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Volumn 9, Issue 9, 2013, Pages

The Suf Iron-Sulfur Cluster Synthesis Pathway Is Required for Apicoplast Maintenance in Malaria Parasites

Author keywords

[No Author keywords available]

Indexed keywords

AZITHROMYCIN; FOSMIDOMYCIN; IRON SULFUR PROTEIN; ISD 11 PROTEIN; ISOPRENOID; PEPTIDES AND PROTEINS; SUFE PROTEIN; SUFS PROTEIN; UNCLASSIFIED DRUG;

EID: 84884678911     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1003655     Document Type: Article
Times cited : (89)

References (71)
  • 1
    • 0034003112 scopus 로고    scopus 로고
    • Iron-sulfur proteins: ancient structures, still full of surprises
    • Beinert H, (2000) Iron-sulfur proteins: ancient structures, still full of surprises. J Biol Inorg Chem 5: 2-15.
    • (2000) J Biol Inorg Chem , vol.5 , pp. 2-15
    • Beinert, H.1
  • 2
    • 33846141121 scopus 로고    scopus 로고
    • Iron-sulfur cluster proteins: electron transfer and beyond
    • Brzoska K, Meczynska S, Kruszewski M, (2006) Iron-sulfur cluster proteins: electron transfer and beyond. Acta Biochim Pol 53: 685-691.
    • (2006) Acta Biochim Pol , vol.53 , pp. 685-691
    • Brzoska, K.1    Meczynska, S.2    Kruszewski, M.3
  • 3
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: nature's modular, multipurpose structures
    • Beinert H, Holm RH, Munck E, (1997) Iron-sulfur clusters: nature's modular, multipurpose structures. Science 277: 653-659.
    • (1997) Science , vol.277 , pp. 653-659
    • Beinert, H.1    Holm, R.H.2    Munck, E.3
  • 4
    • 0026548467 scopus 로고
    • The nifU, nifS and nifV gene products are required for activity of all three nitrogenases of Azotobacter vinelandii
    • Kennedy C, Dean D, (1992) The nifU, nifS and nifV gene products are required for activity of all three nitrogenases of Azotobacter vinelandii. Mol Gen Genet 231: 494-498.
    • (1992) Mol Gen Genet , vol.231 , pp. 494-498
    • Kennedy, C.1    Dean, D.2
  • 5
    • 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, (2000) Biogenesis of iron-sulfur proteins in eukaryotes: a novel task of mitochondria that is inherited from bacteria. Biochim Biophys Acta 1459: 370-382.
    • (2000) Biochim Biophys Acta , vol.1459 , pp. 370-382
    • Muhlenhoff, U.1    Lill, R.2
  • 6
    • 21444455377 scopus 로고    scopus 로고
    • Biogenesis of iron-sulfur proteins in plants
    • Balk J, Lobreaux S, (2005) Biogenesis of iron-sulfur proteins in plants. Trends Plant Sci 10: 324-331.
    • (2005) Trends Plant Sci , vol.10 , pp. 324-331
    • Balk, J.1    Lobreaux, S.2
  • 7
    • 0036853042 scopus 로고    scopus 로고
    • Characterization of a NifS-like chloroplast protein from Arabidopsis. Implications for its role in sulfur and selenium metabolism
    • Pilon-Smits EA, Garifullina GF, Abdel-Ghany S, Kato S, Mihara H, et al. (2002) Characterization of a NifS-like chloroplast protein from Arabidopsis. Implications for its role in sulfur and selenium metabolism. Plant Physiol 130: 1309-1318.
    • (2002) Plant Physiol , vol.130 , pp. 1309-1318
    • Pilon-Smits, E.A.1    Garifullina, G.F.2    Abdel-Ghany, S.3    Kato, S.4    Mihara, H.5
  • 8
    • 0036714247 scopus 로고    scopus 로고
    • The AtNFS2 gene from Arabidopsis thaliana encodes a NifS-like plastidial cysteine desulphurase
    • Leon S, Touraine B, Briat JF, Lobreaux S, (2002) The AtNFS2 gene from Arabidopsis thaliana encodes a NifS-like plastidial cysteine desulphurase. Biochem J 366: 557-564.
    • (2002) Biochem J , vol.366 , pp. 557-564
    • Leon, S.1    Touraine, B.2    Briat, J.F.3    Lobreaux, S.4
  • 10
    • 30444433568 scopus 로고    scopus 로고
    • The Nfs1 interacting protein Isd11 has an essential role in Fe/S cluster biogenesis in mitochondria
    • Adam AC, Bornhovd C, Prokisch H, Neupert W, Hell K, (2006) The Nfs1 interacting protein Isd11 has an essential role in Fe/S cluster biogenesis in mitochondria. EMBO J 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
  • 11
    • 30444449009 scopus 로고    scopus 로고
    • Essential role of Isd11 in mitochondrial iron-sulfur cluster synthesis on Isu scaffold proteins
    • Wiedemann N, Urzica E, Guiard B, Muller H, Lohaus C, et al. (2006) Essential role of Isd11 in mitochondrial iron-sulfur cluster synthesis on Isu scaffold proteins. EMBO J 25: 184-195.
    • (2006) EMBO J , vol.25 , pp. 184-195
    • Wiedemann, N.1    Urzica, E.2    Guiard, B.3    Muller, H.4    Lohaus, C.5
  • 12
    • 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 MA, Zikova A, Stuart KD, et al. (2010) The Fe/S cluster assembly protein Isd11 is essential for tRNA thiolation in Trypanosoma brucei. J Biol Chem 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
  • 13
    • 33745618402 scopus 로고    scopus 로고
    • Evolution of the Isd11-IscS complex reveals a single alpha-proteobacterial endosymbiosis for all eukaryotes
    • Richards TA, van der Giezen M, (2006) Evolution of the Isd11-IscS complex reveals a single alpha-proteobacterial endosymbiosis for all eukaryotes. Mol Biol Evol 23: 1341-1344.
    • (2006) Mol Biol Evol , vol.23 , pp. 1341-1344
    • Richards, T.A.1    van der Giezen, M.2
  • 14
    • 80055094199 scopus 로고    scopus 로고
    • Isd11p protein activates the mitochondrial cysteine desulfurase Nfs1p protein
    • Pandey A, Yoon H, Lyver ER, Dancis A, Pain D, (2011) Isd11p protein activates the mitochondrial cysteine desulfurase Nfs1p protein. J Biol Chem 286: 38242-38252.
    • (2011) J Biol Chem , vol.286 , pp. 38242-38252
    • Pandey, A.1    Yoon, H.2    Lyver, E.R.3    Dancis, A.4    Pain, D.5
  • 16
    • 0242664733 scopus 로고    scopus 로고
    • The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli
    • Outten FW, Wood MJ, Munoz FM, Storz G, (2003) The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli. J Biol Chem 278: 45713-45719.
    • (2003) J Biol Chem , vol.278 , pp. 45713-45719
    • Outten, F.W.1    Wood, M.J.2    Munoz, F.M.3    Storz, G.4
  • 17
    • 0141532194 scopus 로고    scopus 로고
    • Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form a new type of cysteine desulfurase
    • Loiseau L, Ollagnier-de-Choudens S, Nachin L, Fontecave M, Barras F, (2003) Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form a new type of cysteine desulfurase. J Biol Chem 278: 38352-38359.
    • (2003) J Biol Chem , vol.278 , pp. 38352-38359
    • Loiseau, L.1    Ollagnier-de-Choudens, S.2    Nachin, L.3    Fontecave, M.4    Barras, F.5
  • 18
    • 33644511398 scopus 로고    scopus 로고
    • AtSufE is an essential activator of plastidic and mitochondrial desulfurases in Arabidopsis
    • Xu XM, Moller SG, (2006) AtSufE is an essential activator of plastidic and mitochondrial desulfurases in Arabidopsis. EMBO J 25: 900-909.
    • (2006) EMBO J , vol.25 , pp. 900-909
    • Xu, X.M.1    Moller, S.G.2
  • 19
    • 0035103466 scopus 로고    scopus 로고
    • Nuclear-encoded, plastid-targeted genes suggest a single common origin for apicomplexan and dinoflagellate plastids
    • Fast NM, Kissinger JC, Roos DS, Keeling PJ, (2001) Nuclear-encoded, plastid-targeted genes suggest a single common origin for apicomplexan and dinoflagellate plastids. Mol Biol Evol 18: 418-426.
    • (2001) Mol Biol Evol , vol.18 , pp. 418-426
    • Fast, N.M.1    Kissinger, J.C.2    Roos, D.S.3    Keeling, P.J.4
  • 20
    • 2342520626 scopus 로고    scopus 로고
    • Tropical infectious diseases: metabolic maps and functions of the Plasmodium falciparum apicoplast
    • Ralph SA, van Dooren GG, Waller RF, Crawford MJ, Fraunholz MJ, et al. (2004) Tropical infectious diseases: metabolic maps and functions of the Plasmodium falciparum apicoplast. Nat Rev Microbiol 2: 203-216.
    • (2004) Nat Rev Microbiol , vol.2 , pp. 203-216
    • Ralph, S.A.1    van Dooren, G.G.2    Waller, R.F.3    Crawford, M.J.4    Fraunholz, M.J.5
  • 21
    • 4644229658 scopus 로고    scopus 로고
    • Escherichia coli lipoyl synthase binds two distinct [4Fe-4S] clusters per polypeptide
    • Cicchillo RM, Lee KH, Baleanu-Gogonea C, Nesbitt NM, Krebs C, et al. (2004) Escherichia coli lipoyl synthase binds two distinct [4Fe-4S] clusters per polypeptide. Biochemistry 43: 11770-11781.
    • (2004) Biochemistry , vol.43 , pp. 11770-11781
    • Cicchillo, R.M.1    Lee, K.H.2    Baleanu-Gogonea, C.3    Nesbitt, N.M.4    Krebs, C.5
  • 22
    • 78549278373 scopus 로고    scopus 로고
    • Biosynthesis of isoprenoids: crystal structure of the [4Fe-4S] cluster protein IspG
    • Lee M, Grawert T, Quitterer F, Rohdich F, Eppinger J, et al. (2010) Biosynthesis of isoprenoids: crystal structure of the [4Fe-4S] cluster protein IspG. J Mol Biol 404: 600-610.
    • (2010) J Mol Biol , vol.404 , pp. 600-610
    • Lee, M.1    Grawert, T.2    Quitterer, F.3    Rohdich, F.4    Eppinger, J.5
  • 23
    • 67749088357 scopus 로고    scopus 로고
    • Structure of (E)-4-hydroxy-3-methyl-but-2-enyl diphosphate reductase, the terminal enzyme of the non-mevalonate pathway
    • Rekittke I, Wiesner J, Rohrich R, Demmer U, Warkentin E, et al. (2008) Structure of (E)-4-hydroxy-3-methyl-but-2-enyl diphosphate reductase, the terminal enzyme of the non-mevalonate pathway. J Am Chem Soc 130: 17206-17207.
    • (2008) J Am Chem Soc , vol.130 , pp. 17206-17207
    • Rekittke, I.1    Wiesner, J.2    Rohrich, R.3    Demmer, U.4    Warkentin, E.5
  • 24
    • 27744598796 scopus 로고    scopus 로고
    • Biosynthesis of isoprenoids. purification and properties of IspG protein from Escherichia coli
    • Zepeck F, Grawert T, Kaiser J, Schramek N, Eisenreich W, et al. (2005) Biosynthesis of isoprenoids. purification and properties of IspG protein from Escherichia coli. J Org Chem 70: 9168-9174.
    • (2005) J Org Chem , vol.70 , pp. 9168-9174
    • Zepeck, F.1    Grawert, T.2    Kaiser, J.3    Schramek, N.4    Eisenreich, W.5
  • 25
    • 0037134469 scopus 로고    scopus 로고
    • Enzymatic modification of tRNAs: MiaB is an iron-sulfur protein
    • Pierrel F, Bjork GR, Fontecave M, Atta M, (2002) Enzymatic modification of tRNAs: MiaB is an iron-sulfur protein. J Biol Chem 277: 13367-13370.
    • (2002) J Biol Chem , vol.277 , pp. 13367-13370
    • Pierrel, F.1    Bjork, G.R.2    Fontecave, M.3    Atta, M.4
  • 26
    • 34248665846 scopus 로고    scopus 로고
    • Cloning and characterization of ferredoxin and ferredoxin-NADP+ reductase from human malaria parasite
    • Kimata-Ariga Y, Kurisu G, Kusunoki M, Aoki S, Sato D, et al. (2007) Cloning and characterization of ferredoxin and ferredoxin-NADP+ reductase from human malaria parasite. J Biochem 141: 421-428.
    • (2007) J Biochem , vol.141 , pp. 421-428
    • Kimata-Ariga, Y.1    Kurisu, G.2    Kusunoki, M.3    Aoki, S.4    Sato, D.5
  • 27
    • 27744542867 scopus 로고    scopus 로고
    • Reconstitution of an apicoplast-localised electron transfer pathway involved in the isoprenoid biosynthesis of Plasmodium falciparum
    • Rohrich RC, Englert N, Troschke K, Reichenberg A, Hintz M, et al. (2005) Reconstitution of an apicoplast-localised electron transfer pathway involved in the isoprenoid biosynthesis of Plasmodium falciparum. FEBS Lett 579: 6433-6438.
    • (2005) FEBS Lett , vol.579 , pp. 6433-6438
    • Rohrich, R.C.1    Englert, N.2    Troschke, K.3    Reichenberg, A.4    Hintz, M.5
  • 28
    • 80052308799 scopus 로고    scopus 로고
    • Chemical rescue of malaria parasites lacking an apicoplast defines organelle function in blood-stage Plasmodium falciparum
    • Yeh E, DeRisi JL, (2011) Chemical rescue of malaria parasites lacking an apicoplast defines organelle function in blood-stage Plasmodium falciparum. PLoS Biol 9: e1001138.
    • (2011) PLoS Biol , vol.9
    • Yeh, E.1    DeRisi, J.L.2
  • 29
    • 0033520336 scopus 로고    scopus 로고
    • Inhibitors of the nonmevalonate pathway of isoprenoid biosynthesis as antimalarial drugs
    • Jomaa H, Wiesner J, Sanderbrand S, Altincicek B, Weidemeyer C, et al. (1999) Inhibitors of the nonmevalonate pathway of isoprenoid biosynthesis as antimalarial drugs. Science 285: 1573-1576.
    • (1999) Science , vol.285 , pp. 1573-1576
    • Jomaa, H.1    Wiesner, J.2    Sanderbrand, S.3    Altincicek, B.4    Weidemeyer, C.5
  • 30
    • 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, et al. (2011) 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 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
  • 31
    • 13444301270 scopus 로고    scopus 로고
    • Parasite plastids: approaching the endgame
    • Wilson RJ, (2005) Parasite plastids: approaching the endgame. Biol Rev Camb Philos Soc 80: 129-153.
    • (2005) Biol Rev Camb Philos Soc , vol.80 , pp. 129-153
    • Wilson, R.J.1
  • 32
    • 0036710572 scopus 로고    scopus 로고
    • Biogenesis of iron-sulphur clusters in amitochondriate and apicomplexan protists
    • Seeber F, (2002) Biogenesis of iron-sulphur clusters in amitochondriate and apicomplexan protists. Int J Parasitol 32: 1207-1217.
    • (2002) Int J Parasitol , vol.32 , pp. 1207-1217
    • Seeber, F.1
  • 35
    • 2442567822 scopus 로고    scopus 로고
    • A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli
    • Outten FW, Djaman O, Storz G, (2004) A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli. Mol Microbiol 52: 861-872.
    • (2004) Mol Microbiol , vol.52 , pp. 861-872
    • Outten, F.W.1    Djaman, O.2    Storz, G.3
  • 36
    • 77955907263 scopus 로고    scopus 로고
    • Metabolic pathways in the apicoplast of apicomplexa
    • Seeber F, Soldati-Favre D, (2010) Metabolic pathways in the apicoplast of apicomplexa. Int Rev Cell Mol Biol 281: 161-228.
    • (2010) Int Rev Cell Mol Biol , vol.281 , pp. 161-228
    • Seeber, F.1    Soldati-Favre, D.2
  • 37
    • 33845968856 scopus 로고    scopus 로고
    • Mitochondrial drug targets in apicomplexan parasites
    • Mather MW, Henry KW, Vaidya AB, (2007) Mitochondrial drug targets in apicomplexan parasites. Curr Drug Targets 8: 49-60.
    • (2007) Curr Drug Targets , vol.8 , pp. 49-60
    • Mather, M.W.1    Henry, K.W.2    Vaidya, A.B.3
  • 38
    • 0035666657 scopus 로고    scopus 로고
    • Deciphering apicoplast targeting signals-feature extraction from nuclear-encoded precursors of Plasmodium falciparum apicoplast proteins
    • Zuegge J, Ralph S, Schmuker M, McFadden GI, Schneider G, (2001) Deciphering apicoplast targeting signals-feature extraction from nuclear-encoded precursors of Plasmodium falciparum apicoplast proteins. Gene 280: 19-26.
    • (2001) Gene , vol.280 , pp. 19-26
    • Zuegge, J.1    Ralph, S.2    Schmuker, M.3    McFadden, G.I.4    Schneider, G.5
  • 39
    • 0037474121 scopus 로고    scopus 로고
    • Dissecting apicoplast targeting in the malaria parasite Plasmodium falciparum
    • Foth BJ, Ralph SA, Tonkin CJ, Struck NS, Fraunholz M, et al. (2003) Dissecting apicoplast targeting in the malaria parasite Plasmodium falciparum. Science 299: 705-708.
    • (2003) Science , vol.299 , pp. 705-708
    • Foth, B.J.1    Ralph, S.A.2    Tonkin, C.J.3    Struck, N.S.4    Fraunholz, M.5
  • 41
    • 0035896587 scopus 로고    scopus 로고
    • Nuclear localization of yeast Nfs1p is required for cell survival
    • Nakai Y, Nakai M, Hayashi H, Kagamiyama H, (2001) Nuclear localization of yeast Nfs1p is required for cell survival. J Biol Chem 276: 8314-8320.
    • (2001) J Biol Chem , vol.276 , pp. 8314-8320
    • Nakai, Y.1    Nakai, M.2    Hayashi, H.3    Kagamiyama, H.4
  • 42
    • 33746425864 scopus 로고    scopus 로고
    • Efficient site-specific integration in Plasmodium falciparum chromosomes mediated by mycobacteriophage Bxb1 integrase
    • Nkrumah LJ, Muhle RA, Moura PA, Ghosh P, Hatfull GF, et al. (2006) Efficient site-specific integration in Plasmodium falciparum chromosomes mediated by mycobacteriophage Bxb1 integrase. Nat Methods 3: 615-621.
    • (2006) Nat Methods , vol.3 , pp. 615-621
    • Nkrumah, L.J.1    Muhle, R.A.2    Moura, P.A.3    Ghosh, P.4    Hatfull, G.F.5
  • 43
    • 77953022741 scopus 로고    scopus 로고
    • Validation of a modified method for Bxb1 mycobacteriophage integrase-mediated recombination in Plasmodium falciparum by localization of the H-protein of the glycine cleavage complex to the mitochondrion
    • Spalding MD, Allary M, Gallagher JR, Prigge ST, (2010) Validation of a modified method for Bxb1 mycobacteriophage integrase-mediated recombination in Plasmodium falciparum by localization of the H-protein of the glycine cleavage complex to the mitochondrion. Mol Biochem Parasitol 172: 156-160.
    • (2010) Mol Biochem Parasitol , vol.172 , pp. 156-160
    • Spalding, M.D.1    Allary, M.2    Gallagher, J.R.3    Prigge, S.T.4
  • 44
    • 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 GG, Su V, D'Ombrain MC, McFadden GI, (2002) Processing of an apicoplast leader sequence in Plasmodium falciparum and the identification of a putative leader cleavage enzyme. J Biol Chem 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
  • 45
    • 82355181574 scopus 로고    scopus 로고
    • ATP synthase complex of Plasmodium falciparum: dimeric assembly in mitochondrial membranes and resistance to genetic disruption
    • Balabaskaran Nina P, Morrisey JM, Ganesan SM, Ke H, Pershing AM, et al. (2011) ATP synthase complex of Plasmodium falciparum: dimeric assembly in mitochondrial membranes and resistance to genetic disruption. J Biol Chem 286: 41312-41322.
    • (2011) J Biol Chem , vol.286 , pp. 41312-41322
    • Balabaskaran Nina, P.1    Morrisey, J.M.2    Ganesan, S.M.3    Ke, H.4    Pershing, A.M.5
  • 46
    • 78049288246 scopus 로고    scopus 로고
    • SufD and SufC ATPase activity are required for iron acquisition during in vivo Fe-S cluster formation on SufB
    • Saini A, Mapolelo DT, Chahal HK, Johnson MK, Outten FW, (2010) SufD and SufC ATPase activity are required for iron acquisition during in vivo Fe-S cluster formation on SufB. Biochemistry 49: 9402-9412.
    • (2010) Biochemistry , vol.49 , pp. 9402-9412
    • Saini, A.1    Mapolelo, D.T.2    Chahal, H.K.3    Johnson, M.K.4    Outten, F.W.5
  • 47
    • 34948847580 scopus 로고    scopus 로고
    • Multiple antibiotics exert delayed effects against the Plasmodium falciparum apicoplast
    • Dahl EL, Rosenthal PJ, (2007) Multiple antibiotics exert delayed effects against the Plasmodium falciparum apicoplast. Antimicrob Agents Chemother 51: 3485-3490.
    • (2007) Antimicrob Agents Chemother , vol.51 , pp. 3485-3490
    • Dahl, E.L.1    Rosenthal, P.J.2
  • 48
    • 59849125892 scopus 로고    scopus 로고
    • Type II fatty acid synthesis is essential only for malaria parasite late liver stage development
    • Vaughan AM, O'Neill MT, Tarun AS, Camargo N, Phuong TM, et al. (2009) Type II fatty acid synthesis is essential only for malaria parasite late liver stage development. Cell Microbiol 11: 506-520.
    • (2009) Cell Microbiol , vol.11 , pp. 506-520
    • Vaughan, A.M.1    O'Neill, M.T.2    Tarun, A.S.3    Camargo, N.4    Phuong, T.M.5
  • 49
    • 57049187017 scopus 로고    scopus 로고
    • The fatty acid biosynthesis enzyme FabI plays a key role in the development of liver-stage malarial parasites
    • Yu M, Kumar TR, Nkrumah LJ, Coppi A, Retzlaff S, et al. (2008) The fatty acid biosynthesis enzyme FabI plays a key role in the development of liver-stage malarial parasites. Cell Host Microbe 4: 567-578.
    • (2008) Cell Host Microbe , vol.4 , pp. 567-578
    • Yu, M.1    Kumar, T.R.2    Nkrumah, L.J.3    Coppi, A.4    Retzlaff, S.5
  • 50
    • 0037417775 scopus 로고    scopus 로고
    • The initiating steps of a type II fatty acid synthase in Plasmodium falciparum are catalyzed by pfACP, pfMCAT, and pfKASIII
    • Prigge ST, He X, Gerena L, Waters NC, Reynolds KA, (2003) The initiating steps of a type II fatty acid synthase in Plasmodium falciparum are catalyzed by pfACP, pfMCAT, and pfKASIII. Biochemistry 42: 1160-1169.
    • (2003) Biochemistry , vol.42 , pp. 1160-1169
    • Prigge, S.T.1    He, X.2    Gerena, L.3    Waters, N.C.4    Reynolds, K.A.5
  • 51
    • 12344312032 scopus 로고    scopus 로고
    • The malaria parasite Plasmodium falciparum has only one pyruvate dehydrogenase complex, which is located in the apicoplast
    • Foth BJ, Stimmler LM, Handman E, Crabb BS, Hodder AN, et al. (2005) The malaria parasite Plasmodium falciparum has only one pyruvate dehydrogenase complex, which is located in the apicoplast. Mol Microbiol 55: 39-53.
    • (2005) Mol Microbiol , vol.55 , pp. 39-53
    • Foth, B.J.1    Stimmler, L.M.2    Handman, E.3    Crabb, B.S.4    Hodder, A.N.5
  • 52
    • 76449090046 scopus 로고    scopus 로고
    • Plasmodium pyruvate dehydrogenase activity is only essential for the parasite's progression from liver infection to blood infection
    • Pei Y, Tarun AS, Vaughan AM, Herman RW, Soliman JM, et al. (2010) Plasmodium pyruvate dehydrogenase activity is only essential for the parasite's progression from liver infection to blood infection. Mol Microbiol 75: 957-971.
    • (2010) Mol Microbiol , vol.75 , pp. 957-971
    • Pei, Y.1    Tarun, A.S.2    Vaughan, A.M.3    Herman, R.W.4    Soliman, J.M.5
  • 53
    • 33846965950 scopus 로고    scopus 로고
    • Scavenging of the cofactor lipoate is essential for the survival of the malaria parasite Plasmodium falciparum
    • Allary M, Lu JZ, Zhu L, Prigge ST, (2007) Scavenging of the cofactor lipoate is essential for the survival of the malaria parasite Plasmodium falciparum. Mol Microbiol 63: 1331-1344.
    • (2007) Mol Microbiol , vol.63 , pp. 1331-1344
    • Allary, M.1    Lu, J.Z.2    Zhu, L.3    Prigge, S.T.4
  • 54
    • 14844317304 scopus 로고    scopus 로고
    • Mechanistic investigations of lipoic acid biosynthesis in Escherichia coli: both sulfur atoms in lipoic acid are contributed by the same lipoyl synthase polypeptide
    • Cicchillo RM, Booker SJ, (2005) Mechanistic investigations of lipoic acid biosynthesis in Escherichia coli: both sulfur atoms in lipoic acid are contributed by the same lipoyl synthase polypeptide. J Am Chem Soc 127: 2860-2861.
    • (2005) J Am Chem Soc , vol.127 , pp. 2860-2861
    • Cicchillo, R.M.1    Booker, S.J.2
  • 56
    • 80255134483 scopus 로고    scopus 로고
    • The apicoplast
    • McFadden GI, (2011) The apicoplast. Protoplasma 248: 641-650.
    • (2011) Protoplasma , vol.248 , pp. 641-650
    • McFadden, G.I.1
  • 57
    • 77949903316 scopus 로고    scopus 로고
    • Plasmodium falciparum acyl carrier protein crystal structures in disulfide-linked and reduced states and their prevalence during blood stage growth
    • Gallagher JR, Prigge ST, (2010) Plasmodium falciparum acyl carrier protein crystal structures in disulfide-linked and reduced states and their prevalence during blood stage growth. Proteins 78: 575-588.
    • (2010) Proteins , vol.78 , pp. 575-588
    • Gallagher, J.R.1    Prigge, S.T.2
  • 58
    • 84876838869 scopus 로고    scopus 로고
    • Parasites FeS up: iron-sulfur cluster biogenesis in eukaryotic pathogens
    • Dellibovi-Ragheb TA, Gisselberg JE, Prigge ST, (2013) Parasites FeS up: iron-sulfur cluster biogenesis in eukaryotic pathogens. PLoS Pathog 9: e1003227.
    • (2013) PLoS Pathog , vol.9
    • Dellibovi-Ragheb, T.A.1    Gisselberg, J.E.2    Prigge, S.T.3
  • 60
    • 22844435982 scopus 로고    scopus 로고
    • Uncovering the molecular mode of action of the antimalarial drug atovaquone using a bacterial system
    • Mather MW, Darrouzet E, Valkova-Valchanova M, Cooley JW, McIntosh MT, et al. (2005) Uncovering the molecular mode of action of the antimalarial drug atovaquone using a bacterial system. J Biol Chem 280: 27458-27465.
    • (2005) J Biol Chem , vol.280 , pp. 27458-27465
    • Mather, M.W.1    Darrouzet, E.2    Valkova-Valchanova, M.3    Cooley, J.W.4    McIntosh, M.T.5
  • 61
    • 80053194776 scopus 로고    scopus 로고
    • Plasticity and diversity of tRNA anticodon determinants of substrate recognition by eukaryotic A37 isopentenyltransferases
    • Lamichhane TN, Blewett NH, Maraia RJ, (2011) Plasticity and diversity of tRNA anticodon determinants of substrate recognition by eukaryotic A37 isopentenyltransferases. Rna-a Publication of the Rna Society 17: 1846-1857.
    • (2011) Rna-a Publication of the Rna Society , vol.17 , pp. 1846-1857
    • Lamichhane, T.N.1    Blewett, N.H.2    Maraia, R.J.3
  • 62
    • 0028609454 scopus 로고
    • Synthesis and Function of Isopentenyl Adenosine Derivatives in Transfer-Rna
    • Persson BC, Esberg B, Olafsson O, Bjork GR, (1994) Synthesis and Function of Isopentenyl Adenosine Derivatives in Transfer-Rna. Biochimie 76: 1152-1160.
    • (1994) Biochimie , vol.76 , pp. 1152-1160
    • Persson, B.C.1    Esberg, B.2    Olafsson, O.3    Bjork, G.R.4
  • 63
    • 0032725978 scopus 로고    scopus 로고
    • Identification of the miaB gene, involved in methylthiolation of isopentenylated A37 derivatives in the tRNA of Salmonella typhimurium and Escherichia coli
    • Esberg B, Leung HCE, Tsui HCT, Bjork GR, Winkler ME, (1999) Identification of the miaB gene, involved in methylthiolation of isopentenylated A37 derivatives in the tRNA of Salmonella typhimurium and Escherichia coli. Journal of Bacteriology 181: 7256-7265.
    • (1999) Journal of Bacteriology , vol.181 , pp. 7256-7265
    • Esberg, B.1    Leung, H.C.E.2    Tsui, H.C.T.3    Bjork, G.R.4    Winkler, M.E.5
  • 64
    • 34247631048 scopus 로고    scopus 로고
    • MiaB, a bifunctional radical-S-adenosylmethionine enzyme involved in the thiolation and methylation of tRNA, contains two essential [4Fe-4S] clusters
    • Hernandez HL, Pierrel F, Elleingand E, Garcia-Serres R, Huynh BH, et al. (2007) MiaB, a bifunctional radical-S-adenosylmethionine enzyme involved in the thiolation and methylation of tRNA, contains two essential [4Fe-4S] clusters. Biochemistry 46: 5140-5147.
    • (2007) Biochemistry , vol.46 , pp. 5140-5147
    • Hernandez, H.L.1    Pierrel, F.2    Elleingand, E.3    Garcia-Serres, R.4    Huynh, B.H.5
  • 65
    • 23844532238 scopus 로고    scopus 로고
    • The plant-type ferredoxin-NADP(+) reductase/ferrodoxin redox system as a possible drug target against apicomplexan human parasites
    • Seeber F, Aliverti A, Zanetti G, (2005) The plant-type ferredoxin-NADP(+) reductase/ferrodoxin redox system as a possible drug target against apicomplexan human parasites. Current Pharmaceutical Design 11: 3159-3172.
    • (2005) Current Pharmaceutical Design , vol.11 , pp. 3159-3172
    • Seeber, F.1    Aliverti, A.2    Zanetti, G.3
  • 66
    • 0035937117 scopus 로고    scopus 로고
    • Apicomplexan parasites possess distinct nuclear-encoded, but apicoplast-localized, plant-type ferredoxin-NADP(+) reductase and ferredoxin
    • Vollmer M, Thomsen N, Wiek S, Seeber F, (2001) Apicomplexan parasites possess distinct nuclear-encoded, but apicoplast-localized, plant-type ferredoxin-NADP(+) reductase and ferredoxin. Journal of Biological Chemistry 276: 5483-5490.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 5483-5490
    • Vollmer, M.1    Thomsen, N.2    Wiek, S.3    Seeber, F.4
  • 67
    • 0036175587 scopus 로고    scopus 로고
    • The flavoenzyme ferredoxin (flavodoxin)-NADP(H) reductase modulates NADP(H) homeostasis during the soxRS response of Escherichia coli
    • Krapp AR, Rodriguez RE, Poli HO, Paladini DH, Palatnik JF, et al. (2002) The flavoenzyme ferredoxin (flavodoxin)-NADP(H) reductase modulates NADP(H) homeostasis during the soxRS response of Escherichia coli. Journal of Bacteriology 184: 1474-1480.
    • (2002) Journal of Bacteriology , vol.184 , pp. 1474-1480
    • Krapp, A.R.1    Rodriguez, R.E.2    Poli, H.O.3    Paladini, D.H.4    Palatnik, J.F.5
  • 68
    • 80051672532 scopus 로고    scopus 로고
    • Plasmodium falciparum apicoplast transit peptides are unstructured in vitro and during apicoplast import
    • Gallagher JR, Matthews KA, Prigge ST, (2011) Plasmodium falciparum apicoplast transit peptides are unstructured in vitro and during apicoplast import. Traffic 12: 1124-1138.
    • (2011) Traffic , vol.12 , pp. 1124-1138
    • Gallagher, J.R.1    Matthews, K.A.2    Prigge, S.T.3
  • 69
    • 0030769750 scopus 로고    scopus 로고
    • Continuous culture of Plasmodium falciparum: its impact on malaria research
    • Trager W, Jensen JB, (1997) Continuous culture of Plasmodium falciparum: its impact on malaria research. Int J Parasitol 27: 989-1006.
    • (1997) Int J Parasitol , vol.27 , pp. 989-1006
    • Trager, W.1    Jensen, J.B.2
  • 70
    • 77957659562 scopus 로고    scopus 로고
    • Overexpression of biotin synthase and biotin ligase is required for efficient generation of sulfur-35 labeled biotin in E. coli
    • Delli-Bovi TA, Spalding MD, Prigge ST, (2010) Overexpression of biotin synthase and biotin ligase is required for efficient generation of sulfur-35 labeled biotin in E. coli. BMC Biotechnol 10: 73.
    • (2010) BMC Biotechnol , vol.10 , pp. 73
    • Delli-Bovi, T.A.1    Spalding, M.D.2    Prigge, S.T.3


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