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Volumn 6, Issue , 2006, Pages

The crystal structure of superoxide dismutase from Plasmodium falciparum

Author keywords

[No Author keywords available]

Indexed keywords

REACTIVE OXYGEN METABOLITE; SUPEROXIDE DISMUTASE;

EID: 33750335646     PISSN: 14726807     EISSN: 14726807     Source Type: Journal    
DOI: 10.1186/1472-6807-6-20     Document Type: Article
Times cited : (28)

References (40)
  • 2
    • 0020552880 scopus 로고
    • Malaria parasites adopt host cell superoxide dismutase
    • Fairfield AS, Meshnick SR, Eaton JW: Malaria parasites adopt host cell superoxide dismutase. Science 1983, 221(4612):764-766.
    • (1983) Science , vol.221 , Issue.4612 , pp. 764-766
    • Fairfield, A.S.1    Meshnick, S.R.2    Eaton, J.W.3
  • 4
    • 1542375903 scopus 로고    scopus 로고
    • Dual-function stem molecular beacons to assess mRNA expression in AT-rich transcripts of Plasmodium falciparum
    • 494
    • Bustamante LY, Crooke A, Martinez J, Diez A, Bautista JM: Dual-function stem molecular beacons to assess mRNA expression in AT-rich transcripts of Plasmodium falciparum. Biotechniques 2004, 36(3):488-92, 494.
    • (2004) Biotechniques , vol.36 , Issue.3 , pp. 488-492
    • Bustamante, L.Y.1    Crooke, A.2    Martinez, J.3    Diez, A.4    Bautista, J.M.5
  • 5
    • 0021126946 scopus 로고
    • Manganese and iron superoxide dismutases are structural homologs
    • Stallings WC, Pattridge KA, Strong RK, Ludwig ML: Manganese and iron superoxide dismutases are structural homologs. J Biol Chem 1984, 259(17):10695-10699.
    • (1984) J Biol Chem , vol.259 , Issue.17 , pp. 10695-10699
    • Stallings, W.C.1    Pattridge, K.A.2    Strong, R.K.3    Ludwig, M.L.4
  • 6
    • 0020374498 scopus 로고
    • Determination and analysis of the 2 A-structure of copper, zinc superoxide dismutase
    • Tainer JA, Getzoff ED, Beem KM, Richardson JS, Richardson DC: Determination and analysis of the 2 A-structure of copper, zinc superoxide dismutase. J Mol Biol 1982, 160(2):181-217.
    • (1982) J Mol Biol , vol.160 , Issue.2 , pp. 181-217
    • Tainer, J.A.1    Getzoff, E.D.2    Beem, K.M.3    Richardson, J.S.4    Richardson, D.C.5
  • 7
    • 0023945399 scopus 로고
    • Iron- and manganese-containing superoxide dismutases can be distinguished by analysis of their primary structures
    • Parker MW, Blake CC: Iron- and manganese-containing superoxide dismutases can be distinguished by analysis of their primary structures. FEBS Lett 1988, 229(2):377-382.
    • (1988) FEBS Lett , vol.229 , Issue.2 , pp. 377-382
    • Parker, M.W.1    Blake, C.C.2
  • 8
    • 0017849697 scopus 로고
    • Inhibition of superoxide dismutases by azide
    • Misra HP, Fridovich I: Inhibition of superoxide dismutases by azide. Arch Biochem Biophys 1978, 189(2):317-322.
    • (1978) Arch Biochem Biophys , vol.189 , Issue.2 , pp. 317-322
    • Misra, H.P.1    Fridovich, I.2
  • 9
    • 0033920250 scopus 로고    scopus 로고
    • Crystal structure of cambialistic superoxide dismutase from porphyromonas gingivalis
    • Sugio S, Hiraoka BY, Yamakura F: Crystal structure of cambialistic superoxide dismutase from porphyromonas gingivalis. Eur J Biochem 2000, 267(12):3487-3495.
    • (2000) Eur J Biochem , vol.267 , Issue.12 , pp. 3487-3495
    • Sugio, S.1    Hiraoka, B.Y.2    Yamakura, F.3
  • 11
    • 0022359667 scopus 로고
    • Trypanosomatid iron-superoxide dismutase inhibitors. Selectivity and mechanism of N1,N6-bis(2,3-dihydroxybenzoyl)-1,6-diaminohexane
    • Meshnick SR, Kitchener KR, Trang NL: Trypanosomatid iron-superoxide dismutase inhibitors. Selectivity and mechanism of N1,N6-bis(2,3- dihydroxybenzoyl)-1,6-diaminohexane. Biochem Pharmacol 1985, 34(17):3147-3152.
    • (1985) Biochem Pharmacol , vol.34 , Issue.17 , pp. 3147-3152
    • Meshnick, S.R.1    Kitchener, K.R.2    Trang, N.L.3
  • 13
    • 13244252222 scopus 로고    scopus 로고
    • The crystal structure of an eukaryotic iron superoxide dismutase suggests intersubunit cooperation during catalysis
    • Munoz IG, Moran JF, Becana M, Montoya G: The crystal structure of an eukaryotic iron superoxide dismutase suggests intersubunit cooperation during catalysis. Protein Sci 2005, 14(2):387-394.
    • (2005) Protein Sci , vol.14 , Issue.2 , pp. 387-394
    • Munoz, I.G.1    Moran, J.F.2    Becana, M.3    Montoya, G.4
  • 15
    • 0035662341 scopus 로고    scopus 로고
    • Comparative genomics in Plasmodium: A tool for the identification of genes and functional analysis
    • Thompson J, Janse CJ, Waters AP: Comparative genomics in Plasmodium: a tool for the identification of genes and functional analysis. Mol Biochem Parasitol 2001, 118(2):147-154.
    • (2001) Mol Biochem Parasitol , vol.118 , Issue.2 , pp. 147-154
    • Thompson, J.1    Janse, C.J.2    Waters, A.P.3
  • 17
    • 0035873363 scopus 로고    scopus 로고
    • Interspecies conservation of gene order and intron-exon structure in a genomic locus of high gene density and complexity in Plasmodium
    • van Lin LH, Pace T, Janse CJ, Birago C, Ramesar J, Picci L, Ponzi M, Waters AP: Interspecies conservation of gene order and intron-exon structure in a genomic locus of high gene density and complexity in Plasmodium. Nucleic Acids Res 2001, 29(10):2059-2068.
    • (2001) Nucleic Acids Res , vol.29 , Issue.10 , pp. 2059-2068
    • Van Lin, L.H.1    Pace, T.2    Janse, C.J.3    Birago, C.4    Ramesar, J.5    Picci, L.6    Ponzi, M.7    Waters, A.P.8
  • 18
    • 0031555480 scopus 로고    scopus 로고
    • Unique structural features of the monomeric Cu,Zn superoxide dismutase from Escherichia coli, revealed by X-ray crystallography
    • Pesce A, Capasso C, Battistoni A, Folcarelli S, Rotilio G, Desideri A, Bolognesi M: Unique structural features of the monomeric Cu,Zn superoxide dismutase from Escherichia coli, revealed by X-ray crystallography. J Mol Biol 1997, 274(3):408-420.
    • (1997) J Mol Biol , vol.274 , Issue.3 , pp. 408-420
    • Pesce, A.1    Capasso, C.2    Battistoni, A.3    Folcarelli, S.4    Rotilio, G.5    Desideri, A.6    Bolognesi, M.7
  • 20
    • 0033600863 scopus 로고    scopus 로고
    • Interrupting the hydrogen bond network at the active site of human manganese superoxide dismutase
    • Ramilo CA, Leveque V, Guan Y, Lepock JR, Tainer JA, Nick HS, Silverman DN: Interrupting the hydrogen bond network at the active site of human manganese superoxide dismutase. J Biol Chem 1999, 274(39):27711-27716.
    • (1999) J Biol Chem , vol.274 , Issue.39 , pp. 27711-27716
    • Ramilo, C.A.1    Leveque, V.2    Guan, Y.3    Lepock, J.R.4    Tainer, J.A.5    Nick, H.S.6    Silverman, D.N.7
  • 22
    • 3142781225 scopus 로고    scopus 로고
    • Small-molecule inhibitors of protein-protein interactions: Progressing towards the dream
    • Arkin MR, Wells JA: Small-molecule inhibitors of protein-protein interactions: progressing towards the dream. Nat Rev Drug Discov 2004, 3(4):301-317.
    • (2004) Nat Rev Drug Discov , vol.3 , Issue.4 , pp. 301-317
    • Arkin, M.R.1    Wells, J.A.2
  • 24
    • 0002498995 scopus 로고
    • Computer-aided interpretation of analytical sedimentation data for proteins
    • Edited by: Harding SE, Rowe AJ, Horton JC. Cambridge , The Royal Society of Chemistry
    • Laue TM, Shah BD, Ridgeway TM, Pelletier SL: Computer-aided interpretation of analytical sedimentation data for proteins. In Analytical Ultracentrifugation in Biochemistry and Polmer Science Edited by: Harding SE, Rowe AJ, Horton JC. Cambridge , The Royal Society of Chemistry; 1992:90-125.
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polmer Science , pp. 90-125
    • Laue, T.M.1    Shah, B.D.2    Ridgeway, T.M.3    Pelletier, S.L.4
  • 25
    • 0021288878 scopus 로고
    • Superoxide dismutase assays
    • Flohe L, Otting F: Superoxide dismutase assays. Methods Enzymol 1984, 105:93-104.
    • (1984) Methods Enzymol , vol.105 , pp. 93-104
    • Flohe, L.1    Otting, F.2
  • 26
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • San Diego , ACADEMIC PRESS INC
    • Otwinowski Z, Minor W: Processing of X-ray diffraction data collected in oscillation mode. In Macromolecular Crystallography, Pt A Volume 276. San Diego , ACADEMIC PRESS INC; 1997:307-326.
    • (1997) Macromolecular Crystallography, Pt A Volume 276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 27
    • 0028103275 scopus 로고
    • The CCP4 Suite - Programs for Protein Crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4.: The CCP4 Suite - Programs for Protein Crystallography. Acta Crystallogr D Biol Crystallogr 1994, 50:760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 28
    • 84920325457 scopus 로고
    • Amore - An Automated Package for Molecular Replacement
    • Navaza J: Amore - an Automated Package for Molecular Replacement. Acta Crystallogr Sect A 1994, 50:157-163.
    • (1994) Acta Crystallogr Sect A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 30
    • 0346122796 scopus 로고    scopus 로고
    • Applications for macromolecular map interpretation: X-AUTOFIT, X-POWERFIT, X-BUILD, X-LIGAND, and X-SOLVATE
    • Oldfield T: Applications for macromolecular map interpretation: X-AUTOFIT, X-POWERFIT, X-BUILD, X-LIGAND, and X-SOLVATE. Methods Enzymol 2003, 374:271-300.
    • (2003) Methods Enzymol , vol.374 , pp. 271-300
    • Oldfield, T.1
  • 31
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG: The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 1997, 25(24):4876-4882.
    • (1997) Nucleic Acids Res , vol.25 , Issue.24 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 32
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL: Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 1993, 234(3):779-815.
    • (1993) J Mol Biol , vol.234 , Issue.3 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 35
  • 36
    • 0026688441 scopus 로고
    • The structure of human mitochondrial manganese superoxide dismutase reveals a novel tetrameric interface of two 4-helix bundles
    • Borgstahl GE, Parge HE, Hickey MJ, Beyer WFJ, Hallewell RA, Tainer JA: The structure of human mitochondrial manganese superoxide dismutase reveals a novel tetrameric interface of two 4-helix bundles. Cell 1992, 71(1):107-118.
    • (1992) Cell , vol.71 , Issue.1 , pp. 107-118
    • Borgstahl, G.E.1    Parge, H.E.2    Hickey, M.J.3    Beyer, W.F.J.4    Hallewell, R.A.5    Tainer, J.A.6
  • 37
    • 1542305367 scopus 로고    scopus 로고
    • Specificity and phenetic relationships of iron- and manganese-containing superoxide dismutases on the basis of structure and sequence comparisons
    • Wintjens R, Noel C, May AC, Gerbod D, Dufernez F, Capron M, Viscogliosi E, Rooman M: Specificity and phenetic relationships of iron- and manganese-containing superoxide dismutases on the basis of structure and sequence comparisons. J Biol Chem 2004, 279(10):9248-9254.
    • (2004) J Biol Chem , vol.279 , Issue.10 , pp. 9248-9254
    • Wintjens, R.1    Noel, C.2    May, A.C.3    Gerbod, D.4    Dufernez, F.5    Capron, M.6    Viscogliosi, E.7    Rooman, M.8
  • 38
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • Gouet P, Courcelle E, Stuart DI, Metoz F: ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 1999, 15(4):305-308.
    • (1999) Bioinformatics , vol.15 , Issue.4 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 40
    • 0032711685 scopus 로고    scopus 로고
    • Cloning and characterization of iron-containing superoxide dismutase from the human malaria species Plasmodium ovale, P. malariae and P. vivax
    • Baert CB, Deloron P, Viscogliosi E, Delgado-Viscogliosi P, Camus D, Dive D: Cloning and characterization of iron-containing superoxide dismutase from the human malaria species Plasmodium ovale, P. malariae and P. vivax. Parasitol Res 1999, 85(12):1018-1024.
    • (1999) Parasitol Res , vol.85 , Issue.12 , pp. 1018-1024
    • Baert, C.B.1    Deloron, P.2    Viscogliosi, E.3    Delgado-Viscogliosi, P.4    Camus, D.5    Dive, D.6


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