J., Mühlenhoff, U. & Lill, R. An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1. EMBO Rep. 4, 906-911 (2003).
    • (2003) EMBO Rep , vol.4
    • Gerber, J.1    Mühlenhoff, U.2    Lill, R.3
  • 40
    • 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. & Fontecave, M. 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).
    • (2006) J. Biol. Chem , vol.281 , pp. 16256-16263
    • Layer, G.1    Ollagnier-de Choudens, S.2    Sanakis, Y.3    Fontecave, M.4
  • 41
    • 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, 269-291 (2006).
    • (2006) Crit. Rev. Biochem. Mol. Biol , vol.41 , pp. 269-291
    • Bencze, K.Z.1
  • 42
    • 45549107531 scopus 로고    scopus 로고
    • Binding of yeast frataxin to the scaffold for Fe-S cluster biogenesis, Isu
    • Wang, T. & Craig, E. A. Binding of yeast frataxin to the scaffold for Fe-S cluster biogenesis, Isu. J. Biol. Chem. 283, 12674-12679 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 12674-12679
    • Wang, T.1    Craig, E.A.2
  • 43
    • 64049116040 scopus 로고    scopus 로고
    • Bacterial frataxin CyaY is the gatekeeper of iron-sulfur cluster formation catalyzed by IscS
    • Adinolfi, S. et al. Bacterial frataxin CyaY is the gatekeeper of iron-sulfur cluster formation catalyzed by IscS. Nature Struct. Mol. Biol. 16, 390-396 (2009).
    • (2009) Nature Struct. Mol. Biol , vol.16 , pp. 390-396
    • Adinolfi, S.1
  • 44
    • 33747170368 scopus 로고    scopus 로고
    • Evolution of mitochondrial chaperones utilized in Fe-S cluster biogenesis
    • Schilke, B. et al. Evolution of mitochondrial chaperones utilized in Fe-S cluster biogenesis. Curr. Biol. 16, 1660-1665 (2006).
    • (2006) Curr. Biol , vol.16 , pp. 1660-1665
    • Schilke, B.1
  • 45
    • 1842526422 scopus 로고    scopus 로고
    • Crystal structure of IscA, an iron-sulfur cluster assembly protein from Escherichia coli
    • Cupp-Vickery, J. R., Silberg, J. J., Ta, D. T. & Vickery, L. E. Crystal structure of IscA, an iron-sulfur cluster assembly protein from Escherichia coli. J. Mol. Biol. 338, 127-137 (2004).
    • (2004) J. Mol. Biol , vol.338 , pp. 127-137
    • Cupp-Vickery, J.R.1    Silberg, J.J.2    Ta, D.T.3    Vickery, L.E.4
  • 46
    • 3142716203 scopus 로고    scopus 로고
    • Sequence-specific interaction between mitochondrial Fe-S scaffold protein Isu and Hsp70 Ssq1 is essential for their in vivo function
    • Dutkiewicz, R. et al. Sequence-specific interaction between mitochondrial Fe-S scaffold protein Isu and Hsp70 Ssq1 is essential for their in vivo function. J. Biol. Chem. 279, 29167-29174 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 29167-29174
    • Dutkiewicz, R.1
  • 47
    • 33748782301 scopus 로고    scopus 로고
    • Chandramouli, K. & Johnson, M. K. HscA and HscB stimulate [2Fe-2S] cluster transfer from IscU to apoferredoxin in an ATP-dependent reaction. Biochemistry 45, 11087-11095 (2006). This paper and reference 49 define the role of heat-shock proteins in Fe-S-cluster transfer from scaffold to target proteins in vitro.
    • Chandramouli, K. & Johnson, M. K. HscA and HscB stimulate [2Fe-2S] cluster transfer from IscU to apoferredoxin in an ATP-dependent reaction. Biochemistry 45, 11087-11095 (2006). This paper and reference 49 define the role of heat-shock proteins in Fe-S-cluster transfer from scaffold to target proteins in vitro.
  • 48
    • 33744948235 scopus 로고    scopus 로고
    • Characterization of the interaction between the J-protein Jac1 and the scaffold for Fe-S cluster biogenesis, Isu1
    • Andrew, A. J., Dutkiewicz, R., Knieszner, H., Craig, E. A. & Marszalek, J. Characterization of the interaction between the J-protein Jac1 and the scaffold for Fe-S cluster biogenesis, Isu1. J. Biol. Chem. 281, 14580-14587 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 14580-14587
    • Andrew, A.J.1    Dutkiewicz, R.2    Knieszner, H.3    Craig, E.A.4    Marszalek, J.5
  • 49
    • 57049159293 scopus 로고    scopus 로고
    • Studies on the mechanism of catalysis of iron-sulfur cluster transfer from IscU[2Fe2S] by HscA/HscB chaperones
    • Bonomi, F., Iametti, S., Morleo, A., Ta, D. & Vickery, L. E. Studies on the mechanism of catalysis of iron-sulfur cluster transfer from IscU[2Fe2S] by HscA/HscB chaperones. Biochemistry 47, 12795-12801 (2008).
    • (2008) Biochemistry , vol.47 , pp. 12795-12801
    • Bonomi, F.1    Iametti, S.2    Morleo, A.3    Ta, D.4    Vickery, L.E.5
  • 50
    • 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, 1122-1133 (2008).
    • (2008) EMBO J , vol.27 , pp. 1122-1133
    • Bandyopadhyay, S.1
  • 51
    • 40749086415 scopus 로고    scopus 로고
    • Mitochondrial Iba57p is required for Fe/S cluster formation on aconitase and activation of radical SAM enzymes
    • Gelling, C., Dawes, I. W., Richhardt, N., Lill, R. & Mühlenhoff, U. Mitochondrial Iba57p is required for Fe/S cluster formation on aconitase and activation of radical SAM enzymes. Mol. Cell. Biol. 28, 1851-1861 (2008).
    • (2008) Mol. Cell. Biol , vol.28 , pp. 1851-1861
    • Gelling, C.1    Dawes, I.W.2    Richhardt, N.3    Lill, R.4    Mühlenhoff, U.5
  • 52
    • 66949146078 scopus 로고    scopus 로고
    • IscA/SufA paralogs are required for the [4Fe-4S] cluster assembly in enzymes of multiple physiological pathways in Escherichia coli under aerobic growth conditions
    • Tan, G., Lu, J., Bitoun, J. P., Huang, H. & Ding, H. IscA/SufA paralogs are required for the [4Fe-4S] cluster assembly in enzymes of multiple physiological pathways in Escherichia coli under aerobic growth conditions. Biochem J. 420, 463-472 (2009).
    • (2009) Biochem J , vol.420 , pp. 463-472
    • Tan, G.1    Lu, J.2    Bitoun, J.P.3    Huang, H.4    Ding, H.5
  • 53
    • 35348876543 scopus 로고    scopus 로고
    • ErpA, an iron sulfur (Fe S) protein of the A-type essential for respiratory metabolism in Escherichia coli
    • Loiseau, L. et al. ErpA, an iron sulfur (Fe S) protein of the A-type essential for respiratory metabolism in Escherichia coli. Proc. Natl Acad. Sci. USA 104, 13626-13631 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 13626-13631
    • Loiseau, L.1
  • 54
    • 69949162828 scopus 로고    scopus 로고
    • Native Escherichia coli SufA, coexpressed with SufBCDSE, purifies as a [2Fe-2S] protein and acts as an Fe-S transporter to Fe-S target enzymes
    • Gupta, V. et al. Native Escherichia coli SufA, coexpressed with SufBCDSE, purifies as a [2Fe-2S] protein and acts as an Fe-S transporter to Fe-S target enzymes. J. Am. Chem. Soc. 131, 6149-6153 (2009).
    • (2009) J. Am. Chem. Soc , vol.131 , pp. 6149-6153
    • Gupta, V.1
  • 55
    • 47049126468 scopus 로고    scopus 로고
    • The iron-sulphur protein Ind1 is required for effective complex I assembly
    • Bych, K. et al. The iron-sulphur protein Ind1 is required for effective complex I assembly. EMBO J. 27, 1736-1746 (2008).
    • (2008) EMBO J , vol.27 , pp. 1736-1746
    • Bych, K.1
  • 56
    • 0037047411 scopus 로고    scopus 로고
    • A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids
    • Takahashi, Y. & Tokumoto, U. A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids. J. Biol. Chem. 277, 28380-28383 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 28380-28383
    • Takahashi, Y.1    Tokumoto, U.2
  • 57
    • 4644354002 scopus 로고    scopus 로고
    • Interchangeability and distinct properties of bacterial Fe-S cluster assembly systems: Functional replacement of the isc and suf operons in Escherichia coli with the nifSU-like operon from Helicobacter pylori
    • Tokumoto, U., Kitamura, S., Fukuyama, K. & Takahashi, Y. Interchangeability and distinct properties of bacterial Fe-S cluster assembly systems: functional replacement of the isc and suf operons in Escherichia coli with the nifSU-like operon from Helicobacter pylori. J. Biochem. 136, 199-209 (2004).
    • (2004) J. Biochem , vol.136 , pp. 199-209
    • Tokumoto, U.1    Kitamura, S.2    Fukuyama, K.3    Takahashi, Y.4
  • 58
    • 0242664733 scopus 로고    scopus 로고
    • The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in E. coli
    • This paper and reference 59 describe the first functional analyses and interactions of the Suf proteins
    • Outten, F. W., Wood, M. J., Munoz, F. M. & Storz, G. The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in E. coli. J. Biol. Chem. 278, 45713-45719 (2003). This paper and reference 59 describe the first functional analyses and interactions of the Suf proteins.
    • (2003) J. Biol. Chem , vol.278 , pp. 45713-45719
    • Outten, F.W.1    Wood, M.J.2    Munoz, F.M.3    Storz, G.4
  • 59
    • 0141532194 scopus 로고    scopus 로고
    • Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form a new type of cysteine desulfurase
    • Loiseau, L., Ollagnier-de-Choudens, S., Nachin, L., Fontecave, M. & Barras, F. Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form a new type of cysteine desulfurase. J. Biol. Chem. 278, 38352-38359 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 38352-38359
    • Loiseau, L.1    Ollagnier-de-Choudens, S.2    Nachin, L.3    Fontecave, M.4    Barras, F.5
  • 60
    • 33750083296 scopus 로고    scopus 로고
    • Enzymatic activation of sulfur for incorporation into biomolecules in prokaryotes
    • Kessler, D. Enzymatic activation of sulfur for incorporation into biomolecules in prokaryotes. FEMS Microbiol. Rev. 30, 825-840 (2006).
    • (2006) FEMS Microbiol. Rev , vol.30 , pp. 825-840
    • Kessler, D.1
  • 61
    • 34250316177 scopus 로고    scopus 로고
    • SufE transfers sulfur from SufS to SufB for iron-sulfur cluster assembly
    • Layer, G. et al. SufE transfers sulfur from SufS to SufB for iron-sulfur cluster assembly. J. Biol. Chem. 282, 13342-13350 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 13342-13350
    • Layer, G.1
  • 62
    • 33947540909 scopus 로고    scopus 로고
    • The SUF iron-sulfur cluster biosynthetic machinery: Sulfur transfer from the SUFS-SUFE complex to SUFA
    • Sendra, M., Ollagnier de Choudens, S., Lascoux, D., Sanakis, Y. & Fontecave, M. The SUF iron-sulfur cluster biosynthetic machinery: sulfur transfer from the SUFS-SUFE complex to SUFA. FEBS Lett. 581, 1362-1368 (2007).
    • (2007) FEBS Lett , vol.581 , pp. 1362-1368
    • Sendra, M.1    Ollagnier de Choudens, S.2    Lascoux, D.3    Sanakis, Y.4    Fontecave, M.5
  • 63
    • 22444449790 scopus 로고    scopus 로고
    • High-quality homology models derived from NMR and X-ray structures of E. coli proteins YgdK and Suf E suggest that all members of the YgdK/Suf E protein family are enhancers of cysteine desulfurases
    • Liu, G. et al. High-quality homology models derived from NMR and X-ray structures of E. coli proteins YgdK and Suf E suggest that all members of the YgdK/Suf E protein family are enhancers of cysteine desulfurases. Protein Sci. 14, 1597-1608 (2005).
    • (2005) Protein Sci , vol.14 , pp. 1597-1608
    • Liu, G.1
  • 64
    • 0037415722 scopus 로고    scopus 로고
    • SufC: An unorthodox cytoplasmic ABC/ ATPase required for [Fe-S] biogenesis under oxidative stress
    • Nachin, L., Loiseau, L., Expert, D. & Barras, F. SufC: an unorthodox cytoplasmic ABC/ ATPase required for [Fe-S] biogenesis under oxidative stress. EMBO J. 22, 427-437 (2003).
    • (2003) EMBO J , vol.22 , pp. 427-437
    • Nachin, L.1    Loiseau, L.2    Expert, D.3    Barras, F.4
  • 65
    • 18844420058 scopus 로고    scopus 로고
    • Structural characterization of an iron-sulfur cluster assembly protein IscU in a zinc-bound form
    • Liu, J. et al. Structural characterization of an iron-sulfur cluster assembly protein IscU in a zinc-bound form. Proteins 59, 875-881 (2005).
    • (2005) Proteins , vol.59 , pp. 875-881
    • Liu, J.1
  • 66
    • 60649117402 scopus 로고    scopus 로고
    • Structural studies of the Enterococcus faecalis SufU [Fe-S] cluster protein
    • Riboldi, G. P., Verli, H. & Frazzon, J. Structural studies of the Enterococcus faecalis SufU [Fe-S] cluster protein. BMC Biochem. 10, 3 (2009).
    • (2009) BMC Biochem , vol.10 , pp. 3
    • Riboldi, G.P.1    Verli, H.2    Frazzon, J.3
  • 67
    • 33745213111 scopus 로고    scopus 로고
    • CpNifS-dependent iron-sulfur cluster biogenesis in chloroplasts
    • Ye, H., Pilon, M. & Pilon-Smits, E. A. CpNifS-dependent iron-sulfur cluster biogenesis in chloroplasts. New Phytol. 171, 285-292 (2006).
    • (2006) New Phytol , vol.171 , pp. 285-292
    • Ye, H.1    Pilon, M.2    Pilon-Smits, E.A.3
  • 68
    • 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, 993-1007 (2004).
    • (2004) Plant Cell , vol.16 , pp. 993-1007
    • Yabe, T.1
  • 69
    • 2442707887 scopus 로고    scopus 로고
    • The yeast scaffold proteins Isu1p and Isu2p are required inside mitochondria for maturation of cytosolic Fe/S proteins
    • Gerber, J., Neumann, K., Prohl, C., Mühlenhoff, U. & Lill, R. The yeast scaffold proteins Isu1p and Isu2p are required inside mitochondria for maturation of cytosolic Fe/S proteins. Mol. Cell. Biol. 24, 4848-4857 (2004).
    • (2004) Mol. Cell. Biol , vol.24 , pp. 4848-4857
    • Gerber, J.1    Neumann, K.2    Prohl, C.3    Mühlenhoff, U.4    Lill, R.5
  • 70
    • 17144378216 scopus 로고    scopus 로고
    • Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis
    • Rouault, T. A. & Tong, W. H. Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis. Nature Rev. Mol. Cell Biol. 6, 345-351 (2005).
    • (2005) Nature Rev. Mol. Cell Biol , vol.6 , pp. 345-351
    • Rouault, T.A.1    Tong, W.H.2
  • 71
    • 33644623262 scopus 로고    scopus 로고
    • Tong, W. H. & Rouault, T. A. Functions of mitochondrial ISCU and cytosolic ISCU in mammalian iron-sulfur cluster biogenesis and iron homeostasis. Cell Metab. 3, 199-210 (2006). This paper and references 72, 73, 89 and 97 demonstrate the general conservation of Fe-Sprotein biogenesis in vertebrates.
    • Tong, W. H. & Rouault, T. A. Functions of mitochondrial ISCU and cytosolic ISCU in mammalian iron-sulfur cluster biogenesis and iron homeostasis. Cell Metab. 3, 199-210 (2006). This paper and references 72, 73, 89 and 97 demonstrate the general conservation of Fe-Sprotein biogenesis in vertebrates.
  • 72
    • 33746509655 scopus 로고    scopus 로고
    • Role of human mitochondrial Nfs1 in cytosolic iron-sulfur protein biogenesis and iron regulation
    • Biederbick, A. et al. Role of human mitochondrial Nfs1 in cytosolic iron-sulfur protein biogenesis and iron regulation. Mol. Cell. Biol. 26, 5675-5687 (2006).
    • (2006) Mol. Cell. Biol , vol.26 , pp. 5675-5687
    • Biederbick, A.1
  • 73
    • 33644772614 scopus 로고    scopus 로고
    • The mitochondrial ATP-binding cassette transporter Abcb7 is essential in mice and participates in cytosolic iron-sulphur cluster biogenesis
    • Pondarre, C. et al. The mitochondrial ATP-binding cassette transporter Abcb7 is essential in mice and participates in cytosolic iron-sulphur cluster biogenesis. Hum. Mol. Genet. 15, 953-964 (2006).
    • (2006) Hum. Mol. Genet , vol.15 , pp. 953-964
    • Pondarre, C.1
  • 74
    • 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, 3552-3559 (2007).
    • (2007) Blood , vol.109 , pp. 3552-3559
    • Cavadini, P.1
  • 75
    • 21244445718 scopus 로고    scopus 로고
    • A disulfide relay system in the intermembrane space of mitochondria that mediates protein import
    • Mesecke, N. et al. A disulfide relay system in the intermembrane space of mitochondria that mediates protein import. Cell 121, 1059-1070 (2005).
    • (2005) Cell , vol.121 , pp. 1059-1070
    • Mesecke, N.1
  • 76
    • 34247247617 scopus 로고    scopus 로고
    • Netz, D. J., Pierik, A. J., Stümpfig, M., Mühlenhoff, U. & Lill, R. The Cfd1-Nbp35 complex acts as a scaffold for iron-sulfur protein assembly in the yeast cytosol. Nature Chem. Biol. 3, 278-286 (2007). This paper defines various stages of cytosolic Fe-S-protein assembly and identifies Cfd1-Nbp35 as a cytosolic scaffold.
    • Netz, D. J., Pierik, A. J., Stümpfig, M., Mühlenhoff, U. & Lill, R. The Cfd1-Nbp35 complex acts as a scaffold for iron-sulfur protein assembly in the yeast cytosol. Nature Chem. Biol. 3, 278-286 (2007). This paper defines various stages of cytosolic Fe-S-protein assembly and identifies Cfd1-Nbp35 as a cytosolic scaffold.
  • 77
    • 0141848663 scopus 로고    scopus 로고
    • A novel eukaryotic factor for cytosolic Fe-S cluster assembly
    • This paper identifies Cfd1 as the first extra-mitochondrial Fe-S-protein biogenesis component
    • Roy, A., Solodovnikova, N., Nicholson, T., Antholine, W. & Walden, W. E. A novel eukaryotic factor for cytosolic Fe-S cluster assembly. EMBO J. 22, 4826-4835 (2003). This paper identifies Cfd1 as the first extra-mitochondrial Fe-S-protein biogenesis component.
    • (2003) EMBO J , vol.22 , pp. 4826-4835
    • Roy, A.1    Solodovnikova, N.2    Nicholson, T.3    Antholine, W.4    Walden, W.E.5
  • 78
    • 14744279245 scopus 로고    scopus 로고
    • The eukaryotic P-loop NTPase Nbp35: An essential component of the cytosolic and nuclear iron-sulfur protein assembly machinery
    • Hausmann, A. et al. The eukaryotic P-loop NTPase Nbp35: an essential component of the cytosolic and nuclear iron-sulfur protein assembly machinery. Proc. Natl Acad. Sci. USA 102, 3266-3271 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 3266-3271
    • Hausmann, A.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, 1246-1257 (2007).
    • (2007) Structure , vol.15 , pp. 1246-1257
    • Srinivasan, V.1
  • 80
    • 51349089178 scopus 로고    scopus 로고
    • Dre2, a conserved eukaryotic Fe/S cluster protein, functions in cytosolic Fe/S protein biogenesis
    • Zhang, Y. et al. Dre2, a conserved eukaryotic Fe/S cluster protein, functions in cytosolic Fe/S protein biogenesis. Mol. Cell. Biol. 28, 5569-5582 (2008).
    • (2008) Mol. Cell. Biol , vol.28 , pp. 5569-5582
    • Zhang, Y.1
  • 81
    • 44049094146 scopus 로고    scopus 로고
    • A role for IOP1 in mammalian cytosolic iron-sulfur protein biogenesis
    • Song, D. & Lee, F. S. A role for IOP1 in mammalian cytosolic iron-sulfur protein biogenesis. J. Biol. Chem. 283, 9231-9238 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 9231-9238
    • Song, D.1    Lee, F.S.2
  • 82
    • 50249156530 scopus 로고    scopus 로고
    • Human Nbp35 is essential for both cytosolic iron-sulfur protein assembly and iron homeostasis
    • Stehling, O. et al. Human Nbp35 is essential for both cytosolic iron-sulfur protein assembly and iron homeostasis. Mol. Cell. Biol. 28, 5517-5528 (2008).
    • (2008) Mol. Cell. Biol , vol.28 , pp. 5517-5528
    • Stehling, O.1
  • 83
    • 14744294785 scopus 로고    scopus 로고
    • Iron-sulfur protein biogenesis in eukaryotes
    • Lill, R. & Mühlenhoff, U. Iron-sulfur protein biogenesis in eukaryotes. Trends Biochem. Sci. 30, 133-141 (2005).
    • (2005) Trends Biochem. Sci , vol.30 , pp. 133-141
    • Lill, R.1    Mühlenhoff, U.2
  • 84
    • 34548492954 scopus 로고    scopus 로고
    • An iron-sulfur domain of the eukaryotic primase is essential for RNA primer synthesis
    • Klinge, S., Hirst, J., Maman, J. D., Krude, T. & Pellegrini, L. An iron-sulfur domain of the eukaryotic primase is essential for RNA primer synthesis. Nature Struct. Mol. Biol. 14, 875-877 (2007).
    • (2007) Nature Struct. Mol. Biol , vol.14 , pp. 875-877
    • Klinge, S.1    Hirst, J.2    Maman, J.D.3    Krude, T.4    Pellegrini, L.5
  • 85
    • 22144494670 scopus 로고    scopus 로고
    • Degenerate mitochondria
    • 525-530
    • van der Giezen, M. & Tovar, J. Degenerate mitochondria. EMBO Rep. 6, 525-530 (2005).
    • (2005) EMBO Rep , vol.6
    • van der Giezen, M.1    Tovar, J.2
  • 86
    • 33645456207 scopus 로고    scopus 로고
    • Eukaryotic evolution, changes and challenges
    • Embley, T. M. & Martin, W. Eukaryotic evolution, changes and challenges. Nature 440, 623-630 (2006).
    • (2006) Nature , vol.440 , pp. 623-630
    • Embley, T.M.1    Martin, W.2
  • 87
    • 0344633597 scopus 로고    scopus 로고
    • Mitochondrial remnant organelles of Giardia function in iron-sulphur protein maturation
    • Tovar, J. et al. Mitochondrial remnant organelles of Giardia function in iron-sulphur protein maturation. Nature 426, 172-176 (2003).
    • (2003) Nature , vol.426 , pp. 172-176
    • Tovar, J.1
  • 88
    • 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, 624-628 (2008).
    • (2008) Nature , vol.452 , pp. 624-628
    • Goldberg, A.V.1
  • 89
    • 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, 1035-1039 (2005).
    • (2005) Nature , vol.436 , pp. 1035-1039
    • Wingert, R.A.1
  • 90
    • 33644748145 scopus 로고    scopus 로고
    • Mitoferrin is essential for erythroid iron assimilation
    • Shaw, G. C. et al. Mitoferrin is essential for erythroid iron assimilation. Nature 440, 96-100 (2006).
    • (2006) Nature , vol.440 , pp. 96-100
    • Shaw, G.C.1
  • 91
    • 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, 652-660 (2008).
    • (2008) Am. J. Hum. Genet , vol.82 , pp. 652-660
    • Mochel, F.1
  • 92
    • 44349149346 scopus 로고    scopus 로고
    • Myopathy with lactic acidosis is linked to chromosome 12q23.3-24.11 and caused by an intron mutation in the ISCU gene resulting in a splicing defect
    • Olsson, A., Lind, L., Thornell, L. E. & Holmberg, M. Myopathy with lactic acidosis is linked to chromosome 12q23.3-24.11 and caused by an intron mutation in the ISCU gene resulting in a splicing defect. Hum. Mol. Genet. 17, 1666-1667 (2008).
    • (2008) Hum. Mol. Genet , vol.17 , pp. 1666-1667
    • Olsson, A.1    Lind, L.2    Thornell, L.E.3    Holmberg, M.4
  • 93
    • 33646349748 scopus 로고    scopus 로고
    • Mueller, E. G. Trafficking in persulfides: delivering sulfur in biosynthetic pathways. Nature Chem. Biol. 2, 185-194 (2006).
    • Mueller, E. G. Trafficking in persulfides: delivering sulfur in biosynthetic pathways. Nature Chem. Biol. 2, 185-194 (2006).
  • 94
    • 34147210386 scopus 로고    scopus 로고
    • Thio modification of yeast cytosolic tRNA is an iron-sulfur protein-dependent pathway
    • Nakai, Y., Nakai, M., Lill, R., Suzuki, T. & Hayashi, H. Thio modification of yeast cytosolic tRNA is an iron-sulfur protein-dependent pathway. Mol. Cell. Biol. 27, 2841-2847 (2007).
    • (2007) Mol. Cell. Biol , vol.27 , pp. 2841-2847
    • Nakai, Y.1    Nakai, M.2    Lill, R.3    Suzuki, T.4    Hayashi, H.5
  • 96
    • 15444371876 scopus 로고    scopus 로고
    • Activation of the iron-regulon by the yeast Aft1/Aft2 transcription factors depends on mitochondrial, but not cytosolic iron-sulfur protein biogenesis
    • Rutherford, J. C. et al. Activation of the iron-regulon by the yeast Aft1/Aft2 transcription factors depends on mitochondrial, but not cytosolic iron-sulfur protein biogenesis. J. Biol. Chem. 280, 10135-10140 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 10135-10140
    • Rutherford, J.C.1
  • 97
    • 9744248303 scopus 로고    scopus 로고
    • Iron-sulfur protein maturation in human cells: Evidence for a function of frataxin
    • Stehling, O., Elsässer, H. P., Brückel, B., Mühlenhoff, U. & Lill, R. Iron-sulfur protein maturation in human cells: evidence for a function of frataxin. Hum. Mol. Genet. 13, 3007-3015 (2004).
    • (2004) Hum. Mol. Genet , vol.13 , pp. 3007-3015
    • Stehling, O.1    Elsässer, H.P.2    Brückel, B.3    Mühlenhoff, U.4    Lill, R.5
  • 98
    • 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, 1423-1427 (1996).
    • (1996) Science , vol.271 , pp. 1423-1427
    • Campuzano, V.1
  • 99
    • 0034329310 scopus 로고    scopus 로고
    • Human ABC7 transporter: Gene structure and mutation causing X-linked sideroblastic anemia with ataxia (XLSA/A) with disruption of cytosolic iron-sulfur protein maturation
    • Bekri, S. et al. Human ABC7 transporter: gene structure and mutation causing X-linked sideroblastic anemia with ataxia (XLSA/A) with disruption of cytosolic iron-sulfur protein maturation. Blood 96, 3256-3264 (2000).
    • (2000) Blood , vol.96 , pp. 3256-3264
    • Bekri, S.1
  • 100
    • 38349136202 scopus 로고    scopus 로고
    • GTP is required for iron-sulfur cluster biogenesis in mitochondria
    • Amutha, B. et al. GTP is required for iron-sulfur cluster biogenesis in mitochondria. J. Biol. Chem. 283, 1362-1371 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 1362-1371
    • Amutha, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.