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Volumn 83, Issue , 2013, Pages 1-92

Iron-Sulphur clusters, their biosynthesis, and biological functions in protozoan parasites

Author keywords

CIA; Hydrogenosome; Iron sulphur cluster; ISC; Mitochondria; Mitosome; NIF; SUF

Indexed keywords

CYSTEINE; DISULFIDE; DRE2 PROTEIN; FRATAXIN; IRON; NIFS PROTEIN; NIFU PROTEIN; NUCLEAR ARCHITECTURE RELATED PROTEIN 1; NUCLEOTIDE BINDING PROTEIN; NUCLEOTIDE BINDING PROTEIN 35; PROTEIN; SCAFFOLD PROTEIN; SIDEROPHORE; SULFUR; TAH18 PROTEIN; TRANSFER RNA; UNCLASSIFIED DRUG;

EID: 84880412669     PISSN: 0065308X     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-407705-8.00001-X     Document Type: Chapter
Times cited : (35)

References (342)
  • 2
    • 0025831040 scopus 로고
    • The biology of Giardia spp
    • Adam R.D. The biology of Giardia spp. Microbiol. Rev. 1991, 55:706-732.
    • (1991) Microbiol. Rev. , vol.55 , pp. 706-732
    • Adam, R.D.1
  • 3
    • 0034933985 scopus 로고    scopus 로고
    • Biology of Giardia lamblia
    • Adam R.D. Biology of Giardia lamblia. Clin. Microbiol. Rev. 2001, 14:447-475.
    • (2001) Clin. Microbiol. Rev. , vol.14 , pp. 447-475
    • Adam, R.D.1
  • 4
    • 30444433568 scopus 로고    scopus 로고
    • The Nfs1 interacting protein Isd11 has an essential role in Fe/S cluster biogenesis in mitochondria
    • Adam A.C., Bornhovd 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. 2006, 25:174-183.
    • (2006) EMBO J. , vol.25 , pp. 174-183
    • Adam, A.C.1    Bornhovd, C.2    Prokisch, H.3    Neupert, W.4    Hell, K.5
  • 6
    • 0034636795 scopus 로고    scopus 로고
    • IscU as a scaffold for iron-sulfur cluster biosynthesis: sequential assembly of [2Fe-2S] and [4Fe-4S] clusters in IscU
    • Agar J.N., Krebs C., Frazzon J., Huynh B.H., Dean D.R., Johnson M.K. IscU as a scaffold for iron-sulfur cluster biosynthesis: sequential assembly of [2Fe-2S] and [4Fe-4S] clusters in IscU. Biochemistry 2000, 39:7856-7862.
    • (2000) Biochemistry , vol.39 , pp. 7856-7862
    • Agar, J.N.1    Krebs, C.2    Frazzon, J.3    Huynh, B.H.4    Dean, D.R.5    Johnson, M.K.6
  • 8
    • 79956367445 scopus 로고    scopus 로고
    • Assembling Fe/S-clusters and modifying tRNAs: ancient co-factors meet ancient adaptors
    • Alfonzo J.D., Lukes J. Assembling Fe/S-clusters and modifying tRNAs: ancient co-factors meet ancient adaptors. Trends Parasitol. 2011, 27:235-238.
    • (2011) Trends Parasitol. , vol.27 , pp. 235-238
    • Alfonzo, J.D.1    Lukes, J.2
  • 9
    • 33846503255 scopus 로고    scopus 로고
    • Current therapeutics, their problems, and sulfur-containing-amino-acid metabolism as a novel target against infections by "amitochondriate" protozoan parasites
    • Ali V., Nozaki T. Current therapeutics, their problems, and sulfur-containing-amino-acid metabolism as a novel target against infections by "amitochondriate" protozoan parasites. Clin. Microbiol. Rev. 2007, 20:164-187.
    • (2007) Clin. Microbiol. Rev. , vol.20 , pp. 164-187
    • Ali, V.1    Nozaki, T.2
  • 10
    • 1942490139 scopus 로고    scopus 로고
    • An intestinal parasitic protist, Entamoeba histolytica, possesses a non-redundant nitrogen fixation-like system for iron-sulfur cluster assembly under anaerobic conditions
    • Ali V., Shigeta Y., Tokumoto U., Takahashi Y., Nozaki T. An intestinal parasitic protist, Entamoeba histolytica, possesses a non-redundant nitrogen fixation-like system for iron-sulfur cluster assembly under anaerobic conditions. J. Biol. Chem. 2004, 279:16863-16874.
    • (2004) J. Biol. Chem. , vol.279 , pp. 16863-16874
    • Ali, V.1    Shigeta, Y.2    Tokumoto, U.3    Takahashi, Y.4    Nozaki, T.5
  • 11
    • 27144438677 scopus 로고    scopus 로고
    • Erv1 mediates the Mia40-dependent protein import pathway and provides a functional link to the respiratory chain by shuttling electrons to cytochrome c
    • Allen S., Balabanidou V., Sideris D.P., Lisowsky T., Tokatlidis K. Erv1 mediates the Mia40-dependent protein import pathway and provides a functional link to the respiratory chain by shuttling electrons to cytochrome c. J. Mol. Biol. 2005, 353:937-944.
    • (2005) J. Mol. Biol. , vol.353 , pp. 937-944
    • Allen, S.1    Balabanidou, V.2    Sideris, D.P.3    Lisowsky, T.4    Tokatlidis, K.5
  • 12
    • 33845683300 scopus 로고    scopus 로고
    • Nucleotide excision repair disorders and the balance between cancer and aging
    • Andressoo J.O., Hoeijmakers J.H., Mitchell J.R. Nucleotide excision repair disorders and the balance between cancer and aging. Cell Cycle 2006, 5:2886-2888.
    • (2006) Cell Cycle , vol.5 , pp. 2886-2888
    • Andressoo, J.O.1    Hoeijmakers, J.H.2    Mitchell, J.R.3
  • 13
    • 33744948235 scopus 로고    scopus 로고
    • Characterization of the interaction between the J-protein Jac1p and the scaffold for Fe-S cluster biogenesis, Isu1p
    • Andrew A.J., Dutkiewicz R., Knieszner H., Craig E.A., Marszalek J. Characterization of the interaction between the J-protein Jac1p and the scaffold for Fe-S cluster biogenesis, Isu1p. J. Biol. Chem. 2006, 281:14580-14587.
    • (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
  • 14
    • 65549107862 scopus 로고    scopus 로고
    • Manganese import is a key element of the OxyR response to hydrogen peroxide in Escherichia coli
    • Anjem A., Varghese S., Imlay J.A. Manganese import is a key element of the OxyR response to hydrogen peroxide in Escherichia coli. Mol. Microbiol. 2009, 72:844-858.
    • (2009) Mol. Microbiol. , vol.72 , pp. 844-858
    • Anjem, A.1    Varghese, S.2    Imlay, J.A.3
  • 15
    • 0031793544 scopus 로고    scopus 로고
    • The biogenesis and properties of the parasitophorous vacuoles that harbour Leishmania in murine macrophages
    • Antoine J.C., Prina E., Lang T., Courret N. The biogenesis and properties of the parasitophorous vacuoles that harbour Leishmania in murine macrophages. Trends Microbiol. 1998, 6:392-401.
    • (1998) Trends Microbiol. , vol.6 , pp. 392-401
    • Antoine, J.C.1    Prina, E.2    Lang, T.3    Courret, N.4
  • 16
    • 0036186751 scopus 로고    scopus 로고
    • Mitochondrial-type hsp70 genes of the amitochondriate protists, Giardia intestinalis, Entamoeba histolytica and two microsporidians
    • Arisue N., Sanchez L.B., Weiss L.M., Muller M., Hashimoto T. Mitochondrial-type hsp70 genes of the amitochondriate protists, Giardia intestinalis, Entamoeba histolytica and two microsporidians. Parasitol. Int. 2002, 51:9-16.
    • (2002) Parasitol. Int. , vol.51 , pp. 9-16
    • Arisue, N.1    Sanchez, L.B.2    Weiss, L.M.3    Muller, M.4    Hashimoto, T.5
  • 18
    • 0034602344 scopus 로고    scopus 로고
    • A kingdom-level phylogeny of eukaryotes based on combined protein data
    • Baldauf S.L., Roger A.J., Wenk-Siefert I., Doolittle W.F. A kingdom-level phylogeny of eukaryotes based on combined protein data. Science 2000, 290:972-977.
    • (2000) Science , vol.290 , pp. 972-977
    • Baldauf, S.L.1    Roger, A.J.2    Wenk-Siefert, I.3    Doolittle, W.F.4
  • 19
    • 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. 2005, 10:324-331.
    • (2005) Trends Plant Sci. , vol.10 , pp. 324-331
    • Balk, J.1    Lobreaux, S.2
  • 20
    • 79954416607 scopus 로고    scopus 로고
    • Ancient and essential: the assembly of iron-sulfur clusters in plants
    • Balk J., Pilon M. Ancient and essential: the assembly of iron-sulfur clusters in plants. Trends Plant Sci. 2010, 16:218-226.
    • (2010) Trends Plant Sci. , vol.16 , pp. 218-226
    • Balk, J.1    Pilon, M.2
  • 21
    • 2942565619 scopus 로고    scopus 로고
    • The hydrogenase-like Nar1p is essential for maturation of cytosolic and nuclear iron-sulphur proteins
    • Balk J., Pierik A.J., Netz D.J., Muhlenhoff U., Lill R. The hydrogenase-like Nar1p is essential for maturation of cytosolic and nuclear iron-sulphur proteins. EMBO J. 2004, 23:2105-2115.
    • (2004) EMBO J. , vol.23 , pp. 2105-2115
    • Balk, J.1    Pierik, A.J.2    Netz, D.J.3    Muhlenhoff, U.4    Lill, R.5
  • 24
    • 0001436358 scopus 로고
    • Iron uptake by plants from microbial siderophores: a study with 7-nitrobenz-2 oxa-1,3-diazole-desferrioxamine as fluorescent ferrioxamine B analog
    • Bar-Ness E., Hadar Y., Chen Y., Shanzer A., Libman J. Iron uptake by plants from microbial siderophores: a study with 7-nitrobenz-2 oxa-1,3-diazole-desferrioxamine as fluorescent ferrioxamine B analog. Plant Physiol. 1992, 99:1329-1335.
    • (1992) Plant Physiol. , vol.99 , pp. 1329-1335
    • Bar-Ness, E.1    Hadar, Y.2    Chen, Y.3    Shanzer, A.4    Libman, J.5
  • 25
    • 26444455549 scopus 로고    scopus 로고
    • How Escherichia coli and Saccharomyces cerevisiae build Fe/S proteins
    • Barras F., Loiseau L., Py B. How Escherichia coli and Saccharomyces cerevisiae build Fe/S proteins. Adv. Microb. Physiol. 2005, 50:41-101.
    • (2005) Adv. Microb. Physiol. , vol.50 , pp. 41-101
    • Barras, F.1    Loiseau, L.2    Py, B.3
  • 26
    • 0033569878 scopus 로고    scopus 로고
    • Prenylated prelamin A interacts with Narf, a novel nuclear protein
    • Barton R.M., Worman H.J. Prenylated prelamin A interacts with Narf, a novel nuclear protein. J. Biol. Chem. 1999, 274:30008-30018.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30008-30018
    • Barton, R.M.1    Worman, H.J.2
  • 27
    • 0034003112 scopus 로고    scopus 로고
    • Iron-sulfur proteins: ancient structures, still full of surprises
    • Beinert H. Iron-sulfur proteins: ancient structures, still full of surprises. J. Biol. Inorg. Chem. 2000, 5:2-15.
    • (2000) J. Biol. Inorg. Chem. , vol.5 , pp. 2-15
    • Beinert, H.1
  • 28
    • 0000989147 scopus 로고    scopus 로고
    • Aconitase as iron minus sign sulfur protein, enzyme, and iron-regulatory protein
    • Beinert H., Kennedy M.C., Stout C.D. Aconitase as iron minus sign sulfur protein, enzyme, and iron-regulatory protein. Chem. Rev. 1996, 96:2335-2374.
    • (1996) Chem. Rev. , vol.96 , pp. 2335-2374
    • Beinert, H.1    Kennedy, M.C.2    Stout, C.D.3
  • 29
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: nature's modular, multipurpose structures
    • Beinert H., Holm R.H., Munck E. Iron-sulfur clusters: nature's modular, multipurpose structures. Science 1997, 277:653-659.
    • (1997) Science , vol.277 , pp. 653-659
    • Beinert, H.1    Holm, R.H.2    Munck, E.3
  • 31
    • 74849109450 scopus 로고    scopus 로고
    • Systematic molecular genetic analysis of congenital sideroblastic anemia: evidence for genetic heterogeneity and identification of novel mutations
    • Bergmann A.K., Campagna D.R., McLoughlin E.M., Agarwal S., Fleming M.D., Bottomley S.S., Neufeld E.J. Systematic molecular genetic analysis of congenital sideroblastic anemia: evidence for genetic heterogeneity and identification of novel mutations. Pediatr. Blood Cancer 2010, 54:273-278.
    • (2010) Pediatr. Blood Cancer , vol.54 , pp. 273-278
    • Bergmann, A.K.1    Campagna, D.R.2    McLoughlin, E.M.3    Agarwal, S.4    Fleming, M.D.5    Bottomley, S.S.6    Neufeld, E.J.7
  • 32
    • 0346727529 scopus 로고    scopus 로고
    • Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme
    • Berkovitch F., Nicolet Y., Wan J.T., Jarrett J.T., Drennan C.L. Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme. Science 2004, 303:76-79.
    • (2004) Science , vol.303 , pp. 76-79
    • Berkovitch, F.1    Nicolet, Y.2    Wan, J.T.3    Jarrett, J.T.4    Drennan, C.L.5
  • 33
    • 70349649362 scopus 로고    scopus 로고
    • An allelic mutant series of ATM3 reveals its key role in the biogenesis of cytosolic iron-sulfur proteins in Arabidopsis
    • Bernard D.G., Cheng Y., Zhao Y., Balk J. An allelic mutant series of ATM3 reveals its key role in the biogenesis of cytosolic iron-sulfur proteins in Arabidopsis. Plant Physiol. 2009, 151:590-602.
    • (2009) Plant Physiol. , vol.151 , pp. 590-602
    • Bernard, D.G.1    Cheng, Y.2    Zhao, Y.3    Balk, J.4
  • 36
  • 37
    • 34447518814 scopus 로고    scopus 로고
    • A conserved modified wobble nucleoside (mcm5s2U) in lysyl-tRNA is required for viability in yeast
    • Bjork G.R., Huang B., Persson O.P., Bystrom A.S. A conserved modified wobble nucleoside (mcm5s2U) in lysyl-tRNA is required for viability in yeast. RNA 2007, 13:1245-1255.
    • (2007) RNA , vol.13 , pp. 1245-1255
    • Bjork, G.R.1    Huang, B.2    Persson, O.P.3    Bystrom, A.S.4
  • 38
    • 0035823615 scopus 로고    scopus 로고
    • Aft2p, a novel iron-regulated transcription activator that modulates, with Aft1p, intracellular iron use and resistance to oxidative stress in yeast
    • Blaiseau P.L., Lesuisse E., Camadro J.M. Aft2p, a novel iron-regulated transcription activator that modulates, with Aft1p, intracellular iron use and resistance to oxidative stress in yeast. J. Biol. Chem. 2001, 276:34221-34226.
    • (2001) J. Biol. Chem. , vol.276 , pp. 34221-34226
    • Blaiseau, P.L.1    Lesuisse, E.2    Camadro, J.M.3
  • 40
    • 84869227544 scopus 로고    scopus 로고
    • Protein quality control in the intermembrane space of mitochondria
    • Bottinger L., Becker T. Protein quality control in the intermembrane space of mitochondria. J. Mol. Biol. 2012, 424:225-226.
    • (2012) J. Mol. Biol. , vol.424 , pp. 225-226
    • Bottinger, L.1    Becker, T.2
  • 42
    • 62649149894 scopus 로고    scopus 로고
    • Archaeal ApbC/Nbp35 homologs function as iron-sulfur cluster carrier proteins
    • Boyd J.M., Drevland R.M., Downs D.M., Graham D.E. Archaeal ApbC/Nbp35 homologs function as iron-sulfur cluster carrier proteins. J. Bacteriol. 2009, 191:1490-1497.
    • (2009) J. Bacteriol. , vol.191 , pp. 1490-1497
    • Boyd, J.M.1    Drevland, R.M.2    Downs, D.M.3    Graham, D.E.4
  • 43
    • 0037010152 scopus 로고    scopus 로고
    • Iron transport and signaling in Escherichia coli
    • Braun V., Braun M. Iron transport and signaling in Escherichia coli. FEBS Lett. 2002, 529:78-85.
    • (2002) FEBS Lett. , vol.529 , pp. 78-85
    • Braun, V.1    Braun, M.2
  • 44
    • 79953302147 scopus 로고    scopus 로고
    • Recent insights into iron import by bacteria
    • Braun V., Hantke K. Recent insights into iron import by bacteria. Curr. Opin. Chem. Biol. 2011, 15:328-334.
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 328-334
    • Braun, V.1    Hantke, K.2
  • 45
    • 34247210971 scopus 로고    scopus 로고
    • Assembling iron-sulfur clusters in the cytosol
    • Broderick J.B. Assembling iron-sulfur clusters in the cytosol. Nat. Chem. Biol. 2007, 3:243-244.
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 243-244
    • Broderick, J.B.1
  • 46
    • 0027525402 scopus 로고
    • Cysteine is the major low-molecular weight thiol in Giardia duodenalis
    • Brown D.M., Upcroft J.A., Upcroft P. Cysteine is the major low-molecular weight thiol in Giardia duodenalis. Mol. Biochem. Parasitol. 1993, 61:155-158.
    • (1993) Mol. Biochem. Parasitol. , vol.61 , pp. 155-158
    • Brown, D.M.1    Upcroft, J.A.2    Upcroft, P.3
  • 47
    • 0036510621 scopus 로고    scopus 로고
    • Detection of a [3Fe-4S] cluster intermediate of cytosolic aconitase in yeast expressing iron regulatory protein 1. Insights into the mechanism of Fe-S cluster cycling
    • Brown N.M., Kennedy M.C., Antholine W.E., Eisenstein R.S., Walden W.E. Detection of a [3Fe-4S] cluster intermediate of cytosolic aconitase in yeast expressing iron regulatory protein 1. Insights into the mechanism of Fe-S cluster cycling. J. Biol. Chem. 2002, 277:7246-7254.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7246-7254
    • Brown, N.M.1    Kennedy, M.C.2    Antholine, W.E.3    Eisenstein, R.S.4    Walden, W.E.5
  • 48
    • 3042763187 scopus 로고    scopus 로고
    • Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity
    • Bulteau A.L., O'Neill H.A., Kennedy M.C., Ikeda-Saito M., Isaya G., Szweda L.I. Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity. Science 2004, 305:242-245.
    • (2004) Science , vol.305 , pp. 242-245
    • Bulteau, A.L.1    O'Neill, H.A.2    Kennedy, M.C.3    Ikeda-Saito, M.4    Isaya, G.5    Szweda, L.I.6
  • 49
    • 0000703950 scopus 로고    scopus 로고
    • Mechanism of molybdenum nitrogenase
    • Burgess B.K., Lowe D.J. Mechanism of molybdenum nitrogenase. Chem. Rev. 1996, 96:2983-3012.
    • (1996) Chem. Rev. , vol.96 , pp. 2983-3012
    • Burgess, B.K.1    Lowe, D.J.2
  • 55
    • 34249825463 scopus 로고    scopus 로고
    • Characterization of the NADH:ubiquinone oxidoreductase (complex I) in the trypanosomatid Phytomonas serpens (Kinetoplastida)
    • Cermakova P., Verner Z., Man P., Lukes J., Horvath A. Characterization of the NADH:ubiquinone oxidoreductase (complex I) in the trypanosomatid Phytomonas serpens (Kinetoplastida). FEBS J. 2007, 274:3150-3158.
    • (2007) FEBS J. , vol.274 , pp. 3150-3158
    • Cermakova, P.1    Verner, Z.2    Man, P.3    Lukes, J.4    Horvath, A.5
  • 56
    • 33748309413 scopus 로고    scopus 로고
    • Trypanosome alternative oxidase: from molecule to function
    • Chaudhuri M., Ott R.D., Hill G.C. Trypanosome alternative oxidase: from molecule to function. Trends Parasitol. 2006, 22:484-491.
    • (2006) Trends Parasitol. , vol.22 , pp. 484-491
    • Chaudhuri, M.1    Ott, R.D.2    Hill, G.C.3
  • 57
    • 0034841061 scopus 로고    scopus 로고
    • Adenosylmethionine-dependent iron-sulfur enzymes: versatile clusters in a radical new role
    • Cheek J., Broderick J.B. Adenosylmethionine-dependent iron-sulfur enzymes: versatile clusters in a radical new role. J. Biol. Inorg. Chem. 2001, 6:209-226.
    • (2001) J. Biol. Inorg. Chem. , vol.6 , pp. 209-226
    • Cheek, J.1    Broderick, J.B.2
  • 62
    • 0032414310 scopus 로고    scopus 로고
    • Identification of a human mitochondrial ABC transporter, the functional orthologue of yeast Atm1p
    • Csere P., Lill R., Kispal G. Identification of a human mitochondrial ABC transporter, the functional orthologue of yeast Atm1p. FEBS Lett. 1998, 441:266-270.
    • (1998) FEBS Lett. , vol.441 , pp. 266-270
    • Csere, P.1    Lill, R.2    Kispal, G.3
  • 63
    • 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. 2003, 330:1049-1059.
    • (2003) J. Mol. Biol. , vol.330 , pp. 1049-1059
    • Cupp-Vickery, J.R.1    Urbina, H.2    Vickery, L.E.3
  • 64
    • 4444346912 scopus 로고    scopus 로고
    • Crystal structure of the molecular chaperone HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC
    • Cupp-Vickery J.R., Peterson J.C., Ta D.T., Vickery L.E. Crystal structure of the molecular chaperone HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC. J. Mol. Biol. 2004, 342:1265-1278.
    • (2004) J. Mol. Biol. , vol.342 , pp. 1265-1278
    • Cupp-Vickery, J.R.1    Peterson, J.C.2    Ta, D.T.3    Vickery, L.E.4
  • 65
    • 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. 2004, 338:127-137.
    • (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
  • 66
    • 0034723368 scopus 로고    scopus 로고
    • Redox signaling in chloroplasts: cleavage of disulfides by an iron-sulfur cluster
    • Dai S., Schwendtmayer C., Schurmann P., Ramaswamy S., Eklund H. Redox signaling in chloroplasts: cleavage of disulfides by an iron-sulfur cluster. Science 2000, 287:655-658.
    • (2000) Science , vol.287 , pp. 655-658
    • Dai, S.1    Schwendtmayer, C.2    Schurmann, P.3    Ramaswamy, S.4    Eklund, H.5
  • 68
    • 0027494834 scopus 로고
    • Nitrogenase metalloclusters: structures, organization, and synthesis
    • Dean D.R., Bolin J.T., Zheng L. Nitrogenase metalloclusters: structures, organization, and synthesis. J. Bacteriol. 1993, 175:6737-6744.
    • (1993) J. Bacteriol. , vol.175 , pp. 6737-6744
    • Dean, D.R.1    Bolin, J.T.2    Zheng, L.3
  • 69
    • 0029115569 scopus 로고
    • Reduction of exogenous ferric iron by a surface-associated ferric reductase of Listeria spp
    • Deneer H.G., Healey V., Boychuk I. Reduction of exogenous ferric iron by a surface-associated ferric reductase of Listeria spp. Microbiology 1995, 141(Pt 8):1985-1992.
    • (1995) Microbiology , vol.141 , Issue.PART 8 , pp. 1985-1992
    • Deneer, H.G.1    Healey, V.2    Boychuk, I.3
  • 71
    • 3543029271 scopus 로고    scopus 로고
    • Mitochondrial diseases
    • DiMauro S. Mitochondrial diseases. Biochim. Biophys. Acta 2004, 1658:80-88.
    • (2004) Biochim. Biophys. Acta , vol.1658 , pp. 80-88
    • DiMauro, S.1
  • 72
    • 4444317589 scopus 로고    scopus 로고
    • IscA mediates iron delivery for assembly of iron-sulfur clusters in IscU under the limited accessible free iron conditions
    • Ding H., Clark R.J., Ding B. IscA mediates iron delivery for assembly of iron-sulfur clusters in IscU under the limited accessible free iron conditions. J. Biol. Chem. 2004, 279:37499-37504.
    • (2004) J. Biol. Chem. , vol.279 , pp. 37499-37504
    • Ding, H.1    Clark, R.J.2    Ding, B.3
  • 73
    • 23644456197 scopus 로고    scopus 로고
    • Mobilization of the iron centre in IscA for the iron-sulphur cluster assembly in IscU
    • Ding B., Smith E.S., Ding H. Mobilization of the iron centre in IscA for the iron-sulphur cluster assembly in IscU. Biochem. J. 2005, 389:797-802.
    • (2005) Biochem. J. , vol.389 , pp. 797-802
    • Ding, B.1    Smith, E.S.2    Ding, H.3
  • 74
    • 7244239273 scopus 로고    scopus 로고
    • Repair of oxidized iron-sulfur clusters in Escherichia coli
    • Djaman O., Outten F.W., Imlay J.A. Repair of oxidized iron-sulfur clusters in Escherichia coli. J. Biol. Chem. 2004, 279:44590-44599.
    • (2004) J. Biol. Chem. , vol.279 , pp. 44590-44599
    • Djaman, O.1    Outten, F.W.2    Imlay, J.A.3
  • 75
    • 0035902973 scopus 로고    scopus 로고
    • Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster
    • Dobbek H., Svetlitchnyi V., Gremer L., Huber R., Meyer O. Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster. Science 2001, 293:1281-1285.
    • (2001) Science , vol.293 , pp. 1281-1285
    • Dobbek, H.1    Svetlitchnyi, V.2    Gremer, L.3    Huber, R.4    Meyer, O.5
  • 77
  • 80
    • 0037070204 scopus 로고    scopus 로고
    • Heterodisulfide reductase from Methanothermobacter marburgensis contains an active-site [4Fe-4S] cluster that is directly involved in mediating heterodisulfide reduction
    • Duin E.C., Madadi-Kahkesh S., Hedderich R., Clay M.D., Johnson M.K. Heterodisulfide reductase from Methanothermobacter marburgensis contains an active-site [4Fe-4S] cluster that is directly involved in mediating heterodisulfide reduction. FEBS Lett. 2002, 512:263-268.
    • (2002) FEBS Lett. , vol.512 , pp. 263-268
    • Duin, E.C.1    Madadi-Kahkesh, S.2    Hedderich, R.3    Clay, M.D.4    Johnson, M.K.5
  • 82
    • 34248146824 scopus 로고    scopus 로고
    • PIC1, an ancient permease in Arabidopsis chloroplasts, mediates iron transport
    • Duy D., Wanner G., Meda A.R., von Wiren N., Soll J., Philippar K. PIC1, an ancient permease in Arabidopsis chloroplasts, mediates iron transport. Plant Cell 2007, 19:986-1006.
    • (2007) Plant Cell , vol.19 , pp. 986-1006
    • Duy, D.1    Wanner, G.2    Meda, A.R.3    von Wiren, N.4    Soll, J.5    Philippar, K.6
  • 83
    • 79953692401 scopus 로고    scopus 로고
    • The chloroplast permease PIC1 regulates plant growth and development by directing homeostasis and transport of iron
    • Duy D., Stube R., Wanner G., Philippar K. The chloroplast permease PIC1 regulates plant growth and development by directing homeostasis and transport of iron. Plant Physiol. 2011, 155:1709-1722.
    • (2011) Plant Physiol. , vol.155 , pp. 1709-1722
    • Duy, D.1    Stube, R.2    Wanner, G.3    Philippar, K.4
  • 85
    • 0242674702 scopus 로고    scopus 로고
    • Phylogenetic affinity of a Giardia lamblia cysteine desulfurase conforms to canonical pattern of mitochondrial ancestry
    • Emelyanov V.V. Phylogenetic affinity of a Giardia lamblia cysteine desulfurase conforms to canonical pattern of mitochondrial ancestry. FEMS Microbiol. Lett. 2003, 226:257-266.
    • (2003) FEMS Microbiol. Lett. , vol.226 , pp. 257-266
    • Emelyanov, V.V.1
  • 86
    • 0030018746 scopus 로고    scopus 로고
    • Escherichia coli contains a protein that is homologous in function and N-terminal sequence to the protein encoded by the nifS gene of Azotobacter vinelandii and that can participate in the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase
    • Flint D.H. Escherichia coli contains a protein that is homologous in function and N-terminal sequence to the protein encoded by the nifS gene of Azotobacter vinelandii and that can participate in the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase. J. Biol. Chem. 1996, 271:16068-16074.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16068-16074
    • Flint, D.H.1
  • 87
    • 0030056113 scopus 로고    scopus 로고
    • Studies on the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase in Escherichia coli crude extract. Isolation of O-acetylserine sulfhydrylases A and B and beta-cystathionase based on their ability to mobilize sulfur from cysteine and to participate in Fe-S cluster synthesis
    • Flint D.H., Tuminello J.F., Miller T.J. Studies on the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase in Escherichia coli crude extract. Isolation of O-acetylserine sulfhydrylases A and B and beta-cystathionase based on their ability to mobilize sulfur from cysteine and to participate in Fe-S cluster synthesis. J. Biol. Chem. 1996, 271:16053-16067.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16053-16067
    • Flint, D.H.1    Tuminello, J.F.2    Miller, T.J.3
  • 88
    • 33646368396 scopus 로고    scopus 로고
    • Iron-sulfur clusters: ever-expanding roles
    • Fontecave M. Iron-sulfur clusters: ever-expanding roles. Nat. Chem. Biol. 2006, 2:171-174.
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 171-174
    • Fontecave, M.1
  • 89
    • 0342468764 scopus 로고    scopus 로고
    • Microsporidiosis: human diseases and diagnosis
    • Franzen C., Muller A. Microsporidiosis: human diseases and diagnosis. Microbes Infect. 2001, 3:389-400.
    • (2001) Microbes Infect. , vol.3 , pp. 389-400
    • Franzen, C.1    Muller, A.2
  • 92
    • 0141623560 scopus 로고    scopus 로고
    • An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1
    • Gerber J., Muhlenhoff U., Lill R. An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1. EMBO Rep. 2003, 4:906-911.
    • (2003) EMBO Rep. , vol.4 , pp. 906-911
    • Gerber, J.1    Muhlenhoff, U.2    Lill, R.3
  • 93
    • 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., Muhlenhoff U., Lill R. The yeast scaffold proteins Isu1p and Isu2p are required inside mitochondria for maturation of cytosolic Fe/S proteins. Mol. Cell. Biol. 2004, 24:4848-4857.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4848-4857
    • Gerber, J.1    Neumann, K.2    Prohl, C.3    Muhlenhoff, U.4    Lill, R.5
  • 96
    • 28544446058 scopus 로고    scopus 로고
    • Mitochondrial tumour suppressors: a genetic and biochemical update
    • Gottlieb E., Tomlinson I.P. Mitochondrial tumour suppressors: a genetic and biochemical update. Nat. Rev. Cancer 2005, 5:857-866.
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 857-866
    • Gottlieb, E.1    Tomlinson, I.P.2
  • 99
    • 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., Sendra M., Naik S.G., Chahal H.K., Huynh B.H., Outten F.W., Fontecave M., Ollagnier de Choudens S. 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. 2009, 131:6149-6153.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 6149-6153
    • Gupta, V.1    Sendra, M.2    Naik, S.G.3    Chahal, H.K.4    Huynh, B.H.5    Outten, F.W.6    Fontecave, M.7    Ollagnier de Choudens, S.8
  • 101
    • 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., Aguilar Netz D.J., Balk J., Pierik A.J., Muhlenhoff U., Lill R. The eukaryotic P loop NTPase Nbp35: an essential component of the cytosolic and nuclear iron-sulfur protein assembly machinery. Proc. Natl. Acad. Sci. U.S.A. 2005, 102:3266-3271.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 3266-3271
    • Hausmann, A.1    Aguilar Netz, D.J.2    Balk, J.3    Pierik, A.J.4    Muhlenhoff, U.5    Lill, R.6
  • 102
    • 26444560088 scopus 로고    scopus 로고
    • Energy metabolism and its compartmentation in Trypanosoma brucei
    • Hellemond J.J., Bakker B.M., Tielens A.G. Energy metabolism and its compartmentation in Trypanosoma brucei. Adv. Microb. Physiol. 2005, 50:199-226.
    • (2005) Adv. Microb. Physiol. , vol.50 , pp. 199-226
    • Hellemond, J.J.1    Bakker, B.M.2    Tielens, A.G.3
  • 103
    • 0642342084 scopus 로고    scopus 로고
    • Evolutionary biology: essence of mitochondria
    • Henze K., Martin W. Evolutionary biology: essence of mitochondria. Nature 2003, 426:127-128.
    • (2003) Nature , vol.426 , pp. 127-128
    • Henze, K.1    Martin, W.2
  • 104
    • 34250731291 scopus 로고    scopus 로고
    • Monothiol glutaredoxins: a common domain for multiple functions
    • Herrero E., de la Torre-Ruiz M.A. Monothiol glutaredoxins: a common domain for multiple functions. Cell. Mol. Life Sci. 2007, 64:1518-1530.
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 1518-1530
    • Herrero, E.1    de la Torre-Ruiz, M.A.2
  • 106
    • 0037178878 scopus 로고    scopus 로고
    • Hsc66 substrate specificity is directed toward a discrete region of the iron-sulfur cluster template protein IscU
    • Hoff K.G., Ta D.T., Tapley T.L., Silberg J.J., Vickery L.E. Hsc66 substrate specificity is directed toward a discrete region of the iron-sulfur cluster template protein IscU. J. Biol. Chem. 2002, 277:27353-27359.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27353-27359
    • Hoff, K.G.1    Ta, D.T.2    Tapley, T.L.3    Silberg, J.J.4    Vickery, L.E.5
  • 107
    • 0141844533 scopus 로고    scopus 로고
    • Contributions of the LPPVK motif of the iron-sulfur template protein IscU to interactions with the Hsc66-Hsc20 chaperone system
    • Hoff K.G., Cupp-Vickery J.R., Vickery L.E. Contributions of the LPPVK motif of the iron-sulfur template protein IscU to interactions with the Hsc66-Hsc20 chaperone system. J. Biol. Chem. 2003, 278:37582-37589.
    • (2003) J. Biol. Chem. , vol.278 , pp. 37582-37589
    • Hoff, K.G.1    Cupp-Vickery, J.R.2    Vickery, L.E.3
  • 109
    • 7744224797 scopus 로고    scopus 로고
    • Structural basis of biological nitrogen fixation
    • Howard J.B., Rees D.C. Structural basis of biological nitrogen fixation. Chem. Rev. 1996, 96:2965-2982.
    • (1996) Chem. Rev. , vol.96 , pp. 2965-2982
    • Howard, J.B.1    Rees, D.C.2
  • 110
    • 10344254308 scopus 로고    scopus 로고
    • Trichomonas hydrogenosomes contain the NADH dehydrogenase module of mitochondrial complex I
    • Hrdy I., Hirt R.P., Dolezal P., Bardonova L., Foster P.G., Tachezy J., Embley T.M. Trichomonas hydrogenosomes contain the NADH dehydrogenase module of mitochondrial complex I. Nature 2004, 432:618-622.
    • (2004) Nature , vol.432 , pp. 618-622
    • Hrdy, I.1    Hirt, R.P.2    Dolezal, P.3    Bardonova, L.4    Foster, P.G.5    Tachezy, J.6    Embley, T.M.7
  • 111
    • 33846298869 scopus 로고    scopus 로고
    • IOP1, a novel hydrogenase-like protein that modulates hypoxia-inducible factor-1alpha activity
    • Huang J., Song D., Flores A., Zhao Q., Mooney S.M., Shaw L.M., Lee F.S. IOP1, a novel hydrogenase-like protein that modulates hypoxia-inducible factor-1alpha activity. Biochem. J. 2007, 401:341-352.
    • (2007) Biochem. J. , vol.401 , pp. 341-352
    • Huang, J.1    Song, D.2    Flores, A.3    Zhao, Q.4    Mooney, S.M.5    Shaw, L.M.6    Lee, F.S.7
  • 113
    • 79957658850 scopus 로고    scopus 로고
    • Global analysis of gene expression in response to L-cysteine deprivation in the anaerobic protozoan parasite Entamoeba histolytica
    • Husain A., Jeelani G., Sato D., Nozaki T. Global analysis of gene expression in response to L-cysteine deprivation in the anaerobic protozoan parasite Entamoeba histolytica. BMC Genomics 2011, 12:275.
    • (2011) BMC Genomics , vol.12 , pp. 275
    • Husain, A.1    Jeelani, G.2    Sato, D.3    Nozaki, T.4
  • 114
    • 12744251555 scopus 로고    scopus 로고
    • Combining data from genomes, Y2H and 3D structure indicates that BolA is a reductase interacting with a glutaredoxin
    • Huynen M.A., Spronk C.A., Gabaldon T., Snel B. Combining data from genomes, Y2H and 3D structure indicates that BolA is a reductase interacting with a glutaredoxin. FEBS Lett. 2005, 579:591-596.
    • (2005) FEBS Lett. , vol.579 , pp. 591-596
    • Huynen, M.A.1    Spronk, C.A.2    Gabaldon, T.3    Snel, B.4
  • 115
    • 33645065589 scopus 로고    scopus 로고
    • Iron-sulphur clusters and the problem with oxygen
    • Imlay J.A. Iron-sulphur clusters and the problem with oxygen. Mol. Microbiol. 2006, 59:1073-1082.
    • (2006) Mol. Microbiol. , vol.59 , pp. 1073-1082
    • Imlay, J.A.1
  • 118
  • 119
    • 78649983777 scopus 로고    scopus 로고
    • Hydrogen peroxide inactivates the Escherichia coli Isc iron-sulphur assembly system, and OxyR induces the Suf system to compensate
    • Jang S., Imlay J.A. Hydrogen peroxide inactivates the Escherichia coli Isc iron-sulphur assembly system, and OxyR induces the Suf system to compensate. Mol. Microbiol. 2010, 78:1448-1467.
    • (2010) Mol. Microbiol. , vol.78 , pp. 1448-1467
    • Jang, S.1    Imlay, J.A.2
  • 121
    • 77956261155 scopus 로고    scopus 로고
    • Two atypical L-cysteine-regulated NADPH-dependent oxidoreductases involved in redox maintenance, L-cystine and iron reduction, and metronidazole activation in the enteric protozoan Entamoeba histolytica
    • Jeelani G., Husain A., Sato D., Ali V., Suematsu M., Soga T., Nozaki T. Two atypical L-cysteine-regulated NADPH-dependent oxidoreductases involved in redox maintenance, L-cystine and iron reduction, and metronidazole activation in the enteric protozoan Entamoeba histolytica. J. Biol. Chem. 2010, 285:26889-26899.
    • (2010) J. Biol. Chem. , vol.285 , pp. 26889-26899
    • Jeelani, G.1    Husain, A.2    Sato, D.3    Ali, V.4    Suematsu, M.5    Soga, T.6    Nozaki, T.7
  • 123
    • 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. 2005, 74:247-281.
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 247-281
    • Johnson, D.C.1    Dean, D.R.2    Smith, A.D.3    Johnson, M.K.4
  • 124
    • 38149005635 scopus 로고    scopus 로고
    • Global epidemiology and control of Trichomonas vaginalis
    • Johnston V.J., Mabey D.C. Global epidemiology and control of Trichomonas vaginalis. Curr. Opin. Infect. Dis. 2008, 21:56-64.
    • (2008) Curr. Opin. Infect. Dis. , vol.21 , pp. 56-64
    • Johnston, V.J.1    Mabey, D.C.2
  • 125
    • 0033527754 scopus 로고    scopus 로고
    • Purification and biophysical characterization of a new [2Fe-2S] ferredoxin from Azotobacter vinelandii, a putative [Fe-S] cluster assembly/repair protein
    • Jung Y.S., Gao-Sheridan H.S., Christiansen J., Dean D.R., Burgess B.K. Purification and biophysical characterization of a new [2Fe-2S] ferredoxin from Azotobacter vinelandii, a putative [Fe-S] cluster assembly/repair protein. J. Biol. Chem. 1999, 274:32402-32410.
    • (1999) J. Biol. Chem. , vol.274 , pp. 32402-32410
    • Jung, Y.S.1    Gao-Sheridan, H.S.2    Christiansen, J.3    Dean, D.R.4    Burgess, B.K.5
  • 126
    • 0347997282 scopus 로고    scopus 로고
    • Snapshots of the cystine lyase C-DES during catalysis. Studies in solution and in the crystalline state
    • Kaiser J.T., Bruno S., Clausen T., Huber R., Schiaretti F., Mozzarelli A., Kessler D. Snapshots of the cystine lyase C-DES during catalysis. Studies in solution and in the crystalline state. J. Biol. Chem. 2003, 278:357-365.
    • (2003) J. Biol. Chem. , vol.278 , pp. 357-365
    • Kaiser, J.T.1    Bruno, S.2    Clausen, T.3    Huber, R.4    Schiaretti, F.5    Mozzarelli, A.6    Kessler, D.7
  • 127
    • 0035909064 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli Fdx, an adrenodoxin-type ferredoxin involved in the assembly of iron-sulfur clusters
    • Kakuta Y., Horio T., Takahashi Y., Fukuyama K. Crystal structure of Escherichia coli Fdx, an adrenodoxin-type ferredoxin involved in the assembly of iron-sulfur clusters. Biochemistry 2001, 40:11007-11012.
    • (2001) Biochemistry , vol.40 , pp. 11007-11012
    • Kakuta, Y.1    Horio, T.2    Takahashi, Y.3    Fukuyama, K.4
  • 128
    • 0033554855 scopus 로고    scopus 로고
    • IscS is a sulfurtransferase for the in vitro biosynthesis of 4-thiouridine in Escherichia coli tRNA
    • Kambampati R., Lauhon C.T. IscS is a sulfurtransferase for the in vitro biosynthesis of 4-thiouridine in Escherichia coli tRNA. Biochemistry 1999, 38:16561-16568.
    • (1999) Biochemistry , vol.38 , pp. 16561-16568
    • Kambampati, R.1    Lauhon, C.T.2
  • 129
    • 0037415690 scopus 로고    scopus 로고
    • Wobble modification differences and subcellular localization of tRNAs in Leishmania tarentolae: implication for tRNA sorting mechanism
    • Kaneko T., Suzuki T., Kapushoc S.T., Rubio M.A., Ghazvini J., Watanabe K., Simpson L., Suzuki T. Wobble modification differences and subcellular localization of tRNAs in Leishmania tarentolae: implication for tRNA sorting mechanism. EMBO J. 2003, 22:657-667.
    • (2003) EMBO J. , vol.22 , pp. 657-667
    • Kaneko, T.1    Suzuki, T.2    Kapushoc, S.T.3    Rubio, M.A.4    Ghazvini, J.5    Watanabe, K.6    Simpson, L.7    Suzuki, T.8
  • 132
    • 34250763278 scopus 로고    scopus 로고
    • Yct1p, a novel, high-affinity, cysteine-specific transporter from the yeast Saccharomyces cerevisiae
    • Kaur J., Bachhawat A.K. Yct1p, a novel, high-affinity, cysteine-specific transporter from the yeast Saccharomyces cerevisiae. Genetics 2007, 176:877-890.
    • (2007) Genetics , vol.176 , pp. 877-890
    • Kaur, J.1    Bachhawat, A.K.2
  • 133
    • 0033977617 scopus 로고    scopus 로고
    • Evidence from b-tubulin phylogeny that microsporidia evolved from within the fungi
    • Keeling P.J., Luker M.A., Palmer J.D. Evidence from b-tubulin phylogeny that microsporidia evolved from within the fungi. Mol. Biol. Evol. 2000, 17:23-31.
    • (2000) Mol. Biol. Evol. , vol.17 , pp. 23-31
    • Keeling, P.J.1    Luker, M.A.2    Palmer, J.D.3
  • 134
    • 0038352097 scopus 로고    scopus 로고
    • The role of Fe-S proteins in sensing and regulation in bacteria
    • Kiley P.J., Beinert H. The role of Fe-S proteins in sensing and regulation in bacteria. Curr. Opin. Microbiol. 2003, 6:181-185.
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 181-185
    • Kiley, P.J.1    Beinert, H.2
  • 135
    • 0036023053 scopus 로고    scopus 로고
    • Control of singlet oxygen-induced oxidative damage in Escherichia coli
    • Kim S.Y., Kim E.J., Park J.W. Control of singlet oxygen-induced oxidative damage in Escherichia coli. J. Biochem. Mol. Biol. 2002, 35:353-357.
    • (2002) J. Biochem. Mol. Biol. , vol.35 , pp. 353-357
    • Kim, S.Y.1    Kim, E.J.2    Park, J.W.3
  • 138
    • 0035290142 scopus 로고    scopus 로고
    • MUP1, high affinity methionine permease, is involved in cysteine uptake by Saccharomyces cerevisiae
    • Kosugi A., Koizumi Y., Yanagida F., Udaka S. MUP1, high affinity methionine permease, is involved in cysteine uptake by Saccharomyces cerevisiae. Biosci. Biotechnol. Biochem. 2001, 65:728-731.
    • (2001) Biosci. Biotechnol. Biochem. , vol.65 , pp. 728-731
    • Kosugi, A.1    Koizumi, Y.2    Yanagida, F.3    Udaka, S.4
  • 140
    • 0020477453 scopus 로고
    • Spinach siroheme enzymes: isolation and characterization of ferredoxin-sulfite reductase and comparison of properties with ferredoxin-nitrite reductase
    • Krueger R.J., Siegel L.M. Spinach siroheme enzymes: isolation and characterization of ferredoxin-sulfite reductase and comparison of properties with ferredoxin-nitrite reductase. Biochemistry 1982, 21:2892-2904.
    • (1982) Biochemistry , vol.21 , pp. 2892-2904
    • Krueger, R.J.1    Siegel, L.M.2
  • 142
    • 79960563806 scopus 로고    scopus 로고
    • Interaction between sulphur mobilisation proteins SufB and SufC: evidence for an iron-sulphur cluster biogenesis pathway in the apicoplast of Plasmodium falciparum
    • Kumar B., Chaubey S., Shah P., Tanveer A., Charan M., Siddiqi M.I., Habib S. Interaction between sulphur mobilisation proteins SufB and SufC: evidence for an iron-sulphur cluster biogenesis pathway in the apicoplast of Plasmodium falciparum. Int. J. Parasitol. 2011, 41:991-999.
    • (2011) Int. J. Parasitol. , vol.41 , pp. 991-999
    • Kumar, B.1    Chaubey, S.2    Shah, P.3    Tanveer, A.4    Charan, M.5    Siddiqi, M.I.6    Habib, S.7
  • 144
    • 1242318521 scopus 로고    scopus 로고
    • Assembly of iron-sulfur clusters mediated by cysteine desulfurases, IscS, CsdB and CSD, from Escherichia coli
    • Kurihara T., Mihara H., Kato S., Yoshimura T., Esaki N. Assembly of iron-sulfur clusters mediated by cysteine desulfurases, IscS, CsdB and CSD, from Escherichia coli. Biochim. Biophys. Acta 2003, 1647:303-309.
    • (2003) Biochim. Biophys. Acta , vol.1647 , pp. 303-309
    • Kurihara, T.1    Mihara, H.2    Kato, S.3    Yoshimura, T.4    Esaki, N.5
  • 145
    • 0347513216 scopus 로고    scopus 로고
    • Mitochondrial-type iron-sulfur cluster biosynthesis genes (IscS and IscU) in the apicomplexan Cryptosporidium parvum
    • LaGier M.J., Tachezy J., Stejskal F., Kutisova K., Keithly J.S. Mitochondrial-type iron-sulfur cluster biosynthesis genes (IscS and IscU) in the apicomplexan Cryptosporidium parvum. Microbiology 2003, 149:3519-3530.
    • (2003) Microbiology , vol.149 , pp. 3519-3530
    • LaGier, M.J.1    Tachezy, J.2    Stejskal, F.3    Kutisova, K.4    Keithly, J.S.5
  • 146
    • 0018800302 scopus 로고
    • Identification of the iron-sulfur center of spinach ferredoxin-nitrite reductase as a tetranuclear center, and preliminary EPR studies of mechanism
    • Lancaster J.R., Vega J.M., Kamin H., Orme-Johnson N.R., Orme-Johnson W.H., Krueger R.J., Siegel L.M. Identification of the iron-sulfur center of spinach ferredoxin-nitrite reductase as a tetranuclear center, and preliminary EPR studies of mechanism. J. Biol. Chem. 1979, 254:1268-1272.
    • (1979) J. Biol. Chem. , vol.254 , pp. 1268-1272
    • Lancaster, J.R.1    Vega, J.M.2    Kamin, H.3    Orme-Johnson, N.R.4    Orme-Johnson, W.H.5    Krueger, R.J.6    Siegel, L.M.7
  • 147
    • 0032245425 scopus 로고    scopus 로고
    • Targeting of a human iron-sulfur cluster assembly enzyme, nifs, to different subcellular compartments is regulated through alternative AUG utilization
    • Land T., Rouault T.A. Targeting of a human iron-sulfur cluster assembly enzyme, nifs, to different subcellular compartments is regulated through alternative AUG utilization. Mol. Cell 1998, 2:807-815.
    • (1998) Mol. Cell , vol.2 , pp. 807-815
    • Land, T.1    Rouault, T.A.2
  • 148
    • 2542426480 scopus 로고    scopus 로고
    • Substrate specificity for 4-thiouridine modification in Escherichia coli
    • Lauhon C.T., Erwin W.M., Ton G.N. Substrate specificity for 4-thiouridine modification in Escherichia coli. J. Biol. Chem. 2004, 279:23022-23029.
    • (2004) J. Biol. Chem. , vol.279 , pp. 23022-23029
    • Lauhon, C.T.1    Erwin, W.M.2    Ton, G.N.3
  • 149
    • 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. 2006, 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
  • 150
    • 0034647976 scopus 로고    scopus 로고
    • Erv1p from Saccharomyces cerevisiae is a FAD-linked sulfhydryl oxidase
    • Lee J., Hofhaus G., Lisowsky T. Erv1p from Saccharomyces cerevisiae is a FAD-linked sulfhydryl oxidase. FEBS Lett. 2000, 477:62-66.
    • (2000) FEBS Lett. , vol.477 , pp. 62-66
    • Lee, J.1    Hofhaus, G.2    Lisowsky, T.3
  • 151
    • 2442546656 scopus 로고    scopus 로고
    • Structural comparison of MTA phosphorylase and MTA/AdoHcy nucleosidase explains substrate preferences and identifies regions exploitable for inhibitor design
    • Lee J.E., Settembre E.C., Cornell K.A., Riscoe M.K., Sufrin J.R., Ealick S.E., Howell P.L. Structural comparison of MTA phosphorylase and MTA/AdoHcy nucleosidase explains substrate preferences and identifies regions exploitable for inhibitor design. Biochemistry 2004, 43:5159-5169.
    • (2004) Biochemistry , vol.43 , pp. 5159-5169
    • Lee, J.E.1    Settembre, E.C.2    Cornell, K.A.3    Riscoe, M.K.4    Sufrin, J.R.5    Ealick, S.E.6    Howell, P.L.7
  • 152
    • 1642565394 scopus 로고    scopus 로고
    • Induction of the sufA operon encoding Fe-S assembly proteins by superoxide generators and hydrogen peroxide: involvement of OxyR, IHF and an unidentified oxidant-responsive factor
    • Lee J.H., Yeo W.S., Roe J.H. Induction of the sufA operon encoding Fe-S assembly proteins by superoxide generators and hydrogen peroxide: involvement of OxyR, IHF and an unidentified oxidant-responsive factor. Mol. Microbiol. 2004, 51:1745-1755.
    • (2004) Mol. Microbiol. , vol.51 , pp. 1745-1755
    • Lee, J.H.1    Yeo, W.S.2    Roe, J.H.3
  • 153
    • 57349087129 scopus 로고    scopus 로고
    • Oxidant-responsive induction of the suf operon, encoding a Fe-S assembly system, through Fur and IscR in Escherichia coli
    • Lee K.C., Yeo W.S., Roe J.H. Oxidant-responsive induction of the suf operon, encoding a Fe-S assembly system, through Fur and IscR in Escherichia coli. J. Bacteriol. 2008, 190:8244-8247.
    • (2008) J. Bacteriol. , vol.190 , pp. 8244-8247
    • Lee, K.C.1    Yeo, W.S.2    Roe, J.H.3
  • 154
    • 0036295212 scopus 로고    scopus 로고
    • Classification and evolution of P-loop GTPases and related ATPases
    • Leipe D.D., Wolf Y.I., Koonin E.V., Aravind L. Classification and evolution of P-loop GTPases and related ATPases. J. Mol. Biol. 2002, 317:41-72.
    • (2002) J. Mol. Biol. , vol.317 , pp. 41-72
    • Leipe, D.D.1    Wolf, Y.I.2    Koonin, E.V.3    Aravind, L.4
  • 155
    • 0036134621 scopus 로고    scopus 로고
    • Characterization of a putative murine mitochondrial transporter homology of hMRS3/4
    • Li F.Y., Leibiger B., Leibiger I., Larsson C. Characterization of a putative murine mitochondrial transporter homology of hMRS3/4. Mamm. Genome 2002, 13:20-23.
    • (2002) Mamm. Genome , vol.13 , pp. 20-23
    • Li, F.Y.1    Leibiger, B.2    Leibiger, I.3    Larsson, C.4
  • 156
    • 33744956665 scopus 로고    scopus 로고
    • Roles of the mammalian cytosolic cysteine desulfurase, ISCS, and scaffold protein, ISCU, in iron-sulfur cluster assembly
    • Li K., Tong W.H., Hughes R.M., Rouault T.A. Roles of the mammalian cytosolic cysteine desulfurase, ISCS, and scaffold protein, ISCU, in iron-sulfur cluster assembly. J. Biol. Chem. 2006, 281:12344-12351.
    • (2006) J. Biol. Chem. , vol.281 , pp. 12344-12351
    • Li, K.1    Tong, W.H.2    Hughes, R.M.3    Rouault, T.A.4
  • 157
    • 47249127786 scopus 로고    scopus 로고
    • Iron-dependent regulation of frataxin expression: implications for treatment of Friedreich ataxia
    • Li K., Besse E.K., Ha D., Kovtunovych G., Rouault T.A. Iron-dependent regulation of frataxin expression: implications for treatment of Friedreich ataxia. Hum. Mol. Genet. 2008, 17:2265-2273.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 2265-2273
    • Li, K.1    Besse, E.K.2    Ha, D.3    Kovtunovych, G.4    Rouault, T.A.5
  • 158
    • 68949128587 scopus 로고    scopus 로고
    • Function and biogenesis of iron-sulphur proteins
    • Lill R. Function and biogenesis of iron-sulphur proteins. Nature 2009, 460:831-838.
    • (2009) Nature , vol.460 , pp. 831-838
    • Lill, R.1
  • 159
    • 0034255836 scopus 로고    scopus 로고
    • Maturation of cellular Fe-S proteins: an essential function of mitochondria
    • Lill R., Kispal G. Maturation of cellular Fe-S proteins: an essential function of mitochondria. Trends Biochem. Sci. 2000, 25:352-356.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 352-356
    • Lill, R.1    Kispal, G.2
  • 160
    • 0035002973 scopus 로고    scopus 로고
    • Mitochondrial ABC transporters
    • Lill R., Kispal G. Mitochondrial ABC transporters. Res. Microbiol. 2001, 152:331-340.
    • (2001) Res. Microbiol. , vol.152 , pp. 331-340
    • Lill, R.1    Kispal, G.2
  • 161
    • 14744294785 scopus 로고    scopus 로고
    • Iron-sulfur-protein biogenesis in eukaryotes
    • Lill R., Muhlenhoff U. Iron-sulfur-protein biogenesis in eukaryotes. Trends Biochem. Sci. 2005, 30:133-141.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 133-141
    • Lill, R.1    Muhlenhoff, U.2
  • 162
    • 33751177803 scopus 로고    scopus 로고
    • Iron-sulfur protein biogenesis in eukaryotes: components and mechanisms
    • Lill R., Muhlenhoff U. Iron-sulfur protein biogenesis in eukaryotes: components and mechanisms. Annu. Rev. Cell Dev. Biol. 2006, 22:457-486.
    • (2006) Annu. Rev. Cell Dev. Biol. , vol.22 , pp. 457-486
    • Lill, R.1    Muhlenhoff, U.2
  • 163
    • 47249094614 scopus 로고    scopus 로고
    • Maturation of iron-sulfur proteins in eukaryotes: mechanisms, connected processes, and diseases
    • Lill R., Muhlenhoff U. Maturation of iron-sulfur proteins in eukaryotes: mechanisms, connected processes, and diseases. Annu. Rev. Biochem. 2008, 77:669-700.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 669-700
    • Lill, R.1    Muhlenhoff, U.2
  • 166
    • 73149111946 scopus 로고    scopus 로고
    • Lights on iron-sulfur clusters
    • Lillig C.H., Lill R. Lights on iron-sulfur clusters. Chem. Biol. 2009, 16:1213-1214.
    • (2009) Chem. Biol. , vol.16 , pp. 1213-1214
    • Lillig, C.H.1    Lill, R.2
  • 168
    • 51649086651 scopus 로고    scopus 로고
    • Mitochondrial localization of human frataxin is necessary but processing is not for rescuing frataxin deficiency in Trypanosoma brucei
    • Long S., Jirku M., Ayala F.J., Lukes J. Mitochondrial localization of human frataxin is necessary but processing is not for rescuing frataxin deficiency in Trypanosoma brucei. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:13468-13473.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 13468-13473
    • Long, S.1    Jirku, M.2    Ayala, F.J.3    Lukes, J.4
  • 169
    • 45149131789 scopus 로고    scopus 로고
    • Ancestral roles of eukaryotic frataxin: mitochondrial frataxin function and heterologous expression of hydrogenosomal Trichomonas homologues in trypanosomes
    • Long S., Jirku M., Mach J., Ginger M.L., Sutak R., Richardson D., Tachezy J., Lukes J. Ancestral roles of eukaryotic frataxin: mitochondrial frataxin function and heterologous expression of hydrogenosomal Trichomonas homologues in trypanosomes. Mol. Microbiol. 2008, 69:94-109.
    • (2008) Mol. Microbiol. , vol.69 , pp. 94-109
    • Long, S.1    Jirku, M.2    Mach, J.3    Ginger, M.L.4    Sutak, R.5    Richardson, D.6    Tachezy, J.7    Lukes, J.8
  • 170
    • 52249083711 scopus 로고    scopus 로고
    • The import and function of diatom and plant frataxins in the mitochondrion of Trypanosoma brucei
    • Long S., Vavrova Z., Lukes J. The import and function of diatom and plant frataxins in the mitochondrion of Trypanosoma brucei. Mol. Biochem. Parasitol. 2008, 162:100-104.
    • (2008) Mol. Biochem. Parasitol. , vol.162 , pp. 100-104
    • Long, S.1    Vavrova, Z.2    Lukes, J.3
  • 171
    • 80052711195 scopus 로고    scopus 로고
    • Stage-specific requirement for Isa1 and Isa2 proteins in the mitochondrion of Trypanosoma brucei and heterologous rescue by human and Blastocystis orthologues
    • Long S., Changmai P., Tsaousis A.D., Skalicky T., Verner Z., Wen Y.Z., Roger A.J., Lukes J. Stage-specific requirement for Isa1 and Isa2 proteins in the mitochondrion of Trypanosoma brucei and heterologous rescue by human and Blastocystis orthologues. Mol. Microbiol. 2011, 81:1403-1418.
    • (2011) Mol. Microbiol. , vol.81 , pp. 1403-1418
    • Long, S.1    Changmai, P.2    Tsaousis, A.D.3    Skalicky, T.4    Verner, Z.5    Wen, Y.Z.6    Roger, A.J.7    Lukes, J.8
  • 172
    • 16344377473 scopus 로고    scopus 로고
    • A role for iron-sulfur clusters in DNA repair
    • Lukianova O.A., David S.S. A role for iron-sulfur clusters in DNA repair. Curr. Opin. Chem. Biol. 2005, 9:145-151.
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 145-151
    • Lukianova, O.A.1    David, S.S.2
  • 173
    • 0038349270 scopus 로고    scopus 로고
    • MinD and role of the deviant Walker A motif, dimerization and membrane binding in oscillation
    • Lutkenhaus J., Sundaramoorthy M. MinD and role of the deviant Walker A motif, dimerization and membrane binding in oscillation. Mol. Microbiol. 2003, 48:295-303.
    • (2003) Mol. Microbiol. , vol.48 , pp. 295-303
    • Lutkenhaus, J.1    Sundaramoorthy, M.2
  • 178
    • 0037209757 scopus 로고    scopus 로고
    • Bacterial cysteine desulfurases: their function and mechanisms
    • Mihara H., Esaki N. Bacterial cysteine desulfurases: their function and mechanisms. Appl. Microbiol. Biotechnol. 2002, 60:12-23.
    • (2002) Appl. Microbiol. Biotechnol. , vol.60 , pp. 12-23
    • Mihara, H.1    Esaki, N.2
  • 179
    • 0030963659 scopus 로고    scopus 로고
    • Cysteine sulfinate desulfinase, a NIFS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activities. Gene cloning, purification, and characterization of a novel pyridoxal enzyme
    • Mihara H., Kurihara T., Yoshimura T., Soda K., Esaki N. Cysteine sulfinate desulfinase, a NIFS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activities. Gene cloning, purification, and characterization of a novel pyridoxal enzyme. J. Biol. Chem. 1997, 272:22417-22424.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22417-22424
    • Mihara, H.1    Kurihara, T.2    Yoshimura, T.3    Soda, K.4    Esaki, N.5
  • 180
    • 0033591390 scopus 로고    scopus 로고
    • A nifS-like gene, csdB, encodes an Escherichia coli counterpart of mammalian selenocysteine lyase. Gene cloning, purification, characterization and preliminary X-ray crystallographic studies
    • Mihara H., Maeda M., Fujii T., Kurihara T., Hata Y., Esaki N. A nifS-like gene, csdB, encodes an Escherichia coli counterpart of mammalian selenocysteine lyase. Gene cloning, purification, characterization and preliminary X-ray crystallographic studies. J. Biol. Chem. 1999, 274:14768-14772.
    • (1999) J. Biol. Chem. , vol.274 , pp. 14768-14772
    • Mihara, H.1    Maeda, M.2    Fujii, T.3    Kurihara, T.4    Hata, Y.5    Esaki, N.6
  • 181
    • 0034093325 scopus 로고    scopus 로고
    • Kinetic and mutational studies of three NifS homologs from Escherichia coli: mechanistic difference between L-cysteine desulfurase and L-selenocysteine lyase reactions
    • Mihara H., Kurihara T., Yoshimura T., Esaki N. Kinetic and mutational studies of three NifS homologs from Escherichia coli: mechanistic difference between L-cysteine desulfurase and L-selenocysteine lyase reactions. J. Biochem. 2000, 127:559-567.
    • (2000) J. Biochem. , vol.127 , pp. 559-567
    • Mihara, H.1    Kurihara, T.2    Yoshimura, T.3    Esaki, N.4
  • 182
    • 77955332146 scopus 로고    scopus 로고
    • Diversity in mitochondrial metabolic pathways in parasitic protists Plasmodium and Cryptosporidium
    • Mogi T., Kita K. Diversity in mitochondrial metabolic pathways in parasitic protists Plasmodium and Cryptosporidium. Parasitol. Int. 2010, 59:305-312.
    • (2010) Parasitol. Int. , vol.59 , pp. 305-312
    • Mogi, T.1    Kita, K.2
  • 183
    • 0035190234 scopus 로고    scopus 로고
    • A plastidic ABC protein involved in intercompartmental communication of light signaling
    • Moller S.G., Kunkel T., Chua N.H. A plastidic ABC protein involved in intercompartmental communication of light signaling. Genes Dev. 2001, 15:90-103.
    • (2001) Genes Dev. , vol.15 , pp. 90-103
    • Moller, S.G.1    Kunkel, T.2    Chua, N.H.3
  • 184
    • 0033619724 scopus 로고    scopus 로고
    • Refined X-ray structures of the oxidized, at 1.3 A, and reduced, at 1.17 A, [2Fe-2S] ferredoxin from the cyanobacterium Anabaena PCC7119 show redox-linked conformational changes
    • Morales R., Charon M.H., Hudry-Clergeon G., Petillot Y., Norager S., Medina M., Frey M. Refined X-ray structures of the oxidized, at 1.3 A, and reduced, at 1.17 A, [2Fe-2S] ferredoxin from the cyanobacterium Anabaena PCC7119 show redox-linked conformational changes. Biochemistry 1999, 38:15764-15773.
    • (1999) Biochemistry , vol.38 , pp. 15764-15773
    • Morales, R.1    Charon, M.H.2    Hudry-Clergeon, G.3    Petillot, Y.4    Norager, S.5    Medina, M.6    Frey, M.7
  • 185
    • 33745271510 scopus 로고    scopus 로고
    • The asymmetric IscA homodimer with an exposed [2Fe-2S] cluster suggests the structural basis of the Fe-S cluster biosynthetic scaffold
    • Morimoto K., Yamashita E., Kondou Y., Lee S.J., Arisaka F., Tsukihara T., Nakai M. The asymmetric IscA homodimer with an exposed [2Fe-2S] cluster suggests the structural basis of the Fe-S cluster biosynthetic scaffold. J. Mol. Biol. 2006, 360:117-132.
    • (2006) J. Mol. Biol. , vol.360 , pp. 117-132
    • Morimoto, K.1    Yamashita, E.2    Kondou, Y.3    Lee, S.J.4    Arisaka, F.5    Tsukihara, T.6    Nakai, M.7
  • 186
    • 0029786946 scopus 로고    scopus 로고
    • Crystal structure of the 2[4Fe-4S] ferredoxin from Chromatium vinosum: evolutionary and mechanistic inferences for [3/4Fe-4S] ferredoxins
    • Moulis J.M., Sieker L.C., Wilson K.S., Dauter Z. Crystal structure of the 2[4Fe-4S] ferredoxin from Chromatium vinosum: evolutionary and mechanistic inferences for [3/4Fe-4S] ferredoxins. Protein Sci. 1996, 5:1765-1775.
    • (1996) Protein Sci. , vol.5 , pp. 1765-1775
    • Moulis, J.M.1    Sieker, L.C.2    Wilson, K.S.3    Dauter, Z.4
  • 187
    • 33646349748 scopus 로고    scopus 로고
    • Trafficking in persulfides: delivering sulfur in biosynthetic pathways
    • Mueller E.G. Trafficking in persulfides: delivering sulfur in biosynthetic pathways. Nat. Chem. Biol. 2006, 2:185-194.
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 185-194
    • Mueller, E.G.1
  • 188
    • 0041893905 scopus 로고    scopus 로고
    • Biogenesis of iron-sulfur proteins in eukaryotes: a novel task of mitochondria that is inherited from bacteria
    • Muhlenhoff U., Lill R. Biogenesis of iron-sulfur proteins in eukaryotes: a novel task of mitochondria that is inherited from bacteria. Biochim. Biophys. Acta 2000, 1459:370-382.
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 370-382
    • Muhlenhoff, U.1    Lill, R.2
  • 190
    • 4344595102 scopus 로고    scopus 로고
    • Functional characterization of the eukaryotic cysteine desulfurase Nfs1p from Saccharomyces cerevisiae
    • Muhlenhoff U., Balk J., Richhardt N., Kaiser J.T., Sipos K., Kispal G., Lill R. Functional characterization of the eukaryotic cysteine desulfurase Nfs1p from Saccharomyces cerevisiae. J. Biol. Chem. 2004, 279:36906-36915.
    • (2004) J. Biol. Chem. , vol.279 , pp. 36906-36915
    • Muhlenhoff, U.1    Balk, J.2    Richhardt, N.3    Kaiser, J.T.4    Sipos, K.5    Kispal, G.6    Lill, R.7
  • 191
    • 1642514907 scopus 로고    scopus 로고
    • Prominent roles of the NorR and Fur regulators in the Escherichia coli transcriptional response to reactive nitrogen species
    • Mukhopadhyay P., Zheng M., Bedzyk L.A., LaRossa R.A., Storz G. Prominent roles of the NorR and Fur regulators in the Escherichia coli transcriptional response to reactive nitrogen species. Proc. Natl. Acad. Sci. U.S.A. 2004, 101:745-750.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 745-750
    • Mukhopadhyay, P.1    Zheng, M.2    Bedzyk, L.A.3    LaRossa, R.A.4    Storz, G.5
  • 192
    • 0035116079 scopus 로고    scopus 로고
    • SoxR-dependent response to oxidative stress and virulence of Erwinia chrysanthemi: the key role of SufC, an orphan ABC ATPase
    • Nachin L., El Hassouni M., Loiseau L., Expert D., Barras F. SoxR-dependent response to oxidative stress and virulence of Erwinia chrysanthemi: the key role of SufC, an orphan ABC ATPase. Mol. Microbiol. 2001, 39:960-972.
    • (2001) Mol. Microbiol. , vol.39 , pp. 960-972
    • Nachin, L.1    El Hassouni, M.2    Loiseau, L.3    Expert, D.4    Barras, F.5
  • 193
    • 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. 2003, 22:427-437.
    • (2003) EMBO J. , vol.22 , pp. 427-437
    • Nachin, L.1    Loiseau, L.2    Expert, D.3    Barras, F.4
  • 194
    • 38049129044 scopus 로고    scopus 로고
    • The Leishmania-macrophage interaction: a metabolic perspective
    • Naderer T., McConville M.J. The Leishmania-macrophage interaction: a metabolic perspective. Cell. Microbiol. 2008, 10:301-308.
    • (2008) Cell. Microbiol. , vol.10 , pp. 301-308
    • Naderer, T.1    McConville, M.J.2
  • 195
    • 0035896587 scopus 로고    scopus 로고
    • Nuclear localization of yeast Nfs1p is required for cell survival
    • Nakai Y., Nakai M., Hayashi H., Kagamiyama H. Nuclear localization of yeast Nfs1p is required for cell survival. J. Biol. Chem. 2001, 276:8314-8320.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8314-8320
    • Nakai, Y.1    Nakai, M.2    Hayashi, H.3    Kagamiyama, H.4
  • 196
  • 197
    • 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. 2007, 27:2841-2847.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 2841-2847
    • Nakai, Y.1    Nakai, M.2    Lill, R.3    Suzuki, T.4    Hayashi, H.5
  • 198
    • 34247247617 scopus 로고    scopus 로고
    • The Cfd1-Nbp35 complex acts as a scaffold for iron-sulfur protein assembly in the yeast cytosol
    • Netz D.J., Pierik A.J., Stumpfig M., Muhlenhoff U., Lill R. The Cfd1-Nbp35 complex acts as a scaffold for iron-sulfur protein assembly in the yeast cytosol. Nat. Chem. Biol. 2007, 3:278-286.
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 278-286
    • Netz, D.J.1    Pierik, A.J.2    Stumpfig, M.3    Muhlenhoff, U.4    Lill, R.5
  • 200
    • 84859492661 scopus 로고    scopus 로고
    • A bridging [4Fe-4S] cluster and nucleotide binding are essential for function of the Cfd1-Nbp35 complex as a scaffold in iron-sulfur protein maturation
    • Netz D.J., Pierik A.J., Stumpfig M., Bill E., Sharma A.K., Pallesen L.J., Walden W.E., Lill R. A bridging [4Fe-4S] cluster and nucleotide binding are essential for function of the Cfd1-Nbp35 complex as a scaffold in iron-sulfur protein maturation. J. Biol. Chem. 2012, 287:12365-12378.
    • (2012) J. Biol. Chem. , vol.287 , pp. 12365-12378
    • Netz, D.J.1    Pierik, A.J.2    Stumpfig, M.3    Bill, E.4    Sharma, A.K.5    Pallesen, L.J.6    Walden, W.E.7    Lill, R.8
  • 203
    • 0027299821 scopus 로고
    • Uptake of iron-siderophore complexes across the bacterial outer membrane
    • discussion 7-8
    • Nikaido H. Uptake of iron-siderophore complexes across the bacterial outer membrane. Trends Microbiol. 1993, 1:5-7. discussion 7-8.
    • (1993) Trends Microbiol. , vol.1 , pp. 5-7
    • Nikaido, H.1
  • 204
    • 26844478710 scopus 로고    scopus 로고
    • Sulfur-containing amino acid metabolism in parasitic protozoa
    • Nozaki T., Ali V., Tokoro M. Sulfur-containing amino acid metabolism in parasitic protozoa. Adv. Parasitol. 2005, 60:1-99.
    • (2005) Adv. Parasitol. , vol.60 , pp. 1-99
    • Nozaki, T.1    Ali, V.2    Tokoro, M.3
  • 206
    • 84876929324 scopus 로고    scopus 로고
    • NIF-type iron-sulfur cluster assembly system is duplicated and distributed in the mitochondria and cytosol of Mastigamoeba balamuthi
    • Nývltová E., Šuták R., Harant K., Šedinová M., Hrdy I., Paces J., Vlček Č., Tachezy J. NIF-type iron-sulfur cluster assembly system is duplicated and distributed in the mitochondria and cytosol of Mastigamoeba balamuthi. Proc. Natl. Acad. Sci. USA. 2013, 110:7371-7376.
    • (2013) Proc. Natl. Acad. Sci. USA. , vol.110 , pp. 7371-7376
    • Nývltová, E.1    Šuták, R.2    Harant, K.3    Šedinová, M.4    Hrdy, I.5    Paces, J.6    Vlček, Č.7    Tachezy, J.8
  • 207
    • 0034719118 scopus 로고    scopus 로고
    • Characterization of the NifU and NifS Fe-S cluster formation proteins essential for viability in Helicobacter pylori
    • Olson J.W., Agar J.N., Johnson M.K., Maier R.J. Characterization of the NifU and NifS Fe-S cluster formation proteins essential for viability in Helicobacter pylori. Biochemistry 2000, 39:16213-16219.
    • (2000) Biochemistry , vol.39 , pp. 16213-16219
    • Olson, J.W.1    Agar, J.N.2    Johnson, M.K.3    Maier, R.J.4
  • 208
    • 2442567822 scopus 로고    scopus 로고
    • A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli
    • Outten F.W., Djaman O., Storz G. A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli. Mol. Microbiol. 2004, 52:861-872.
    • (2004) Mol. Microbiol. , vol.52 , pp. 861-872
    • Outten, F.W.1    Djaman, O.2    Storz, G.3
  • 210
    • 67649386835 scopus 로고    scopus 로고
    • Mitochondrial tRNA import in Trypanosoma brucei is independent of thiolation and the Rieske protein
    • Paris Z., Rubio M.A., Lukes J., Alfonzo J.D. Mitochondrial tRNA import in Trypanosoma brucei is independent of thiolation and the Rieske protein. RNA 2009, 15:1398-1406.
    • (2009) RNA , vol.15 , pp. 1398-1406
    • Paris, Z.1    Rubio, M.A.2    Lukes, J.3    Alfonzo, J.D.4
  • 211
    • 77954619982 scopus 로고    scopus 로고
    • The Fe/S cluster assembly protein Isd11 is essential for tRNA thiolation in Trypanosoma brucei
    • Paris Z., Changmai P., Rubio M.A., Zikova A., Stuart K.D., Alfonzo J.D., Lukes J. The Fe/S cluster assembly protein Isd11 is essential for tRNA thiolation in Trypanosoma brucei. J. Biol. Chem. 2010, 285:22394-22402.
    • (2010) J. Biol. Chem. , vol.285 , pp. 22394-22402
    • Paris, Z.1    Changmai, P.2    Rubio, M.A.3    Zikova, A.4    Stuart, K.D.5    Alfonzo, J.D.6    Lukes, J.7
  • 214
    • 0032483966 scopus 로고    scopus 로고
    • X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution
    • Peters J.W., Lanzilotta W.N., Lemon B.J., Seefeldt L.C. X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution. Science 1998, 282:1853-1858.
    • (1998) Science , vol.282 , pp. 1853-1858
    • Peters, J.W.1    Lanzilotta, W.N.2    Lemon, B.J.3    Seefeldt, L.C.4
  • 215
    • 2942724221 scopus 로고    scopus 로고
    • Dual targeting of yeast catalase A to peroxisomes and mitochondria
    • Petrova V.Y., Drescher D., Kujumdzieva A.V., Schmitt M.J. Dual targeting of yeast catalase A to peroxisomes and mitochondria. Biochem. J. 2004, 380:393-400.
    • (2004) Biochem. J. , vol.380 , pp. 393-400
    • Petrova, V.Y.1    Drescher, D.2    Kujumdzieva, A.V.3    Schmitt, M.J.4
  • 216
    • 37349036175 scopus 로고    scopus 로고
    • CGFS-type monothiol glutaredoxins from the cyanobacterium Synechocystis PCC6803 and other evolutionary distant model organisms possess a glutathione-ligated [2Fe-2S] cluster
    • Picciocchi A., Saguez C., Boussac A., Cassier-Chauvat C., Chauvat F. CGFS-type monothiol glutaredoxins from the cyanobacterium Synechocystis PCC6803 and other evolutionary distant model organisms possess a glutathione-ligated [2Fe-2S] cluster. Biochemistry 2007, 46:15018-15026.
    • (2007) Biochemistry , vol.46 , pp. 15018-15026
    • Picciocchi, A.1    Saguez, C.2    Boussac, A.3    Cassier-Chauvat, C.4    Chauvat, F.5
  • 217
    • 77955251744 scopus 로고    scopus 로고
    • Pyruvate:ferredoxin oxidoreductase and bifunctional aldehyde-alcohol dehydrogenase are essential for energy metabolism under oxidative stress in Entamoeba histolytica
    • Pineda E., Encalada R., Rodriguez-Zavala J.S., Olivos-Garcia A., Moreno-Sanchez R., Saavedra E. Pyruvate:ferredoxin oxidoreductase and bifunctional aldehyde-alcohol dehydrogenase are essential for energy metabolism under oxidative stress in Entamoeba histolytica. FEBS J. 2010, 277:3382-3395.
    • (2010) FEBS J. , vol.277 , pp. 3382-3395
    • Pineda, E.1    Encalada, R.2    Rodriguez-Zavala, J.S.3    Olivos-Garcia, A.4    Moreno-Sanchez, R.5    Saavedra, E.6
  • 220
    • 77952813340 scopus 로고    scopus 로고
    • Building Fe-S proteins: bacterial strategies
    • Py B., Barras F. Building Fe-S proteins: bacterial strategies. Nat. Rev. Microbiol. 2010, 8:436-446.
    • (2010) Nat. Rev. Microbiol. , vol.8 , pp. 436-446
    • Py, B.1    Barras, F.2
  • 222
    • 0033582421 scopus 로고    scopus 로고
    • The yeast frataxin homologue mediates mitochondrial iron efflux. Evidence for a mitochondrial iron cycle
    • Radisky D.C., Babcock M.C., Kaplan J. The yeast frataxin homologue mediates mitochondrial iron efflux. Evidence for a mitochondrial iron cycle. J. Biol. Chem. 1999, 274:4497-4499.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4497-4499
    • Radisky, D.C.1    Babcock, M.C.2    Kaplan, J.3
  • 223
    • 0001689934 scopus 로고    scopus 로고
    • Nickel-containing carbon monoxide dehydrogenase/acetyl-CoA synthase
    • Ragsdale S.W., Kumar M. Nickel-containing carbon monoxide dehydrogenase/acetyl-CoA synthase. Chem. Rev. 1996, 96:2515-2540.
    • (1996) Chem. Rev. , vol.96 , pp. 2515-2540
    • Ragsdale, S.W.1    Kumar, M.2
  • 224
    • 8444244485 scopus 로고    scopus 로고
    • Evolutionary pressures on apicoplast transit peptides
    • Ralph S.A., Foth B.J., Hall N., McFadden G.I. Evolutionary pressures on apicoplast transit peptides. Mol. Biol. Evol. 2004, 21:2183-2194.
    • (2004) Mol. Biol. Evol. , vol.21 , pp. 2183-2194
    • Ralph, S.A.1    Foth, B.J.2    Hall, N.3    McFadden, G.I.4
  • 225
    • 1642573170 scopus 로고    scopus 로고
    • Mitochondrial functional interactions between frataxin and Isu1p, the iron-sulfur cluster scaffold protein, in Saccharomyces cerevisiae
    • Ramazzotti A., Vanmansart V., Foury F. Mitochondrial functional interactions between frataxin and Isu1p, the iron-sulfur cluster scaffold protein, in Saccharomyces cerevisiae. FEBS Lett. 2004, 557:215-220.
    • (2004) FEBS Lett. , vol.557 , pp. 215-220
    • Ramazzotti, A.1    Vanmansart, V.2    Foury, F.3
  • 228
    • 0033777079 scopus 로고    scopus 로고
    • Nitrogenase: standing at the crossroads
    • Rees D.C., Howard J.B. Nitrogenase: standing at the crossroads. Curr. Opin. Chem. Biol. 2000, 4:559-566.
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 559-566
    • Rees, D.C.1    Howard, J.B.2
  • 229
    • 0038670302 scopus 로고    scopus 로고
    • The interface between the biological and inorganic worlds: iron-sulfur metalloclusters
    • Rees D.C., Howard J.B. The interface between the biological and inorganic worlds: iron-sulfur metalloclusters. Science 2003, 300:929-931.
    • (2003) Science , vol.300 , pp. 929-931
    • Rees, D.C.1    Howard, J.B.2
  • 230
    • 0017615796 scopus 로고
    • An energy-conserving pyruvate-to-acetate pathway in Entamoeba histolytica. Pyruvate synthase and a new acetate thiokinase
    • Reeves R.E., Warren L.G., Susskind B., Lo H.S. An energy-conserving pyruvate-to-acetate pathway in Entamoeba histolytica. Pyruvate synthase and a new acetate thiokinase. J. Biol. Chem. 1977, 252:726-731.
    • (1977) J. Biol. Chem. , vol.252 , pp. 726-731
    • Reeves, R.E.1    Warren, L.G.2    Susskind, B.3    Lo, H.S.4
  • 231
    • 33745618402 scopus 로고    scopus 로고
    • Evolution of the Isd11-IscS complex reveals a single alpha-proteobacterial endosymbiosis for all eukaryotes
    • Richards T.A., van der Giezen M. Evolution of the Isd11-IscS complex reveals a single alpha-proteobacterial endosymbiosis for all eukaryotes. Mol. Biol. Evol. 2006, 23:1341-1344.
    • (2006) Mol. Biol. Evol. , vol.23 , pp. 1341-1344
    • Richards, T.A.1    van der Giezen, M.2
  • 232
    • 26244464441 scopus 로고    scopus 로고
    • The essential mitochondrial protein Erv1 cooperates with Mia40 in biogenesis of intermembrane space proteins
    • Rissler M., Wiedemann N., Pfannschmidt S., Gabriel K., Guiard B., Pfanner N., Chacinska A. The essential mitochondrial protein Erv1 cooperates with Mia40 in biogenesis of intermembrane space proteins. J. Mol. Biol. 2005, 353:485-492.
    • (2005) J. Mol. Biol. , vol.353 , pp. 485-492
    • Rissler, M.1    Wiedemann, N.2    Pfannschmidt, S.3    Gabriel, K.4    Guiard, B.5    Pfanner, N.6    Chacinska, A.7
  • 233
    • 0036226063 scopus 로고    scopus 로고
    • Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes
    • Rodriguez-Manzaneque M.T., Tamarit J., Belli G., Ros J., Herrero E. Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes. Mol. Biol. Cell 2002, 13:1109-1121.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1109-1121
    • Rodriguez-Manzaneque, M.T.1    Tamarit, J.2    Belli, G.3    Ros, J.4    Herrero, E.5
  • 235
    • 0036252812 scopus 로고    scopus 로고
    • Molecular insights into Friedreich's ataxia and antioxidant-based therapies
    • Rotig A., Sidi D., Munnich A., Rustin P. Molecular insights into Friedreich's ataxia and antioxidant-based therapies. Trends Mol. Med. 2002, 8:221-224.
    • (2002) Trends Mol. Med. , vol.8 , pp. 221-224
    • Rotig, A.1    Sidi, D.2    Munnich, A.3    Rustin, P.4
  • 236
    • 84858015433 scopus 로고    scopus 로고
    • Biogenesis of iron-sulfur clusters in mammalian cells: new insights and relevance to human disease
    • Rouault T.A. Biogenesis of iron-sulfur clusters in mammalian cells: new insights and relevance to human disease. Dis. Model. Mech. 2012, 5:155-164.
    • (2012) Dis. Model. Mech. , vol.5 , pp. 155-164
    • Rouault, T.A.1
  • 237
    • 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. 2008, 24:398-407.
    • (2008) Trends Genet. , vol.24 , pp. 398-407
    • Rouault, T.A.1    Tong, W.H.2
  • 242
    • 0031569858 scopus 로고    scopus 로고
    • Isolation and chromosomal mapping of a novel ATP-binding cassette transporter conserved in mouse and human
    • Savary S., Allikmets R., Denizot F., Luciani M.F., Mattei M.G., Dean M., Chimini G. Isolation and chromosomal mapping of a novel ATP-binding cassette transporter conserved in mouse and human. Genomics 1997, 41:275-278.
    • (1997) Genomics , vol.41 , pp. 275-278
    • Savary, S.1    Allikmets, R.2    Denizot, F.3    Luciani, M.F.4    Mattei, M.G.5    Dean, M.6    Chimini, G.7
  • 243
    • 33847687662 scopus 로고    scopus 로고
    • Respiratory complex I: mechanistic and structural insights provided by the crystal structure of the hydrophilic domain
    • Sazanov L.A. Respiratory complex I: mechanistic and structural insights provided by the crystal structure of the hydrophilic domain. Biochemistry 2007, 46:2275-2288.
    • (2007) Biochemistry , vol.46 , pp. 2275-2288
    • Sazanov, L.A.1
  • 244
    • 33644872938 scopus 로고    scopus 로고
    • Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus
    • Sazanov L.A., Hinchliffe P. Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus. Science 2006, 311:1430-1436.
    • (2006) Science , vol.311 , pp. 1430-1436
    • Sazanov, L.A.1    Hinchliffe, P.2
  • 245
    • 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. U.S.A. 1999, 96:10206-10211.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 10206-10211
    • Schilke, B.1    Voisine, C.2    Beinert, H.3    Craig, E.4
  • 246
    • 82355191521 scopus 로고    scopus 로고
    • The Trichomonas vaginalis hydrogenosome proteome is highly reduced relative to mitochondria, yet complex compared with mitosomes
    • Schneider R.E., Brown M.T., Shiflett A.M., Dyall S.D., Hayes R.D., Xie Y., Loo J.A., Johnson P.J. The Trichomonas vaginalis hydrogenosome proteome is highly reduced relative to mitochondria, yet complex compared with mitosomes. Int. J. Parasitol. 2011, 41:1421-1434.
    • (2011) Int. J. Parasitol. , vol.41 , pp. 1421-1434
    • Schneider, R.E.1    Brown, M.T.2    Shiflett, A.M.3    Dyall, S.D.4    Hayes, R.D.5    Xie, Y.6    Loo, J.A.7    Johnson, P.J.8
  • 247
    • 0033064808 scopus 로고    scopus 로고
    • Iron acquisition systems in the pathogenic Neisseria
    • Schryvers A.B., Stojiljkovic I. Iron acquisition systems in the pathogenic Neisseria. Mol. Microbiol. 1999, 32:1117-1123.
    • (1999) Mol. Microbiol. , vol.32 , pp. 1117-1123
    • Schryvers, A.B.1    Stojiljkovic, I.2
  • 248
    • 0034255455 scopus 로고    scopus 로고
    • The cysteine desulfurase, IscS, has a major role in in vivo Fe-S cluster formation in Escherichia coli
    • Schwartz C.J., Djaman O., Imlay J.A., Kiley P.J. The cysteine desulfurase, IscS, has a major role in in vivo Fe-S cluster formation in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 2000, 97:9009-9014.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 9009-9014
    • Schwartz, C.J.1    Djaman, O.2    Imlay, J.A.3    Kiley, P.J.4
  • 249
    • 0035909963 scopus 로고    scopus 로고
    • IscR, an Fe-S cluster-containing transcription factor, represses expression of Escherichia coli genes encoding Fe-S cluster assembly proteins
    • Schwartz C.J., Giel J.L., Patschkowski T., Luther C., Ruzicka F.J., Beinert H., Kiley P.J. IscR, an Fe-S cluster-containing transcription factor, represses expression of Escherichia coli genes encoding Fe-S cluster assembly proteins. Proc. Natl. Acad. Sci. U.S.A. 2001, 98:14895-14900.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 14895-14900
    • Schwartz, C.J.1    Giel, J.L.2    Patschkowski, T.3    Luther, C.4    Ruzicka, F.J.5    Beinert, H.6    Kiley, P.J.7
  • 251
    • 0036710572 scopus 로고    scopus 로고
    • Biogenesis of iron-sulphur clusters in amitochondriate and apicomplexan protists
    • Seeber F. Biogenesis of iron-sulphur clusters in amitochondriate and apicomplexan protists. Int. J. Parasitol. 2002, 32:1207-1217.
    • (2002) Int. J. Parasitol. , vol.32 , pp. 1207-1217
    • Seeber, F.1
  • 252
    • 23844532238 scopus 로고    scopus 로고
    • The plant-type ferredoxin-NADP+reductase/ferredoxin redox system as a possible drug target against apicomplexan human parasites
    • Seeber F., Aliverti A., Zanetti G. The plant-type ferredoxin-NADP+reductase/ferredoxin redox system as a possible drug target against apicomplexan human parasites. Curr. Pharm. Des. 2005, 11:3159-3172.
    • (2005) Curr. Pharm. Des. , vol.11 , pp. 3159-3172
    • Seeber, F.1    Aliverti, A.2    Zanetti, G.3
  • 255
    • 84866513533 scopus 로고    scopus 로고
    • Monothiol glutaredoxins function in storing and transporting [Fe2S2] clusters assembled on IscU scaffold proteins
    • Shakamuri P., Zhang B., Johnson M.K. Monothiol glutaredoxins function in storing and transporting [Fe2S2] clusters assembled on IscU scaffold proteins. J. Am. Chem. Soc. 2012, 134:15213-15216.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 15213-15216
    • Shakamuri, P.1    Zhang, B.2    Johnson, M.K.3
  • 256
    • 34447316711 scopus 로고    scopus 로고
    • Mitochondrial frataxin interacts with ISD11 of the NFS1/ISCU complex and multiple mitochondrial chaperones
    • Shan Y., Napoli E., Cortopassi G. Mitochondrial frataxin interacts with ISD11 of the NFS1/ISCU complex and multiple mitochondrial chaperones. Hum. Mol. Genet. 2007, 16:929-941.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 929-941
    • Shan, Y.1    Napoli, E.2    Cortopassi, G.3
  • 257
    • 77956235790 scopus 로고    scopus 로고
    • Cytosolic iron-sulfur cluster assembly (CIA) system: factors, mechanism, and relevance to cellular iron regulation
    • Sharma A.K., Pallesen L.J., Spang R.J., Walden W.E. Cytosolic iron-sulfur cluster assembly (CIA) system: factors, mechanism, and relevance to cellular iron regulation. J. Biol. Chem. 2010, 285:26745-26751.
    • (2010) J. Biol. Chem. , vol.285 , pp. 26745-26751
    • Sharma, A.K.1    Pallesen, L.J.2    Spang, R.J.3    Walden, W.E.4
  • 258
    • 68049086933 scopus 로고    scopus 로고
    • Human ISD11 is essential for both iron-sulfur cluster assembly and maintenance of normal cellular iron homeostasis
    • Shi Y., Ghosh M.C., Tong W.H., Rouault T.A. Human ISD11 is essential for both iron-sulfur cluster assembly and maintenance of normal cellular iron homeostasis. Hum. Mol. Genet. 2009, 18:3014-3025.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 3014-3025
    • Shi, Y.1    Ghosh, M.C.2    Tong, W.H.3    Rouault, T.A.4
  • 260
    • 0025744263 scopus 로고
    • Binding to cellular receptors results in increased iron release from transferrin at mildly acidic pH
    • Sipe D.M., Murphy R.F. Binding to cellular receptors results in increased iron release from transferrin at mildly acidic pH. J. Biol. Chem. 1991, 266:8002-8007.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8002-8007
    • Sipe, D.M.1    Murphy, R.F.2
  • 261
    • 0037216551 scopus 로고    scopus 로고
    • Lack of the ApbC or ApbE protein results in a defect in Fe-S cluster metabolism in Salmonella enterica serovar Typhimurium
    • Skovran E., Downs D.M. Lack of the ApbC or ApbE protein results in a defect in Fe-S cluster metabolism in Salmonella enterica serovar Typhimurium. J. Bacteriol. 2003, 185:98-106.
    • (2003) J. Bacteriol. , vol.185 , pp. 98-106
    • Skovran, E.1    Downs, D.M.2
  • 262
    • 33749415299 scopus 로고    scopus 로고
    • Knock-downs of iron-sulfur cluster assembly proteins IscS and IscU down-regulate the active mitochondrion of procyclic Trypanosoma brucei
    • Smid O., Horakova E., Vilimova V., Hrdy I., Cammack R., Horvath A., Lukes J., Tachezy J. Knock-downs of iron-sulfur cluster assembly proteins IscS and IscU down-regulate the active mitochondrion of procyclic Trypanosoma brucei. J. Biol. Chem. 2006, 281:28679-28686.
    • (2006) J. Biol. Chem. , vol.281 , pp. 28679-28686
    • Smid, O.1    Horakova, E.2    Vilimova, V.3    Hrdy, I.4    Cammack, R.5    Horvath, A.6    Lukes, J.7    Tachezy, J.8
  • 265
    • 79955547953 scopus 로고    scopus 로고
    • Mouse knock-out of IOP1 protein reveals its essential role in mammalian cytosolic iron-sulfur protein biogenesis
    • Song D., Lee F.S. Mouse knock-out of IOP1 protein reveals its essential role in mammalian cytosolic iron-sulfur protein biogenesis. J. Biol. Chem. 2007, 286:15797-15805.
    • (2007) J. Biol. Chem. , vol.286 , pp. 15797-15805
    • Song, D.1    Lee, F.S.2
  • 266
    • 72149100164 scopus 로고    scopus 로고
    • Human ISCA1 interacts with IOP1/NARFL and functions in both cytosolic and mitochondrial iron-sulfur protein biogenesis
    • Song D., Tu Z., Lee F.S. Human ISCA1 interacts with IOP1/NARFL and functions in both cytosolic and mitochondrial iron-sulfur protein biogenesis. J. Biol. Chem. 2009, 284:35297-35307.
    • (2009) J. Biol. Chem. , vol.284 , pp. 35297-35307
    • Song, D.1    Tu, Z.2    Lee, F.S.3
  • 268
    • 77956248535 scopus 로고    scopus 로고
    • Frataxin and mitochondrial FeS cluster biogenesis
    • Stemmler T.L., Lesuisse E., Pain D., Dancis A. Frataxin and mitochondrial FeS cluster biogenesis. J. Biol. Chem. 2010, 285:26737-26743.
    • (2010) J. Biol. Chem. , vol.285 , pp. 26737-26743
    • Stemmler, T.L.1    Lesuisse, E.2    Pain, D.3    Dancis, A.4
  • 270
    • 0028861990 scopus 로고
    • Transferrin-binding protein complex is the receptor for transferrin uptake in Trypanosoma brucei
    • Steverding D., Stierhof Y.D., Fuchs H., Tauber R., Overath P. Transferrin-binding protein complex is the receptor for transferrin uptake in Trypanosoma brucei. J. Cell Biol. 1995, 131:1173-1182.
    • (1995) J. Cell Biol. , vol.131 , pp. 1173-1182
    • Steverding, D.1    Stierhof, Y.D.2    Fuchs, H.3    Tauber, R.4    Overath, P.5
  • 271
    • 21244503033 scopus 로고    scopus 로고
    • Crystal structure of mitochondrial respiratory membrane protein complex II
    • Sun F., Huo X., Zhai Y., Wang A., Xu J., Su D., Bartlam M., Rao Z. Crystal structure of mitochondrial respiratory membrane protein complex II. Cell 2005, 121:1043-1057.
    • (2005) Cell , vol.121 , pp. 1043-1057
    • Sun, F.1    Huo, X.2    Zhai, Y.3    Wang, A.4    Xu, J.5    Su, D.6    Bartlam, M.7    Rao, Z.8
  • 273
    • 0034804608 scopus 로고    scopus 로고
    • Mitochondrial type iron-sulfur cluster assembly in the amitochondriate eukaryotes Trichomonas vaginalis and Giardia intestinalis, as indicated by the phylogeny of IscS
    • Tachezy J., Sanchez L.B., Muller M. Mitochondrial type iron-sulfur cluster assembly in the amitochondriate eukaryotes Trichomonas vaginalis and Giardia intestinalis, as indicated by the phylogeny of IscS. Mol. Biol. Evol. 2001, 18:1919-1928.
    • (2001) Mol. Biol. Evol. , vol.18 , pp. 1919-1928
    • Tachezy, J.1    Sanchez, L.B.2    Muller, M.3
  • 274
    • 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. 2002, 277:28380-28383.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28380-28383
    • Takahashi, Y.1    Tokumoto, U.2
  • 276
    • 9644264011 scopus 로고    scopus 로고
    • Blastocystis in humans and animals: new insights using modern methodologies
    • Tan K.S. Blastocystis in humans and animals: new insights using modern methodologies. Vet. Parasitol. 2004, 126:121-144.
    • (2004) Vet. Parasitol. , vol.126 , pp. 121-144
    • Tan, K.S.1
  • 277
    • 54249101651 scopus 로고    scopus 로고
    • New insights on classification, identification, and clinical relevance of Blastocystis spp
    • Tan K.S. New insights on classification, identification, and clinical relevance of Blastocystis spp. Clin. Microbiol. Rev. 2008, 21:639-665.
    • (2008) Clin. Microbiol. Rev. , vol.21 , pp. 639-665
    • Tan, K.S.1
  • 278
    • 66949146078 scopus 로고    scopus 로고
    • IscA/SufA paralogues 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 paralogues are required for the [4Fe-4S] cluster assembly in enzymes of multiple physiological pathways in Escherichia coli under aerobic growth conditions. Biochem. J. 2009, 420:463-472.
    • (2009) Biochem. J. , vol.420 , pp. 463-472
    • Tan, G.1    Lu, J.2    Bitoun, J.P.3    Huang, H.4    Ding, H.5
  • 279
    • 0032739921 scopus 로고    scopus 로고
    • Direct evidence for mRNA binding and post-transcriptional regulation by Escherichia coli aconitases
    • Tang Y., Guest J.R. Direct evidence for mRNA binding and post-transcriptional regulation by Escherichia coli aconitases. Microbiology 1999, 145(Pt 11):3069-3079.
    • (1999) Microbiology , vol.145 , Issue.PART 11 , pp. 3069-3079
    • Tang, Y.1    Guest, J.R.2
  • 280
    • 11144339526 scopus 로고    scopus 로고
    • Mia40, a novel factor for protein import into the intermembrane space of mitochondria is able to bind metal ions
    • Terziyska N., Lutz T., Kozany C., Mokranjac D., Mesecke N., Neupert W., Herrmann J.M., Hell K. Mia40, a novel factor for protein import into the intermembrane space of mitochondria is able to bind metal ions. FEBS Lett. 2005, 579:179-184.
    • (2005) FEBS Lett. , vol.579 , pp. 179-184
    • Terziyska, N.1    Lutz, T.2    Kozany, C.3    Mokranjac, D.4    Mesecke, N.5    Neupert, W.6    Herrmann, J.M.7    Hell, K.8
  • 282
    • 84859845591 scopus 로고    scopus 로고
    • Giardia-from genome to proteome
    • Thompson R.C., Monis P. Giardia-from genome to proteome. Adv. Parasitol. 2012, 78:57-95.
    • (2012) Adv. Parasitol. , vol.78 , pp. 57-95
    • Thompson, R.C.1    Monis, P.2
  • 283
    • 34347204504 scopus 로고    scopus 로고
    • Generating disulfides in multicellular organisms: emerging roles for a new flavoprotein family
    • Thorpe C., Coppock D.L. Generating disulfides in multicellular organisms: emerging roles for a new flavoprotein family. J. Biol. Chem. 2007, 282:13929-13933.
    • (2007) J. Biol. Chem. , vol.282 , pp. 13929-13933
    • Thorpe, C.1    Coppock, D.L.2
  • 284
    • 70149106811 scopus 로고    scopus 로고
    • Surprising variety in energy metabolism within Trypanosomatidae
    • Tielens A.G., van Hellemond J.J. Surprising variety in energy metabolism within Trypanosomatidae. Trends Parasitol. 2009, 25:482-490.
    • (2009) Trends Parasitol. , vol.25 , pp. 482-490
    • Tielens, A.G.1    van Hellemond, J.J.2
  • 285
    • 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. 2004, 136:199-209.
    • (2004) J. Biochem. , vol.136 , pp. 199-209
    • Tokumoto, U.1    Kitamura, S.2    Fukuyama, K.3    Takahashi, Y.4
  • 286
    • 0034331239 scopus 로고    scopus 로고
    • Distinct iron-sulfur cluster assembly complexes exist in the cytosol and mitochondria of human cells
    • Tong W.H., Rouault T. Distinct iron-sulfur cluster assembly complexes exist in the cytosol and mitochondria of human cells. EMBO J. 2000, 19:5692-5700.
    • (2000) EMBO J. , vol.19 , pp. 5692-5700
    • Tong, W.H.1    Rouault, T.2
  • 287
    • 33644623262 scopus 로고    scopus 로고
    • Functions of mitochondrial ISCU and cytosolic ISCU in mammalian iron-sulfur cluster biogenesis and iron homeostasis
    • Tong W.H., Rouault T.A. Functions of mitochondrial ISCU and cytosolic ISCU in mammalian iron-sulfur cluster biogenesis and iron homeostasis. Cell Metab. 2006, 3:199-210.
    • (2006) Cell Metab. , vol.3 , pp. 199-210
    • Tong, W.H.1    Rouault, T.A.2
  • 288
    • 0041691163 scopus 로고    scopus 로고
    • Subcellular compartmentalization of human Nfu, an iron-sulfur cluster scaffold protein, and its ability to assemble a [4Fe-4S] cluster
    • Tong W.H., Jameson G.N., Huynh B.H., Rouault T.A. Subcellular compartmentalization of human Nfu, an iron-sulfur cluster scaffold protein, and its ability to assemble a [4Fe-4S] cluster. Proc. Natl. Acad. Sci. U.S.A. 2003, 100:9762-9767.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 9762-9767
    • Tong, W.H.1    Jameson, G.N.2    Huynh, B.H.3    Rouault, T.A.4
  • 290
    • 38149112638 scopus 로고    scopus 로고
    • Protein targeting to the malaria parasite plastid
    • Tonkin C.J., Kalanon M., McFadden G.I. Protein targeting to the malaria parasite plastid. Traffic 2008, 9:166-175.
    • (2008) Traffic , vol.9 , pp. 166-175
    • Tonkin, C.J.1    Kalanon, M.2    McFadden, G.I.3
  • 292
    • 0037447049 scopus 로고    scopus 로고
    • Mechanisms of protein import into mitochondria
    • Truscott K.N., Brandner K., Pfanner N. Mechanisms of protein import into mitochondria. Curr. Biol. 2003, 13:R326-R337.
    • (2003) Curr. Biol. , vol.13
    • Truscott, K.N.1    Brandner, K.2    Pfanner, N.3
  • 293
    • 44349083493 scopus 로고    scopus 로고
    • A novel route for ATP acquisition by the remnant mitochondria of Encephalitozoon cuniculi
    • Tsaousis A.D., Kunji E.R., Goldberg A.V., Lucocq J.M., Hirt R.P., Embley T.M. A novel route for ATP acquisition by the remnant mitochondria of Encephalitozoon cuniculi. Nature 2008, 453:553-556.
    • (2008) Nature , vol.453 , pp. 553-556
    • Tsaousis, A.D.1    Kunji, E.R.2    Goldberg, A.V.3    Lucocq, J.M.4    Hirt, R.P.5    Embley, T.M.6
  • 295
    • 0347379904 scopus 로고    scopus 로고
    • Pse1p mediates the nuclear import of the iron-responsive transcription factor Aft1p in Saccharomyces cerevisiae
    • Ueta R., Fukunaka A., Yamaguchi-Iwai Y. Pse1p mediates the nuclear import of the iron-responsive transcription factor Aft1p in Saccharomyces cerevisiae. J. Biol. Chem. 2003, 278:50120-50127.
    • (2003) J. Biol. Chem. , vol.278 , pp. 50120-50127
    • Ueta, R.1    Fukunaka, A.2    Yamaguchi-Iwai, Y.3
  • 296
    • 0035902569 scopus 로고    scopus 로고
    • Biotin synthase contains two distinct iron-sulfur cluster binding sites: chemical and spectroelectrochemical analysis of iron-sulfur cluster interconversions
    • Ugulava N.B., Gibney B.R., Jarrett J.T. Biotin synthase contains two distinct iron-sulfur cluster binding sites: chemical and spectroelectrochemical analysis of iron-sulfur cluster interconversions. Biochemistry 2001, 40:8343-8351.
    • (2001) Biochemistry , vol.40 , pp. 8343-8351
    • Ugulava, N.B.1    Gibney, B.R.2    Jarrett, J.T.3
  • 297
    • 0035138734 scopus 로고    scopus 로고
    • Drug targets and mechanisms of resistance in the anaerobic protozoa
    • Upcroft P., Upcroft J.A. Drug targets and mechanisms of resistance in the anaerobic protozoa. Clin. Microbiol. Rev. 2001, 14:150-164.
    • (2001) Clin. Microbiol. Rev. , vol.14 , pp. 150-164
    • Upcroft, P.1    Upcroft, J.A.2
  • 298
    • 66649099001 scopus 로고    scopus 로고
    • Crucial role of conserved cysteine residues in the assembly of two iron-sulfur clusters on the CIA protein Nar1
    • Urzica E., Pierik A.J., Muhlenhoff U., Lill R. Crucial role of conserved cysteine residues in the assembly of two iron-sulfur clusters on the CIA protein Nar1. Biochemistry 2009, 48:4946-4958.
    • (2009) Biochemistry , vol.48 , pp. 4946-4958
    • Urzica, E.1    Pierik, A.J.2    Muhlenhoff, U.3    Lill, R.4
  • 299
    • 0024402191 scopus 로고
    • Sequences similar to genes for two mitochondrial proteins and portions of ribosomal RNA in tandemly arrayed 6-kilobase-pair DNA of a malarial parasite
    • Vaidya A.B., Akella R., Suplick K. Sequences similar to genes for two mitochondrial proteins and portions of ribosomal RNA in tandemly arrayed 6-kilobase-pair DNA of a malarial parasite. Mol. Biochem. Parasitol. 1989, 35:97-107.
    • (1989) Mol. Biochem. Parasitol. , vol.35 , pp. 97-107
    • Vaidya, A.B.1    Akella, R.2    Suplick, K.3
  • 300
    • 0027435034 scopus 로고
    • Unidirectional dominance of cytoplasmic inheritance in two genetic crosses of Plasmodium falciparum
    • Vaidya A.B., Morrisey J., Plowe C.V., Kaslow D.C., Wellems T.E. Unidirectional dominance of cytoplasmic inheritance in two genetic crosses of Plasmodium falciparum. Mol. Cell. Biol. 1993, 13:7349-7357.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7349-7357
    • Vaidya, A.B.1    Morrisey, J.2    Plowe, C.V.3    Kaslow, D.C.4    Wellems, T.E.5
  • 301
    • 0034603818 scopus 로고    scopus 로고
    • Microsporidia: accumulating evidence that a group of amitochondriate and suspectedly primitive eukaryotes are just curious fungi
    • Van de Peer Y., Ben Ali A., Meyer A. Microsporidia: accumulating evidence that a group of amitochondriate and suspectedly primitive eukaryotes are just curious fungi. Gene 2000, 246:1-8.
    • (2000) Gene , vol.246 , pp. 1-8
    • Van de Peer, Y.1    Ben Ali, A.2    Meyer, A.3
  • 302
    • 2942536494 scopus 로고    scopus 로고
    • The iron-sulfur cluster assembly genes iscS and iscU of Entamoeba histolytica were acquired by horizontal gene transfer
    • Van Der Giezen M., Cox S., Tovar J. The iron-sulfur cluster assembly genes iscS and iscU of Entamoeba histolytica were acquired by horizontal gene transfer. BMC Evol. Biol. 2004, 4:7.
    • (2004) BMC Evol. Biol. , vol.4 , pp. 7
    • Van Der Giezen, M.1    Cox, S.2    Tovar, J.3
  • 303
    • 0037189526 scopus 로고    scopus 로고
    • Processing of an apicoplast leader sequence in Plasmodium falciparum and the identification of a putative leader cleavage enzyme
    • van Dooren G.G., Su V., D'Ombrain M.C., McFadden G.I. Processing of an apicoplast leader sequence in Plasmodium falciparum and the identification of a putative leader cleavage enzyme. J. Biol. Chem. 2002, 277:23612-23619.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23612-23619
    • van Dooren, G.G.1    Su, V.2    D'Ombrain, M.C.3    McFadden, G.I.4
  • 305
    • 33847206046 scopus 로고    scopus 로고
    • Control of Fur synthesis by the non-coding RNA RyhB and iron-responsive decoding
    • Vecerek B., Moll I., Blasi U. Control of Fur synthesis by the non-coding RNA RyhB and iron-responsive decoding. EMBO J. 2007, 26:965-975.
    • (2007) EMBO J. , vol.26 , pp. 965-975
    • Vecerek, B.1    Moll, I.2    Blasi, U.3
  • 306
    • 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. 2007, 42:95-111.
    • (2007) Crit. Rev. Biochem. Mol. Biol. , vol.42 , pp. 95-111
    • Vickery, L.E.1    Cupp-Vickery, J.R.2
  • 307
    • 67149111967 scopus 로고    scopus 로고
    • Iron-sulfur (Fe/S) protein biogenesis: phylogenomic and genetic studies of A-type carriers
    • Vinella D., Brochier-Armanet C., Loiseau L., Talla E., Barras F. Iron-sulfur (Fe/S) protein biogenesis: phylogenomic and genetic studies of A-type carriers. PLoS Genet. 2009, 5:e1000497.
    • (2009) PLoS Genet. , vol.5
    • Vinella, D.1    Brochier-Armanet, C.2    Loiseau, L.3    Talla, E.4    Barras, F.5
  • 308
    • 0036046297 scopus 로고    scopus 로고
    • Iron transport and regulation, cell signalling and genomics: lessons from Escherichia coli and Pseudomonas
    • Visca P., Leoni L., Wilson M.J., Lamont I.L. Iron transport and regulation, cell signalling and genomics: lessons from Escherichia coli and Pseudomonas. Mol. Microbiol. 2002, 45:1177-1190.
    • (2002) Mol. Microbiol. , vol.45 , pp. 1177-1190
    • Visca, P.1    Leoni, L.2    Wilson, M.J.3    Lamont, I.L.4
  • 313
    • 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. 2008, 283:12674-12679.
    • (2008) J. Biol. Chem. , vol.283 , pp. 12674-12679
    • Wang, T.1    Craig, E.A.2
  • 314
    • 44949208513 scopus 로고    scopus 로고
    • DNA triplexes and Friedreich ataxia
    • Wells R.D. DNA triplexes and Friedreich ataxia. FASEB J. 2008, 22:1625-1634.
    • (2008) FASEB J. , vol.22 , pp. 1625-1634
    • Wells, R.D.1
  • 316
    • 27744455707 scopus 로고    scopus 로고
    • Microsporidian mitochondrial proteins: expression in Antonospora locustae spores and identification of genes coding for two further proteins
    • Williams B.A., Keeling P.J. Microsporidian mitochondrial proteins: expression in Antonospora locustae spores and identification of genes coding for two further proteins. J. Eukaryot. Microbiol. 2005, 52:271-276.
    • (2005) J. Eukaryot. Microbiol. , vol.52 , pp. 271-276
    • Williams, B.A.1    Keeling, P.J.2
  • 317
    • 0036307786 scopus 로고    scopus 로고
    • Progress with parasite plastids
    • Wilson R.J. Progress with parasite plastids. J. Mol. Biol. 2002, 319:257-274.
    • (2002) J. Mol. Biol. , vol.319 , pp. 257-274
    • Wilson, R.J.1
  • 320
    • 0038409882 scopus 로고    scopus 로고
    • A dimer of the FeS cluster biosynthesis protein IscA from cyanobacteria binds a [2Fe2S] cluster between two protomers and transfers it to [2Fe2S] and [4Fe4S] apo proteins
    • Wollenberg M., Berndt C., Bill E., Schwenn J.D., Seidler A. A dimer of the FeS cluster biosynthesis protein IscA from cyanobacteria binds a [2Fe2S] cluster between two protomers and transfers it to [2Fe2S] and [4Fe4S] apo proteins. Eur. J. Biochem. 2003, 270:1662-1671.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 1662-1671
    • Wollenberg, M.1    Berndt, C.2    Bill, E.3    Schwenn, J.D.4    Seidler, A.5
  • 322
  • 323
    • 2942659075 scopus 로고    scopus 로고
    • AtNAP7 is a plastidic SufC-like ATP-binding cassette/ATPase essential for Arabidopsis embryogenesis
    • Xu X.M., Moller S.G. AtNAP7 is a plastidic SufC-like ATP-binding cassette/ATPase essential for Arabidopsis embryogenesis. Proc. Natl. Acad. Sci. U.S.A. 2004, 101:9143-9148.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 9143-9148
    • Xu, X.M.1    Moller, S.G.2
  • 324
    • 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 2008, 9:2355-2362.
    • (2008) Chembiochem , vol.9 , pp. 2355-2362
    • Xu, X.M.1    Moller, S.G.2
  • 326
    • 14844295427 scopus 로고    scopus 로고
    • AtNAP1 represents an atypical SufB protein in Arabidopsis plastids
    • Xu X.M., Adams S., Chua N.H., Moller S.G. AtNAP1 represents an atypical SufB protein in Arabidopsis plastids. J. Biol. Chem. 2005, 280:6648-6654.
    • (2005) J. Biol. Chem. , vol.280 , pp. 6648-6654
    • Xu, X.M.1    Adams, S.2    Chua, N.H.3    Moller, S.G.4
  • 327
    • 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., Morimoto K., Kikuchi S., Nishio K., Terashima I., Nakai M. 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 2004, 16:993-1007.
    • (2004) Plant Cell , vol.16 , pp. 993-1007
    • Yabe, T.1    Morimoto, K.2    Kikuchi, S.3    Nishio, K.4    Terashima, I.5    Nakai, M.6
  • 328
    • 79957624384 scopus 로고    scopus 로고
    • CgCYN1, a plasma membrane cystine-specific transporter of Candida glabrata with orthologues prevalent among pathogenic yeast and fungi
    • Yadav A.K., Bachhawat A.K. CgCYN1, a plasma membrane cystine-specific transporter of Candida glabrata with orthologues prevalent among pathogenic yeast and fungi. J. Biol. Chem. 2011, 286:19714-19723.
    • (2011) J. Biol. Chem. , vol.286 , pp. 19714-19723
    • Yadav, A.K.1    Bachhawat, A.K.2
  • 329
    • 0030054971 scopus 로고    scopus 로고
    • Iron-regulated DNA binding by the AFT1 protein controls the iron regulon in yeast
    • Yamaguchi-Iwai Y., Stearman R., Dancis A., Klausner R.D. Iron-regulated DNA binding by the AFT1 protein controls the iron regulon in yeast. EMBO J. 1996, 15:3377-3384.
    • (1996) EMBO J. , vol.15 , pp. 3377-3384
    • Yamaguchi-Iwai, Y.1    Stearman, R.2    Dancis, A.3    Klausner, R.D.4
  • 330
    • 77953669993 scopus 로고    scopus 로고
    • Human iron-sulfur cluster assembly, cellular iron homeostasis, and disease
    • Ye H., Rouault T.A. Human iron-sulfur cluster assembly, cellular iron homeostasis, and disease. Biochemistry 2010, 49:4945-4956.
    • (2010) Biochemistry , vol.49 , pp. 4945-4956
    • Ye, H.1    Rouault, T.A.2
  • 332
    • 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. 2006, 171:285-292.
    • (2006) New Phytol. , vol.171 , pp. 285-292
    • Ye, H.1    Pilon, M.2    Pilon-Smits, E.A.3
  • 333
    • 0029773976 scopus 로고    scopus 로고
    • The role of ligand exchange in the uptake of iron from microbial siderophores by gramineous plants
    • Yehuda Z., Shenker M., Romheld V., Marschner H., Hadar Y., Chen Y. The role of ligand exchange in the uptake of iron from microbial siderophores by gramineous plants. Plant Physiol. 1996, 112:1273-1280.
    • (1996) Plant Physiol. , vol.112 , pp. 1273-1280
    • Yehuda, Z.1    Shenker, M.2    Romheld, V.3    Marschner, H.4    Hadar, Y.5    Chen, Y.6
  • 334
    • 2942744572 scopus 로고    scopus 로고
    • Frataxin-mediated iron delivery to ferrochelatase in the final step of heme biosynthesis
    • Yoon T., Cowan J.A. Frataxin-mediated iron delivery to ferrochelatase in the final step of heme biosynthesis. J. Biol. Chem. 2004, 279:25943-25946.
    • (2004) J. Biol. Chem. , vol.279 , pp. 25943-25946
    • Yoon, T.1    Cowan, J.A.2
  • 335
    • 0030961537 scopus 로고    scopus 로고
    • Strains of Synechocystis sp. PCC 6803 with altered PsaC. I. Mutations incorporated in the cysteine ligands of the two [4Fe-4S] clusters FA and FB of photosystem I
    • Yu J., Vassiliev I.R., Jung Y.S., Golbeck J.H., McIntosh L. Strains of Synechocystis sp. PCC 6803 with altered PsaC. I. Mutations incorporated in the cysteine ligands of the two [4Fe-4S] clusters FA and FB of photosystem I. J. Biol. Chem. 1997, 272:8032-8039.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8032-8039
    • Yu, J.1    Vassiliev, I.R.2    Jung, Y.S.3    Golbeck, J.H.4    McIntosh, L.5
  • 337
    • 21244448393 scopus 로고    scopus 로고
    • Frataxin and mitochondrial carrier proteins, Mrs3p and Mrs4p, cooperate in providing iron for heme synthesis
    • Zhang Y., Lyver E.R., Knight S.A., Lesuisse E., Dancis A. Frataxin and mitochondrial carrier proteins, Mrs3p and Mrs4p, cooperate in providing iron for heme synthesis. J. Biol. Chem. 2005, 280:19794-19807.
    • (2005) J. Biol. Chem. , vol.280 , pp. 19794-19807
    • Zhang, Y.1    Lyver, E.R.2    Knight, S.A.3    Lesuisse, E.4    Dancis, A.5
  • 338
    • 33747330134 scopus 로고    scopus 로고
    • Mrs3p, Mrs4p, and frataxin provide iron for Fe-S cluster synthesis in mitochondria
    • Zhang Y., Lyver E.R., Knight S.A., Pain D., Lesuisse E., Dancis A. Mrs3p, Mrs4p, and frataxin provide iron for Fe-S cluster synthesis in mitochondria. J. Biol. Chem. 2006, 281:22493-22502.
    • (2006) J. Biol. Chem. , vol.281 , pp. 22493-22502
    • Zhang, Y.1    Lyver, E.R.2    Knight, S.A.3    Pain, D.4    Lesuisse, E.5    Dancis, A.6
  • 340
    • 0027450059 scopus 로고
    • Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis
    • 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. U.S.A. 1993, 90:2754-2758.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 2754-2758
    • Zheng, L.1    White, R.H.2    Cash, V.L.3    Jack, R.F.4    Dean, D.R.5
  • 341
    • 0034932337 scopus 로고    scopus 로고
    • DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide
    • Zheng M., Wang X., Templeton L.J., Smulski D.R., LaRossa R.A., Storz G. DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide. J. Bacteriol. 2001, 183:4562-4570.
    • (2001) J. Bacteriol. , vol.183 , pp. 4562-4570
    • Zheng, M.1    Wang, X.2    Templeton, L.J.3    Smulski, D.R.4    LaRossa, R.A.5    Storz, G.6
  • 342
    • 84872077167 scopus 로고    scopus 로고
    • The N-terminal sequences of four major hydrogenosomal proteins are not essential for import into hydrogenosomes of Trichomonas vaginalis
    • Zimorski V., Major P., Hoffmann K., Brás X.P., Martin W.F., Gould S.B. The N-terminal sequences of four major hydrogenosomal proteins are not essential for import into hydrogenosomes of Trichomonas vaginalis. J. Eukaryot. Microbiol. 2013, 60:89-97.
    • (2013) J. Eukaryot. Microbiol. , vol.60 , pp. 89-97
    • Zimorski, V.1    Major, P.2    Hoffmann, K.3    Brás, X.P.4    Martin, W.F.5    Gould, S.B.6


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