메뉴 건너뛰기




Volumn 17, Issue 4, 2012, Pages 608-633

Peroxiredoxins in parasites

Author keywords

[No Author keywords available]

Indexed keywords

ANTIMONY; ANTIPARASITIC AGENT; ANTITRYPANOSOMAL AGENT; BENZNIDAZOLE; CONOIDIN A; METRONIDAZOLE; PEROXIREDOXIN; PEROXIREDOXIN 1; PEROXIREDOXIN 1A; PEROXIREDOXIN 5; PEROXIREDOXIN 6; PEROXIREDOXIN AHPE; PEROXIREDOXIN Q; PMX 464; QUINOLINE DERIVATIVE; UNCLASSIFIED DRUG; VACCINE;

EID: 84860294541     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2011.4404     Document Type: Review
Times cited : (82)

References (278)
  • 1
    • 33749614548 scopus 로고    scopus 로고
    • Resistance to oxidative stress is associated with metastasis in mucocutaneous leishmaniasis
    • DOI 10.1086/507646
    • Acestor N, Masina S, Ives A, Walker J, Saravia N, and Fasel N. Resistance to oxidative stress is associated with metastasis in mucocutaneous leishmaniasis. J Infect Dis 194: 1160-1167, 2006. (Pubitemid 44547657)
    • (2006) Journal of Infectious Diseases , vol.194 , Issue.8 , pp. 1160-1167
    • Acestor, N.1    Masina, S.2    Ives, A.3    Walker, J.4    Saravia, N.G.5    Fasel, N.6
  • 2
    • 77954935933 scopus 로고    scopus 로고
    • A model of redox kinetics implicates the thiol proteome in cellular hydrogen peroxide responses
    • Adimora N, Jones D, and Kemp M. A model of redox kinetics implicates the thiol proteome in cellular hydrogen peroxide responses. Antioxid Redox Signal 13: 731-743, 2010.
    • (2010) Antioxid Redox Signal , vol.13 , pp. 731-743
    • Adimora, N.1    Jones, D.2    Kemp, M.3
  • 4
    • 17144439425 scopus 로고    scopus 로고
    • 2-Cys peroxiredoxin PfTrx-Px1 is involved in the antioxidant defence of Plasmodium falciparum
    • DOI 10.1016/S0166-6851(03)00161-0
    • Akerman S and Muller S. 2-Cys peroxiredoxin PfTrx-Px1 is involved in the antioxidant defence of Plasmodium falciparum. Mol Biochem Parasitol 130: 75-81, 2003. (Pubitemid 37289125)
    • (2003) Molecular and Biochemical Parasitology , vol.130 , Issue.2 , pp. 75-81
    • Akerman, S.E.1    Muller, S.2
  • 5
    • 12844271131 scopus 로고    scopus 로고
    • Peroxiredoxin-linked detoxification of hydroperoxides in Toxoplasma gondii
    • DOI 10.1074/jbc.M406367200
    • Akerman S and Muller S. Peroxiredoxin-linked detoxification of hydroperoxides in Toxoplasma gondii. J Biol Chem 280: 564-570, 2005. (Pubitemid 40165022)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.1 , pp. 564-570
    • Akerman, S.E.1    Muller, S.2
  • 6
    • 0036710531 scopus 로고    scopus 로고
    • Molecular and enzymatic characterisation of Schistosoma mansoni thioredoxin
    • DOI 10.1016/S0020-7519(02)00108-X, PII S002075190200108X
    • Alger H, Sayed A, Stadecker M, and Williams D. Molecular and enzymatic characterisation of Schistosoma mansoni thioredoxin. Int J Parasitol 32: 1285-1292, 2002. (Pubitemid 35232180)
    • (2002) International Journal for Parasitology , vol.32 , Issue.10 , pp. 1285-1292
    • Alger, H.M.1    Sayed, A.A.2    Stadecker, M.J.3    Williams, D.L.4
  • 8
    • 52449084934 scopus 로고    scopus 로고
    • Structural and mechanistic insights into type II trypanosomatid tryparedoxin- Dependent peroxidases
    • Alphey MS, König J, and Fairlamb AH. Structural and mechanistic insights into type II trypanosomatid tryparedoxin- dependent peroxidases. Biochem J 414: 375, 2008.
    • (2008) Biochem J , vol.414 , pp. 375
    • Alphey, M.S.1    König, J.2    Fairlamb, A.H.3
  • 9
    • 79953183972 scopus 로고    scopus 로고
    • Intraphagosomal peroxynitrite as a macrophage-derived cytotoxin against internalized Trypanosoma cruzi: Consequences for oxidative killing and role of microbial peroxiredoxins in infectivity
    • Alvarez M, Peluffo G, Piacenza L, and Radi R. Intraphagosomal peroxynitrite as a macrophage-derived cytotoxin against internalized Trypanosoma cruzi: consequences for oxidative killing and role of microbial peroxiredoxins in infectivity. J Biol Chem 286: 6627-6640, 2011.
    • (2011) J Biol Chem , vol.286 , pp. 6627-6640
    • Alvarez, M.1    Peluffo, G.2    Piacenza, L.3    Radi, R.4
  • 10
    • 47749151024 scopus 로고    scopus 로고
    • Comparison of immunogenicity, protective efficacy of single and cocktail DNA vaccine of Brugia malayi abundant larval transcript (ALT-2) and thioredoxin peroxidase (TPX) in mice
    • Anand S, Murugan V, Prabhu P, Anandharaman V, Reddy M, and Kaliraj P. Comparison of immunogenicity, protective efficacy of single and cocktail DNA vaccine of Brugia malayi abundant larval transcript (ALT-2) and thioredoxin peroxidase (TPX) in mice. Acta Trop 107: 106-112, 2008.
    • (2008) Acta Trop , vol.107 , pp. 106-112
    • Anand, S.1    Murugan, V.2    Prabhu, P.3    Anandharaman, V.4    Reddy, M.5    Kaliraj, P.6
  • 13
    • 45049087808 scopus 로고    scopus 로고
    • Immunolocalization and enzymatic functional characterization of the thioredoxin system in Entamoeba histolytica
    • Arias D, Carranza P, Lujan H, Iglesias A, and Guerrero S. Immunolocalization and enzymatic functional characterization of the thioredoxin system in Entamoeba histolytica. Free Radic Biol Med 45: 32-39, 2008.
    • (2008) Free Radic Biol Med , vol.45 , pp. 32-39
    • Arias, D.1    Carranza, P.2    Lujan, H.3    Iglesias, A.4    Guerrero, S.5
  • 17
    • 0034798612 scopus 로고    scopus 로고
    • Cloning and characterization of the metacyclogenin gene, which is specifically expressed during Trypanosoma cruzi metacyclogenesis
    • DOI 10.1016/S0166-6851(01)00346-2, PII S0166685101003462
    • Avila A, Yamada-Ogatta S, da Silva Monteiro V, Krieger M, Nakamura C, de Souza W, and Goldenberg S. Cloning and characterization of the metacyclogenin gene, which is specifically expressed during Trypanosoma cruzi metacyclogenesis. Mol Biochem Parasitol 117: 169-177, 2001. (Pubitemid 32972278)
    • (2001) Molecular and Biochemical Parasitology , vol.117 , Issue.2 , pp. 169-177
    • Avila, A.R.1    Yamada-Ogatta, S.F.2    Da, S.M.V.3    Krieger, M.A.4    Nakamura, C.V.5    De Souza, W.6    Goldenberg, S.7
  • 18
    • 1542619337 scopus 로고    scopus 로고
    • Stress Signaling from Irradiated to Non-Irradiated Cells
    • DOI 10.2174/1568009043481641
    • Azzam EI, de Toledo SM, and Little JB. Stress signaling from irradiated to non-irradiated cells. Curr Cancer Drug Targets 4: 53-64, 2004. (Pubitemid 38332564)
    • (2004) Current Cancer Drug Targets , vol.4 , Issue.1 , pp. 53-64
    • Azzam, E.I.1    De Toledo, S.M.2    Little, J.B.3
  • 19
    • 80053072690 scopus 로고    scopus 로고
    • Identification and biochemical characterization of two novel peroxir- Edoxins in a liver fluke, Clonorchis sinensis
    • Bae Y, Kim S, Lee E, Sohn W, and Kong Y. Identification and biochemical characterization of two novel peroxir- edoxins in a liver fluke, Clonorchis sinensis. Parasitology 138: 1143-1153, 2011.
    • (2011) Parasitology , vol.138 , pp. 1143-1153
    • Bae, Y.1    Kim, S.2    Lee, E.3    Sohn, W.4    Kong, Y.5
  • 20
    • 0037646517 scopus 로고    scopus 로고
    • 61
    • DOI 10.1074/jbc.M209888200
    • Baker LM and Poole LB. Catalytic mechanism of thiol peroxidase from Escherichia coli. Sulfenic acid formation and overoxidation of essential CYS61. J Biol Chem 278: 9203-9211, 2003. (Pubitemid 36800402)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.11 , pp. 9203-9211
    • Baker, L.M.S.1    Poole, L.B.2
  • 21
    • 0035823608 scopus 로고    scopus 로고
    • Cloning and characterization of three differentially expressed peroxidoxin genes from Leishmania chagasi. Evidence for an enzymatic detoxification of hydroxyl radicals
    • Barr S and Gedamu L. Cloning and characterization of three differentially expressed peroxidoxin genes from Leishmania chagasi. Evidence for an enzymatic detoxification of hydroxyl radicals. J Biol Chem 276: 34279-34287, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 34279-34287
    • Barr, S.1    Gedamu, L.2
  • 22
    • 0037518119 scopus 로고    scopus 로고
    • Role of peroxidoxins in Leishmania chagasi survival. Evidence of an enzymatic defense against nitrosative stress
    • DOI 10.1074/jbc.M212990200
    • Barr SD and Gedamu L. Role of peroxidoxins in Leishmania chagasi survival. Evidence of an enzymatic defense against nitrosative stress. J Biochem 278: 10816-10823, 2003. (Pubitemid 36800355)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.12 , pp. 10816-10823
    • Barr, S.D.1    Gedamu, L.2
  • 23
    • 67349155642 scopus 로고    scopus 로고
    • The oligomeric conformation of peroxiredoxins links redox state to function
    • Barranco-Medina S, Lázaro J-J, and Dietz K-J. The oligomeric conformation of peroxiredoxins links redox state to function. FEBS Lett 583: 1809-1816, 2009.
    • (2009) FEBS Lett , vol.583 , pp. 1809-1816
    • Barranco-Medina, S.1    Lázaro, J.-J.2    Dietz, K.-J.3
  • 26
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: SignalP 3.0
    • DOI 10.1016/j.jmb.2004.05.028, PII S0022283604005972
    • Bendtsen JD, Nielsen H, von Heijne G, and Brunak S. Improved prediction of signal peptides: SignalP 3.0. J Mol Biol 340: 783-795, 2004. (Pubitemid 38829638)
    • (2004) Journal of Molecular Biology , vol.340 , Issue.4 , pp. 783-795
    • Bendtsen, J.D.1    Nielsen, H.2    Von Heijne, G.3    Brunak, S.4
  • 28
    • 36549005658 scopus 로고    scopus 로고
    • Rhoptries: an arsenal of secreted virulence factors
    • DOI 10.1016/j.mib.2007.09.013, PII S1369527407001385, Growth and Development
    • Bradley P and Sibley L. Rhoptries: an arsenal of secreted virulence factors. Curr Opin Microbiol 10: 582-587, 2007. (Pubitemid 350180592)
    • (2007) Current Opinion in Microbiology , vol.10 , Issue.6 , pp. 582-587
    • Bradley, P.J.1    Sibley, L.D.2
  • 29
    • 33745711863 scopus 로고    scopus 로고
    • Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi (microsporidia): A reference map for proteins expressed in late sporogonial stages
    • DOI 10.1002/pmic.200500796
    • Brosson D, Kuhn L, Delbac F, Garin J, Vivares CP, and Texier C. Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi (microsporidia): a reference map for proteins expressed in late sporogonial stages. Proteomics 6: 3625-3635, 2006. (Pubitemid 44000190)
    • (2006) Proteomics , vol.6 , Issue.12 , pp. 3625-3635
    • Brosson, D.1    Kuhn, L.2    Delbac, F.3    Garin, J.4    Vivares, C.P.5    Texier, C.6
  • 30
    • 0030778936 scopus 로고    scopus 로고
    • Removal of hydrogen peroxide by the 29 kDa protein of Entamoeba histolytica
    • Bruchhaus I, Richter S, and Tannich E. Removal of hydrogen peroxide by the 29 kDa protein of Entamoeba histolytica. Biochem J 326: 785-789, 1997. (Pubitemid 27438052)
    • (1997) Biochemical Journal , vol.326 , Issue.3 , pp. 785-789
    • Bruchhaus, I.1    Richter, S.2    Tannich, E.3
  • 31
    • 78549246255 scopus 로고    scopus 로고
    • Molecular genetics evidence for the in vivo roles of the two major NADPH-dependent disulfide reductases in the malaria parasite
    • Buchholz K, Putrianti ED, Rahlfs S, Schirmer RH, Becker K, and Matuschewski K. Molecular genetics evidence for the in vivo roles of the two major NADPH-dependent disulfide reductases in the malaria parasite. J Biol Chem 285: 37388-37395, 2010.
    • (2010) J Biol Chem , vol.285 , pp. 37388-37395
    • Buchholz, K.1    Putrianti, E.D.2    Rahlfs, S.3    Schirmer, R.H.4    Becker, K.5    Matuschewski, K.6
  • 32
    • 0037959650 scopus 로고    scopus 로고
    • Kinetics and redox-sensitive oligomerisation reveal negative subunit cooperativity in tryparedoxin peroxidase of trypanosoma brucei brucei
    • DOI 10.1515/BC.2003.069
    • Budde H, Flohé L, Hecht H-J, Hofmann B, Stehr M, Wissing J, and Lünsdorf H. Kinetics and redox-sensitive oligomerisation reveal negative subunit cooperativity in tryparedoxin peroxidase of Trypanosoma brucei brucei. Biol Chem 384: 619-633, 2003. (Pubitemid 36609177)
    • (2003) Biological Chemistry , vol.384 , Issue.4 , pp. 619-633
    • Budde, H.1    Flohe, L.2    Hecht, H.-J.3    Hofmann, B.4    Stehr, M.5    Wissing, J.6    Lunsdorf, H.7
  • 33
    • 0141717106 scopus 로고    scopus 로고
    • Verification of the interaction of a tryparedoxin peroxidase with tryparedoxin by ESI-MS/MS
    • DOI 10.1515/BC.2003.146
    • Budde H, Flohe L, Hofmann B, and Nimtz M. Verification of the interaction of a tryparedoxin peroxidase with tryparedoxin by ESI-MS/MS. Biol Chem 384: 1305-1309, 2003. (Pubitemid 37168699)
    • (2003) Biological Chemistry , vol.384 , Issue.9 , pp. 1305-1309
    • Budde, H.1    Flohe, L.2    Hofmann, B.3    Nimtz, M.4
  • 34
    • 0035001263 scopus 로고    scopus 로고
    • Protection against cutaneous leishmaniasis induced by recombinant antigens in murine and nonhuman primate models of the human disease
    • DOI 10.1128/IAI.69.6.4103-4108.2001
    • Campos-Neto A, Porrozzi R, Greeson K, Coler R, Webb J, Seiky Y, Reed S, and Grimaldi G. Protection against cutaneous leishmaniasis induced by recombinant antigens in murine and nonhuman primate models of the human disease. Infect Immun 69: 4103-4108, 2001. (Pubitemid 32493335)
    • (2001) Infection and Immunity , vol.69 , Issue.6 , pp. 4103-4108
    • Campos-Neto, A.1    Porrozzi, R.2    Greeson, K.3    Coler, R.N.4    Webb, J.R.5    Seiky, Y.A.W.6    Reed, S.G.7    Grimaldi Jr., G.8
  • 35
    • 0036890478 scopus 로고    scopus 로고
    • Specificity and kinetics of a mitochondrial peroxiredoxin of Leishmania infantum
    • DOI 10.1016/S0891-5849(02)01088-2, PII S0891584902010882
    • Castro H, Budde H, Flohé L, Hofmann B, Lünsdorf H, Wissing J, and Tomás A. Specificity and kinetics of a mitochondrial peroxiredoxin of Leishmania infantum. Free Radic Biol Med 33: 1563-1574, 2002. (Pubitemid 35351600)
    • (2002) Free Radical Biology and Medicine , vol.33 , Issue.11 , pp. 1563-1574
    • Castro, H.1    Budde, H.2    Flohe, L.3    Hofmann, B.4    Lunsdorf, H.5    Wissing, J.6    Toms, A.M.7
  • 36
    • 55049141724 scopus 로고    scopus 로고
    • Leishmania infantum: Provision of reducing equivalents to the mitochondrial tryparedoxin/tryparedoxin peroxidase system
    • Castro H, Romao S, Gadelha F, and Tomás A. Leishmania infantum: provision of reducing equivalents to the mitochondrial tryparedoxin/tryparedoxin peroxidase system. Exp Parasitol 120: 421-423, 2008.
    • (2008) Exp Parasitol , vol.120 , pp. 421-423
    • Castro, H.1    Romao, S.2    Gadelha, F.3    Tomás, A.4
  • 38
    • 0036889825 scopus 로고    scopus 로고
    • Complementary antioxidant defense by cytoplasmic and mitochondrial peroxiredoxins in Leishmania infantum
    • DOI 10.1016/S0891-5849(02)01089-4, PII S0891584902010894
    • Castro H, Sousa C, Santos M, Cordeiro-da-Silva A, Flohé L, and Tomás A. Complementary antioxidant defense by cytoplasmic and mitochondrial peroxiredoxins in Leishmania infantum. Free Radic Biol Med 33: 1552-1562, 2002. (Pubitemid 35351599)
    • (2002) Free Radical Biology and Medicine , vol.33 , Issue.11 , pp. 1552-1562
    • Castro, H.1    Sousa, C.2    Santos, M.3    Cordeiro-da-Silva, A.4    Flohe, L.5    Tomas, A.M.6
  • 39
    • 46449133760 scopus 로고    scopus 로고
    • Peroxidases of trypanosomatids
    • DOI 10.1089/ars.2008.2050
    • Castro H and Tomás A. Peroxidases of Trypanosomatids. Antioxid Redox Signal 10: 1593-1606, 2008. (Pubitemid 351934269)
    • (2008) Antioxidants and Redox Signaling , vol.10 , Issue.9 , pp. 1593-1606
    • Castro, H.1    Tomas, A.M.2
  • 40
    • 1542335652 scopus 로고    scopus 로고
    • Escherichia coli periplasmic thiol peroxidase acts as lipid hydroperoxide peroxidase and the principal antioxidative function during anaerobic growth
    • Cha M-K, Kim W-C, Lim C-J, Kim K, and Kim I-H. Escherichia coli periplasmic thiol peroxidase acts as lipid hydroperoxide peroxidase and the principal antioxidative function during anaerobic growth. J Biol Chem 279: 8769- 8778, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 8769-8778
    • Cha, M.-K.1    Kim, W.-C.2    Lim, C.-J.3    Kim, K.4    Kim, I.-H.5
  • 41
    • 0028072911 scopus 로고
    • Thioredoxin-dependent peroxide reductase from yeast
    • Chae H, Chung S, and Rhee S. Thioredoxin-dependent peroxide reductase from yeast. J Biol Chem 269: 27670- 27678, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 27670-27678
    • Chae, H.1    Chung, S.2    Rhee, S.3
  • 42
    • 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
    • DOI 10.1073/pnas.91.15.7017
    • Chae H, Robison K, Poole L, Church G, Storz G, and Rhee S. Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiolspecific antioxidant define a large family of antioxidant enzymes. Proc Natl Acad Sci U S A 91: 7017-7021, 1994. (Pubitemid 24226793)
    • (1994) Proceedings of the National Academy of Sciences of the United States of America , vol.91 , Issue.15 , pp. 7017-7021
    • Chae, H.Z.1    Robison, K.2    Poole, L.B.3    Church, G.4    Storz, G.5    Rhee, S.G.6
  • 43
    • 77951893193 scopus 로고    scopus 로고
    • Molecular cloning and characterization of two genes encoding 2-Cys peroxiredoxins from Fasciola gigantica
    • Chaithirayanon K and Sobhon P. Molecular cloning and characterization of two genes encoding 2-Cys peroxiredoxins from Fasciola gigantica. Exp Parasitol 125: 106-113, 2010.
    • (2010) Exp Parasitol , vol.125 , pp. 106-113
    • Chaithirayanon, K.1    Sobhon, P.2
  • 44
    • 0032103063 scopus 로고    scopus 로고
    • Molecular cloning of an enzymatically active thioredoxin peroxidase from Onchocerca volvulus
    • DOI 10.1016/S0166-6851(98)00041-3, PII S0166685198000413
    • Chandrashekar R, Curtis K, Lu W, and Weil G. Molecular cloning of an enzymatically active thioredoxin peroxidase from Onchocerca volvulus. Mol Biochem Parasitol 93: 309-312, 1998. (Pubitemid 28277067)
    • (1998) Molecular and Biochemical Parasitology , vol.93 , Issue.2 , pp. 309-312
    • Chandrashekar, R.1    Curtis, K.C.2    Lu, W.3    Weil, G.J.4
  • 45
    • 0033622036 scopus 로고    scopus 로고
    • Removal of hydrogen peroxide by a 1-cysteine peroxiredoxin enzyme of the filarial parasite Dirofilaria immitis
    • Chandrashekar R, Tsuji N, Morales TH, Carmody AB, Ozols VO, Welton J, and Tang L. Removal of hydrogen peroxide by a 1-cysteine peroxiredoxin enzyme of the filarial parasite Dirofilaria immitis. Parasitol Res 86: 200-206, 2000.
    • (2000) Parasitol Res , vol.86 , pp. 200-206
    • Chandrashekar, R.1    Tsuji, N.2    Morales, T.H.3    Carmody, A.B.4    Ozols, V.O.5    Welton, J.6    Tang, L.7
  • 46
    • 10944237769 scopus 로고    scopus 로고
    • Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine
    • DOI 10.1074/jbc.M409482200
    • Chang T-S, Jeong W, Woo HA, Lee SM, Park S, and Rhee SG. Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine. J Biol Chem 279: 50994-51001, 2004. (Pubitemid 40017840)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.49 , pp. 50994-51001
    • Chang, T.-S.1    Jeong, W.2    Hyun, A.W.3    Sun, M.L.4    Park, S.5    Sue, G.R.6
  • 47
    • 0033752685 scopus 로고    scopus 로고
    • Molecular cloning and characterization of peroxiredoxin from Entamoeba moshkovskii
    • Cheng X and Tachibana H. Molecular cloning and characterization of peroxiredoxin from Entamoeba moshkovskii. Arch Med Res 31: S65-S66, 2000.
    • (2000) Arch Med Res , vol.31
    • Cheng, X.1    Tachibana, H.2
  • 48
    • 8844281596 scopus 로고    scopus 로고
    • Molecular characterization of peroxiredoxin from Entamoeba moshkovskii and a comparison with Entamoeba histolytica
    • DOI 10.1016/j.molbiopara.2004.08.009, PII S016668510400235X
    • Cheng X-J, Yoshihara E, Takeuchi T, and Tachibana H. Molecular characterization of peroxiredoxin from Entamoeba moshkovskii and a comparison with Entamoeba histolytica. Mol Biochem Parasitol 138: 195-203, 2004. (Pubitemid 39536229)
    • (2004) Molecular and Biochemical Parasitology , vol.138 , Issue.2 , pp. 195-203
    • Cheng, X.-J.1    Yoshihara, E.2    Takeuchi, T.3    Tachibana, H.4
  • 49
    • 0031945918 scopus 로고    scopus 로고
    • Crystal structure of a novel human peroxidase enzyme at 2.0 A, resolution
    • DOI 10.1038/nsb0598-400
    • Choi HJ, Kang SW, Yang CH, Rhee SG, and Ryu SE. Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution. Nat Struct Biol 5: 400-406, 1998. (Pubitemid 28211179)
    • (1998) Nature Structural Biology , vol.5 , Issue.5 , pp. 400-406
    • Choi, H.-J.1    Kang, S.W.2    Yang, C.-H.3    Rhee, S.G.4    Ryu, S.-E.5
  • 50
  • 51
    • 34547870667 scopus 로고    scopus 로고
    • + T cells
    • DOI 10.1128/IAI.00394-07
    • Coler RN, Goto Y, Bogatzki L, Raman V, and Reed SG. Leish-111f, a recombinant polyprotein vaccine that protects against visceral Leishmaniasis by elicitation of CD4 + T cells. Infect Immun 75: 4648-4654, 2007. (Pubitemid 47378126)
    • (2007) Infection and Immunity , vol.75 , Issue.9 , pp. 4648-4654
    • Coler, R.N.1    Goto, Y.2    Bogatzki, L.3    Raman, V.4    Reed, S.G.5
  • 52
    • 78349305451 scopus 로고    scopus 로고
    • Evolutionary origin of a secondary structure: Pi-helices as cryptic but widespread insertional variations of alpha-helices that enhance protein functionality
    • Cooley RB, Arp DJ, and Karplus PA. Evolutionary origin of a secondary structure: pi-helices as cryptic but widespread insertional variations of alpha-helices that enhance protein functionality. J Mol Biol 404: 232-246, 2010.
    • (2010) J Mol Biol , vol.404 , pp. 232-246
    • Cooley, R.B.1    Arp, D.J.2    Karplus, P.A.3
  • 53
    • 1242272091 scopus 로고    scopus 로고
    • The Amitochondriate Eukaryote Trichomonas vaginalis Contains a Divergent Thioredoxin-linked Peroxiredoxin Antioxidant System
    • DOI 10.1074/jbc.M304359200
    • Coombs GH, Westrop GD, Suchan P, Puzova G, Hirt RP, Embley TM, Mottram JC, and Müller S. The amitochondriate eukaryote Trichomonas vaginalis contains a divergent thioredoxin-linked peroxiredoxin antioxidant system. J Biol Chem 279: 5249-5256, 2004. (Pubitemid 38220544)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.7 , pp. 5249-5256
    • Coombs, G.H.1    Westrop, G.D.2    Suchan, P.3    Puzova, G.4    Hirt, R.P.5    Embley, T.M.6    Mottram, J.C.7    Muller, S.8
  • 54
    • 0037417158 scopus 로고    scopus 로고
    • Identification of antibodies to Leishmania silent information regulatory 2 (SIR2) protein homologue during canine natural infections: Pathological implications
    • DOI 10.1016/S0165-2478(03)00020-8
    • Cordeiro-da-Silva A, Cardoso L, Araujo N, Castro H, Tomas A, Rodrigues M, Cabral M, Vergnes B, Sereno D, and Ouaissi A. Identification of antibodies to Leishmania silent information regulatory 2 (SIR2) protein homologue during canine natural infections: pathological implications. Immunol Lett 86: 155-162, 2003. (Pubitemid 36324276)
    • (2003) Immunology Letters , vol.86 , Issue.2 , pp. 155-162
    • Cordeiro-da-Silva, A.1    Cardoso, L.2    Araujo, N.3    Castro, H.4    Tomas, A.5    Rodrigues, M.6    Cabral, M.7    Vergnes, B.8    Sereno, D.9    Ouaissi, A.10
  • 55
    • 70349988784 scopus 로고    scopus 로고
    • Proteomic characterization of the released/secreted proteins of Leishmania (Viannia) braziliensis promastigotes
    • Cuervo P, De Jesus J, Saboia-Vahia L, Mendonça-Lima L, Domont G, and Cupolillo E. Proteomic characterization of the released/secreted proteins of Leishmania (Viannia) braziliensis promastigotes. J Proteomics 73: 79-92, 2009.
    • (2009) J Proteomics , vol.73 , pp. 79-92
    • Cuervo, P.1    De Jesus, J.2    Saboia-Vahia, L.3    Mendonça-Lima, L.4    Domont, G.5    Cupolillo, E.6
  • 56
    • 0028263005 scopus 로고
    • Mechanism of inhibition of trypanothione reductase and glutathione reductase by trivalent organic arsenicals
    • Cunningham ML, Zvelebil MJ, and Fairlamb AH. Mechanism of inhibition of trypanothione reductase and glutathione reductase by trivalent organic arsenicals. Eur J Biochem 221: 285-295, 1994. (Pubitemid 24120573)
    • (1994) European Journal of Biochemistry , vol.221 , Issue.1 , pp. 285-295
    • Cunningham, M.L.1    Zvelebil, M.J.J.M.2    Fairlamb, A.H.3
  • 57
    • 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
    • DOI 10.1111/j.1365-2958.2006.05344.x
    • Davis P, Zhang X, Guo J, Townsend R, and Stanley S. 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. (Pubitemid 44359380)
    • (2006) Molecular Microbiology , vol.61 , Issue.6 , pp. 1523-1532
    • Davis, P.H.1    Zhang, X.2    Guo, J.3    Townsend, R.R.4    Stanley Jr., S.L.5
  • 59
    • 61349152342 scopus 로고    scopus 로고
    • Changes in the proteome and infectivity of Leishmania infantum induced by in vitro exposure to a nitric oxide donor
    • Dea-Ayuela M, Ordonez-Gutierrez L, and Bolas-Fernandez F. Changes in the proteome and infectivity of Leishmania infantum induced by in vitro exposure to a nitric oxide donor. Int J Med Microbiol 299: 221-232, 2009.
    • (2009) Int J Med Microbiol , vol.299 , pp. 221-232
    • Dea-Ayuela, M.1    Ordonez-Gutierrez, L.2    Bolas-Fernandez, F.3
  • 60
    • 0035943382 scopus 로고    scopus 로고
    • Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 Å resolution
    • DOI 10.1006/jmbi.2001.4853
    • Declercq JP, Evrard C, Clippe A, Stricht DV, Bernard A, and Knoops B. Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 Å resolution. J Mol Biol 311: 751-759, 2001. (Pubitemid 32803733)
    • (2001) Journal of Molecular Biology , vol.311 , Issue.4 , pp. 751-759
    • Declercq, J.-P.1    Evrard, C.2    Clippe, A.3    Stricht, D.V.4    Bernard, A.5    Knoops, B.6
  • 61
    • 13444274373 scopus 로고    scopus 로고
    • Biochemical characterization of Toxoplasma gondii 1-Cys peroxiredoxin 2 with mechanistic similarities to typical 2-Cys Prx
    • DOI 10.1016/j.molbiopara.2004.12.008
    • Deponte M and Becker K. Biochemical characterization of Toxoplasma gondii 1-Cys peroxiredoxin 2 with mechanistic similarities to typical 2-Cys Prx. Mol Biochem Parasitol 140: 87-96, 2005. (Pubitemid 40203418)
    • (2005) Molecular and Biochemical Parasitology , vol.140 , Issue.1 , pp. 87-96
    • Deponte, M.1    Becker, K.2
  • 62
    • 38749134528 scopus 로고    scopus 로고
    • Peroxiredoxin systems of protozoal parasites
    • edited by Flohé L and Harris JR. New York: Springer
    • DeponteM, Rahlfs S, and Becker K. Peroxiredoxin systems of protozoal parasites. In: Peroxiredoxin Systems, edited by Flohé L and Harris JR. New York: Springer, 2007, pp. 219-229.
    • (2007) Peroxiredoxin Systems , pp. 219-229
    • Deponte, M.1    Rahlfs, S.2    Becker, K.3
  • 63
    • 0027601567 scopus 로고
    • A redescription of Entamoeba histolytica Schaudinn, 1903 (Emended Walker, 1911) separating it from Entamoeba dispar Brumpt, 1925
    • Diamond LS and Clark CG. A redescription of Entamoeba histolytica Schaudinn, 1903 (Emended Walker, 1911) separating it from Entamoeba dispar Brumpt, 1925. J Eukaryot Microbiol 40: 340-344, 1993.
    • (1993) J Eukaryot Microbiol , vol.40 , pp. 340-344
    • Diamond, L.S.1    Clark, C.G.2
  • 64
    • 80051673172 scopus 로고    scopus 로고
    • Differential expression of Trypanosoma cruzi I associated with clinical forms of Chagas disease: Overexpression of oxidative stress proteins in acute patient isolate
    • Diaz M, Solari A, and Gonzalez C. Differential expression of Trypanosoma cruzi I associated with clinical forms of Chagas disease: overexpression of oxidative stress proteins in acute patient isolate. J Proteomics 74: 1673-1682, 2011.
    • (2011) J Proteomics , vol.74 , pp. 1673-1682
    • Diaz, M.1    Solari, A.2    Gonzalez, C.3
  • 65
    • 79960934330 scopus 로고    scopus 로고
    • A tryparedoxin-dependent peroxidase protects African trypanosomes from membrane damage
    • Diechtierow M and Krauth-Siegel R. A tryparedoxin-dependent peroxidase protects African trypanosomes from membrane damage. Free Radic Biol Med 51: 856-868, 2011.
    • (2011) Free Radic Biol Med , vol.51 , pp. 856-868
    • Diechtierow, M.1    Krauth-Siegel, R.2
  • 66
    • 0347595338 scopus 로고    scopus 로고
    • The antioxidant systems in Toxoplasma gondii and the role of cytosolic catalase in defence against oxidative injury
    • DOI 10.1046/j.1365-2958.2003.03823.x
    • Ding M, Kwok LY, Schluter D, Clayton C, and Soldati D. The antioxidant systems in Toxoplasma gondii and the role of cytosolic catalase in defence against oxidative injury. Mol Microbiol 51: 47-61, 2004. (Pubitemid 38031070)
    • (2004) Molecular Microbiology , vol.51 , Issue.1 , pp. 47-61
    • Kwok, L.Y.1    Schluter, D.2    Clayton, C.3    Soldati, D.4
  • 67
    • 11144316758 scopus 로고    scopus 로고
    • Thioredoxin peroxidase secreted by Fasciola hepatica induces the alternative activation of macrophages
    • DOI 10.1128/IAI.73.1.166-173.2005
    • Donnelly S, O'Neill S, Sekiya M, Mulcahy G, and Dalton J. Thioredoxin peroxidase secreted by Fasciola hepatica induces the alternative activation of macrophages. Infect Immun 73: 166-173, 2005. (Pubitemid 40041106)
    • (2005) Infection and Immunity , vol.73 , Issue.1 , pp. 166-173
    • Donnelly, S.1    O'Neill, S.M.2    Sekiya, M.3    Mulcahy, G.4    Dalton, J.P.5
  • 68
    • 55549093092 scopus 로고    scopus 로고
    • Helminth 2-Cys peroxiredoxin drives Th2 responses through a mechanism involving alternatively activated macrophages
    • Donnelly S, Stack C, O'Neill S, Sayed A, Williams D, and Dalton J. Helminth 2-Cys peroxiredoxin drives Th2 responses through a mechanism involving alternatively activated macrophages. FASEB J 22: 4022-4032, 2008.
    • (2008) FASEB J , vol.22 , pp. 4022-4032
    • Donnelly, S.1    Stack, C.2    O'Neill, S.3    Sayed, A.4    Williams, D.5    Dalton, J.6
  • 69
    • 58149479333 scopus 로고    scopus 로고
    • Schistosoma mansoni ex vivo lungstage larvae excretory-secretory antigens as vaccine candidates against schistosomiasis
    • El Ridi R and Tallima H. Schistosoma mansoni ex vivo lungstage larvae excretory-secretory antigens as vaccine candidates against schistosomiasis. Vaccine 27: 666-673, 2009.
    • (2009) Vaccine , vol.27 , pp. 666-673
    • El Ridi, R.1    Tallima, H.2
  • 70
    • 0028129543 scopus 로고
    • Antioxidant defences in the microaerophilic protozoan Trichomonas vaginalis: Comparison of metronidazole-resistant and sensitive strains
    • Ellis JE, Yarlett N, Cole D, Humphreys MJ, and Lloyd D. Antioxidant defences in the microaerophilic protozoan Trichomonas vaginalis: comparison of metronidazole-resistant and sensitive strains. Microbiology 140: 2489-2494, 1994. (Pubitemid 24297057)
    • (1994) Microbiology , vol.140 , Issue.9 , pp. 2489-2494
    • Ellis, J.E.1    Yarlett, N.2    Cole, D.3    Humphreys, M.J.4    Lloyd, D.5
  • 71
    • 34248531753 scopus 로고    scopus 로고
    • Locating proteins in the cell using TargetP, SignalP and related tools
    • DOI 10.1038/nprot.2007.131, PII NPROT.2007.131
    • Emanuelsson O, Brunak S, von Heijne G, and Nielsen H. Locating proteins in the cell using TargetP, SignalP and related tools. Nat Protoc 2: 953-971, 2007. (Pubitemid 46745592)
    • (2007) Nature Protocols , vol.2 , Issue.4 , pp. 953-971
    • Emanuelsson, O.1    Brunak, S.2    Von, H.G.3    Nielsen, H.4
  • 72
    • 80052472498 scopus 로고    scopus 로고
    • Cloning, expression and dynamic simulation of TRYP6 from Leishmania major (MRHO/IR/ 75/ER)
    • Eslami G, Frikha F, Salehi R, Khamesipour A, Hejazi H, and Nilforoushzadeh M. Cloning, expression and dynamic simulation of TRYP6 from Leishmania major (MRHO/IR/ 75/ER). Mol Biol Rep 38: 3765-3776, 2011.
    • (2011) Mol Biol Rep , vol.38 , pp. 3765-3776
    • Eslami, G.1    Frikha, F.2    Salehi, R.3    Khamesipour, A.4    Hejazi, H.5    Nilforoushzadeh, M.6
  • 73
    • 0021327406 scopus 로고
    • Entamoeba histolytica: A eukaryote without glutathione metabolism
    • Fahey R, Newton G, Arrick B, and Overdank-Bogart T. Entamoeba histolytica: a eukaryote without glutathione metabolism. Science 224: 70-72, 1984. (Pubitemid 14171643)
    • (1984) Science , vol.224 , Issue.4644 , pp. 70-72
    • Fahey, R.C.1    Newton, G.L.2    Arrick, B.3
  • 75
    • 0142153849 scopus 로고    scopus 로고
    • Bacterial catalase in the microsporidian Nosema locustae: Implications for microsporidian metabolism and genome evolution
    • DOI 10.1128/EC.2.5.1069-1075.2003
    • Fast NM, Law JS, Williams BAP, and Keeling PJ. Bacterial catalase in the microsporidian Nosema locustae: implications for microsporidian metabolism and genome evolution. Eukaryot cell 2: 1069-1075, 2003. (Pubitemid 37298721)
    • (2003) Eukaryotic Cell , vol.2 , Issue.5 , pp. 1069-1075
    • Fast, N.M.1    Law, J.S.2    Williams, B.A.P.3    Keeling, P.J.4
  • 76
    • 0000122573 scopus 로고
    • PHYLIP - Phylogeny Inference Package (Version 3.2)
    • Felsenstein J. PHYLIP - Phylogeny Inference Package (Version 3.2). Cladistics 5: 164-166, 1989.
    • (1989) Cladistics , vol.5 , pp. 164-166
    • Felsenstein, J.1
  • 79
    • 77956207316 scopus 로고    scopus 로고
    • Changing paradigms in thiology from antioxidant defense toward redox regulation
    • Flohé L. Changing paradigms in thiology from antioxidant defense toward redox regulation. Methods Enzymol 473: 1-39, 2010.
    • (2010) Methods Enzymol , vol.473 , pp. 1-39
    • Flohé, L.1
  • 81
    • 0347916885 scopus 로고    scopus 로고
    • Peroxiredoxins in antioxidant defense and redox regulation
    • Flohé L, Budde H, and Hofmann B. Peroxiredoxins in antioxidant defense and redox regulation. Biofactors 19: 3-10, 2003. (Pubitemid 38073139)
    • (2003) BioFactors , vol.19 , Issue.1-2 , pp. 3-10
    • Flohe, L.1    Budde, H.2    Hofmann, B.3
  • 82
    • 0027513131 scopus 로고
    • Structural analysis and demonstration of the 29 kDa antigen of pathogenic Entamoeba histolytica as the major accessible free thiol-containing surface protein
    • Flores BM, Batzer MA, Stein MA, Petersen C, Diedrich DL, and Torian BE. Structural analysis and demonstration of the 29 kDa antigen of pathogenic Entamoeba histolytica as the major accessible free thiol-containing surface protein. Mol Microbiol 7: 755-763, 1993. (Pubitemid 23090357)
    • (1993) Molecular Microbiology , vol.7 , Issue.5 , pp. 755-763
    • Flores, B.M.1    Batzer, M.A.2    Stein, M.A.3    Petersen, C.4    Diedrich, D.L.5    Torian, B.E.6
  • 88
    • 77950806408 scopus 로고    scopus 로고
    • New algorithms and methods to estimate maximum-likelihood phylogenies: Assessing the performance of PhyML 3.0
    • Guindon S, Dufayard JF, Lefort V, Anisimova M, Hordijk W, and Gascuel O. New algorithms and methods to estimate maximum-likelihood phylogenies: assessing the performance of PhyML 3.0. Syst Biol 59: 307-321, 2010.
    • (2010) Syst Biol , vol.59 , pp. 307-321
    • Guindon, S.1    Dufayard, J.F.2    Lefort, V.3    Anisimova, M.4    Hordijk, W.5    Gascuel, O.6
  • 89
    • 64149085448 scopus 로고    scopus 로고
    • Typical 2-Cys peroxiredoxins-structures, mechanisms and functions
    • Hall A, Karplus PA, and Poole LB. Typical 2-Cys peroxiredoxins- structures, mechanisms and functions. FEBS J 276: 2469-2477, 2009.
    • (2009) FEBS J , vol.276 , pp. 2469-2477
    • Hall, A.1    Karplus, P.A.2    Poole, L.B.3
  • 90
    • 79958059617 scopus 로고    scopus 로고
    • Structurebased insights into the catalytic power and conformational dexterity of peroxiredoxins
    • Hall A, Nelson KJ, Poole LB, and Karplus PA. Structurebased insights into the catalytic power and conformational dexterity of peroxiredoxins. Antioxid Redox Signal 15: 795- 815, 2011.
    • (2011) Antioxid Redox Signal , vol.15 , pp. 795-815
    • Hall, A.1    Nelson, K.J.2    Poole, L.B.3    Karplus, P.A.4
  • 91
    • 67649595320 scopus 로고    scopus 로고
    • Redox-dependent dynamics of a dual thioredoxin fold protein: Evolution of specialized folds
    • Hall A, Parsonage D, Horita D, Karplus PA, Poole LB, and Barbar E. Redox-dependent dynamics of a dual thioredoxin fold protein: evolution of specialized folds. Biochemistry 48: 5984-5993, 2009.
    • (2009) Biochemistry , vol.48 , pp. 5984-5993
    • Hall, A.1    Parsonage, D.2    Horita, D.3    Karplus, P.A.4    Poole, L.B.5    Barbar, E.6
  • 92
    • 77956171017 scopus 로고    scopus 로고
    • Structural evidence that peroxiredoxin catalytic power is based on transition-state stabilization
    • Hall A, Parsonage D, Poole LB, and Karplus PA. Structural evidence that peroxiredoxin catalytic power is based on transition-state stabilization. J Mol Biol 402: 194-209, 2010.
    • (2010) J Mol Biol , vol.402 , pp. 194-209
    • Hall, A.1    Parsonage, D.2    Poole, L.B.3    Karplus, P.A.4
  • 93
    • 70349840614 scopus 로고    scopus 로고
    • Structural changes common to catalysis in the Tpx peroxiredoxin subfamily
    • Hall A, Sankaran B, Poole LB, and Karplus PA. structural changes common to catalysis in the Tpx peroxiredoxin subfamily. J Mol Biol 393: 867-881, 2009.
    • (2009) J Mol Biol , vol.393 , pp. 867-881
    • Hall, A.1    Sankaran, B.2    Poole, L.B.3    Karplus, P.A.4
  • 94
    • 0036672707 scopus 로고    scopus 로고
    • Homology modeling and docking mechanism of the mercaptosuccinate and methotrexate to P. falciparum 1- Cys peroxiredoxin: A preliminary molecular study
    • Hamza A. Homology modeling and docking mechanism of the mercaptosuccinate and methotrexate to P. falciparum 1- Cys peroxiredoxin: a preliminary molecular study. J Biomol Struct Dyn 20: 7-20, 2002.
    • (2002) J Biomol Struct Dyn , vol.20 , pp. 7-20
    • Hamza, A.1
  • 96
    • 33646909087 scopus 로고    scopus 로고
    • Expression of a mitochondrial peroxiredoxin prevents programmed cell death in Leishmania donovani
    • DOI 10.1128/EC.5.5.861-870.2006
    • Harder S, Bente M, Isermann K, and Bruchhaus I. Expression of a mitochondrial peroxiredoxin prevents programmed cell death in Leishmania donovani. Eukaryot Cell 5: 861-870, 2006. (Pubitemid 43794484)
    • (2006) Eukaryotic Cell , vol.5 , Issue.5 , pp. 861-870
    • Harder, S.1    Bente, M.2    Isermann, K.3    Bruchhaus, I.4
  • 97
    • 38749099103 scopus 로고    scopus 로고
    • Peroxiredoxins in the central nervous system
    • edited by Flohé L and Harris JR. New York: Springer
    • Hattori F and Oikawa S. Peroxiredoxins in the central nervous system. In: Peroxiredoxin Systems, edited by Flohé L and Harris JR. New York: Springer, 2007, pp. 357-374.
    • (2007) Peroxiredoxin Systems , pp. 357-374
    • Hattori, F.1    Oikawa, S.2
  • 99
    • 77955283075 scopus 로고    scopus 로고
    • "Manifesto" for advancing the control and elimination of neglected tropical diseases
    • Hotez P and Pecoul B. "Manifesto" for advancing the control and elimination of neglected tropical diseases. PLoS Negl Trop Dis 4: e718, 2010.
    • (2010) PLoS Negl Trop Dis , vol.4
    • Hotez, P.1    Pecoul, B.2
  • 100
    • 46749101803 scopus 로고    scopus 로고
    • Immunolocalization of the antioxidant protein TPx of Echinococcus granulosus
    • abstract of Chinese-language article
    • Hou Q, Wang H, Zhang Z, Cao W, Zhang F, and Zhang W. [Immunolocalization of the antioxidant protein TPx of Echinococcus granulosus] (abstract of Chinese-language article). Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi 23: 998-1000, 2007.
    • (2007) Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi , vol.23 , pp. 998-1000
    • Hou, Q.1    Wang, H.2    Zhang, Z.3    Cao, W.4    Zhang, F.5    Zhang, W.6
  • 101
    • 38049132516 scopus 로고    scopus 로고
    • Divergence of trypanothione-dependent tryparedoxin cascade into cytosolic and mitochondrial pathways in arsenite-resistant variants of Leishmania amazonensis
    • Hsu J-Y, Lin Y-C, Chiang S-C, and Lee S. Divergence of trypanothione-dependent tryparedoxin cascade into cytosolic and mitochondrial pathways in arsenite-resistant variants of Leishmania amazonensis. Mol Biochem Parasitol 157: 193-204, 2008.
    • (2008) Mol Biochem Parasitol , vol.157 , pp. 193-204
    • Hsu, J.-Y.1    Lin, Y.-C.2    Chiang, S.-C.3    Lee, S.4
  • 103
    • 70350050576 scopus 로고    scopus 로고
    • Thiol and sulfenic acid oxidation of AhpE, the one-cysteine peroxiredoxin from Mycobacterium tuberculosis: Kinetics, acidity constants, and conformational dynamics
    • Hugo M, Turell L, Manta B, Botti H, Monteiro G, Netto L, Alvarez B, Radi R, and Trujillo M. Thiol and sulfenic acid oxidation of AhpE, the one-cysteine peroxiredoxin from Mycobacterium tuberculosis: kinetics, acidity constants, and conformational dynamics. Biochemistry 48: 9416-9426, 2009.
    • (2009) Biochemistry , vol.48 , pp. 9416-9426
    • Hugo, M.1    Turell, L.2    Manta, B.3    Botti, H.4    Monteiro, G.5    Netto, L.6    Alvarez, B.7    Radi, R.8    Trujillo, M.9
  • 104
    • 38649086440 scopus 로고    scopus 로고
    • Trichostatin A regulates peroxiredoxin expression and virulence of the parasite Entamoeba histolytica
    • DOI 10.1016/j.molbiopara.2007.11.014, PII S0166685107003325
    • Isakov E, Siman-Tov R, Weber C, Guillen N, and Ankri S. Trichostatin A regulates peroxiredoxin expression and virulence of the parasite Entamoeba histolytica. Mol Biochem Parasitol 158: 82-94, 2008. (Pubitemid 351172466)
    • (2008) Molecular and Biochemical Parasitology , vol.158 , Issue.1 , pp. 82-94
    • Isakov, E.1    Siman-Tov, R.2    Weber, C.3    Guillen, N.4    Ankri, S.5
  • 105
    • 38749124409 scopus 로고    scopus 로고
    • Stress-induced peroxiredoxins
    • edited by Flohé L and Harris JR. New York: Springer
    • Ishii T and Yanagawa T. Stress-induced peroxiredoxins. In: Peroxiredoxin Systems, edited by Flohé L and Harris JR. New York: Springer, 2007, pp. 375-384.
    • (2007) Peroxiredoxin Systems , pp. 375-384
    • Ishii, T.1    Yanagawa, T.2
  • 106
    • 41049101045 scopus 로고    scopus 로고
    • Crucial role of cytosolic tryparedoxin peroxidase in Leishmania donovani survival, drug response and virulence
    • DOI 10.1111/j.1365-2958.2008.06154.x
    • Iyer J, Kaprakkaden A, Choudhary M, and Shaha C. Crucial role of cytosolic tryparedoxin peroxidase in Leishmania donovani survival, drug response and virulence. Mol Microbiol 68: 372-391, 2008. (Pubitemid 351422957)
    • (2008) Molecular Microbiology , vol.68 , Issue.2 , pp. 372-391
    • Iyer, J.P.1    Kaprakkaden, A.2    Choudhary, M.L.3    Shaha, C.4
  • 107
    • 33749005947 scopus 로고    scopus 로고
    • The thiol-based redox networks of pathogens: Unexploited targets in the search for new drugs
    • Free Radicals in Biology and Medicine: From Inflammation to Biotechnology
    • Jaeger T and Flohe L. The thiol-based redox networks of pathogens: unexploited targets in the search for new drugs. Biofactors 27: 109-120, 2006. (Pubitemid 44444593)
    • (2006) BioFactors , vol.27 , Issue.1-4 , pp. 109-120
    • Jaeger, T.1    Flohe, L.2
  • 108
    • 85047681481 scopus 로고    scopus 로고
    • Proteomic analysis of Fasciola hepatica excretory-secretory products
    • DOI 10.1002/1615-9861(200109)1:9<1128::AID-PROT1128>3.0.CO;2-0
    • Jefferies J, Campbell A, van Rossum A, Barrett J, and Brophy P. Proteomic analysis of Fasciola hepatica excretorysecretory products. Proteomics 1: 1128-1132, 2001. (Pubitemid 33696478)
    • (2001) Proteomics , vol.1 , Issue.9 , pp. 1128-1132
    • Jefferies, J.R.1    Campbell, A.M.2    Van Rossum, A.J.3    Barrett, J.4    Brophy, P.M.5
  • 109
    • 0034723165 scopus 로고    scopus 로고
    • Thioredoxin-dependent hydroperoxide peroxidase activity of bacterioferritin comigratory protein (BCP) as a new member of the thiol- specific antioxidant protein (TSA)/alkyl hydroperoxide peroxidase C (AhpC) family
    • DOI 10.1074/jbc.275.4.2924
    • Jeong W, Cha MK, and Kim IH. Thioredoxin-dependent hydroperoxide peroxidase activity of bacterioferritin comigratory protein (BCP) as a new member of the thiolspecific antioxidant protein (TSA)/Alkyl hydroperoxide peroxidase C (AhpC) family. J Biol Chem 275: 2924-2930, 2000. (Pubitemid 30082068)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.4 , pp. 2924-2930
    • Jeong, W.1    Cha, M.-K.2    Kim, I.-H.3
  • 110
    • 7444235416 scopus 로고    scopus 로고
    • Entamoeba histolytica: cDNAs cloned as 30 kDa collagen-binding proteins (CBP) belong to an antioxidant molecule family. Protection of hamsters from amoebic liver abscess by immunization with recombinant CBP
    • DOI 10.1016/j.exppara.2004.06.007, PII S0014489404001158
    • Jiménez-Delgadillo B, Chaudhuri PP, Baylón-Pacheco L, López-Monteon A, Talamás-Rohana P, and Rosales-Encina JL. Entamoeba histolytica: cDNAs cloned as 30 kDa collagenbinding proteins (CBP) belong to an antioxidant molecule family. Protection of hamsters from amoebic liver abscess by immunization with recombinant CBP. Exp Parasitol 108: 7-17, 2004. (Pubitemid 39445850)
    • (2004) Experimental Parasitology , vol.108 , Issue.1-2 , pp. 7-17
    • Jimenez-Delgadillo, B.1    Chaudhuri, P.P.2    Baylon-Pacheco, L.3    Lopez-Monteon, A.4    Talamas-Rohana, P.5    Rosales-Encina, J.L.6
  • 111
    • 79951964628 scopus 로고    scopus 로고
    • Comparative proteomic analysis of the promastigotes and amastigotes of Leishmania donovani
    • abstract of Chinese-language article
    • Jing B, Deng S, Zhang R, and Zhang J. [Comparative proteomic analysis of the promastigotes and amastigotes of Leishmania donovani] (abstract of Chinese-language article). Zhongguo Ji Sheng Chong Xue Yu Ji Sheng Chong Bing Za Zhi 27: 102-106, 2009.
    • (2009) Zhongguo Ji Sheng Chong Xue Yu Ji Sheng Chong Bing Za Zhi , vol.27 , pp. 102-106
    • Jing, B.1    Deng, S.2    Zhang, R.3    Zhang, J.4
  • 112
    • 33748755649 scopus 로고    scopus 로고
    • Identification, sequencing and expression of peroxidoxin genes from Leishmania aethiopica
    • DOI 10.1016/j.actatropica.2006.08.001, PII S0001706X06001367
    • Jirata D, Kuru T, Genetu A, Barr S, Hailu A, Aseffa A, and Gedamu L. Identification, sequencing and expression of peroxidoxin genes from Leishmania aethiopica. Acta Trop 99: 88-96, 2006. (Pubitemid 44402246)
    • (2006) Acta Tropica , vol.99 , Issue.1 , pp. 88-96
    • Jirata, D.1    Kuru, T.2    Genetu, A.3    Barr, S.4    Hailu, A.5    Aseffa, A.6    Gedamu, L.7
  • 113
    • 38749116271 scopus 로고    scopus 로고
    • The peroxiredoxin repair proteins
    • edited by Flohé L and Harris JR. New York: Springer
    • Jönsson T and Lowther W. The peroxiredoxin repair proteins. In: Peroxiredoxin Systems, edited by Flohé L and Harris JR. New York: Springer, 2007, pp. 115-141.
    • (2007) Peroxiredoxin Systems , pp. 115-141
    • Jönsson, T.1    Lowther, W.2
  • 114
    • 67649220210 scopus 로고    scopus 로고
    • Identification of a serodiagnostic antigen, legumain, by immunoproteomic analysis of excretory-secretory products of Clonorchis sinensis adult worms
    • Ju J, Joo H, Lee M, Cho S, Cheun H, Kim J, Lee Y, Lee K, Sohn W, Kim D, Kim I, Park B, and Kim T. Identification of a serodiagnostic antigen, legumain, by immunoproteomic analysis of excretory-secretory products of Clonorchis sinensis adult worms. Proteomics 9: 3066-3078, 2009.
    • (2009) Proteomics , vol.9 , pp. 3066-3078
    • Ju, J.1    Joo, H.2    Lee, M.3    Cho, S.4    Cheun, H.5    Kim, J.6    Lee, Y.7    Lee, K.8    Sohn, W.9    Kim, D.10    Kim, I.11    Park, B.12    Kim, T.13
  • 115
    • 0032513056 scopus 로고    scopus 로고
    • Characterization of a mammalian peroxiredoxin that contains one conserved cysteine
    • DOI 10.1074/jbc.273.11.6303
    • Kang S, Baines I, and Rhee S. Characterization of a mammalian peroxiredoxin that contains one conserved cysteine. J Biol Chem 273: 6303-6311, 1998. (Pubitemid 28144720)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.11 , pp. 6303-6311
    • Kang, S.W.1    Baines, I.C.2    Rhee, S.G.3
  • 116
    • 28244495868 scopus 로고    scopus 로고
    • 2-Cys peroxiredoxin function in intracellular signal transduction: Therapeutic implications
    • DOI 10.1016/j.molmed.2005.10.006, PII S1471491405002406
    • Kang S, Rhee S, Chang T-S, Jeong W, and Choi M. 2-Cys peroxiredoxin function in intracellular signal transduction: therapeutic implications. Trends Mol Med 11: 571-578, 2005. (Pubitemid 41713999)
    • (2005) Trends in Molecular Medicine , vol.11 , Issue.12 , pp. 571-578
    • Kang, S.W.1    Rhee, S.G.2    Chang, T.-S.3    Jeong, W.4    Choi, M.H.5
  • 117
    • 17144413378 scopus 로고    scopus 로고
    • Roles of 1-Cys peroxiredoxin in haem detoxification in the human malaria parasite Plasmodium falciparum
    • DOI 10.1111/j.1742-4658.2005.04611.x
    • Kawazu S, Ikenoue N, Takemae H, Komaki-Yasuda K, and Kano S. Roles of 1-Cys peroxiredoxin in haem detoxification in the human malaria parasite Plasmodium falciparum. FEBS J 272: 1784-1791, 2005. (Pubitemid 40516227)
    • (2005) FEBS Journal , vol.272 , Issue.7 , pp. 1784-1791
    • Kawazu, S.-I.1    Ikenoue, N.2    Takemae, H.3    Komaki-Yasuda, K.4    Kano, S.5
  • 120
    • 0033844270 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a peroxiredoxin from the human malaria parasite Plasmodium falciparum
    • DOI 10.1016/S0166-6851(00)00243-7, PII S0166685100002437
    • Kawazu S, Tsuji N, Hatabu T, Kawai S, Matsumoto Y, and Kano S. Molecular cloning and characterization of a peroxiredoxin from the human malaria parasite Plasmodium falciparum. Mol Biochem Parasitol 109: 165-169, 2000. (Pubitemid 30665413)
    • (2000) Molecular and Biochemical Parasitology , vol.109 , Issue.2 , pp. 165-169
    • Kawazu, S.-I.1    Tsuji, N.2    Hatabu, T.3    Kawai, S.4    Matsumoto, Y.5    Kano, S.6
  • 122
    • 70350228923 scopus 로고    scopus 로고
    • Immunodominant antigens in Naegleria fowleri excretory- Secretory proteins were potential pathogenic factors
    • Kim J, Yang A, Sohn H, Kim D, Song K, and Shin H. Immunodominant antigens in Naegleria fowleri excretory- secretory proteins were potential pathogenic factors. Parasitol Res 105: 1675-1681, 2009.
    • (2009) Parasitol Res , vol.105 , pp. 1675-1681
    • Kim, J.1    Yang, A.2    Sohn, H.3    Kim, D.4    Song, K.5    Shin, H.6
  • 123
    • 0023929362 scopus 로고
    • The isolation and purification of a specific ''protector'' protein which inhibits enzyme inactivation by a thiol/Fe(III)/O2 mixed-function oxidation system
    • Kim K, Kim IH, Lee KY, Rhee SG, and Stadtman ER. The isolation and purification of a specific ''protector'' protein which inhibits enzyme inactivation by a thiol/Fe(III)/O2 mixed-function oxidation system. J Biochem 263: 4704-4711, 1988.
    • (1988) J Biochem , vol.263 , pp. 4704-4711
    • Kim, K.1    Kim, I.H.2    Lee, K.Y.3    Rhee, S.G.4    Stadtman, E.R.5
  • 124
    • 0038532262 scopus 로고    scopus 로고
    • The tetrameric structure of Haemophilus influenza hybrid Prx5 reveals interactions between electron donor and acceptor proteins
    • DOI 10.1074/jbc.M209553200
    • Kim SJ, Woo JR, Hwang YS, Jeong DG, Shin DH, Kim K, and Ryu SE. The tetrameric structure of Haemophilus influenza hybrid Prx5 reveals interactions between electron donor and acceptor proteins. J Biochem 278: 10790-10798, 2003. (Pubitemid 36800352)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.12 , pp. 10790-10798
    • Kim, S.J.1    Woo, J.R.2    Hwang, Y.S.3    Jeong, D.G.4    Shin, D.H.5    Kim, K.6    Ryu, S.E.7
  • 125
    • 78449236372 scopus 로고    scopus 로고
    • Identification of Leishmania proteins preferentially released in infected cells using change mediated antigen technology (CMAT)
    • pii e842
    • Kima P, Bonilla J, Cho E, Ndjamen B, Canton J, Leal N, and Handfield M. Identification of Leishmania proteins preferentially released in infected cells using change mediated antigen technology (CMAT). PLoS Negl Trop Dis 4: pii e842, 2010.
    • (2010) PLoS Negl Trop Dis , vol.4
    • Kima, P.1    Bonilla, J.2    Cho, E.3    Ndjamen, B.4    Canton, J.5    Leal, N.6    Handfield, M.7
  • 127
    • 0024315131 scopus 로고
    • A 60-kDa Plasmodium falciparum protein at the moving junction formed between merozoite and erythrocyte during invasion
    • Klotz FW, Hadley TJ, Aikawa M, Leech J, Howard RJ, and Miller LH. A 60-kDa Plasmodium falciparum protein at the moving junction formed between merozoite and erythrocyte during invasion. Mol Biochem Parasitol 36: 177-185, 1989.
    • (1989) Mol Biochem Parasitol , vol.36 , pp. 177-185
    • Klotz, F.W.1    Hadley, T.J.2    Aikawa, M.3    Leech, J.4    Howard, R.J.5    Miller, L.H.6
  • 128
    • 38749091365 scopus 로고    scopus 로고
    • Evolution of the peroxiredoxins
    • edited by Flohé L and Harris JR. New York: Springer
    • Knoops B, Loumaye E, and Van Der Eecken V. Evolution of the peroxiredoxins. In: Peroxiredoxin Systems, edited by Flohé L and Harris JR. New York: Springer, 2007, pp. 27-40.
    • (2007) Peroxiredoxin Systems , pp. 27-40
    • Knoops, B.1    Loumaye, E.2    Van Der Eecken, V.3
  • 129
    • 0038643671 scopus 로고    scopus 로고
    • Disruption of the Plasmodium falciparum 2-Cys peroxiredoxin gene renders parasites hypersensitive to reactive oxygen and nitrogen species
    • DOI 10.1016/S0014-5793(03)00694-X
    • Komaki-Yasuda K, Kawazu S, and Kano S. Disruption of the Plasmodium falciparum 2-Cys peroxiredoxin gene renders parasites hypersensitive to reactive oxygen and nitrogen species. FEBS Lett 547: 140-144, 2003. (Pubitemid 36829394)
    • (2003) FEBS Letters , vol.547 , Issue.1-3 , pp. 140-144
    • Komaki-Yasuda, K.1    Kawazu, S.-I.2    Kano, S.3
  • 130
    • 52049108023 scopus 로고    scopus 로고
    • 5¢ sequence- and chromatin modificationdependent gene expression in Plasmodium falciparum erythrocytic stage
    • Komaki-Yasuda K, Okuwaki M, Kano S, Nagata K, and Kawazu S. 5¢ sequence- and chromatin modificationdependent gene expression in Plasmodium falciparum erythrocytic stage. Mol Biochem Parasitol 162: 40-51, 2008.
    • (2008) Mol Biochem Parasitol , vol.162 , pp. 40-51
    • Komaki-Yasuda, K.1    Okuwaki, M.2    Kano, S.3    Nagata, K.4    Kawazu, S.5
  • 132
    • 0034306117 scopus 로고    scopus 로고
    • A novel peroxiredoxin of the plant Sedum lineare is a homologue of Escherichia coli bacterioferritin co-migratory protein (Bcp)
    • Kong W, Shiota S, Shi Y, Nakayama H, and Nakayama K. A novel peroxiredoxin of the plant Sedum lineare is a homologue of Escherichia coli bacterioferritin co-migratory protein (Bcp). Biochem J 351: 107-114, 2000.
    • (2000) Biochem J , vol.351 , pp. 107-114
    • Kong, W.1    Shiota, S.2    Shi, Y.3    Nakayama, H.4    Nakayama, K.5
  • 133
    • 35449006342 scopus 로고    scopus 로고
    • A comparative study of type I and type II tryparedoxin peroxidases in Leishmania major
    • DOI 10.1111/j.1742-4658.2007.06087.x
    • Konig J and Fairlamb A. A comparative study of type I and type II tryparedoxin peroxidases in Leishmania major. FEBS J 274: 5643-5658, 2007. (Pubitemid 47622078)
    • (2007) FEBS Journal , vol.274 , Issue.21 , pp. 5643-5658
    • Konig, J.1    Fairlamb, A.H.2
  • 134
    • 79953128738 scopus 로고    scopus 로고
    • Antitumor quinol PMX464 is a cytocidal antitrypanosomal inhibitor targeting trypanothione metabolism
    • Konig J, Wyllie S, Wells G, Stevens M, Wyatt P, and Fairlamb A. Antitumor quinol PMX464 is a cytocidal antitrypanosomal inhibitor targeting trypanothione metabolism. J Biol Chem 286: 8523-8533, 2011.
    • (2011) J Biol Chem , vol.286 , pp. 8523-8533
    • Konig, J.1    Wyllie, S.2    Wells, G.3    Stevens, M.4    Wyatt, P.5    Fairlamb, A.6
  • 135
    • 38749141425 scopus 로고    scopus 로고
    • The trypanothione system
    • edited by Flohé L and Harris JR. New York: Springer
    • Krauth-Siegel L, Comini M, and Schlecker T. The trypanothione system. In: Peroxiredoxin Systems, edited by Flohé L and Harris JR. New York: Springer, 2007, pp. 231-251.
    • (2007) Peroxiredoxin Systems , pp. 231-251
    • Krauth-Siegel, L.1    Comini, M.2    Schlecker, T.3
  • 136
    • 13444280474 scopus 로고    scopus 로고
    • Dithiol proteins as guardians of the intracellular redox milieu in parasites: Old and new drug targets in trypanosomes and malaria-causing plasmodia
    • DOI 10.1002/anie.200300639
    • Krauth-Siegel R, Bauer H, and Schirmer R. Dithiol proteins as guardians of the intracellular redox milieu in parasites: old and new drug targets in trypanosomes and malariacausing plasmodia. Angew Chem Int Ed Engl 44: 690-715, 2005. (Pubitemid 40203977)
    • (2005) Angewandte Chemie - International Edition , vol.44 , Issue.5 , pp. 690-715
    • Krauth-Siegel, R.L.1    Bauer, H.2    Schirmer, R.H.3
  • 137
    • 0035815346 scopus 로고    scopus 로고
    • Isolation and functional analysis of two thioredoxin peroxidases (peroxiredoxins) from Plasmodium falciparum
    • Krnajski Z, Walter R, and Müller S. Isolation and functional analysis of two thioredoxin peroxidases (peroxiredoxins) from Plasmodium falciparum. Mol Biochem Parasitol 113: 303- 308, 2001.
    • (2001) Mol Biochem Parasitol , vol.113 , pp. 303-308
    • Krnajski, Z.1    Walter, R.2    Müller, S.3
  • 138
    • 33748787143 scopus 로고    scopus 로고
    • 2-Cys peroxiredoxins from Schistosoma japonicum: The expression profile and localization in the life cycle
    • DOI 10.1016/j.molbiopara.2006.05.004, PII S0166685106001460
    • Kumagai T, Osada Y, and Kanazawa T. 2-Cys peroxiredoxins from Schistosoma japonicum: the expression profile and localization in the life cycle. Mol Biochem Parasitol 149: 135-143, 2006. (Pubitemid 44403931)
    • (2006) Molecular and Biochemical Parasitology , vol.149 , Issue.2 , pp. 135-143
    • Kumagai, T.1    Osada, Y.2    Kanazawa, T.3
  • 139
    • 58549104705 scopus 로고    scopus 로고
    • Peroxiredoxin- 1 from Schistosoma japonicum functions as a scavenger against hydrogen peroxide but not nitric oxide
    • Kumagai T, Osada Y, Ohta N, and Kanazawa T. Peroxiredoxin- 1 from Schistosoma japonicum functions as a scavenger against hydrogen peroxide but not nitric oxide. Mol Biochem Parasitol 164: 26-31, 2009.
    • (2009) Mol Biochem Parasitol , vol.164 , pp. 26-31
    • Kumagai, T.1    Osada, Y.2    Ohta, N.3    Kanazawa, T.4
  • 140
    • 0033783654 scopus 로고    scopus 로고
    • Molecular and enzymatic characterization of Schistosoma mansoni thioredoxin peroxidase
    • Kwatia M, Botkin D, and Williams D. Molecular and enzymatic characterization of Schistosoma mansoni thioredoxin peroxidase. J Parasitol 86: 908-915, 2000.
    • (2000) J Parasitol , vol.86 , pp. 908-915
    • Kwatia, M.1    Botkin, D.2    Williams, D.3
  • 141
    • 0347595338 scopus 로고    scopus 로고
    • The antioxidant systems in Toxoplasma gondii and the role of cytosolic catalase in defence against oxidative injury
    • DOI 10.1046/j.1365-2958.2003.03823.x
    • Kwok L, Schlüter D, Clayton C, and Soldati D. The antioxidant systems in Toxoplasma gondii and the role of cytosolic catalase in defence against oxidative injury. Mol Microbiol 51: 47-61, 2003. (Pubitemid 38031070)
    • (2004) Molecular Microbiology , vol.51 , Issue.1 , pp. 47-61
    • Kwok, L.Y.1    Schluter, D.2    Clayton, C.3    Soldati, D.4
  • 142
    • 78650567500 scopus 로고    scopus 로고
    • Cryptosporidium parvum: Radiation-induced alteration of the oocyst proteome
    • Lee SU, Joung M, Nam T, Park WY, Ji YH, and Yu JR. Cryptosporidium parvum: radiation-induced alteration of the oocyst proteome. Exp Parasitol 127: 25-30, 2011.
    • (2011) Exp Parasitol , vol.127 , pp. 25-30
    • Lee, S.U.1    Joung, M.2    Nam, T.3    Park, W.Y.4    Ji, Y.H.5    Yu, J.R.6
  • 143
    • 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, and Duchene M. 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.
    • (2009) Mol Microbiol , vol.72 , pp. 518-536
    • Leitsch, D.1    Kolarich, D.2    Binder, M.3    Stadlmann, J.4    Altmann, F.5    Duchene, M.6
  • 144
    • 0032582721 scopus 로고    scopus 로고
    • Identification and characterisation of a functional peroxidoxin from Leishmania major
    • DOI 10.1016/S0166-6851(98)00122-4, PII S0166685198001224
    • Levick M, Tetaud E, Fairlamb A, and Blackwell J. Identification and characterisation of a functional peroxidoxin from Leishmania major. Mol Biochem Parasitol 96: 125-137, 1998. (Pubitemid 28511029)
    • (1998) Molecular and Biochemical Parasitology , vol.96 , Issue.1-2 , pp. 125-137
    • Levick, M.P.1    Tetaud, E.2    Fairlamb, A.H.3    Blackwell, J.M.4
  • 145
    • 0346056673 scopus 로고    scopus 로고
    • Functional expression and characterization of Echinococcus granulosus thioredoxin peroxidase suggests a role in protection against oxidative damage
    • DOI 10.1016/j.gene.2003.10.027
    • Li J, Zhang W, Loukas A, Lin R, Ito A, Zhang L, Jones M, and McManus D. Functional expression and characteriza- tion of Echinococcus granulosus thioredoxin peroxidase suggests a role in protection against oxidative damage. Gene 326: 157-165, 2004. (Pubitemid 38068497)
    • (2004) Gene , vol.326 , Issue.1-2 , pp. 157-165
    • Li, J.1    Zhang, W.-B.2    Loukas, A.3    Lin, R.-Y.4    Ito, A.5    Zhang, L.-H.6    Jones, M.7    McManus, D.P.8
  • 147
    • 67649867930 scopus 로고    scopus 로고
    • Insights into the alkyl peroxide reduction pathway of Xanthomonas campestris bacterioferritin comigratory protein from the trapped intermediate-ligand complex structures
    • Liao S-J, Yang C-Y, Chin K-H, Wang AHJ, and Chou S-H. Insights into the alkyl peroxide reduction pathway of Xanthomonas campestris bacterioferritin comigratory protein from the trapped intermediate-ligand complex structures. J Mol Biol 390: 951-966, 2009.
    • (2009) J Mol Biol , vol.390 , pp. 951-966
    • Liao, S.-J.1    Yang, C.-Y.2    Chin, K.-H.3    Wang, A.H.J.4    Chou, S.-H.5
  • 149
    • 19344372534 scopus 로고    scopus 로고
    • Distinct overexpression of cytosolic and mitochondrial tryparedoxin peroxidases results in preferential detoxification of different oxidants in arsenite-resistant Leishmania amazonensis with and without DNA amplification
    • DOI 10.1016/j.molbiopara.2005.03.009, PII S0166685105001064
    • Lin Y-C, Hsu J-Y, Chiang S-C, and Lee S. Distinct overexpression of cytosolic and mitochondrial tryparedoxin peroxidases results in preferential detoxification of different oxidants in arsenite-resistant Leishmania amazonensis with and without DNA amplification. Mol Biochem Parasitol 142: 66-75, 2005. (Pubitemid 40720129)
    • (2005) Molecular and Biochemical Parasitology , vol.142 , Issue.1 , pp. 66-75
    • Lin, Y.-C.1    Hsu, J.-Y.2    Chiang, S.-C.3    Lee, S.T.4
  • 152
    • 0032521486 scopus 로고    scopus 로고
    • Thioredoxin peroxidase from Onchocerca volvulus: A major hydrogen peroxide detoxifying enzyme in filarial parasites
    • DOI 10.1016/S0166-6851(97)00230-2, PII S0166685197002302
    • Lu W, Egerton G, Bianco A, and Williams S. Thioredoxin peroxidase from Onchocerca volvulus: a major hydrogen peroxide detoxifying enzyme in filarial parasites. Mol Biochem Parasitol 91: 221-235, 1998. (Pubitemid 28161455)
    • (1998) Molecular and Biochemical Parasitology , vol.91 , Issue.2 , pp. 221-235
    • Lu, W.1    Egerton, G.L.2    Bianco, A.E.3    Williams, S.A.4
  • 153
    • 29644443262 scopus 로고    scopus 로고
    • Identification of differentially expressed genes in virulent and nonvirulent Entamoeba species: Potential implications for amebic pathogenesis
    • DOI 10.1128/IAI.74.1.340-351.2006
    • MacFarlane R and Singh U. Identification of differentially expressed genes in virulent and nonvirulent Entamoeba species: potential implications for amebic pathogenesis. Infect Immun 74: 340-351, 2006. (Pubitemid 43023090)
    • (2006) Infection and Immunity , vol.74 , Issue.1 , pp. 340-351
    • MacFarlane, R.C.1    Singh, U.2
  • 154
    • 79955669959 scopus 로고    scopus 로고
    • Proliferative responses of Brugia malayi TPX-1 and its epitopic peptide(29-43) in an endemic population of human lymphatic filariasis
    • Madhumathi J, Anugraha G, Prince P, Pradiba D, and Kaliraj P. Proliferative responses of Brugia malayi TPX-1 and its epitopic peptide(29-43) in an endemic population of human lymphatic filariasis. Microbes Infect 13: 602-606, 2011.
    • (2011) Microbes Infect , vol.13 , pp. 602-606
    • Madhumathi, J.1    Anugraha, G.2    Prince, P.3    Pradiba, D.4    Kaliraj, P.5
  • 155
    • 78650475501 scopus 로고    scopus 로고
    • Identification of a highly immunoreactive epitope of Brugia malayi TPx recognized by the endemic sera
    • Madhumathi J, Prince P, Gayatri S, Aparnaa R, and Kaliraj P. Identification of a highly immunoreactive epitope of Brugia malayi TPx recognized by the endemic sera. J Parasitol 96: 1228-1229, 2010.
    • (2010) J Parasitol , vol.96 , pp. 1228-1229
    • Madhumathi, J.1    Prince, P.2    Gayatri, S.3    Aparnaa, R.4    Kaliraj, P.5
  • 157
    • 18844400905 scopus 로고    scopus 로고
    • Peroxiredoxin 6, a 1-Cys peroxiredoxin, functions in antioxidant defense and lung phospholipid metabolism
    • Manevich Y and Fisher AB. Peroxiredoxin 6, a 1-Cys peroxiredoxin, functions in antioxidant defense and lung phospholipid metabolism. Free Radic Biol Med 38: 1422- 1432, 2005.
    • (2005) Free Radic Biol Med , vol.38 , pp. 1422-1432
    • Manevich, Y.1    Fisher, A.B.2
  • 158
    • 39149108128 scopus 로고    scopus 로고
    • Thioredoxin peroxidase from Echinococcus granulosus: A candidate to extend the antigenic panel for the immunodiagnosis of human cystic echinococcosis
    • DOI 10.1016/j.diagmicrobio.2007.10.004, PII S0732889307004634
    • Margutti P, Ortona E, Delunardo F, Tagliani A, Profumo E, Rigano R, Buttari B, Teggi A, and Siracusano A. Thioredoxin peroxidase from Echinococcus granulosus: a candidate to extend the antigenic panel for the immunodiagnosis of human cystic echinococcosis. Diagn Microbiol Infect Dis 60: 279-285, 2008. (Pubitemid 351253606)
    • (2008) Diagnostic Microbiology and Infectious Disease , vol.60 , Issue.3 , pp. 279-285
    • Margutti, P.1    Ortona, E.2    Delunardo, F.3    Tagliani, A.4    Profumo, E.5    Rigano, R.6    Buttari, B.7    Teggi, A.8    Siracusano, A.9
  • 159
    • 80052000644 scopus 로고    scopus 로고
    • Toxoplasma gondii peroxiredoxin promotes altered macrophage function, caspase-1-dependent IL-1b secretion enhances parasite replication
    • Marshall E, Elshekiha H, Hakimi M-A, and Flynn R. Toxoplasma gondii peroxiredoxin promotes altered macrophage function, caspase-1-dependent IL-1b secretion enhances parasite replication. Vet Res 42: 80, 2011.
    • (2011) Vet Res , vol.42 , pp. 80
    • Marshall, E.1    Elshekiha, H.2    Hakimi, M.-A.3    Flynn, R.4
  • 160
    • 0030742427 scopus 로고    scopus 로고
    • Cloning of peroxiredoxin, a novel antioxidant enzyme, from the helminth parasite Fasciola hepatica
    • DOI 10.1017/S0031182097001170
    • McGonigle S, Curley G, and Dalton J. Cloning of peroxiredoxin, a novel antioxidant enzyme, from the helminth parasite Fasciola hepatica. Parasitology 115: 101-104, 1997. (Pubitemid 27337233)
    • (1997) Parasitology , vol.115 , Issue.1 , pp. 101-104
    • McGonigle, S.1    Curley, G.P.2    Dalton, J.P.3
  • 161
    • 77949654515 scopus 로고    scopus 로고
    • Evaluation of hepatic changes and local and systemic immune responses in goats immunized with recombinant Peroxiredoxin (Prx) and challenged with Fasciola hepatica
    • Mendes R, Perez-Ecija R, Zafra R, Buffoni L, Martinez- Moreno A, Dalton J, Mulcahy G, and Perez J. Evaluation of hepatic changes and local and systemic immune responses in goats immunized with recombinant Peroxiredoxin (Prx) and challenged with Fasciola hepatica. Vaccine 28: 2832-2840, 2010.
    • (2010) Vaccine , vol.28 , pp. 2832-2840
    • Mendes, R.1    Perez-Ecija, R.2    Zafra, R.3    Buffoni, L.4    Martinez-Moreno, A.5    Dalton, J.6    Mulcahy, G.7    Perez, J.8
  • 162
    • 54249088577 scopus 로고    scopus 로고
    • Protein import into hydrogenosomes of Trichomonas vaginalis involves both N-terminal and internal targeting signals: A case study of thioredoxin reductases
    • Mentel M, Zimorski V, Haferkamp P, Martin W, and Henze K. Protein import into hydrogenosomes of Trichomonas vaginalis involves both N-terminal and internal targeting signals: a case study of thioredoxin reductases. Eukaryot Cell 7: 1750-1757, 2008.
    • (2008) Eukaryot Cell , vol.7 , pp. 1750-1757
    • Mentel, M.1    Zimorski, V.2    Haferkamp, P.3    Martin, W.4    Henze, K.5
  • 163
    • 33846690105 scopus 로고    scopus 로고
    • Trypanosoma cruzi strains, Tulahuen 2 and Y, besides the difference in resistance to oxidative stress, display differential glucose-6-phosphate and 6-phosphogluconate dehydrogenases activities
    • DOI 10.1016/j.actatropica.2006.12.001, PII S0001706X06002452
    • Mielniczki-Pereira A, Chiavegatto C, Lopez J, Colli W, Alves M, and Gadelha F. Trypanosoma cruzi strains, Tulahuen 2 and Y, besides the difference in resistance to oxidative stress, display differential glucose-6-phosphate and 6-phosphogluconate dehydrogenases activities. Acta Trop 101: 54-60, 2007. (Pubitemid 46198791)
    • (2007) Acta Tropica , vol.101 , Issue.1 , pp. 54-60
    • Mielniczki-Pereira, A.A.1    Chiavegatto, C.M.2    Lopez, J.A.3    Colli, W.4    Alves, M.J.M.5    Gadelha, F.R.6
  • 164
    • 4143066916 scopus 로고    scopus 로고
    • Mechanisms of resistance to oxidative and nitrosative stress: Implications for fungal survival in mammalian hosts
    • Missall T, Lodge J, and Mcewen J. Mechanisms of resistance to oxidative and nitrosative stress: implications for fungal survival in mammalian hosts. Eukaryot Cell 3: 835- 846, 2004.
    • (2004) Eukaryot Cell , vol.3 , pp. 835-846
    • Missall, T.1    Lodge, J.2    Mcewen, J.3
  • 165
    • 13744260680 scopus 로고    scopus 로고
    • Distinct stress responses of two functional laccases in Cryptococcus neoformans are revealed in the absence of the thiol-specific antioxidant Tsa1
    • DOI 10.1128/EC.4.1.202-208.2005
    • Missall T, Moran J, Corbett J, and Lodge J. Distinct stress responses of two functional laccases in Cryptococcus neoformans are revealed in the absence of the thiol-specific antioxidant Tsa1. Eukaryot Cell 4: 202-208, 2005. (Pubitemid 40234437)
    • (2005) Eukaryotic Cell , vol.4 , Issue.1 , pp. 202-208
    • Missall, T.A.1    Moran, J.M.2    Corbett, J.A.3    Lodge, J.K.4
  • 166
    • 33645054564 scopus 로고    scopus 로고
    • Posttranslational, translational, and transcriptional responses to nitric oxide stress in Cryptococcus neoformans: Implications for virulence
    • Missall TA, Pusateri ME, Donlin MJ, Chambers KT, Corbett JA, and Lodge JK. Posttranslational, translational, and transcriptional responses to nitric oxide stress in Cryptococcus neoformans: implications for virulence. Eukaryot Cell 5: 518-529, 2006.
    • (2006) Eukaryot Cell , vol.5 , pp. 518-529
    • Missall, T.A.1    Pusateri, M.E.2    Donlin, M.J.3    Chambers, K.T.4    Corbett, J.A.5    Lodge, J.K.6
  • 167
    • 1542511805 scopus 로고    scopus 로고
    • Thiol peroxidase is critical for virulence and resistance to nitric oxide and peroxide in the fungal pathogen, Cryptococcus neoformans
    • DOI 10.1111/j.1365-2958.2004.03921.x
    • Missall TA, Pusateri ME, and Lodge JK. Thiol peroxidase is critical for virulence and resistance to nitric oxide and peroxide in the fungal pathogen, Cryptococcus neoformans. Mol Microbiol 51: 1447-1458, 2004. (Pubitemid 38338905)
    • (2004) Molecular Microbiology , vol.51 , Issue.5 , pp. 1447-1458
    • Missall, T.A.1    Pusateri, M.E.2    Lodge, J.K.3
  • 168
    • 0023718663 scopus 로고
    • Antioxidant systems in Schistosoma mansoni: Correlation between susceptibility to oxidant killing and the levels of scavengers of hydrogen peroxide and oxygen free radicals
    • Mkoji GM, Smith JM, and Prichard RK. Antioxidant systems in Schistosoma mansoni: correlation between susceptibility to oxidant killing and the levels of scavengers of hydrogen peroxide and oxygen free radicals. Int J Parasitol 18: 661-666, 1988.
    • (1988) Int J Parasitol , vol.18 , pp. 661-666
    • Mkoji, G.M.1    Smith, J.M.2    Prichard, R.K.3
  • 169
    • 77955332146 scopus 로고    scopus 로고
    • Diversity in mitochondrial metabolic pathways in parasitic protists Plasmodium and Cryptosporidium
    • Mogi T and Kita K. Diversity in mitochondrial metabolic pathways in parasitic protists Plasmodium and Cryptosporidium. Parasitol Int 59: 305-312, 2010.
    • (2010) Parasitol Int , vol.59 , pp. 305-312
    • Mogi, T.1    Kita, K.2
  • 170
    • 33748950227 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a 2-Cys peroxiredoxin from Taenia solium
    • DOI 10.1645/GE-754R.1
    • Molina-López J, Jiménez L, Ochoa-Sánchez A, and Landa A. Molecular cloning and characterization of a 2-Cys peroxiredoxin from Taenia solium. J Parasitol 92: 796-802, 2006. (Pubitemid 44435598)
    • (2006) Journal of Parasitology , vol.92 , Issue.4 , pp. 796-802
    • Molina-Lopez, J.1    Jimenez, L.2    Ochoa-Sanchez, A.3    Landa, A.4
  • 171
    • 34247604468 scopus 로고    scopus 로고
    • Reduction of 1-Cys peroxiredoxins by ascorbate changes the thiol-specific antioxidant paradigm, revealing another function of vitamin C
    • Monteiro G, Horta B, Pimenta D, Augusto O, and Netto L. Reduction of 1-Cys peroxiredoxins by ascorbate changes the thiol-specific antioxidant paradigm, revealing another function of vitamin C. Proc Natl Acad Sci U S A 104: 4886- 4891, 2007.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 4886-4891
    • Monteiro, G.1    Horta, B.2    Pimenta, D.3    Augusto, O.4    Netto, L.5
  • 172
    • 77949545224 scopus 로고    scopus 로고
    • Funding for research and development and the financial crisis
    • Moran M. Funding for research and development and the financial crisis. Lancet Infect Dis 10: 214-215, 2010.
    • (2010) Lancet Infect Dis , vol.10 , pp. 214-215
    • Moran, M.1
  • 175
    • 33745851827 scopus 로고    scopus 로고
    • 5 reductase-like protein causes kinetoplast DNA Loss in Trypanosoma brucei
    • DOI 10.1074/jbc.M602880200
    • Motyka S, Drew M, Yildirir G, and Englund P. Overexpression of a cytochrome b5 reductase-like protein causes kinetoplast DNA loss in Trypanosoma brucei. J Biol Chem 281: 18499-18506, 2006. (Pubitemid 44035509)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.27 , pp. 18499-18506
    • Motyka, S.A.1    Drew, M.E.2    Yildirir, G.3    Englund, P.T.4
  • 176
    • 70449507123 scopus 로고    scopus 로고
    • Phenotypic screen of early-developing larvae of the blood fluke, Schistosoma mansoni, using RNA interference
    • Mourao M, Dinguirard N, Franco G, and Yoshino T. Phenotypic screen of early-developing larvae of the blood fluke, Schistosoma mansoni, using RNA interference. PLoS Negl Trop Dis 3: e502, 2009.
    • (2009) PLoS Negl Trop Dis , vol.3
    • Mourao, M.1    Dinguirard, N.2    Franco, G.3    Yoshino, T.4
  • 177
    • 73449138216 scopus 로고    scopus 로고
    • Role of the endogenous antioxidant system in the protection of Schistosoma mansoni primary sporocysts against exogenous oxidative stress
    • Mourao Mde M, Dinguirard N, Franco G, and Yoshino T. Role of the endogenous antioxidant system in the protection of Schistosoma mansoni primary sporocysts against exogenous oxidative stress. PLoS Negl Trop Dis 3: e550, 2009.
    • (2009) PLoS Negl Trop Dis , vol.3
    • Mourao Mde, M.1    Dinguirard, N.2    Franco, G.3    Yoshino, T.4
  • 179
    • 0027787578 scopus 로고
    • The hydrogenosome
    • Müller M. The hydrogenosome. J Gen Microbiol 139: 2879- 2889, 1993.
    • (1993) J Gen Microbiol , vol.139 , pp. 2879-2889
    • Müller, M.1
  • 180
    • 4444359792 scopus 로고    scopus 로고
    • Redox and antioxidant systems of the malaria parasite Plasmodium falciparum
    • DOI 10.1111/j.1365-2958.2004.04257.x
    • Müller S. Redox and antioxidant systems of the malaria parasite Plasmodium falciparum. Mol Microbiol 53: 1291-1305, 2004. (Pubitemid 39209105)
    • (2004) Molecular Microbiology , vol.53 , Issue.5 , pp. 1291-1305
    • Muller, S.1
  • 182
    • 0033557291 scopus 로고    scopus 로고
    • Macrophage microbicidal mechanisms in vivo: Reactive nitrogen versus oxygen intermediates in the killing of intracellular visceral Leishmania donovani
    • DOI 10.1084/jem.189.4.741
    • Murray H and Nathan C. Macrophage microbicidal mechanisms in vivo: reactive nitrogen versus oxygen intermediates in the killing of intracellular visceral Leishmania donovani. J Exp Med 189: 741-746, 1999. (Pubitemid 29193376)
    • (1999) Journal of Experimental Medicine , vol.189 , Issue.4 , pp. 741-746
    • Murray, H.W.1    Nathan, F.2
  • 183
    • 79551493261 scopus 로고    scopus 로고
    • Analysis of the peroxiredoxin family: Using active- Site structure and sequence information for global classification and residue analysis
    • Nelson KJ, Knutson ST, Soito L, Klomsiri C, Poole LB, and Fetrow JS. Analysis of the peroxiredoxin family: using active- site structure and sequence information for global classification and residue analysis. Proteins 79: 947-964, 2010.
    • (2010) Proteins , vol.79 , pp. 947-964
    • Nelson, K.J.1    Knutson, S.T.2    Soito, L.3    Klomsiri, C.4    Poole, L.B.5    Fetrow, J.S.6
  • 184
    • 0029886243 scopus 로고    scopus 로고
    • Removal of hydrogen peroxide by thiol-specific antioxidant enzyme (TSA) is involved with its antioxidant properties. TSA possesses thiol peroxidase activity
    • Netto L, Chae H, Kang S, Rhee S, and Stadtman E. Removal of hydrogen peroxide by thiol-specific antioxidant enzyme (TSA) is involved with its antioxidant properties. TSA possesses thiol peroxidase activity. J Biol Chem 271: 15315- 15321, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 15315-15321
    • Netto, L.1    Chae, H.2    Kang, S.3    Rhee, S.4    Stadtman, E.5
  • 185
  • 186
    • 28244462440 scopus 로고    scopus 로고
    • Plasmodium falciparum 2-Cys peroxiredoxin reacts with plasmoredoxin and peroxynitrite
    • DOI 10.1515/BC.2005.129
    • Nickel C, Trujillo M, Rahlfs S, Deponte M, Radi R, and Becker K. Plasmodium falciparum 2-Cys peroxiredoxin reacts with plasmoredoxin and peroxynitrite. Biol Chem 386: 1129-1136, 2005. (Pubitemid 41705367)
    • (2005) Biological Chemistry , vol.386 , Issue.11 , pp. 1129-1136
    • Nickel, C.1    Trujillo, M.2    Rahlfs, S.3    Deponte, M.4    Radi, R.5    Becker, K.6
  • 187
    • 0030861413 scopus 로고    scopus 로고
    • A unique cascade of oxidoreductases catalyses trypanothione-mediated peroxide metabolism in Crithidia fasciculata
    • Nogoceke E, Gommel D, Kiess M, Kalisz H, and Flohe L. A unique cascade of oxidoreductases catalyses trypanothione- mediated peroxide metabolism in Crithidia fasciculata. Biol Chem 378: 827-836, 1997. (Pubitemid 27388943)
    • (1997) Biological Chemistry , vol.378 , Issue.8 , pp. 827-836
    • Nogoceke, E.1    Gommel, D.U.2    Kiess, M.3    Kalisz, H.M.4    Flohe, L.5
  • 188
    • 65549139721 scopus 로고    scopus 로고
    • Molecular characterization of cytosolic and mitochondrial tryparedoxin peroxidase in Trypanosoma cruzi populations susceptible and resistant to benznidazole
    • Nogueira F, Ruiz J, Robello C, Romanha A, and Murta S. Molecular characterization of cytosolic and mitochondrial tryparedoxin peroxidase in Trypanosoma cruzi populations susceptible and resistant to benznidazole. Parasitol Res 104: 835-844, 2009.
    • (2009) Parasitol Res , vol.104 , pp. 835-844
    • Nogueira, F.1    Ruiz, J.2    Robello, C.3    Romanha, A.4    Murta, S.5
  • 189
    • 0025369916 scopus 로고
    • Trichomonas vaginalis requires traces of oxygen and high concentrations of carbon dioxide for optimal growth
    • DOI 10.1016/0166-6851(90)90097-6
    • Paget TA and Lloyd D. Trichomonas vaginalis requires traces of oxygen and high concentrations of carbon dioxide for optimal growth. Mol Biochem Parasitol 41: 65-72, 1990. (Pubitemid 20176669)
    • (1990) Molecular and Biochemical Parasitology , vol.41 , Issue.1 , pp. 65-72
    • Paget, T.A.1    Lloyd, D.2
  • 191
    • 23244466487 scopus 로고    scopus 로고
    • Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin
    • DOI 10.1021/bi050448i
    • Parsonage D, Youngblood DS, Sarma GN, Wood ZA, Karplus PA, and Poole LB. Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin. Biochemistry 44: 10583-10592, 2005. (Pubitemid 41098235)
    • (2005) Biochemistry , vol.44 , Issue.31 , pp. 10583-10592
    • Parsonage, D.1    Youngblood, D.S.2    Sarma, G.N.3    Wood, Z.A.4    Karplus, P.A.5    Poole, L.B.6
  • 192
    • 78149469953 scopus 로고    scopus 로고
    • Multiple catalytically active thioredoxin folds: A winning strategy for many functions
    • Pedone E, Limauro D, D'Ambrosio K, De Simone G, and Bartolucci S. Multiple catalytically active thioredoxin folds: a winning strategy for many functions. Cell Mol Life Sci 67: 3797-3814, 2010.
    • (2010) Cell Mol Life Sci , vol.67 , pp. 3797-3814
    • Pedone, E.1    Limauro, D.2    D'Ambrosio, K.3    De Simone, G.4    Bartolucci, S.5
  • 193
    • 0034717135 scopus 로고    scopus 로고
    • Mitochondria of Saccharomyces cerevisiae contain one-conserved cysteine type peroxiredoxin with thioredoxin peroxidase activity
    • Pedrajas J, Miranda-Vizuete A, Javanmardy N, Gustafsson J, and Spyrou G. Mitochondria of Saccharomyces cerevisiae contain one-conserved cysteine type peroxiredoxin with thioredoxin peroxidase activity. J Biol Chem 275: 16296- 16301, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 16296-16301
    • Pedrajas, J.1    Miranda-Vizuete, A.2    Javanmardy, N.3    Gustafsson, J.4    Spyrou, G.5
  • 194
    • 79959248739 scopus 로고    scopus 로고
    • Quantitative proteome profiling informs on phenotypic traits that adapt Leishmania donovani for axenic and intracellular proliferation
    • Pescher P, Blisnick T, Bastin P, and Spath G. Quantitative proteome profiling informs on phenotypic traits that adapt Leishmania donovani for axenic and intracellular proliferation. Cell Microbiol 13: 978-991, 2011.
    • (2011) Cell Microbiol , vol.13 , pp. 978-991
    • Pescher, P.1    Blisnick, T.2    Bastin, P.3    Spath, G.4
  • 198
    • 68049131348 scopus 로고    scopus 로고
    • Fighting the oxidative assault: The Trypanosoma cruzi journey to infection
    • Piacenza L, Alvarez M, Peluffo G, and Radi R. Fighting the oxidative assault: the Trypanosoma cruzi journey to infection. Curr Opin Microbiol 12: 415-421, 2009.
    • (2009) Curr Opin Microbiol , vol.12 , pp. 415-421
    • Piacenza, L.1    Alvarez, M.2    Peluffo, G.3    Radi, R.4
  • 199
    • 40449096623 scopus 로고    scopus 로고
    • Peroxiredoxins play a major role in protecting Trypanosoma cruzi against macrophage- and endogenously-derived peroxynitrite
    • DOI 10.1042/BJ20071138
    • Piacenza L, Peluffo G, Alvarez M, Kelly J, Wilkinson S, and Radi R. Peroxiredoxins play a major role in protecting Trypanosoma cruzi against macrophage- and endogenouslyderived peroxynitrite. Biochem J 410: 359-368, 2008. (Pubitemid 351346194)
    • (2008) Biochemical Journal , vol.410 , Issue.2 , pp. 359-368
    • Piacenza, L.1    Peluffo, G.2    Alvarez, M.N.3    Kelly, J.M.4    Wilkinson, S.R.5    Radi, R.6
  • 200
    • 69349103734 scopus 로고    scopus 로고
    • Enzymes of the antioxidant network as novel determiners of Trypanosoma cruzi virulence
    • Piacenza L, Zago M, Peluffo G, Alvarez M, Basombrio M, and Radi R. Enzymes of the antioxidant network as novel determiners of Trypanosoma cruzi virulence. Int J Parasitol 39: 1455-1464, 2009.
    • (2009) Int J Parasitol , vol.39 , pp. 1455-1464
    • Piacenza, L.1    Zago, M.2    Peluffo, G.3    Alvarez, M.4    Basombrio, M.5    Radi, R.6
  • 201
    • 79951941737 scopus 로고    scopus 로고
    • Tryparedoxin peroxidases from Trypanosoma cruzi: High efficiency in the catalytic elimination of hydrogen peroxide and peroxynitrite
    • Piñeyro M, Arcari T, Robello C, Radi R, and Trujillo M. Tryparedoxin peroxidases from Trypanosoma cruzi: High efficiency in the catalytic elimination of hydrogen peroxide and peroxynitrite. Arch Biochem Biophys 507: 287-295, 2011.
    • (2011) Arch Biochem Biophys , vol.507 , pp. 287-295
    • Piñeyro, M.1    Arcari, T.2    Robello, C.3    Radi, R.4    Trujillo, M.5
  • 204
    • 34548440314 scopus 로고    scopus 로고
    • Dual targeting of antioxidant and metabolic enzymes to the mitochondrion and the apicoplast of Toxoplasma gondii
    • Pino P, Foth BJ, Kwok LY, Sheiner, L, Schepers R, Soldati T, and Soldati-Favre D. Dual targeting of antioxidant and metabolic enzymes to the mitochondrion and the apicoplast of Toxoplasma gondii. PLoS Pathog 3: e115, 2007.
    • (2007) PLoS Pathog , vol.3
    • Pino, P.1    Foth, B.J.2    Kwok, L.Y.3    Sheiner, L.4    Schepers, R.5    Soldati, T.6    Soldati-Favre, D.7
  • 205
    • 9744232974 scopus 로고    scopus 로고
    • Bacterial defenses against oxidants: Mechanistic features of cysteine-based peroxidases and their flavoprotein reductases
    • DOI 10.1016/j.abb.2004.09.006, PII S0003986104005181
    • Poole LB. Bacterial defenses against oxidants: mechanistic features of cysteine-based peroxidases and their flavoprotein reductases. Arch Biochem Biophys 433: 240-254, 2005. (Pubitemid 39586595)
    • (2005) Archives of Biochemistry and Biophysics , vol.433 , Issue.1 , pp. 240-254
    • Poole, L.B.1
  • 206
    • 40849097418 scopus 로고    scopus 로고
    • Discovering mechanisms of signalingmediated cysteine oxidation
    • Poole L and Nelson K. Discovering mechanisms of signalingmediated cysteine oxidation. Curr Opin Chem Biol 12: 18, 2008.
    • (2008) Curr Opin Chem Biol , vol.12 , pp. 18
    • Poole, L.1    Nelson, K.2
  • 207
    • 0030774921 scopus 로고    scopus 로고
    • Peroxidase activity of a TSA-like antioxidant protein from a pathogenic amoeba
    • DOI 10.1016/S0891-5849(97)00066-X, PII S089158499700066X
    • Poole LB, Chae HZ, Flores BM, Reed SL, Rhee SG, and Torian BE. Peroxidase activity of a TSA-like antioxidant protein from a pathogenic amoeba. Free Radic Biol Med 23: 955-959, 1997. (Pubitemid 27402621)
    • (1997) Free Radical Biology and Medicine , vol.23 , Issue.6 , pp. 955-959
    • Poole, L.B.1    Chae, H.Z.2    Flores, B.M.3    Reed, S.L.4    Rhee, S.G.5    Torian, B.E.6
  • 208
    • 0036371370 scopus 로고    scopus 로고
    • Identification of cysteine sulfenic acid in AhpC of alkyl hydroperoxide reductase
    • DOI 10.1016/S0076-6879(02)48632-6, 13, Part B: Protein Sensors and Reactive Oxygen Species
    • Poole LB and Ellis HR. Identification of cysteine sulfenic acid in AhpC of alkyl hydroperoxide reductase. In: Methods in Enzymology, edited by Sies H and Packer L. Maryland Heights, MO: Academic Press, 2002, pp. 122-136. (Pubitemid 41103104)
    • (2002) Methods in Enzymology , vol.348 , pp. 122-136
    • Poole, L.B.1    Ellis, H.R.2
  • 209
    • 20644461004 scopus 로고    scopus 로고
    • Rubrerythrin and peroxiredoxin: Two novel putative peroxidases in the hydrogenosomes of the microaerophilic protozoon Trichomonas vaginalis
    • DOI 10.1016/j.molbiopara.2005.04.003, PII S0166685105001337
    • Putz S, Gelius-Dietrich G, Piotrowski M, and Henze K. Rubrerythrin and peroxiredoxin: two novel putative peroxidases in the hydrogenosomes of the microaerophilic protozoon Trichomonas vaginalis. Mol Biochem Parasitol 142: 212-223, 2005. (Pubitemid 40835913)
    • (2005) Molecular and Biochemical Parasitology , vol.142 , Issue.2 , pp. 212-223
    • Putz, S.1    Gelius-Dietrich, G.2    Piotrowski, M.3    Henze, K.4
  • 210
    • 0035081036 scopus 로고    scopus 로고
    • Thioredoxin peroxidases of the malarial parasite Plasmodium falciparum
    • DOI 10.1046/j.1432-1327.2001.02005.x
    • Rahlfs S and Becker K. Thioredoxin peroxidases of the malarial parasite Plasmodium falciparum. Eur J Biochem 268: 1404-1409, 2001. (Pubitemid 32231894)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.5 , pp. 1404-1409
    • Rahlfs, S.1    Becker, K.2
  • 211
    • 79955589986 scopus 로고    scopus 로고
    • Lack of protective efficacy in buffaloes vaccinated with Fasciola gigantica leucine aminopeptidase and peroxiredoxin recombinant proteins
    • Raina O, Nagar G, Varghese A, Prajitha G, Alex A, Maharana B, and Joshi P. Lack of protective efficacy in buffaloes vaccinated with Fasciola gigantica leucine aminopeptidase and peroxiredoxin recombinant proteins. Acta Trop 118: 217-222, 2011.
    • (2011) Acta Trop , vol.118 , pp. 217-222
    • Raina, O.1    Nagar, G.2    Varghese, A.3    Prajitha, G.4    Alex, A.5    Maharana, B.6    Joshi, P.7
  • 213
    • 79951643450 scopus 로고    scopus 로고
    • Multiple functions of peroxiredoxins: Peroxidases, sensors and regulators of the intracellular messenger H2O2, and protein chaperones
    • Rhee SG and Woo HA. Multiple functions of peroxiredoxins: peroxidases, sensors and regulators of the intracellular messenger H2O2, and protein chaperones. Antioxid Redox Signal 15: 781-794, 2011.
    • (2011) Antioxid Redox Signal , vol.15 , pp. 781-794
    • Rhee, S.G.1    Woo, H.A.2
  • 214
    • 79953219814 scopus 로고    scopus 로고
    • A genome-wide chromatin-associated nuclear peroxiredoxin from the malaria parasite Plasmodium falciparum
    • Richard D, Bartfai R, Volz J, Ralph SA, Müller S, Stunnenberg HG, and Cowman AF. A genome-wide chromatin-associated nuclear peroxiredoxin from the malaria parasite Plasmodium falciparum. J Biol Chem 286: 11746-11755, 2011.
    • (2011) J Biol Chem , vol.286 , pp. 11746-11755
    • Richard, D.1    Bartfai, R.2    Volz, J.3    Ralph, S.A.4    Müller, S.5    Stunnenberg, H.G.6    Cowman, A.F.7
  • 215
    • 61349124238 scopus 로고    scopus 로고
    • The cytosolic tryparedoxin of Leishmania infantum is essential for parasite survival
    • Romao S, Castro H, Sousa C, Carvalho S, and Tomas AM. The cytosolic tryparedoxin of Leishmania infantum is essential for parasite survival. Int J Parasitol 39: 703-711, 2009.
    • (2009) Int J Parasitol , vol.39 , pp. 703-711
    • Romao, S.1    Castro, H.2    Sousa, C.3    Carvalho, S.4    Tomas, A.M.5
  • 218
    • 0032211284 scopus 로고    scopus 로고
    • Echinococcus granulosus: Cloning of a thioredoxin peroxidase
    • DOI 10.1006/expr.1998.4339
    • Salinas G, Fernandez V, Fernandez C, and Selkirk M. Echinococcus granulosus: cloning of a thioredoxin peroxidase. Exp Parasitol 90: 298-301, 1998. (Pubitemid 28525106)
    • (1998) Experimental Parasitology , vol.90 , Issue.3 , pp. 298-301
    • Salinas, G.1    Fernandez, V.2    Fernandez, C.3    Selkirk, M.E.4
  • 219
    • 77951783796 scopus 로고    scopus 로고
    • Application of an improved enzymelinked immunosorbent assay method for serological diagnosis of canine leishmaniasis
    • Santarem N, Silvestre R, Cardoso L, Schallig H, Reed S, and Cordeiro-da-Silva A. Application of an improved enzymelinked immunosorbent assay method for serological diagnosis of canine leishmaniasis. J Clin Microbiol 48: 1866-1874, 2010.
    • (2010) J Clin Microbiol , vol.48 , pp. 1866-1874
    • Santarem, N.1    Silvestre, R.2    Cardoso, L.3    Schallig, H.4    Reed, S.5    Cordeiro-da-Silva, A.6
  • 220
    • 24744460729 scopus 로고    scopus 로고
    • Antibodies against a Leishmania infantum peroxiredoxin as a possible marker for diagnosis of visceral leishmaniasis and for monitoring the efficacy of treatment
    • DOI 10.1016/j.imlet.2005.04.006, PII S0165247805001057
    • Santarem N, Tomas A, Ouaissi A, Tavares J, Ferreira N, Manso A, Campino L, Correia J, and Cordeiro-da-Silva A. Antibodies against a Leishmania infantum peroxiredoxin as a possible marker for diagnosis of visceral leishmaniasis and for monitoring the efficacy of treatment. Immunol Lett 101: 18-23, 2005. (Pubitemid 41297494)
    • (2005) Immunology Letters , vol.101 , Issue.1 , pp. 18-23
    • Santarem, N.1    Tomas, A.2    Ouaissi, A.3    Tavares, J.4    Ferreira, N.5    Manso, A.6    Campino, L.7    Correia, J.M.8    Cordeiro-da-Silva, A.9
  • 221
    • 37149026375 scopus 로고    scopus 로고
    • The lysine- and glutamic acid-rich protein KERP1 plays a role in Entamoeba histolytica liver abscess pathogenesis
    • DOI 10.1111/j.1462-5822.2007.01030.x
    • Santi-Rocca J, Weber C, Guigon G, Sismeiro O, Coppee J, and Guillen N. The lysine- and glutamic acid-rich protein KERP1 plays a role in Entamoeba histolytica liver abscess pathogenesis. Cell Microbiol 10: 202-217, 2008. (Pubitemid 350252854)
    • (2008) Cellular Microbiology , vol.10 , Issue.1 , pp. 202-217
    • Santi-Rocca, J.1    Weber, C.2    Guigon, G.3    Sismeiro, O.4    Coppee, J.-Y.5    Guillen, N.6
  • 223
    • 58149107439 scopus 로고    scopus 로고
    • The histone methylase KMTox interacts with the redox-sensor peroxiredoxin-1 and targets genes involved in Toxoplasma gondii antioxidant defences
    • Sautel C, Ortet P, Saksouk N, Kieffer S, Garin J, Bastien O, and Hakimi M. The histone methylase KMTox interacts with the redox-sensor peroxiredoxin-1 and targets genes involved in Toxoplasma gondii antioxidant defences. Mol Microbiol 71: 212-226, 2009.
    • (2009) Mol Microbiol , vol.71 , pp. 212-226
    • Sautel, C.1    Ortet, P.2    Saksouk, N.3    Kieffer, S.4    Garin, J.5    Bastien, O.6    Hakimi, M.7
  • 224
    • 33745195480 scopus 로고    scopus 로고
    • Redox balance mechanisms in Schistosoma mansoni rely on peroxiredoxins and albumin and implicate peroxiredoxins as novel drug targets
    • Sayed AA, Cook SK, and Williams DL. Redox balance mechanisms in Schistosoma mansoni rely on peroxiredoxins and albumin and implicate peroxiredoxins as novel drug targets. J Biol Chem 281: 17001-17010, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 17001-17010
    • Sayed, A.A.1    Cook, S.K.2    Williams, D.L.3
  • 225
    • 2942532835 scopus 로고    scopus 로고
    • Biochemical characterization of 2-cys peroxiredoxins from Schistosoma mansoni
    • DOI 10.1074/jbc.M401748200
    • Sayed AA and Williams DL. Biochemical characterization of 2-Cys peroxiredoxins from Schistosoma mansoni. J Biol Chem 279: 26159-26166, 2004. (Pubitemid 38798761)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.25 , pp. 26159-26166
    • Sayed, A.A.1    Williams, D.L.2
  • 227
    • 0032128444 scopus 로고    scopus 로고
    • Identification of a peroxidoxin protein (OvPXN-2) of the human parasitic nematode Onchocerca volvulus by sequential protein fractionation
    • DOI 10.1016/S0166-6851(98)00034-6, PII S0166685198000346
    • Schrum S, Bialonski A, Marti T, and Zipfel P. Identification of a peroxidoxin protein (OvPXN-2) of the human parasitic nematode Onchocerca volvulus by sequential protein fractionation. Mol Biochem Parasitol 94: 131-135, 1998. (Pubitemid 28345155)
    • (1998) Molecular and Biochemical Parasitology , vol.94 , Issue.1 , pp. 131-135
    • Schrum, S.1    Bialonski, A.2    Marti, T.3    Zipfel, P.F.4
  • 228
    • 77955907263 scopus 로고    scopus 로고
    • Metabolic pathways in the apicoplast of apicomplexa
    • Seeber F and Soldati-Favre D. Metabolic pathways in the apicoplast of apicomplexa. Int Rev Cell Mol Biol 281: 161- 228, 2010.
    • (2010) Int Rev Cell Mol Biol , vol.281 , pp. 161-228
    • Seeber, F.1    Soldati-Favre, D.2
  • 229
    • 33748787130 scopus 로고    scopus 로고
    • Biochemical characterisation of the recombinant peroxiredoxin (FhePrx) of the liver fluke, Fasciola hepatica
    • DOI 10.1016/j.febslet.2006.08.019, PII S0014579306009872
    • Sekiya M, Mulcahy G, Irwin J, Stack C, Donnelly S, Xu W, Collins P, and Dalton J. Biochemical characterisation of the recombinant peroxiredoxin (FhePrx) of the liver fluke, Fasciola hepatica. FEBS Lett 580: 5016-5022, 2006. (Pubitemid 44404083)
    • (2006) FEBS Letters , vol.580 , Issue.21 , pp. 5016-5022
    • Sekiya, M.1    Mulcahy, G.2    Irwin, J.A.3    Stack, C.M.4    Donnelly, S.M.5    Xu, W.6    Collins, P.7    Dalton, J.P.8
  • 230
    • 57649114086 scopus 로고    scopus 로고
    • Enzymatic mechanism controls redox-mediated protein-DNA interactions at the replication origin of kinetoplast DNA minicircles
    • Sela D, Yaffe N, and Shlomai J. Enzymatic mechanism controls redox-mediated protein-DNA interactions at the replication origin of kinetoplast DNA minicircles. J Biol Chem 283: 32034-32044, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 32034-32044
    • Sela, D.1    Yaffe, N.2    Shlomai, J.3
  • 235
    • 78651278810 scopus 로고    scopus 로고
    • PREX: PeroxiRedoxin classification indEX, a database of subfamily assignments across the diverse peroxiredoxin family
    • Soito L, Williamson C, Knutson ST, Fetrow JS, Poole LB, and Nelson KJ. PREX: PeroxiRedoxin classification indEX, a database of subfamily assignments across the diverse peroxiredoxin family. Nucleic Acids Res 39: D332-D337, 2011.
    • (2011) Nucleic Acids Res , vol.39
    • Soito, L.1    Williamson, C.2    Knutson, S.T.3    Fetrow, J.S.4    Poole, L.B.5    Nelson, K.J.6
  • 236
    • 0028906577 scopus 로고
    • Protection of gerbils from amebic liver abscess by immunization with recombinant Entamoeba histolytica 29-kilodalton antigen
    • Soong CJ, Torian BE, Abd-Alla MD, Jackson TF, Gatharim V, and Ravdin JI. Protection of gerbils from amebic liver abscess by immunization with recombinant Entamoeba histolytica 29-kilodalton antigen. Infect Immun 63: 472-477, 1995.
    • (1995) Infect Immun , vol.63 , pp. 472-477
    • Soong, C.J.1    Torian, B.E.2    Abd-Alla, M.D.3    Jackson, T.F.4    Gatharim, V.5    Ravdin, J.I.6
  • 237
    • 33846797935 scopus 로고    scopus 로고
    • Heterologous priming-boosting with DNA and modified vaccinia virus Ankara expressing tryparedoxin peroxidase promotes long-term memory against Leishmania major in susceptible BALB/c Mice
    • DOI 10.1128/IAI.01490-06
    • Stober C, Lange U, Roberts M, Alcami A, and Blackwell J. Heterologous priming-boosting with DNA and modified vaccinia virus Ankara expressing tryparedoxin peroxidase promotes long-term memory against Leishmania major in susceptible BALB/c Mice. Infect Immun 75: 852-860, 2007. (Pubitemid 46203449)
    • (2007) Infection and Immunity , vol.75 , Issue.2 , pp. 852-860
    • Stober, C.B.1    Lange, U.G.2    Roberts, M.T.M.3    Alcami, A.4    Blackwell, J.M.5
  • 238
    • 0034331004 scopus 로고    scopus 로고
    • Chemical genetics: Ligand-based discovery of gene function
    • Stockwell BR. Chemical genetics: ligand-based discovery of gene function. Nat Rev Genet 1: 116-125, 2000.
    • (2000) Nat Rev Genet , vol.1 , pp. 116-125
    • Stockwell, B.R.1
  • 239
    • 50049110849 scopus 로고    scopus 로고
    • Characterization of the antioxidant enzyme, thioredoxin peroxidase, from the carcinogenic human liver fluke, Opisthorchis viverrini
    • Suttiprapa S, Loukas A, Laha T, Wongkham S, Kaewkes S, Gaze S, Brindley P, and Sripa B. Characterization of the antioxidant enzyme, thioredoxin peroxidase, from the carcinogenic human liver fluke, Opisthorchis viverrini. Mol Biochem Parasitol 160: 116-122, 2008.
    • (2008) Mol Biochem Parasitol , vol.160 , pp. 116-122
    • Suttiprapa, S.1    Loukas, A.2    Laha, T.3    Wongkham, S.4    Kaewkes, S.5    Gaze, S.6    Brindley, P.7    Sripa, B.8
  • 240
    • 34547673497 scopus 로고    scopus 로고
    • Peroxynitrite: Biochemistry, pathophysiology and development of therapeutics
    • DOI 10.1038/nrd2222, PII NRD2222
    • Szabó C, Ischiropoulos H, and Radi R. Peroxynitrite: biochemistry, pathophysiology and development of therapeutics. Nat Rev Drug Discov 6: 662-680, 2007. (Pubitemid 47207751)
    • (2007) Nature Reviews Drug Discovery , vol.6 , Issue.8 , pp. 662-680
    • Szabo, C.1    Ischiropoulos, H.2    Radi, R.3
  • 241
    • 84862555422 scopus 로고    scopus 로고
    • This reference has been deleted
    • This reference has been deleted.
  • 242
    • 0033963677 scopus 로고    scopus 로고
    • Entamoeba dispar: Cloning and characterization of peroxiredoxin genes
    • DOI 10.1006/expr.1999.4461
    • Tachibana H and Cheng XJ. Entamoeba dispar: cloning and characterization of peroxiredoxin genes. Exp Parasitol 94: 51-55, 2000. (Pubitemid 30062522)
    • (2000) Experimental Parasitology , vol.94 , Issue.1 , pp. 51-55
    • Tachibana, H.1    Cheng, X.-J.2
  • 243
    • 70350023725 scopus 로고    scopus 로고
    • Isolation and characterization of a potentially virulent species Entamoeba nuttalli from captive Japanese macaques
    • Tachibana H, Yanagi T, Akatsuka A, Kobayashi S, Kanbara H, and Tsutsumi V. Isolation and characterization of a potentially virulent species Entamoeba nuttalli from captive Japanese macaques. Parasitology 136: 1169-1177, 2009.
    • (2009) Parasitology , vol.136 , pp. 1169-1177
    • Tachibana, H.1    Yanagi, T.2    Akatsuka, A.3    Kobayashi, S.4    Kanbara, H.5    Tsutsumi, V.6
  • 244
    • 34247497373 scopus 로고    scopus 로고
    • An Entamoeba sp. strain isolated from rhesus monkey is virulent but genetically different from Entamoeba histolytica
    • DOI 10.1016/j.molbiopara.2007.02.006, PII S0166685107000631
    • Tachibana H, Yanagi T, Pandey K, Cheng X, Kobayashi S, Sherchand J, and Kanbara H. An Entamoeba sp. strain isolated from rhesus monkey is virulent but genetically different from Entamoeba histolytica. Mol Biochem Parasitol 153: 107-114, 2007. (Pubitemid 46654245)
    • (2007) Molecular and Biochemical Parasitology , vol.153 , Issue.2 , pp. 107-114
    • Tachibana, H.1    Yanagi, T.2    Pandey, K.3    Cheng, X.-J.4    Kobayashi, S.5    Sherchand, J.B.6    Kanbara, H.7
  • 247
    • 0034889645 scopus 로고    scopus 로고
    • Molecular characterisation of mitochondrial and cytosolic trypanothione-dependent tryparedoxin peroxidases in Trypanosoma brucei
    • DOI 10.1016/S0166-6851(01)00320-6, PII S0166685101003206
    • Tetaud E, Giroud C, Prescott A, Parkin D, Baltz D, Biteau N, Baltz T, and Fairlamb A. Molecular characterisation of mitochondrial and cytosolic trypanothione-dependent tryparedoxin peroxidases in Trypanosoma brucei. Mol Biochem Parasitol 116: 171-183, 2001. (Pubitemid 32777826)
    • (2001) Molecular and Biochemical Parasitology , vol.116 , Issue.2 , pp. 171-183
    • Tetaud, E.1    Giroud, C.2    Prescott, A.R.3    Parkin, D.W.4    Baltz, D.5    Biteau, N.6    Baltz, T.7    Fairlamb, A.H.8
  • 248
    • 79251542985 scopus 로고    scopus 로고
    • Is overoxidation of peroxiredoxin physiologically significant?
    • Thamsen M, Kumsta C, Li F, and Jakob U. Is overoxidation of peroxiredoxin physiologically significant? Antioxid Redox Signal 14: 725-730, 2011.
    • (2011) Antioxid Redox Signal , vol.14 , pp. 725-730
    • Thamsen, M.1    Kumsta, C.2    Li, F.3    Jakob, U.4
  • 249
    • 4544264011 scopus 로고    scopus 로고
    • Trypanosoma brucei and Trypanosoma cruzi tryparedoxin peroxidases catalytically detoxify peroxynitrite via oxidation of fast reacting thiols
    • DOI 10.1074/jbc.M404317200
    • Trujillo M, Budde H, Piñeyro MD, Stehr M, Robello C, Flohé L, and Radi R. Trypanosoma brucei and Trypanosoma cruzi tryparedoxin peroxidases catalytically detoxify peroxynitrite via oxidation of fast reacting thiols. J Biol Chem 279: 34175-34182, 2004. (Pubitemid 39318040)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.33 , pp. 34175-34182
    • Trajillo, M.1    Budde, H.2    Pineyro, M.D.3    Stehr, M.4    Robello, C.5    Flohe, L.6    Radi, R.7
  • 250
    • 38749120994 scopus 로고    scopus 로고
    • Kinetics of peroxiredoxins and their role in the decomposition of peroxynitrite
    • edited by Flohé L and Harris JR. New York: Springer
    • Trujillo M, Ferrer-Sueta G, Thomson L, Flohé L, and Radi R. Kinetics of peroxiredoxins and their role in the decomposition of peroxynitrite. In: Peroxiredoxin Systems, edited by Flohé L and Harris JR. New York: Springer, 2007, pp. 83-113.
    • (2007) Peroxiredoxin Systems , pp. 83-113
    • Trujillo, M.1    Ferrer-Sueta, G.2    Thomson, L.3    Flohé, L.4    Radi, R.5
  • 251
    • 0034009971 scopus 로고    scopus 로고
    • Cloning and characterisation of a peroxiredoxin from the swine roundworm Ascaris suum
    • DOI 10.1016/S0020-7519(99)00180-0, PII S0020751900001800
    • Tsuji N, Kasuga-Aoki H, Isobe T, and Yoshihara S. Cloning and characterisation of a peroxiredoxin from the swine roundworm Ascaris suum. Int J Parasitol 30: 125-128, 2000. (Pubitemid 30127875)
    • (2000) International Journal for Parasitology , vol.30 , Issue.2 , pp. 125-128
    • Tsuji, N.1    Kasuga-Aoki, H.2    Isobe, T.3    Yoshihara, S.4
  • 252
    • 70349239330 scopus 로고    scopus 로고
    • Characterization of one typical 2-Cys peroxiredoxin gene of Taenia solium and Taenia crassiceps
    • Vaca-Paniagua F, Parra-Unda R, and Landa A. Characterization of one typical 2-Cys peroxiredoxin gene of Taenia solium and Taenia crassiceps. Parasitol Res 105: 781- 787, 2009.
    • (2009) Parasitol Res , vol.105 , pp. 781-787
    • Vaca-Paniagua, F.1    Parra-Unda, R.2    Landa, A.3
  • 253
    • 44849097478 scopus 로고    scopus 로고
    • Taenia solium: Antioxidant metabolism enzymes as targets for cestocidal drugs and vaccines
    • DOI 10.2174/156802608783790857
    • Vaca-Paniagua F, Torres-Rivera A, Parra-Unda R, and Landa A. Taenia solium: antioxidant metabolism enzymes as targets for cestocidal drugs and vaccines. Curr Top Med Chem 8: 393-399, 2008. (Pubitemid 351791017)
    • (2008) Current Topics in Medicinal Chemistry , vol.8 , Issue.5 , pp. 393-399
    • Vaca-Paniagua, F.1    Torres-Rivera, A.2    Parra-Unda, R.3    Landa, A.4
  • 254
    • 34147210988 scopus 로고    scopus 로고
    • Hydrogen Peroxide Sensing and Signaling
    • DOI 10.1016/j.molcel.2007.03.016, PII S1097276507001864
    • Veal E, Day A, and Morgan B. Hydrogen peroxide sensing and signaling. Mol Cell 26: 1-14, 2007. (Pubitemid 46578115)
    • (2007) Molecular Cell , vol.26 , Issue.1 , pp. 1-14
    • Veal, E.A.1    Day, A.M.2    Morgan, B.A.3
  • 256
    • 34547815610 scopus 로고    scopus 로고
    • Antioxidant gene expression and function in in vitro-developing Schistosoma mansoni mother sporocysts: Possible role in self-protection
    • DOI 10.1017/S0031182007002697, PII S0031182007002697
    • Vermeire J and Yoshino T. Antioxidant gene expression and function in in vitro-developing Schistosoma mansoni mother sporocysts: possible role in self-protection. Parasitology 134: 1369-1378, 2007. (Pubitemid 47236798)
    • (2007) Parasitology , vol.134 , Issue.10 , pp. 1369-1378
    • Vermeire, J.J.1    Yoshino, T.P.2
  • 257
    • 34948837440 scopus 로고    scopus 로고
    • The significance of type II and PrxQ peroxiredoxins for antioxidative stress response in the purple bacterium Rhodobacter sphaeroides
    • DOI 10.1074/jbc.M702855200
    • Wakita M, Masuda S, Motohashi K, Hisabori T, Ohta H, and Takamiya K. The significance of type II and PrxQ peroxiredoxins for antioxidative stress response in the purple bacterium Rhodobacter sphaeroides. J Biol Chem 282: 27792-27801, 2007. (Pubitemid 47529504)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.38 , pp. 27792-27801
    • Wakita, M.1    Masuda, S.2    Motohashi, K.3    Hisabori, T.4    Ohta, H.5    Takamiya, K.-I.6
  • 258
    • 30544434167 scopus 로고    scopus 로고
    • Comparative protein profiling identifies elongation factor-1beta and tryparedoxin peroxidase as factors associated with metastasis in Leishmania guyanensis
    • DOI 10.1016/j.molbiopara.2005.10.008, PII S016668510500304X
    • Walker J, Acestor N, Gongora R, Quadroni M, Segura I, Fasel N, and Saravia N. Comparative protein profiling identifies elongation factor-1beta and tryparedoxin peroxidase as factors associated with metastasis in Leishmania guyanensis. Mol Biochem Parasitol 145: 254-264, 2006. (Pubitemid 43083367)
    • (2006) Molecular and Biochemical Parasitology , vol.145 , Issue.2 , pp. 254-264
    • Walker, J.1    Acestor, N.2    Gongora, R.3    Quadroni, M.4    Segura, I.5    Fasel, N.6    Saravia, N.G.7
  • 259
    • 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, and Bruchhaus I. 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.
    • (1999) J Biol Chem , vol.274 , pp. 26051-26056
    • Wassmann, C.1    Hellberg, A.2    Tannich, E.3    Bruchhaus, I.4
  • 260
    • 0041355353 scopus 로고    scopus 로고
    • RNA interference identifies two hydroperoxide metabolizing enzymes that are essential to the bloodstream form of the African trypanosome
    • DOI 10.1074/jbc.M303035200
    • Wilkinson S, Horn D, Prathalingam S, and Kelly J. 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. (Pubitemid 37048342)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.34 , pp. 31640-31646
    • Wilkinson, S.R.1    Horn, D.2    Prathalingam, S.R.3    Kelly, J.M.4
  • 261
    • 0034678059 scopus 로고    scopus 로고
    • Distinct mitochondrial and cytosolic enzymes mediate trypanothione- dependent peroxide metabolism in Trypanosoma cruzi
    • DOI 10.1074/jbc.275.11.8220
    • Wilkinson S, Temperton N, Mondragon A, and Kelly J. Distinct mitochondrial and cytosolic enzymes mediate trypanothione-dependent peroxide metabolism in Trypanosoma cruzi. J Biol Chem 275: 8220-8225, 2000. (Pubitemid 30159739)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.11 , pp. 8220-8225
    • Wilkinson, S.R.1    Temperton, N.J.2    Mondragon, A.3    Kelly, J.M.4
  • 262
    • 0035144556 scopus 로고    scopus 로고
    • + T helper cell and B-cell responses against a novel egg antigen, thioredoxin peroxidase
    • DOI 10.1128/IAI.69.2.1134-1141.2001
    • Williams D, Asahi H, Botkin D, and Stadecker M. Schistosome infection stimulates host CD4 (+) T helper cell and B-cell responses against a novel egg antigen, thioredoxin peroxidase. Infect Immun 69: 1134-1141, 2001. (Pubitemid 32109582)
    • (2001) Infection and Immunity , vol.69 , Issue.2 , pp. 1134-1141
    • Williams, D.L.1    Asahi, H.2    Botkin, D.J.3    Stadecker, M.J.4
  • 263
    • 48449107159 scopus 로고    scopus 로고
    • Thiol chemistry and specificity in redox signaling
    • Winterbourn C and Hampton M. Thiol chemistry and specificity in redox signaling. Free Radic Biol Med 45: 549- 561, 2008.
    • (2008) Free Radic Biol Med , vol.45 , pp. 549-561
    • Winterbourn, C.1    Hampton, M.2
  • 264
    • 76749102420 scopus 로고    scopus 로고
    • Inactivation of peroxiredoxin I by phosphorylation allows localized H2O2 accumulation for cell signaling
    • Woo HA, Yim SH, Shin DH, Kang D, Yu DY, and Rhee SG. Inactivation of peroxiredoxin I by phosphorylation allows localized H2O2 accumulation for cell signaling. Cell 140: 517-528, 2010.
    • (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    Rhee, S.G.6
  • 265
    • 0242668686 scopus 로고    scopus 로고
    • Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling
    • DOI 10.1126/science.1080405
    • Wood ZA, Poole LB, and Karplus PA. Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science 300: 650-653, 2003. (Pubitemid 36520591)
    • (2003) Science , vol.300 , Issue.5619 , pp. 650-653
    • Wood, Z.A.1    Poole, L.B.2    Karplus, P.A.3
  • 266
    • 0037197672 scopus 로고    scopus 로고
    • Dimers to doughnuts: Redox-sensitive oligomerization of 2-cysteine peroxiredoxins
    • DOI 10.1021/bi012173m
    • Wood ZA, Poole LB, Hantgan RR, and Karplus PA. Dimers to doughnuts: redox-sensitive oligomerization of 2-cysteine peroxiredoxins. Biochemistry 41: 5493-5504, 2002. (Pubitemid 34429383)
    • (2002) Biochemistry , vol.41 , Issue.17 , pp. 5493-5504
    • Wood, Z.A.1    Poole, L.B.2    Hantgan, R.R.3    Karplus, P.A.4
  • 268
    • 0037222255 scopus 로고    scopus 로고
    • Structure, mechanism and regulation of peroxiredoxins
    • DOI 10.1016/S0968-0004(02)00003-8, PII S0968000402000038
    • Wood ZA, Schröder E, Harris JR, and Poole LB. Structure, mechanism and regulation of peroxiredoxins. Trends Biochem Sci 28: 32-40, 2003. (Pubitemid 36051004)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.1 , pp. 32-40
    • Wood, Z.A.1    Schroder, E.2    Harris, J.R.3    Poole, L.B.4
  • 269
    • 4544289321 scopus 로고    scopus 로고
    • Dual action of antimonial drugs on thiol redox metabolism in the human pathogen Leishmania donovani
    • Wyllie S, Cunningham ML, and Fairlamb AH. Dual action of antimonial drugs on thiol redox metabolism in the human pathogen Leishmania donovani. J Biol Chem 279: 39925- 39932, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 39925-39932
    • Wyllie, S.1    Cunningham, M.L.2    Fairlamb, A.H.3
  • 270
    • 77954761899 scopus 로고    scopus 로고
    • Elevated levels of tryparedoxin peroxidase in antimony unresponsive Leishmania donovani field isolates
    • Wyllie S, Mandal G, Singh N, Sundar S, Fairlamb A, and Chatterjee M. Elevated levels of tryparedoxin peroxidase in antimony unresponsive Leishmania donovani field isolates. Mol Biochem Parasitol 173: 162-164, 2010.
    • (2010) Mol Biochem Parasitol , vol.173 , pp. 162-164
    • Wyllie, S.1    Mandal, G.2    Singh, N.3    Sundar, S.4    Fairlamb, A.5    Chatterjee, M.6
  • 271
    • 13844267219 scopus 로고    scopus 로고
    • Expression of mRNAs and proteins for peroxiredoxins in Plasmodium falciparum erythrocytic stage
    • DOI 10.1016/j.parint.2004.08.005
    • Yano K, Komaki-Yasuda K, Kobayashi T, Takemae H, Kita K, Kano S, and Kawazu S-I. Expression of mRNAs and proteins for peroxiredoxins in Plasmodium falciparum erythrocytic stage. Parasitol Int 54: 35-41, 2005. (Pubitemid 40248723)
    • (2005) Parasitology International , vol.54 , Issue.1 , pp. 35-41
    • Yano, K.1    Komaki-Yasuda, K.2    Kobayashi, T.3    Takemae, H.4    Kita, K.5    Kano, S.6    Kawazu, S.-I.7
  • 272
    • 33744546817 scopus 로고    scopus 로고
    • 2-Cys Peroxiredoxin TPx-1 is involved in gametocyte development in Plasmodium berghei
    • DOI 10.1016/j.molbiopara.2006.02.018, PII S0166685106000764
    • Yano K, Komaki-Yasuda K, Tsuboi T, Torii M, Kano S, and Kawazu S. 2-Cys Peroxiredoxin TPx-1 is involved in gametocyte development in Plasmodium berghei. Mol Biochem Parasitol 148: 44-51, 2006. (Pubitemid 43810229)
    • (2006) Molecular and Biochemical Parasitology , vol.148 , Issue.1 , pp. 44-51
    • Yano, K.1    Komaki-Yasuda, K.2    Tsuboi, T.3    Torii, M.4    Kano, S.5    Kawazu, S.-i.6
  • 273
    • 43049127225 scopus 로고    scopus 로고
    • Disruption of the Plasmodium berghei 2-Cys peroxiredoxin TPx-1 gene hinders the sporozoite development in the vector mosquito
    • DOI 10.1016/j.molbiopara.2008.03.002, PII S0166685108000650
    • Yano K, Otsuki H, Arai M, Komaki-Yasuda K, Tsuboi T, Torii M, Kano S, and Kawazu S. 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. (Pubitemid 351621905)
    • (2008) Molecular and Biochemical Parasitology , vol.159 , Issue.2 , pp. 142-145
    • Yano, K.1    Otsuki, H.2    Arai, M.3    Komaki-Yasuda, K.4    Tsuboi, T.5    Torii, M.6    Kano, S.7    Kawazu, S.-I.8
  • 275
    • 77956533669 scopus 로고    scopus 로고
    • Conformational and oligomeric effects on the cysteine pKa of tryparedoxin peroxidase
    • Yuan Y, Knaggs MH, Poole LB, Fetrow JS, and Salsbury FA. Conformational and oligomeric effects on the cysteine pKa of tryparedoxin peroxidase. J Biomol Struct Dyn 28: 51-70, 2010.
    • (2010) J Biomol Struct Dyn , vol.28 , pp. 51-70
    • Yuan, Y.1    Knaggs, M.H.2    Poole, L.B.3    Fetrow, J.S.4    Salsbury, F.A.5
  • 276
    • 39049181435 scopus 로고    scopus 로고
    • RNA interference to the expression of peroxiredoxin-related genes in Trichomonas vaginalis
    • Abstract of Chinese-language article
    • Zhang J, Fu Y, Xu X, Wu T, and Cao F. [RNA interference to the expression of peroxiredoxin-related genes in Trichomonas vaginalis]. (Abstract of Chinese-language article). Zhongguo Ji Sheng Chong Xue Yu Ji Sheng Chong Bing Za Zhi 23: 437-440, 2005.
    • (2005) Zhongguo Ji Sheng Chong Xue Yu Ji Sheng Chong Bing Za Zhi , vol.23 , pp. 437-440
    • Zhang, J.1    Fu, Y.2    Xu, X.3    Wu, T.4    Cao, F.5
  • 277
    • 79953779813 scopus 로고    scopus 로고
    • Analysis of thioredoxin peroxidase as a promising antigen for diagnosis of Fasciola gigantica infection: A preliminary study
    • Zhang W, Rogniaux H, Huang W, Chauvin A, and Moreau E. Analysis of thioredoxin peroxidase as a promising antigen for diagnosis of Fasciola gigantica infection: a preliminary study. Parasitol Int 60: 206-208, 2011.
    • (2011) Parasitol Int , vol.60 , pp. 206-208
    • Zhang, W.1    Rogniaux, H.2    Huang, W.3    Chauvin, A.4    Moreau, E.5
  • 278
    • 0031826863 scopus 로고    scopus 로고
    • The peroxidoxin 2 protein of the human parasite Onchocerca volvulus: Recombinant expression, immunolocalization, and demonstration of homologous molecules in other species
    • DOI 10.1007/s004360050461
    • Zipfel P, Schrum S, Bialonski A, and Buttner D. The peroxidoxin 2 protein of the human parasite Onchocerca volvulus: recombinant expression, immunolocalization, and demonstration of homologous molecules in other species. Parasitol Res 84: 623-631, 1998. (Pubitemid 28370751)
    • (1998) Parasitology Research , vol.84 , Issue.8 , pp. 623-631
    • Zipfel, P.F.1    Schrum, S.2    Bialonski, A.3    Buttner, D.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.