REFERENCES
- Schirmer RH, Muller JG, Krauth-Siegel RL. Disulfide-reductase inhibitors as chemotherapeutic agents: the design of drugs for trypano-somiasis and malaria. Angew Chem Int Edn 1995; 34: 141–154.
- Kanzok SM, Schirmer RH, TUrbachova I, Iozef R, Becker K. The thioredoxin system of the malaria parasite Plasmodium falciparum. Glutathione reduction revisited. J Biol Chem 2000; 275: 40180–40186.
- Kmajski Z, Gilberger T, Walter RD, Muller S. The malaria parasite Plasmodium falciparum possesses a functional thioredoxin system. Mol Biochem Parasitol 2001; 112: 219–228.
- Farber PM, Arscott LD, Williams Jr CH, Becker K, Schirmer RH. Recombinant Plasmodium falciparum glutathione reductase is inhibited by the antimalarial dye methylene blue. FEBS Lett 1998: 422: 311–314.
- Kawazu S, Komaki K, Tsuji N et al. Molecular characterization of a 2-Cys peroxiredoxin from the human malaria parasite Plasmodium falciparum. Mol Biochem Parasitol 2001; 116: 73–79.
- Kawazu S, Tsuji N, Hatabu T, Kawai S, Matsumoto Y, Kano S. Molecular cloning and characterization of a peroxiredoxin from the human malaria parasite Plasmodium falciparum. Mol Biochem Parasitol 2000; 109: 165–169.
- Kmajski Z, Walter RD, Muller S. Isolation and functional analysis of two thioredoxin peroxidases (peroxiredoxins) from Plasmodium falciparum. Mol Biochem Parasitol 2001; 113: 303–308.
- Rahlfs S, Becker K. Thioredoxin peroxidases of the malarial parasite Plasmodium falciparum. Eur J Biochem 2001; 268: 1404–1409.
- Rahlfs S, Fischer M, Becker K. Plasmodium falciparum possesses a classical glutaredoxin and a second, glutaredoxin-like protein with a PICOT homology domain. J Biol Chem 2001; 276: 37133–37140.
- Harwaldt P, Rahlfs S, Becker K. Glutathione S-transferase of the malarial parasite Plasmodium falciparum: characterization of a potential drug target. Biol Chem 2002; 383: 821–830.
- Liebau E, Bergmann B, Campbell AM et al. The glutathione S-transferase from Plasmodium falciparum. Mol Biochem Parasitol 2002; 124: 85–90.
- Holmgren A. Antioxidant function of thioredoxin and glutaredoxin systems. Antioxid Redox Signal 2000; 2: 811–820.
- Becker K, Rahlfs S, Nickel C, Schirmer RH. Glutathione - function and metabolism in the malarial parasite Plasmodium falciparum. Biol Chem 2003; 384: 551–566.
- Rodriguez-Manzaneque MT, Ros J, Cabiscol E, Sorribas A, Herrero E. Grx5 glutaredoxin plays a central role in protection against protein oxidative damage in Saccharomyces cerevisiae. Mol Cell Biol 1999; 19: 8180–8190.
- Witte S, Villalba M, Bi K, Liu Y, Isakov N, Altman A. Inhibition of the c-Jun N-terminal kinase/AP-1 and NF-kappaB pathways by PICOT, a novel protein kinase C-interacting protein with a thioredoxin homology domain. J Biol Chem 2000; 275: 1902–1909.
- Isakov N, Witte S, Altman A. PICOT-HD: a highly conserved protein domain that is often associated with thioredoxin and glutaredoxin modules. Trends Biochem Sci 2000; 25: 537–539.
- Rodriguez-Manzaneque MT, 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.
- Belli G, Polaina J, Tamarit J et al. Structure-function analysis of yeast Grx5 monothiol glutaredoxin defines essential amino acids for the function of the protein. J Biol Chem 2002; 277: 37590–37596.
- Shenton D, Perrone G, Quinn KA, Dawes IW, Grant CM. Regulation of protein S-thiolation by glutaredoxin 5 in the yeast Saccharomyces cerevisiae. J Biol Chem 2002; 277: 16853–16859.
- Kanzok SM, Fechner A, Bauer H et al. Substitution of the thioredoxin system for glutathione reductase in Drosophila melanogaster. Science 2001; 296: 643–646.
- Takemoto T, Zhang QM, Yonei S. Different mechanisms of thioredoxin in its reduced and oxidized forms in defense against hydrogen peroxide in Escherichia coli. Free Radic Biol Med 1998; 24: 556–562.
- Das KC, Das CK. Thioredoxin, a singlet oxygen quencher and hydroxyl radical scavenger: redox independent functions. Biochem Biophys Res Commun 2000; 277: 443–447.
- Bjtimstedt M, Hamberg M, Kumar S, Xue J, Holmgren A. Human thioredoxin reductase directly reduces lipid hydro-peroxides by NADPH and selenocystine strongly stimulates the reaction via catalytically generated selenols. J Biol Chem 1995; 270: 11761–11764.
- Mitsui A, Hirakawa T, Yodoi J. Reactive oxygen-reducing and protein-refolding activities of adult T cell leukemia-derived factor/human thioredoxin. Biochem Biophys Res Commun 1992; 186: 1220–1226.
- Becker K, Kanzok SM, Iozef R, Fischer M, Schirmer RH, Rahlfs S. Plasmoredoxin, a novel redox-active protein unique for malarial parasites. Eur J Biochem 2003; 270: 1057–1064.
- Gardner MJ, Hall N, Fung E et al. Genome sequence of the human malaria parasite Plasmodium falciparum. Nature 2002; 419: 498–511.
- Bahl A, Brunk B, Coppel RL et al. PlasmoDB: the Plasmodium genome resource. An integrated database providing tools for accessing, analyzing and mapping expression and sequence data(both finished and unfinished). Nucleic Acids Res 2002; 30: 87–90.
- Kissinger JC, Brunk BP, Crabtree Jet al. The Plasmodium genome database. Nature 2002; 419: 490–492.
- Lasonder E, Ishihama Y, Andersen JS et al. Analysis of the Plasmodium fakiparum proteome by high-accuracy mass spectrometry. Nature 2002; 419: 537–542.
- Schmidt A, Krauth-Siegel RL. Enzymes of the trypanothione metabolism as targets for antitrypanosomal drug development. Curr Top Med Chem 2002; 2: 1239–1259.
- Sarma GN, Savvides SN, Becker K, Schirmer M, Schirmer RH, Karplus PA. Glutathione reductase of the malarial parasite Plasmodium falciparum: crystal structure and inhibitor development. J Mol Biol 2003; 308: 893–907.