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Volumn 270, Issue 6, 2003, Pages 1057-1064

Plasmoredoxin, a novel redox-active protein unique for malarial parasites

Author keywords

Antioxidant; Malaria; Plasmodium falciparum; Redox metabolism; Thioredoxin superfamily

Indexed keywords

COMPLEMENTARY DNA; DITHIOTHREITOL; DNA; GLUTAREDOXIN; GLUTATHIONE; GLUTATHIONE TRANSFERASE; HYDROGEN PEROXIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PLASMAREDOXIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; RIBONUCLEOTIDE REDUCTASE; THIOREDOXIN; TRYPANOTHIONE; UNCLASSIFIED DRUG;

EID: 0344643424     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03495.x     Document Type: Article
Times cited : (45)

References (34)
  • 1
    • 0035060361 scopus 로고    scopus 로고
    • Mode of action and mechanisms of resistance for antimalarial drugs
    • Olliaro, P. (2001) Mode of action and mechanisms of resistance for antimalarial drugs. Pharmacol. Ther. 89, 207-219.
    • (2001) Pharmacol. Ther. , vol.89 , pp. 207-219
    • Olliaro, P.1
  • 2
  • 3
    • 33748233963 scopus 로고
    • Disulfide-reductase inhibitors as chemotherapeutic agents: The design of drugs for trypanosomiasis and malaria
    • Schirmer, R.H., Müller, J.G. & Krauth-Siegel, R.L. (1995) Disulfide-reductase inhibitors as chemotherapeutic agents: the design of drugs for trypanosomiasis and malaria. Angew. Chem. Int. Ed. Engl. 34, 141-154.
    • (1995) Angew. Chem. Int. Ed. Engl. , vol.34 , pp. 141-154
    • Schirmer, R.H.1    Müller, J.G.2    Krauth-Siegel, R.L.3
  • 4
    • 0033215010 scopus 로고    scopus 로고
    • Enzymes of parasite thiol metabolism as drug targets
    • Krauth-Siegel, R.L. & Coombs, G.H. (1999) Enzymes of parasite thiol metabolism as drug targets. Parasitol. Today 15, 404-409.
    • (1999) Parasitol. Today , vol.15 , pp. 404-409
    • Krauth-Siegel, R.L.1    Coombs, G.H.2
  • 5
    • 0033775650 scopus 로고    scopus 로고
    • Thioredoxin reductase as a pathophysiological factor and drug target
    • Becker, K., Gromer, S., Schirmer, R.H. & Müller, S. (2000) Thioredoxin reductase as a pathophysiological factor and drug target. Eur. J. Biochem. 267, 6118-6125.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6118-6125
    • Becker, K.1    Gromer, S.2    Schirmer, R.H.3    Müller, S.4
  • 7
    • 0036119803 scopus 로고    scopus 로고
    • Thioredoxin, thioredoxin reductase, and thioredoxin peroxidase of the malaria parasite Plasmodium falciparum
    • Kanzok, S.M., Rahlfs, S., Becker, K. & Schirmer, R.H. (2002) Thioredoxin, thioredoxin reductase, and thioredoxin peroxidase of the malaria parasite Plasmodium falciparum. Methods Enzymol. 347, 370-381.
    • (2002) Methods Enzymol. , vol.347 , pp. 370-381
    • Kanzok, S.M.1    Rahlfs, S.2    Becker, K.3    Schirmer, R.H.4
  • 8
    • 0036305476 scopus 로고    scopus 로고
    • The thioredoxin system of Plasmodium falciparum and other parasites
    • Rahlfs, S., Schirmer, R.H. & Becker, K. (2002) The thioredoxin system of Plasmodium falciparum and other parasites. Cell. Mol. Life Sci. 59, 1024-1041.
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1024-1041
    • Rahlfs, S.1    Schirmer, R.H.2    Becker, K.3
  • 9
    • 0034704081 scopus 로고    scopus 로고
    • The thioredoxin system of the malaria parasite Plasmodium falciparum. Glutathione reduction revisited
    • Kanzok, S.M., Schirmer, R.H., Türbachova, I., Iozef, R. & Becker, K. (2000) The thioredoxin system of the malaria parasite Plasmodium falciparum. Glutathione reduction revisited. J. Biol. Chem. 275, 40180-40186.
    • (2000) J. Biol. Chem. , vol.275 , pp. 40180-40186
    • Kanzok, S.M.1    Schirmer, R.H.2    Türbachova, I.3    Iozef, R.4    Becker, K.5
  • 10
    • 0033844270 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a peroxiredoxin from the human malaria parasite Plasmodium falciparum
    • Kawazu, S., Tsuji, N., Hatabu, T., Kawai, S., Matsumoto, Y. & Kano, S. (2000) Molecular cloning and characterization of a peroxiredoxin from the human malaria parasite Plasmodium falciparum. Mol. Biochem. Parasitol. 109, 165-169.
    • (2000) Mol. Biochem. Parasitol. , vol.109 , pp. 165-169
    • Kawazu, S.1    Tsuji, N.2    Hatabu, T.3    Kawai, S.4    Matsumoto, Y.5    Kano, S.6
  • 11
    • 0035081036 scopus 로고    scopus 로고
    • Thioredoxin peroxidases of the malarial parasite Plasmodium falciparum
    • Rahlfs, S. & Becker, K. (2001) Thioredoxin peroxidases of the malarial parasite Plasmodium falciparum. Eur. J. Biochem. 268, 1404-1409.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1404-1409
    • Rahlfs, S.1    Becker, K.2
  • 13
    • 0035815346 scopus 로고    scopus 로고
    • Isolation and functional analysis of two thioredoxin peroxidases (peroxiredoxins) from Plasmodium falciparum
    • Krnajski, Z., Walter, R.D. & Müller, S. (2001) Isolation and functional analysis of two thioredoxin peroxidases (peroxiredoxins) from Plasmodium falciparum. Mol. Biochem. Parasitol. 113, 303-308.
    • (2001) Mol. Biochem. Parasitol. , vol.113 , pp. 303-308
    • Krnajski, Z.1    Walter, R.D.2    Müller, S.3
  • 15
    • 0043096998 scopus 로고    scopus 로고
    • Recombinant Plasmodium falciparum glutathione reductase is inhibited by the antimalarial dye methylene blue
    • Färber, P.M., Arscott, L.D., Williams, C.H. Jr, Becker, K. & Schirmer, R.H. (1998) Recombinant Plasmodium falciparum glutathione reductase is inhibited by the antimalarial dye methylene blue. FEBS Lett. 422, 311-314.
    • (1998) FEBS Lett. , vol.422 , pp. 311-314
    • Färber, P.M.1    Arscott, L.D.2    Williams C.H., Jr.3    Becker, K.4    Schirmer, R.H.5
  • 16
    • 0035985070 scopus 로고    scopus 로고
    • Glutathione S-transferase of the malarial parasite Plasmodium falciparum. Characterization of a potential drug target
    • Harwaldt, P., Rahlfs, S. & Becker, K. (2002) Glutathione S-transferase of the malarial parasite Plasmodium falciparum. Characterization of a potential drug target. Biol. Chem. 383, 821-830.
    • (2002) Biol. Chem. , vol.383 , pp. 821-830
    • Harwaldt, P.1    Rahlfs, S.2    Becker, K.3
  • 17
    • 0035813229 scopus 로고    scopus 로고
    • Plasmodium falciparum possesses a classical glutaredoxin and a second, glutaredoxin-like protein with a PICOT homology domain
    • Rahlfs, S., Fischer, M. & Becker, K. (2001) Plasmodium falciparum possesses a classical glutaredoxin and a second, glutaredoxin-like protein with a PICOT homology domain. J. Biol. Chem. 276, 37133-37140.
    • (2001) J. Biol. Chem. , vol.276 , pp. 37133-37140
    • Rahlfs, S.1    Fischer, M.2    Becker, K.3
  • 18
    • 0033775891 scopus 로고    scopus 로고
    • Physiological functions of thioredoxin and thioredoxin reductase
    • Arnér, E.S. & Holmgren, A. (2000) Physiological functions of thioredoxin and thioredoxin reductase. Eur. J. Biochem. 267, 6102-6109.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6102-6109
    • Arnér, E.S.1    Holmgren, A.2
  • 19
    • 0034534165 scopus 로고    scopus 로고
    • Antioxidant function of thioredoxin and glutaredoxin
    • Holmgren, A. (2000) Antioxidant function of thioredoxin and glutaredoxin. Antioxid. Redox. Signal. 2, 811-820.
    • (2000) Antioxid. Redox. Signal. , vol.2 , pp. 811-820
    • Holmgren, A.1
  • 20
    • 0029165589 scopus 로고
    • Thioredoxin - A fold for all reasons
    • Martin, J.L. (1995) Thioredoxin - a fold for all reasons. Structure 3, 245-250.
    • (1995) Structure , vol.3 , pp. 245-250
    • Martin, J.L.1
  • 21
    • 0033913980 scopus 로고    scopus 로고
    • Nucleoredoxin, glutaredoxin, and thioredoxin differentially regulate NF-kappaB, AP-1, and CREB activation in HEK293 cells
    • Hirota, K., Matsui, M., Murata, M., Takashima, Y., Cheng, F.S., Itoh, T., Fukuda, K. & Yodoi, J. (2000) Nucleoredoxin, glutaredoxin, and thioredoxin differentially regulate NF-kappaB, AP-1, and CREB activation in HEK293 cells. Biochem. Biophys. Res. Commun. 274, 177-182.
    • (2000) Biochem. Biophys. Res. Commun. , vol.274 , pp. 177-182
    • Hirota, K.1    Matsui, M.2    Murata, M.3    Takashima, Y.4    Cheng, F.S.5    Itoh, T.6    Fukuda, K.7    Yodoi, J.8
  • 22
    • 0033796101 scopus 로고    scopus 로고
    • The role of the redox protein thioredoxin in cell growth and cancer
    • Powis, G., Mustacich, D. & Coon, A. (2000) The role of the redox protein thioredoxin in cell growth and cancer. Free Radic. Biol. Med. 29, 312-322.
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 312-322
    • Powis, G.1    Mustacich, D.2    Coon, A.3
  • 23
    • 0031719952 scopus 로고    scopus 로고
    • The yeast Saccharomyces cerevisiae contains two glutaredoxin genes that are required for protection against reactive oxygen species
    • Luikenhuis, S., Perrone, G., Dawes, I.W. & Grant, C. (1998) The yeast Saccharomyces cerevisiae contains two glutaredoxin genes that are required for protection against reactive oxygen species. Mol. Biol. Cell 9, 1081-1091.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1081-1091
    • Luikenhuis, S.1    Perrone, G.2    Dawes, I.W.3    Grant, C.4
  • 24
    • 0034076851 scopus 로고    scopus 로고
    • A single glutaredoxin or thioredoxin gene is essential for viability in the yeast Saccharomyces cerevisiae
    • Draculic, T., Dawes, I.W. & Grant, C.M. (2000) A single glutaredoxin or thioredoxin gene is essential for viability in the yeast Saccharomyces cerevisiae. Mol. Microbiol. 36, 1167-1174.
    • (2000) Mol. Microbiol. , vol.36 , pp. 1167-1174
    • Draculic, T.1    Dawes, I.W.2    Grant, C.M.3
  • 26
    • 0030861413 scopus 로고    scopus 로고
    • A unique cascade of oxidoreductases catalyses trypanothione-mediated peroxide metabolism in Crithidia fasciculata
    • Nogoceke, E., Gommel, D.U., Kiess, M., Kalisz, H.M. & Flohé, L. (1997) A unique cascade of oxidoreductases catalyses trypanothione-mediated peroxide metabolism in Crithidia fasciculata. Biol. Chem. 378, 827-836.
    • (1997) Biol. Chem. , vol.378 , pp. 827-836
    • Nogoceke, E.1    Gommel, D.U.2    Kiess, M.3    Kalisz, H.M.4    Flohé, L.5
  • 27
    • 0018786967 scopus 로고
    • Ribonucleotide reductase from calf thymus. Purification and properties
    • Engstrom, Y., Eriksson, S., Thelander, L. & Akerman, M. (1979) Ribonucleotide reductase from calf thymus. Purification and properties. Biochemistry 18, 2941-2948.
    • (1979) Biochemistry , vol.18 , pp. 2941-2948
    • Engstrom, Y.1    Eriksson, S.2    Thelander, L.3    Akerman, M.4
  • 28
    • 0023931727 scopus 로고
    • Ribonucleotide reductase of Brevibacterium ammoniagenes is a manganese enzyme
    • Willing, A., Follmann, H. & Auling, G. (1988) Ribonucleotide reductase of Brevibacterium ammoniagenes is a manganese enzyme. Eur. J. Biochem. 170, 603-611.
    • (1988) Eur. J. Biochem. , vol.170 , pp. 603-611
    • Willing, A.1    Follmann, H.2    Auling, G.3
  • 34
    • 0001136010 scopus 로고
    • Glutathione reductase
    • Dolphin, D., Avramovic, O. & Poulson, R., eds. Wiley & Sons, New York, USA
    • Schirmer, R.H., Krauth-Siegel, R.L. & Schulz, G.E. (1989) Glutathione reductase. In Coenzymes and Cofactors: Glutathione, (Dolphin, D., Avramovic, O. & Poulson, R., eds), Vol. 3 Part A, pp. 553-596. Wiley & Sons, New York, USA.
    • (1989) Coenzymes and Cofactors: Glutathione , vol.3 , Issue.PART A , pp. 553-596
    • Schirmer, R.H.1    Krauth-Siegel, R.L.2    Schulz, G.E.3


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