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Volumn 8, Issue 1, 2014, Pages 35-

Functional Characterization of Peroxiredoxins from the Human Protozoan Parasite Giardia intestinalis

Author keywords

[No Author keywords available]

Indexed keywords

BENZENE DERIVATIVE; CUMENE HYDROPEROXIDE; HYDROGEN PEROXIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PEROXIREDOXIN; PEROXYNITRITE; PEROXYNITROUS ACID; RECOMBINANT PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; TERT BUTYL HYDROPEROXIDE;

EID: 84893796588     PISSN: 19352727     EISSN: 19352735     Source Type: Journal    
DOI: 10.1371/journal.pntd.0002631     Document Type: Article
Times cited : (34)

References (65)
  • 1
    • 0034933985 scopus 로고    scopus 로고
    • Biology of Giardia lamblia
    • Adam RD, (2001) Biology of Giardia lamblia. Clin Microbiol Rev 14: 447-475.
    • (2001) Clin Microbiol Rev , vol.14 , pp. 447-475
    • Adam, R.D.1
  • 2
    • 0035991398 scopus 로고    scopus 로고
    • Current trends in research into the waterborne parasite Giardia
    • Lane S, Lloyd D, (2002) Current trends in research into the waterborne parasite Giardia. Crit Rev Microbiol 28: 123-147.
    • (2002) Crit Rev Microbiol , vol.28 , pp. 123-147
    • Lane, S.1    Lloyd, D.2
  • 3
  • 6
    • 34848894621 scopus 로고    scopus 로고
    • Genomic minimalism in the early diverging intestinal parasite Giardia lamblia
    • Morrison HG, McArthur AG, Gillin FD, Aley SB, Adam RD, et al. (2007) Genomic minimalism in the early diverging intestinal parasite Giardia lamblia. Science 317: 1921-1926.
    • (2007) Science , vol.317 , pp. 1921-1926
    • Morrison, H.G.1    McArthur, A.G.2    Gillin, F.D.3    Aley, S.B.4    Adam, R.D.5
  • 7
    • 0013855388 scopus 로고
    • Small bowel tonometry: assessment of small gut mucosal oxygen tension in dog and man
    • Dawson AM, Trenchard D, Guz A, (1965) Small bowel tonometry: assessment of small gut mucosal oxygen tension in dog and man. Nature 206: 943-944.
    • (1965) Nature , vol.206 , pp. 943-944
    • Dawson, A.M.1    Trenchard, D.2    Guz, A.3
  • 8
    • 0025233771 scopus 로고
    • Intraoperative tissue oximetry in the human gastrointestinal tract
    • Sheridan WG, Lowndes RH, Young HL, (1990) Intraoperative tissue oximetry in the human gastrointestinal tract. Am J Surg 159: 314-319.
    • (1990) Am J Surg , vol.159 , pp. 314-319
    • Sheridan, W.G.1    Lowndes, R.H.2    Young, H.L.3
  • 9
    • 0033551085 scopus 로고    scopus 로고
    • Noninvasive measurement of anatomic structure and intraluminal oxygenation in the gastrointestinal tract of living mice with spatial and spectral EPR imaging
    • He G, Shankar RA, Chzhan M, Samouilov A, Kuppusamy P, et al. (1999) Noninvasive measurement of anatomic structure and intraluminal oxygenation in the gastrointestinal tract of living mice with spatial and spectral EPR imaging. Proc Natl Acad Sci U S A 96: 4586-4591.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 4586-4591
    • He, G.1    Shankar, R.A.2    Chzhan, M.3    Samouilov, A.4    Kuppusamy, P.5
  • 10
    • 84873299448 scopus 로고    scopus 로고
    • Role of oxygen gradients in shaping redox relationships between the human intestine and its microbiota
    • Espey MG, (2013) Role of oxygen gradients in shaping redox relationships between the human intestine and its microbiota. Free Radic Biol Med 55: 130-140.
    • (2013) Free Radic Biol Med , vol.55 , pp. 130-140
    • Espey, M.G.1
  • 11
    • 84874662091 scopus 로고    scopus 로고
    • Biology of nitrogen oxides in the gastrointestinal tract
    • Lundberg JO, Weitzberg E, (2013) Biology of nitrogen oxides in the gastrointestinal tract. Gut 62: 616-629.
    • (2013) Gut , vol.62 , pp. 616-629
    • Lundberg, J.O.1    Weitzberg, E.2
  • 12
    • 0029661970 scopus 로고    scopus 로고
    • A H2O-producing NADH oxidase from the protozoan parasite Giardia duodenalis
    • Brown DM, Upcroft JA, Upcroft P, (1996) A H2O-producing NADH oxidase from the protozoan parasite Giardia duodenalis. Eur J Biochem 241: 155-161.
    • (1996) Eur J Biochem , vol.241 , pp. 155-161
    • Brown, D.M.1    Upcroft, J.A.2    Upcroft, P.3
  • 13
    • 42949120247 scopus 로고    scopus 로고
    • The O2-scavenging flavodiiron protein in the human parasite Giardia intestinalis
    • Di Matteo A, Scandurra FM, Testa F, Forte E, Sarti P, et al. (2008) The O2-scavenging flavodiiron protein in the human parasite Giardia intestinalis. J Biol Chem 283: 4061-4068.
    • (2008) J Biol Chem , vol.283 , pp. 4061-4068
    • Di Matteo, A.1    Scandurra, F.M.2    Testa, F.3    Forte, E.4    Sarti, P.5
  • 14
    • 79951971253 scopus 로고    scopus 로고
    • Giardia intestinalis escapes oxidative stress by colonizing the small intestine: A molecular hypothesis
    • Mastronicola D, Giuffrè A, Testa F, Mura A, Forte E, et al. (2011) Giardia intestinalis escapes oxidative stress by colonizing the small intestine: A molecular hypothesis. IUBMB Life 63: 21-25.
    • (2011) IUBMB Life , vol.63 , pp. 21-25
    • Mastronicola, D.1    Giuffrè, A.2    Testa, F.3    Mura, A.4    Forte, E.5
  • 16
    • 77956262736 scopus 로고    scopus 로고
    • Flavohemoglobin and nitric oxide detoxification in the human protozoan parasite Giardia intestinalis
    • Mastronicola D, Testa F, Forte E, Bordi E, Pucillo LP, et al. (2010) Flavohemoglobin and nitric oxide detoxification in the human protozoan parasite Giardia intestinalis. Biochem Biophys Res Commun 399: 654-658.
    • (2010) Biochem Biophys Res Commun , vol.399 , pp. 654-658
    • Mastronicola, D.1    Testa, F.2    Forte, E.3    Bordi, E.4    Pucillo, L.P.5
  • 17
    • 84860393559 scopus 로고    scopus 로고
    • The superoxide reductase from the early diverging eukaryote Giardia intestinalis
    • Testa F, Mastronicola D, Cabelli DE, Bordi E, Pucillo LP, et al. (2011) The superoxide reductase from the early diverging eukaryote Giardia intestinalis. Free Radic Biol Med 51: 1567-1574.
    • (2011) Free Radic Biol Med , vol.51 , pp. 1567-1574
    • Testa, F.1    Mastronicola, D.2    Cabelli, D.E.3    Bordi, E.4    Pucillo, L.P.5
  • 18
    • 0023484562 scopus 로고
    • Ingestion of Giardia lamblia trophozoites by human mononuclear phagocytes
    • Hill DR, Pearson RD, (1987) Ingestion of Giardia lamblia trophozoites by human mononuclear phagocytes. Infect Immun 55: 3155-3161.
    • (1987) Infect Immun , vol.55 , pp. 3155-3161
    • Hill, D.R.1    Pearson, R.D.2
  • 20
    • 0034528565 scopus 로고    scopus 로고
    • The microaerophilic flagellate Giardia intestinalis: oxygen and its reaction products collapse membrane potential and cause cytotoxicity
    • Lloyd D, Harris JC, Maroulis S, Biagini GA, Wadley RB, et al. (2000) The microaerophilic flagellate Giardia intestinalis: oxygen and its reaction products collapse membrane potential and cause cytotoxicity. Microbiology 146: 3109-3118.
    • (2000) Microbiology , vol.146 , pp. 3109-3118
    • Lloyd, D.1    Harris, J.C.2    Maroulis, S.3    Biagini, G.A.4    Wadley, R.B.5
  • 22
    • 79958059617 scopus 로고    scopus 로고
    • Structure-based insights into the catalytic power and conformational dexterity of peroxiredoxins
    • Hall A, Nelson K, Poole LB, Karplus PA, (2011) Structure-based insights into the catalytic power and conformational dexterity of peroxiredoxins. Antioxid Redox Signal 15: 795-815.
    • (2011) Antioxid Redox Signal , vol.15 , pp. 795-815
    • Hall, A.1    Nelson, K.2    Poole, L.B.3    Karplus, P.A.4
  • 23
    • 84858279884 scopus 로고    scopus 로고
    • Overview of peroxiredoxins in oxidant defense and redox regulation
    • Unit7 9, Chapter 7
    • Poole LB, Hall A, Nelson KJ, (2011) Overview of peroxiredoxins in oxidant defense and redox regulation. Curr Protoc Toxicol Chapter 7: Unit7 9.
    • (2011) Curr Protoc Toxicol
    • Poole, L.B.1    Hall, A.2    Nelson, K.J.3
  • 24
    • 0028226006 scopus 로고
    • Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes
    • Chae HZ, Robison K, Poole LB, Church G, Storz G, et al. (1994) Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes. Proc Natl Acad Sci U S A 91: 7017-7021.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 7017-7021
    • Chae, H.Z.1    Robison, K.2    Poole, L.B.3    Church, G.4    Storz, G.5
  • 25
    • 0034648827 scopus 로고    scopus 로고
    • Peroxynitrite reductase activity of bacterial peroxiredoxins
    • Bryk R, Griffin P, Nathan C, (2000) Peroxynitrite reductase activity of bacterial peroxiredoxins. Nature 407: 211-215.
    • (2000) Nature , vol.407 , pp. 211-215
    • Bryk, R.1    Griffin, P.2    Nathan, C.3
  • 26
    • 84884169659 scopus 로고    scopus 로고
    • Peroxynitrite, a stealthy biological oxidant
    • Radi R, (2013) Peroxynitrite, a stealthy biological oxidant. J Biol Chem 288: 26464-26472.
    • (2013) J Biol Chem , vol.288 , pp. 26464-26472
    • Radi, R.1
  • 27
    • 33745631769 scopus 로고    scopus 로고
    • Cell signaling. H2O2, a necessary evil for cell signaling
    • Rhee SG, (2006) Cell signaling. H2O2, a necessary evil for cell signaling. Science 312: 1882-1883.
    • (2006) Science , vol.312 , pp. 1882-1883
    • Rhee, S.G.1
  • 28
    • 76749102420 scopus 로고    scopus 로고
    • Inactivation of peroxiredoxin I by phosphorylation allows localized H(2)O(2) accumulation for cell signaling
    • Woo HA, Yim SH, Shin DH, Kang D, Yu DY, et al. (2010) Inactivation of peroxiredoxin I by phosphorylation allows localized H(2)O(2) accumulation for cell signaling. Cell 140: 517-528.
    • (2010) Cell , vol.140 , pp. 517-528
    • Woo, H.A.1    Yim, S.H.2    Shin, D.H.3    Kang, D.4    Yu, D.Y.5
  • 29
    • 66649131702 scopus 로고    scopus 로고
    • Redox-regulated chaperones
    • Kumsta C, Jakob U, (2009) Redox-regulated chaperones. Biochemistry 48: 4666-4676.
    • (2009) Biochemistry , vol.48 , pp. 4666-4676
    • Kumsta, C.1    Jakob, U.2
  • 30
    • 84857835586 scopus 로고    scopus 로고
    • Novel roles of peroxiredoxins in inflammation, cancer and innate immunity
    • Ishii T, Warabi E, Yanagawa T, (2012) Novel roles of peroxiredoxins in inflammation, cancer and innate immunity. J Clin Biochem Nutr 50: 91-105.
    • (2012) J Clin Biochem Nutr , vol.50 , pp. 91-105
    • Ishii, T.1    Warabi, E.2    Yanagawa, T.3
  • 32
    • 33746505480 scopus 로고    scopus 로고
    • Structural and biochemical characterization of a mitochondrial peroxiredoxin from Plasmodium falciparum
    • Boucher IW, McMillan PJ, Gabrielsen M, Akerman SE, Brannigan JA, et al. (2006) Structural and biochemical characterization of a mitochondrial peroxiredoxin from Plasmodium falciparum. Mol Microbiol 61: 948-959.
    • (2006) Mol Microbiol , vol.61 , pp. 948-959
    • Boucher, I.W.1    McMillan, P.J.2    Gabrielsen, M.3    Akerman, S.E.4    Brannigan, J.A.5
  • 33
    • 15444362698 scopus 로고    scopus 로고
    • Crystal structure of the tryparedoxin peroxidase from the human parasite Trypanosoma cruzi
    • Pineyro MD, Pizarro JC, Lema F, Pritsch O, Cayota A, et al. (2005) Crystal structure of the tryparedoxin peroxidase from the human parasite Trypanosoma cruzi. J Struct Biol 150: 11-22.
    • (2005) J Struct Biol , vol.150 , pp. 11-22
    • Pineyro, M.D.1    Pizarro, J.C.2    Lema, F.3    Pritsch, O.4    Cayota, A.5
  • 34
    • 84861234069 scopus 로고    scopus 로고
    • Representational difference analysis identifies specific genes in the interaction of Giardia duodenalis with the murine intestinal epithelial cell line, IEC-6
    • Ma'ayeh SY, Brook-Carter PT, (2012) Representational difference analysis identifies specific genes in the interaction of Giardia duodenalis with the murine intestinal epithelial cell line, IEC-6. Int J Parasitol 42: 501-509.
    • (2012) Int J Parasitol , vol.42 , pp. 501-509
    • Ma'ayeh, S.Y.1    Brook-Carter, P.T.2
  • 35
    • 0016701378 scopus 로고
    • Reduced nicotinamide adenine dinucleotide phosphate (NADPH)-dependent formation and breakdown of hydrogen peroxide during mixed function oxidation reactions in liver microsomes
    • Hildebraunt AG, Roots I, (1975) Reduced nicotinamide adenine dinucleotide phosphate (NADPH)-dependent formation and breakdown of hydrogen peroxide during mixed function oxidation reactions in liver microsomes. Arch Biochem Biophys 171: 385-397.
    • (1975) Arch Biochem Biophys , vol.171 , pp. 385-397
    • Hildebraunt, A.G.1    Roots, I.2
  • 36
    • 37049135943 scopus 로고
    • The chemistry of pernitrites. Part I. Kinetics of decomposition of pernitrous acid
    • Hughes MN, Nicklin HG, (1968) The chemistry of pernitrites. Part I. Kinetics of decomposition of pernitrous acid. J Chem Soc A pp. 450-452.
    • (1968) J Chem Soc A , pp. 450-452
    • Hughes, M.N.1    Nicklin, H.G.2
  • 37
    • 52049096372 scopus 로고    scopus 로고
    • Kinetic studies on peroxynitrite reduction by peroxiredoxins
    • Trujillo M, Ferrer-Sueta G, Radi R, (2008) Kinetic studies on peroxynitrite reduction by peroxiredoxins. Methods Enzymol 441: 173-196.
    • (2008) Methods Enzymol , vol.441 , pp. 173-196
    • Trujillo, M.1    Ferrer-Sueta, G.2    Radi, R.3
  • 38
    • 0020651210 scopus 로고
    • Axenic culture of Giardia lamblia in TYI-S-33 medium supplemented with bile
    • Keister DB, (1983) Axenic culture of Giardia lamblia in TYI-S-33 medium supplemented with bile. Trans R Soc Trop Med Hyg 77: 487-488.
    • (1983) Trans R Soc Trop Med Hyg , vol.77 , pp. 487-488
    • Keister, D.B.1
  • 40
    • 80054078476 scopus 로고    scopus 로고
    • Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega
    • Sievers F, Wilm A, Dineen D, Gibson TJ, Karplus K, et al. (2011) Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega. Mol Syst Biol 7: 539.
    • (2011) Mol Syst Biol , vol.7 , pp. 539
    • Sievers, F.1    Wilm, A.2    Dineen, D.3    Gibson, T.J.4    Karplus, K.5
  • 41
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: discriminating signal peptides from transmembrane regions
    • Petersen TN, Brunak S, von Heijne G, Nielsen H, (2011) SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat Methods 8: 785-786.
    • (2011) Nat Methods , vol.8 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 42
    • 0037064080 scopus 로고    scopus 로고
    • Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid
    • Yang KS, Kang SW, Woo HA, Hwang SC, Chae HZ, et al. (2002) Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid. J Biol Chem 277: 38029-38036.
    • (2002) J Biol Chem , vol.277 , pp. 38029-38036
    • Yang, K.S.1    Kang, S.W.2    Woo, H.A.3    Hwang, S.C.4    Chae, H.Z.5
  • 43
    • 0025730414 scopus 로고
    • Peroxynitrite oxidation of sulfhydryls. The cytotoxic potential of superoxide and nitric oxide
    • Radi R, Beckman JS, Bush KM, Freeman BA, (1991) Peroxynitrite oxidation of sulfhydryls. The cytotoxic potential of superoxide and nitric oxide. J Biol Chem 266: 4244-4250.
    • (1991) J Biol Chem , vol.266 , pp. 4244-4250
    • Radi, R.1    Beckman, J.S.2    Bush, K.M.3    Freeman, B.A.4
  • 44
    • 0041355353 scopus 로고    scopus 로고
    • RNA interference identifies two hydroperoxide metabolizing enzymes that are essential to the bloodstream form of the african trypanosome
    • Wilkinson SR, Horn D, Prathalingam SR, Kelly JM, (2003) RNA interference identifies two hydroperoxide metabolizing enzymes that are essential to the bloodstream form of the african trypanosome. J Biol Chem 278: 31640-31646.
    • (2003) J Biol Chem , vol.278 , pp. 31640-31646
    • Wilkinson, S.R.1    Horn, D.2    Prathalingam, S.R.3    Kelly, J.M.4
  • 45
    • 69349103734 scopus 로고    scopus 로고
    • Enzymes of the antioxidant network as novel determiners of Trypanosoma cruzi virulence
    • Piacenza L, Zago MP, Peluffo G, Alvarez MN, Basombrio MA, et al. (2009) Enzymes of the antioxidant network as novel determiners of Trypanosoma cruzi virulence. Int J Parasitol 39: 1455-1464.
    • (2009) Int J Parasitol , vol.39 , pp. 1455-1464
    • Piacenza, L.1    Zago, M.P.2    Peluffo, G.3    Alvarez, M.N.4    Basombrio, M.A.5
  • 46
    • 22844441185 scopus 로고    scopus 로고
    • An unusual surface peroxiredoxin protects invasive Entamoeba histolytica from oxidant attack
    • Choi MH, Sajed D, Poole L, Hirata K, Herdman S, et al. (2005) An unusual surface peroxiredoxin protects invasive Entamoeba histolytica from oxidant attack. Mol Biochem Parasitol 143: 80-89.
    • (2005) Mol Biochem Parasitol , vol.143 , pp. 80-89
    • Choi, M.H.1    Sajed, D.2    Poole, L.3    Hirata, K.4    Herdman, S.5
  • 47
    • 33748486043 scopus 로고    scopus 로고
    • Comparative proteomic analysis of two Entamoeba histolytica strains with different virulence phenotypes identifies peroxiredoxin as an important component of amoebic virulence
    • Davis PH, Zhang X, Guo J, Townsend RR, Stanley SL Jr, (2006) Comparative proteomic analysis of two Entamoeba histolytica strains with different virulence phenotypes identifies peroxiredoxin as an important component of amoebic virulence. Mol Microbiol 61: 1523-1532.
    • (2006) Mol Microbiol , vol.61 , pp. 1523-1532
    • Davis, P.H.1    Zhang, X.2    Guo, J.3    Townsend, R.R.4    Stanley Jr., S.L.5
  • 48
    • 58149305444 scopus 로고    scopus 로고
    • Entamoeba histolytica modulates a complex repertoire of novel genes in response to oxidative and nitrosative stresses: implications for amebic pathogenesis
    • Vicente JB, Ehrenkaufer GM, Saraiva LM, Teixeira M, Singh U, (2009) Entamoeba histolytica modulates a complex repertoire of novel genes in response to oxidative and nitrosative stresses: implications for amebic pathogenesis. Cell Microbiol 11: 51-69.
    • (2009) Cell Microbiol , vol.11 , pp. 51-69
    • Vicente, J.B.1    Ehrenkaufer, G.M.2    Saraiva, L.M.3    Teixeira, M.4    Singh, U.5
  • 49
    • 43049127225 scopus 로고    scopus 로고
    • Disruption of the Plasmodium berghei 2-Cys peroxiredoxin TPx-1 gene hinders the sporozoite development in the vector mosquito
    • Yano K, Otsuki H, Arai M, Komaki-Yasuda K, Tsuboi T, et al. (2008) Disruption of the Plasmodium berghei 2-Cys peroxiredoxin TPx-1 gene hinders the sporozoite development in the vector mosquito. Mol Biochem Parasitol 159: 142-145.
    • (2008) Mol Biochem Parasitol , vol.159 , pp. 142-145
    • Yano, K.1    Otsuki, H.2    Arai, M.3    Komaki-Yasuda, K.4    Tsuboi, T.5
  • 50
    • 33744546817 scopus 로고    scopus 로고
    • 2-Cys Peroxiredoxin TPx-1 is involved in gametocyte development in Plasmodium berghei
    • Yano K, Komaki-Yasuda K, Tsuboi T, Torii M, Kano S, et al. (2006) 2-Cys Peroxiredoxin TPx-1 is involved in gametocyte development in Plasmodium berghei. Mol Biochem Parasitol 148: 44-51.
    • (2006) Mol Biochem Parasitol , vol.148 , pp. 44-51
    • Yano, K.1    Komaki-Yasuda, K.2    Tsuboi, T.3    Torii, M.4    Kano, S.5
  • 51
    • 84871358773 scopus 로고    scopus 로고
    • 2-Cys peroxiredoxin of Plasmodium falciparum is involved in resistance to heat stress of the parasite
    • Kimura R, Komaki-Yasuda K, Kawazu S, Kano S, (2013) 2-Cys peroxiredoxin of Plasmodium falciparum is involved in resistance to heat stress of the parasite. Parasitol Int 62: 137-143.
    • (2013) Parasitol Int , vol.62 , pp. 137-143
    • Kimura, R.1    Komaki-Yasuda, K.2    Kawazu, S.3    Kano, S.4
  • 52
    • 41049101045 scopus 로고    scopus 로고
    • Crucial role of cytosolic tryparedoxin peroxidase in Leishmania donovani survival, drug response and virulence
    • Iyer JP, Kaprakkaden A, Choudhary ML, Shaha C, (2008) Crucial role of cytosolic tryparedoxin peroxidase in Leishmania donovani survival, drug response and virulence. Mol Microbiol 68: 372-391.
    • (2008) Mol Microbiol , vol.68 , pp. 372-391
    • Iyer, J.P.1    Kaprakkaden, A.2    Choudhary, M.L.3    Shaha, C.4
  • 54
    • 65549139721 scopus 로고    scopus 로고
    • Molecular characterization of cytosolic and mitochondrial tryparedoxin peroxidase in Trypanosoma cruzi populations susceptible and resistant to benznidazole
    • Nogueira FB, Ruiz JC, Robello C, Romanha AJ, Murta SM, (2009) Molecular characterization of cytosolic and mitochondrial tryparedoxin peroxidase in Trypanosoma cruzi populations susceptible and resistant to benznidazole. Parasitol Res 104: 835-844.
    • (2009) Parasitol Res , vol.104 , pp. 835-844
    • Nogueira, F.B.1    Ruiz, J.C.2    Robello, C.3    Romanha, A.J.4    Murta, S.M.5
  • 55
    • 0033543649 scopus 로고    scopus 로고
    • Metronidazole resistance in the protozoan parasite Entamoeba histolytica is associated with increased expression of iron-containing superoxide dismutase and peroxiredoxin and decreased expression of ferredoxin 1 and flavin reductase
    • Wassmann C, Hellberg A, Tannich E, Bruchhaus I, (1999) Metronidazole resistance in the protozoan parasite Entamoeba histolytica is associated with increased expression of iron-containing superoxide dismutase and peroxiredoxin and decreased expression of ferredoxin 1 and flavin reductase. J Biol Chem 274: 26051-26056.
    • (1999) J Biol Chem , vol.274 , pp. 26051-26056
    • Wassmann, C.1    Hellberg, A.2    Tannich, E.3    Bruchhaus, I.4
  • 56
    • 64149123281 scopus 로고    scopus 로고
    • Trichomonas vaginalis: metronidazole and other nitroimidazole drugs are reduced by the flavin enzyme thioredoxin reductase and disrupt the cellular redox system. Implications for nitroimidazole toxicity and resistance
    • Leitsch D, Kolarich D, Binder M, Stadlmann J, Altmann F, et al. (2009) Trichomonas vaginalis: metronidazole and other nitroimidazole drugs are reduced by the flavin enzyme thioredoxin reductase and disrupt the cellular redox system. Implications for nitroimidazole toxicity and resistance. Mol Microbiol 72: 518-536.
    • (2009) Mol Microbiol , vol.72 , pp. 518-536
    • Leitsch, D.1    Kolarich, D.2    Binder, M.3    Stadlmann, J.4    Altmann, F.5
  • 57
    • 0030596199 scopus 로고    scopus 로고
    • A thioredoxin reductase-class of disulphide reductase in the protozoan parasite Giardia duodenalis
    • Brown DM, Upcroft JA, Upcroft P, (1996) A thioredoxin reductase-class of disulphide reductase in the protozoan parasite Giardia duodenalis. Mol Biochem Parasitol 83: 211-220.
    • (1996) Mol Biochem Parasitol , vol.83 , pp. 211-220
    • Brown, D.M.1    Upcroft, J.A.2    Upcroft, P.3
  • 58
    • 79960472745 scopus 로고    scopus 로고
    • Pyruvate:ferredoxin oxidoreductase and thioredoxin reductase are involved in 5-nitroimidazole activation while flavin metabolism is linked to 5-nitroimidazole resistance in Giardia lamblia
    • Leitsch D, Burgess AG, Dunn LA, Krauer KG, Tan K, et al. (2011) Pyruvate:ferredoxin oxidoreductase and thioredoxin reductase are involved in 5-nitroimidazole activation while flavin metabolism is linked to 5-nitroimidazole resistance in Giardia lamblia. J Antimicrob Chemother 66: 1756-1765.
    • (2011) J Antimicrob Chemother , vol.66 , pp. 1756-1765
    • Leitsch, D.1    Burgess, A.G.2    Dunn, L.A.3    Krauer, K.G.4    Tan, K.5
  • 59
    • 0030628364 scopus 로고    scopus 로고
    • Role of nitric oxide and superoxide in Giardia lamblia killing
    • Fernandes PD, Assreuy J, (1997) Role of nitric oxide and superoxide in Giardia lamblia killing. Braz J Med Biol Res 30: 93-99.
    • (1997) Braz J Med Biol Res , vol.30 , pp. 93-99
    • Fernandes, P.D.1    Assreuy, J.2
  • 60
    • 33645049877 scopus 로고    scopus 로고
    • A likely molecular basis of the susceptibility of Giardia lamblia towards oxygen
    • Li L, Wang CC, (2006) A likely molecular basis of the susceptibility of Giardia lamblia towards oxygen. Mol Microbiol 59: 202-211.
    • (2006) Mol Microbiol , vol.59 , pp. 202-211
    • Li, L.1    Wang, C.C.2
  • 62
    • 43049100037 scopus 로고    scopus 로고
    • Release of metabolic enzymes by Giardia in response to interaction with intestinal epithelial cells
    • Ringqvist E, Palm JE, Skarin H, Hehl AB, Weiland M, et al. (2008) Release of metabolic enzymes by Giardia in response to interaction with intestinal epithelial cells. Mol Biochem Parasitol 159: 85-91.
    • (2008) Mol Biochem Parasitol , vol.159 , pp. 85-91
    • Ringqvist, E.1    Palm, J.E.2    Skarin, H.3    Hehl, A.B.4    Weiland, M.5
  • 63
    • 0029900905 scopus 로고    scopus 로고
    • Nitric oxide synthase generates superoxide and nitric oxide in arginine-depleted cells leading to peroxynitrite-mediated cellular injury
    • Xia Y, Dawson VL, Dawson TM, Snyder SH, Zweier JL, (1996) Nitric oxide synthase generates superoxide and nitric oxide in arginine-depleted cells leading to peroxynitrite-mediated cellular injury. Proc Natl Acad Sci U S A 93: 6770-6774.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 6770-6774
    • Xia, Y.1    Dawson, V.L.2    Dawson, T.M.3    Snyder, S.H.4    Zweier, J.L.5
  • 64
    • 55049133247 scopus 로고    scopus 로고
    • Methotrexate-induced nitrosative stress may play a critical role in small intestinal damage in the rat
    • Kolli VK, Abraham P, Rabi S, (2008) Methotrexate-induced nitrosative stress may play a critical role in small intestinal damage in the rat. Arch Toxicol 82: 763-770.
    • (2008) Arch Toxicol , vol.82 , pp. 763-770
    • Kolli, V.K.1    Abraham, P.2    Rabi, S.3
  • 65
    • 0037221491 scopus 로고    scopus 로고
    • Regulation of intestinal nuclear factor-kappaB activity and E-selectin expression during sepsis: a role for peroxynitrite
    • Lush CW, Cepinskas G, Kvietys PR, (2003) Regulation of intestinal nuclear factor-kappaB activity and E-selectin expression during sepsis: a role for peroxynitrite. Gastroenterology 124: 118-128.
    • (2003) Gastroenterology , vol.124 , pp. 118-128
    • Lush, C.W.1    Cepinskas, G.2    Kvietys, P.R.3


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