메뉴 건너뛰기




Volumn 22, Issue 4, 1996, Pages 295-314

Antioxidant defense mechanisms in parasitic protozoa

Author keywords

antioxidants; Entamoeba histolytica; Giardia; Leishmania; parasites; Plasmodium; protozoa; Trypanosoma

Indexed keywords

ANTIOXIDANT; GLUTATHIONE; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; HYDROGEN PEROXIDE; REACTIVE OXYGEN METABOLITE;

EID: 0030458544     PISSN: 1040841X     EISSN: None     Source Type: Journal    
DOI: 10.3109/10408419609105484     Document Type: Article
Times cited : (93)

References (144)
  • 1
    • 0024330563 scopus 로고
    • Microbial superoxide dismutases
    • Hassan, H. M., Microbial superoxide dismutases, Adv. Genet., 26, 65, 1989.
    • (1989) Adv. Genet. , vol.26 , pp. 65
    • Hassan, H.M.1
  • 2
    • 0028113130 scopus 로고
    • Superoxide dismutase
    • James, E. R., Superoxide dismutase, Parasitol. Today, 10, 481, 1994.
    • (1994) Parasitol. Today , vol.10 , pp. 481
    • James, E.R.1
  • 3
    • 0028804901 scopus 로고
    • Bacterial (Cu.Zn)-superoxide dismutase: Phylogenetically distinct from the eukaryotic enzyme, and not so rare after all!
    • Kroll, J. S., Langford, P. R., Wilks, K. E., and Keil, A. D., Bacterial (Cu.Zn)-superoxide dismutase: phylogenetically distinct from the eukaryotic enzyme, and not so rare after all!, Microbiology, 141, 2271, 1995.
    • (1995) Microbiology , vol.141 , pp. 2271
    • Kroll, J.S.1    Langford, P.R.2    Wilks, K.E.3    Keil, A.D.4
  • 4
    • 0029918858 scopus 로고    scopus 로고
    • Functional significance of the Cu.Zn-SOD in Escherichia coli
    • Benov, L. and Fridovich, I., Functional significance of the Cu.Zn-SOD in Escherichia coli, Arch. Biochem. Biophys., 327, 249, 1996.
    • (1996) Arch. Biochem. Biophys. , vol.327 , pp. 249
    • Benov, L.1    Fridovich, I.2
  • 5
    • 0014320055 scopus 로고
    • Techniques of axenic cultivation of Entamoeba histolytica Schaudinn, 1903 and E. histolytica-like amoebae
    • Diamond, L. S., Techniques of axenic cultivation of Entamoeba histolytica Schaudinn, 1903 and E. histolytica-like amoebae, J. Parasitol., 54, 715, 1968.
    • (1968) J. Parasitol. , vol.54 , pp. 715
    • Diamond, L.S.1
  • 6
    • 0017846267 scopus 로고
    • A new medium for the axenic cultivation of Entamoeba histolytica and other Entamoebae
    • Diamond, L. S., Harlow, D. R., and Cunnick, C. C., A new medium for the axenic cultivation of Entamoeba histolytica and other Entamoebae, Trans. R. Soc. Trop. Med. Hyg., 72, 431, 1978.
    • (1978) Trans. R. Soc. Trop. Med. Hyg. , vol.72 , pp. 431
    • Diamond, L.S.1    Harlow, D.R.2    Cunnick, C.C.3
  • 7
    • 0343994896 scopus 로고
    • Importance of O-R potential in initiating cultures of axenically grown Entamoeba histolytica from small inocula
    • Singh, B. N., Das, S. R., and Dutta, G. P., Importance of O-R potential in initiating cultures of axenically grown Entamoeba histolytica from small inocula, Curr. Sci., 42, 227, 1973.
    • (1973) Curr. Sci. , vol.42 , pp. 227
    • Singh, B.N.1    Das, S.R.2    Dutta, G.P.3
  • 8
    • 0344128364 scopus 로고
    • Effect of O-R potential on the growth and multiplication of axenic Entamoeba histolytica
    • Singh, B. N., Dutta, G. P., and Das, S. R., Effect of O-R potential on the growth and multiplication of axenic Entamoeba histolytica, Curr. Sci., 43, 71, 1974.
    • (1974) Curr. Sci. , vol.43 , pp. 71
    • Singh, B.N.1    Dutta, G.P.2    Das, S.R.3
  • 9
    • 0019464089 scopus 로고
    • Entamoeba histolytica and Giardia lamblia: Growth responses to reducing agents
    • Gillin, F. D. and Diamond, L. S., Entamoeba histolytica and Giardia lamblia: growth responses to reducing agents, Exp. Parasitol., 51, 382, 1981.
    • (1981) Exp. Parasitol. , vol.51 , pp. 382
    • Gillin, F.D.1    Diamond, L.S.2
  • 10
    • 0021729633 scopus 로고
    • Metabolism of Entamoeba histolytica Schaudinn, 1903
    • Reeves, R. E., Metabolism of Entamoeba histolytica Schaudinn, 1903, Adv. Parasitol., 23, 105, 1984.
    • (1984) Adv. Parasitol. , vol.23 , pp. 105
    • Reeves, R.E.1
  • 11
    • 0344991005 scopus 로고
    • pH as the critical factor in cultivation of Entamoeba histolytica
    • Mehlotra, R. K., Shukla, O. P., and Singh, B. N., pH as the critical factor in cultivation of Entamoeba histolytica, Ind. J. Parasitol., 10, 135, 1986.
    • (1986) Ind. J. Parasitol. , vol.10 , pp. 135
    • Mehlotra, R.K.1    Shukla, O.P.2    Singh, B.N.3
  • 12
    • 0016382328 scopus 로고
    • Entamoeba histolytica. I. Aerobic metabolism
    • Weinbach, E. C. and Diamond, L. S., Entamoeba histolytica. I. Aerobic metabolism, Exp. Parasitol., 35, 232, 1974.
    • (1974) Exp. Parasitol. , vol.35 , pp. 232
    • Weinbach, E.C.1    Diamond, L.S.2
  • 13
    • 0018745110 scopus 로고
    • Growth responses of axenic Entamoeba histolytica to hydrogen, carbon dioxide and oxygen
    • Band, R. N. and Cirrito, H., Growth responses of axenic Entamoeba histolytica to hydrogen, carbon dioxide and oxygen, J. Protozool., 26, 282, 1979.
    • (1979) J. Protozool. , vol.26 , pp. 282
    • Band, R.N.1    Cirrito, H.2
  • 14
    • 26744447347 scopus 로고
    • Superoxide dismutase activity of Acanthamoeba and two anaerobic Entamoeba species
    • Sykes, D. E. and Band, R. N., Superoxide dismutase activity of Acanthamoeba and two anaerobic Entamoeba species, J. Cell Biol., 75, 86a, 1977.
    • (1977) J. Cell Biol. , vol.75
    • Sykes, D.E.1    Band, R.N.2
  • 15
  • 16
    • 0025946099 scopus 로고
    • Pathogenic and non-pathogenic Entamoeba histolytica: Identification and molecular cloning of an iron-containing superoxide dismutase
    • Tannich, E., Bruchhaus, I., Walter, R. D., and Horstmann, R. D., Pathogenic and non-pathogenic Entamoeba histolytica: identification and molecular cloning of an iron-containing superoxide dismutase, Mol. Biochem. Parasitol., 49, 61, 1991.
    • (1991) Mol. Biochem. Parasitol. , vol.49 , pp. 61
    • Tannich, E.1    Bruchhaus, I.2    Walter, R.D.3    Horstmann, R.D.4
  • 17
    • 0019628368 scopus 로고
    • Susceptibility of Entamoeba histolytica to oxygen intermediates
    • Murray, H. W., Aley, S. B., and Scott, W. A., Susceptibility of Entamoeba histolytica to oxygen intermediates, Mol. Biochem. Parasitol., 3, 381, 1981.
    • (1981) Mol. Biochem. Parasitol. , vol.3 , pp. 381
    • Murray, H.W.1    Aley, S.B.2    Scott, W.A.3
  • 19
    • 77956868541 scopus 로고
    • A roll tube method for cultivation of strict anaerobes
    • Norris, J. R. and Ribbons, D. W., Eds., Academic Press, New York
    • Hungate, R. E., A roll tube method for cultivation of strict anaerobes, in Methods in Microbiology, 3B, Norris, J. R. and Ribbons, D. W., Eds., Academic Press, New York, 1969, 117.
    • (1969) Methods in Microbiology , vol.3 B , pp. 117
    • Hungate, R.E.1
  • 20
    • 0019830957 scopus 로고
    • Entamoeba histolytica and Giardia lamblia: Effects of cysteine and oxygen tension on trophozoite attachment and survival in culture media
    • Gillin, F. D. and Diamond, L. S., Entamoeba histolytica and Giardia lamblia: effects of cysteine and oxygen tension on trophozoite attachment and survival in culture media, Exp. Parasitol., 52, 9, 1981.
    • (1981) Exp. Parasitol. , vol.52 , pp. 9
    • Gillin, F.D.1    Diamond, L.S.2
  • 21
    • 17744407386 scopus 로고
    • Reducing agents and Entamoeba histolytica
    • Mehlotra, R. K. and Shukla, O. P., Reducing agents and Entamoeba histolytica, Parasitol. Today, 4, 82, 1988.
    • (1988) Parasitol. Today , vol.4 , pp. 82
    • Mehlotra, R.K.1    Shukla, O.P.2
  • 22
    • 0026316667 scopus 로고
    • Molecular and cellular characterization of the 29-kilodalton peripheral membrane protein of Entamoeba histolytica: Differentiation between pathogenic and non-pathogenic isolates
    • Reed, S. L., Flores, B. M., Batzer, M. A., Stein, M. A., Stroeher, V. L., Carlton, J. E., Diedrich, D. L., and Torian, B. E., Molecular and cellular characterization of the 29-kilodalton peripheral membrane protein of Entamoeba histolytica: differentiation between pathogenic and non-pathogenic isolates, Infect. Immun., 60, 542, 1992.
    • (1992) Infect. Immun. , vol.60 , pp. 542
    • Reed, S.L.1    Flores, B.M.2    Batzer, M.A.3    Stein, M.A.4    Stroeher, V.L.5    Carlton, J.E.6    Diedrich, D.L.7    Torian, B.E.8
  • 23
    • 0027196296 scopus 로고
    • Analysis of the genomic sequence encoding the 29-kDa cysteine-rich protein of Entamoeba histolytica
    • Bruchhaus, I. and Tannich, E., Analysis of the genomic sequence encoding the 29-kDa cysteine-rich protein of Entamoeba histolytica, Trop. Med. Parasitol., 44, 116, 1993.
    • (1993) Trop. Med. Parasitol. , vol.44 , pp. 116
    • Bruchhaus, I.1    Tannich, E.2
  • 24
    • 0028914574 scopus 로고
    • Identification of an Entamoeba histolytica gene encoding a protein homologous to prokaryotic disulphide oxidoreductases
    • Bruchhaus, I. and Tannich, E., Identification of an Entamoeba histolytica gene encoding a protein homologous to prokaryotic disulphide oxidoreductases, Mol. Biochem. Parasitol., 70, 187, 1995.
    • (1995) Mol. Biochem. Parasitol. , vol.70 , pp. 187
    • Bruchhaus, I.1    Tannich, E.2
  • 25
    • 0028054245 scopus 로고
    • Induction of the iron-containing superoxide dismutase in Entamoeba histolytica by a superoxide anion-generating system or by iron chelation
    • Bruchhaus, I. and Tannich, E., Induction of the iron-containing superoxide dismutase in Entamoeba histolytica by a superoxide anion-generating system or by iron chelation, Mol. Biochem. Parasitol., 67, 281, 1994.
    • (1994) Mol. Biochem. Parasitol. , vol.67 , pp. 281
    • Bruchhaus, I.1    Tannich, E.2
  • 26
    • 0018884074 scopus 로고
    • Axenic growth of Giardia lamblia in Diamond's TP-S-1 medium
    • Visvesvara, G. S., Axenic growth of Giardia lamblia in Diamond's TP-S-1 medium, Trans. R. Soc. Trop. Med. Hyg., 74, 213, 1980.
    • (1980) Trans. R. Soc. Trop. Med. Hyg. , vol.74 , pp. 213
    • Visvesvara, G.S.1
  • 27
    • 0020651210 scopus 로고
    • Axenic culture of Giardia lamblia in TYI-S-33 medium supplemented with bile
    • Keister, D. B., Axenic culture of Giardia lamblia in TYI-S-33 medium supplemented with bile, Trans. R. Soc. Trop. Med. Hyg., 77, 487, 1983.
    • (1983) Trans. R. Soc. Trop. Med. Hyg. , vol.77 , pp. 487
    • Keister, D.B.1
  • 30
    • 0027525402 scopus 로고
    • Cysteine is the major low-molecular weight thiol in Giardia duodenalis
    • Brown, D. M., Upcroft, J. A., and Upcroft, P., Cysteine is the major low-molecular weight thiol in Giardia duodenalis, Mol. Biochem. Parasitol., 61, 155, 1993.
    • (1993) Mol. Biochem. Parasitol. , vol.61 , pp. 155
    • Brown, D.M.1    Upcroft, J.A.2    Upcroft, P.3
  • 33
    • 0028384696 scopus 로고
    • The uptake and metabolism of cysteine by Giardia lamblia trophozoites
    • Lujan, H. D. and Nash, T. E., The uptake and metabolism of cysteine by Giardia lamblia trophozoites, J. Euk. Microbiol., 41, 169, 1994.
    • (1994) J. Euk. Microbiol. , vol.41 , pp. 169
    • Lujan, H.D.1    Nash, T.E.2
  • 34
    • 0024342966 scopus 로고
    • Novel biochemical pathways in parasitic protozoa
    • Fairlamb, A. H., Novel biochemical pathways in parasitic protozoa, Parasitology, 99, S93, 1989.
    • (1989) Parasitology , vol.99
    • Fairlamb, A.H.1
  • 35
    • 0019076947 scopus 로고
    • Purification and properties of NADPH:flavin oxidoreductase from Entamoeba histolytica
    • Lo, H.-S. and Reeves, R. E., Purification and properties of NADPH:flavin oxidoreductase from Entamoeba histolytica, Mol. Biochem. Parasitol., 2, 23, 1980.
    • (1980) Mol. Biochem. Parasitol. , vol.2 , pp. 23
    • Lo, H.-S.1    Reeves, R.E.2
  • 36
    • 0023879239 scopus 로고
    • The purification and properties of two soluble reduced nicotinamide:acceptor oxidoreductases from Trichomonas vaginalis
    • Linstead, D. J. and Bradley, S., The purification and properties of two soluble reduced nicotinamide:acceptor oxidoreductases from Trichomonas vaginalis, Mol. Biochem. Parasitol., 27, 125, 1988.
    • (1988) Mol. Biochem. Parasitol. , vol.27 , pp. 125
    • Linstead, D.J.1    Bradley, S.2
  • 37
    • 0000146018 scopus 로고
    • Cultivation in a semi-defined medium of animal infective forms of Trypanosoma brucei, T. equiperdum, T. evansi, T. rhodesiense and T. gambiense
    • Baltz, T., Baltz, D., Giroud, G., and Crockett, J., Cultivation in a semi-defined medium of animal infective forms of Trypanosoma brucei, T. equiperdum, T. evansi, T. rhodesiense and T. gambiense, EMBO J., 4, 1273, 1985.
    • (1985) EMBO J. , vol.4 , pp. 1273
    • Baltz, T.1    Baltz, D.2    Giroud, G.3    Crockett, J.4
  • 38
    • 0022410467 scopus 로고
    • Cysteine eliminates the feeder cell requirement for cultivation of Trypanosoma brucei bloodstream forms in vitro
    • Duszenko, M., Ferguson, M. A. J., Lamont, G. S., Rifkin, M. R., and Cross, G. A. M., Cysteine eliminates the feeder cell requirement for cultivation of Trypanosoma brucei bloodstream forms in vitro, J. Exp. Med., 162, 1256, 1985.
    • (1985) J. Exp. Med. , vol.162 , pp. 1256
    • Duszenko, M.1    Ferguson, M.A.J.2    Lamont, G.S.3    Rifkin, M.R.4    Cross, G.A.M.5
  • 39
    • 0025350785 scopus 로고
    • Differentiation of Trypanosoma brucei bloodstream trypomastigotes from long slender to short stumpy-like forms in axenic culture
    • Hamm, B., Schindler, A., Mecke, D., and Duszenko, M., Differentiation of Trypanosoma brucei bloodstream trypomastigotes from long slender to short stumpy-like forms in axenic culture, Mol. Biochem. Parasitol., 40, 13, 1990.
    • (1990) Mol. Biochem. Parasitol. , vol.40 , pp. 13
    • Hamm, B.1    Schindler, A.2    Mecke, D.3    Duszenko, M.4
  • 40
    • 0026593156 scopus 로고
    • Cysteine is an essential growth factor for Trypanosoma brucei bloodstream forms
    • Duszenko, M., Muhlstadt, K., and Broder, A., Cysteine is an essential growth factor for Trypanosoma brucei bloodstream forms, Mol. Biochem. Parasitol., 50, 269, 1992.
    • (1992) Mol. Biochem. Parasitol. , vol.50 , pp. 269
    • Duszenko, M.1    Muhlstadt, K.2    Broder, A.3
  • 41
    • 0017694023 scopus 로고
    • Hydrogen peroxide generation in Trypanosoma cruzi
    • Boveris, A. and Stoppani, A. O. M., Hydrogen peroxide generation in Trypanosoma cruzi, Experientia, 33, 1306, 1977.
    • (1977) Experientia , vol.33 , pp. 1306
    • Boveris, A.1    Stoppani, A.O.M.2
  • 42
    • 0017654397 scopus 로고
    • Heme lysis of the bloodstream forms of Trypanosoma brucei
    • Meshnick, S. R., Chang, K.-P., and Cerami, A., Heme lysis of the bloodstream forms of Trypanosoma brucei, Biochem. Pharmacol., 26, 1923, 1977.
    • (1977) Biochem. Pharmacol. , vol.26 , pp. 1923
    • Meshnick, S.R.1    Chang, K.-P.2    Cerami, A.3
  • 43
    • 0018148432 scopus 로고
    • An approach to the development of new drugs for African trypanosomiasis
    • Meshnick, S. R., Blobstein, S. H., Grady, R. W., and Cerami, A., An approach to the development of new drugs for African trypanosomiasis, J. Exp. Med., 148, 569, 1978.
    • (1978) J. Exp. Med. , vol.148 , pp. 569
    • Meshnick, S.R.1    Blobstein, S.H.2    Grady, R.W.3    Cerami, A.4
  • 45
    • 0029917178 scopus 로고    scopus 로고
    • Cloning of an Fe-superoxide dismutase gene homologue from Trypanosoma cruzi
    • Temperton, N. J., Wilkinson, S. R., and Kelly, L. M., Cloning of an Fe-superoxide dismutase gene homologue from Trypanosoma cruzi, Mol. Biochem. Parasitol., 76, 339, 1996.
    • (1996) Mol. Biochem. Parasitol. , vol.76 , pp. 339
    • Temperton, N.J.1    Wilkinson, S.R.2    Kelly, L.M.3
  • 46
    • 0021933665 scopus 로고
    • Identification of a novel, thiol-containing co-factor essential for glutathione reductase enzyme activity in trypanosomatids
    • Fairlamb, A. and Cerami, A., Identification of a novel, thiol-containing co-factor essential for glutathione reductase enzyme activity in trypanosomatids, Mol. Biochem. Parasitol., 14, 187, 1985.
    • (1985) Mol. Biochem. Parasitol. , vol.14 , pp. 187
    • Fairlamb, A.1    Cerami, A.2
  • 47
    • 0022002912 scopus 로고
    • Trypanothione: A novel bis (glutathionyl) spermidine co-factor for glutathione reductase in trypanosomatids
    • Fairlamb, A., Blackburn, P., Ulrich, P., Chait, B., and Cerami, A., Trypanothione: a novel bis (glutathionyl) spermidine co-factor for glutathione reductase in trypanosomatids, Science, 22, 1485, 1985.
    • (1985) Science , vol.22 , pp. 1485
    • Fairlamb, A.1    Blackburn, P.2    Ulrich, P.3    Chait, B.4    Cerami, A.5
  • 48
    • 0022475723 scopus 로고
    • Hydrogen peroxide metabolism in Trypanosoma brucei
    • Penketh, P. G. and Klein, R. A., Hydrogen peroxide metabolism in Trypanosoma brucei, Mol. Biochem. Parasitol., 20, 111, 1986.
    • (1986) Mol. Biochem. Parasitol. , vol.20 , pp. 111
    • Penketh, P.G.1    Klein, R.A.2
  • 49
    • 0023263401 scopus 로고
    • Trypanothione dependent peroxide metabolism in Crithidia fasciculata and Trypanosoma brncei
    • Henderson, G. B., Fairlamb, A. H., and Cerami, A., Trypanothione dependent peroxide metabolism in Crithidia fasciculata and Trypanosoma brncei, Mol. Biochem. Parasitol., 24, 39, 1987.
    • (1987) Mol. Biochem. Parasitol. , vol.24 , pp. 39
    • Henderson, G.B.1    Fairlamb, A.H.2    Cerami, A.3
  • 51
    • 0027375651 scopus 로고
    • Trypanothione-dependent peroxide metabolism in Trypanosoma cruzi different stages
    • Carnieri, E. G. S., Moreno, S. N. J., and Docampo, R., Trypanothione-dependent peroxide metabolism in Trypanosoma cruzi different stages, Mol. Biochem. Parasitol., 61, 79, 1993.
    • (1993) Mol. Biochem. Parasitol. , vol.61 , pp. 79
    • Carnieri, E.G.S.1    Moreno, S.N.J.2    Docampo, R.3
  • 52
    • 0028148024 scopus 로고
    • Ascorbate variations and dehydroascorbate reductase activity in Trypanosoma cruzi epimastigotes and trypomastigotes
    • Clark, D., Albrecht, M., and Arevalo, J., Ascorbate variations and dehydroascorbate reductase activity in Trypanosoma cruzi epimastigotes and trypomastigotes, Mol. Biochem. Parasitol., 66, 143, 1994.
    • (1994) Mol. Biochem. Parasitol. , vol.66 , pp. 143
    • Clark, D.1    Albrecht, M.2    Arevalo, J.3
  • 53
    • 0018357483 scopus 로고
    • Activation of macrophages in vivo and in vitro: Correlation between hydrogen peroxide release and killing of T. cruzi
    • Nathan, C., Nogueira, N., Juangbhanich, C., Ellis, J., and Cohn, Z., Activation of macrophages in vivo and in vitro: correlation between hydrogen peroxide release and killing of T. cruzi, J. Exp. Med., 149, 1056, 1979.
    • (1979) J. Exp. Med. , vol.149 , pp. 1056
    • Nathan, C.1    Nogueira, N.2    Juangbhanich, C.3    Ellis, J.4    Cohn, Z.5
  • 54
    • 0019471126 scopus 로고
    • Susceptibility of Leishmania to oxygen intermediates and killing by normal macrophages
    • Murray, H. W., Susceptibility of Leishmania to oxygen intermediates and killing by normal macrophages, J. Exp. Med., 153, 1302, 1981.
    • (1981) J. Exp. Med. , vol.153 , pp. 1302
    • Murray, H.W.1
  • 55
    • 0020039579 scopus 로고
    • Oxidant-mediated damage of Leishmania donovani promastigotes
    • Reiner, N. E. and Kazura, J. W., Oxidant-mediated damage of Leishmania donovani promastigotes, Infect. Immun., 36, 1023, 1982.
    • (1982) Infect. Immun. , vol.36 , pp. 1023
    • Reiner, N.E.1    Kazura, J.W.2
  • 56
    • 0019440296 scopus 로고
    • Interaction of Leishmania with a macrophage cell-line: Correlation between intracellular killing and the generation of oxygen intermediates
    • Murray, H. W., Interaction of Leishmania with a macrophage cell-line: correlation between intracellular killing and the generation of oxygen intermediates, J. Exp. Med., 153, 1690, 1981.
    • (1981) J. Exp. Med. , vol.153 , pp. 1690
    • Murray, H.W.1
  • 57
    • 0019968229 scopus 로고
    • Cell-mediated immune response in experimental visceral leishmaniasis. I. Correlation between resistance to Leishmania donovani and lymphokine-generating capacity
    • Murray, H. W., Masur, H., and Keithly, J. S., Cell-mediated immune response in experimental visceral leishmaniasis. I. Correlation between resistance to Leishmania donovani and lymphokine-generating capacity, J. Immunol., 129, 344, 1982.
    • (1982) J. Immunol. , vol.129 , pp. 344
    • Murray, H.W.1    Masur, H.2    Keithly, J.S.3
  • 58
    • 0019978017 scopus 로고
    • Cell-mediated immune response in experimental visceral leishmaniasis. II. Oxygen-dependent killing of intracellular Leishmania donovani amastigotes
    • Murray, H. W., Cell-mediated immune response in experimental visceral leishmaniasis. II. Oxygen-dependent killing of intracellular Leishmania donovani amastigotes, J. Immunol., 129, 351, 1982.
    • (1982) J. Immunol. , vol.129 , pp. 351
    • Murray, H.W.1
  • 59
    • 0020607592 scopus 로고
    • Killing of intracellular Leishmania donovani by human mononuclear phagocytes: Evidence for oxygen-dependent and -independent leishmanicidal activity
    • Murray, H. W. and Cartelli, D. M., Killing of intracellular Leishmania donovani by human mononuclear phagocytes: evidence for oxygen-dependent and -independent leishmanicidal activity, J. Clin. Invest., 72, 32, 1983.
    • (1983) J. Clin. Invest. , vol.72 , pp. 32
    • Murray, H.W.1    Cartelli, D.M.2
  • 60
    • 0019987001 scopus 로고
    • Failure of the phagocytic oxidative response to protect human monocyte-derived macrophages from infection by Leishmania donovani
    • Pearson, R. D., Harcus, J. L., Symes, P. H., Romito, R., and Donowitz, G. R., Failure of the phagocytic oxidative response to protect human monocyte-derived macrophages from infection by Leishmania donovani, J. Immunol., 129, 1282, 1982.
    • (1982) J. Immunol. , vol.129 , pp. 1282
    • Pearson, R.D.1    Harcus, J.L.2    Symes, P.H.3    Romito, R.4    Donowitz, G.R.5
  • 61
    • 0020543155 scopus 로고
    • Differential survival of Leishmania donovani amastigotes in human monocytes
    • Pearson, R. D., Harcus, J. L., Roberts, D., and Donowitz, G. R., Differential survival of Leishmania donovani amastigotes in human monocytes, J. Immunol., 131, 1994, 1983.
    • (1983) J. Immunol. , vol.131 , pp. 1994
    • Pearson, R.D.1    Harcus, J.L.2    Roberts, D.3    Donowitz, G.R.4
  • 62
    • 0021181879 scopus 로고
    • A study of the differential respiratory burst activity elicited by promastigotes and amastigotes of Leishmania donovani in murine resident peritoneal macrophages
    • Channon, J. Y., Roberts, M. B., and Blackwell, J. M., A study of the differential respiratory burst activity elicited by promastigotes and amastigotes of Leishmania donovani in murine resident peritoneal macrophages, Immunology, 53, 345, 1984.
    • (1984) Immunology , vol.53 , pp. 345
    • Channon, J.Y.1    Roberts, M.B.2    Blackwell, J.M.3
  • 63
    • 0022343132 scopus 로고
    • A study of the sensitivity of Leishmania donovani promastigotes and amastigotes to hydrogen peroxide. I. Differences in sensitivity correlate with parasite-mediated removal of hydrogen peroxide
    • Channon, J. Y. and Blackwell, J. M., A study of the sensitivity of Leishmania donovani promastigotes and amastigotes to hydrogen peroxide. I. Differences in sensitivity correlate with parasite-mediated removal of hydrogen peroxide, Parasitology, 91, 197, 1985.
    • (1985) Parasitology , vol.91 , pp. 197
    • Channon, J.Y.1    Blackwell, J.M.2
  • 65
    • 0027494350 scopus 로고
    • Phenotype of recombinant Leishmania donovani and Trypanosoma cruzi which over-express trypanothione reductase: Sensitivity towards agents that are thought to induce oxidative stress
    • Kelly, J. M., Taylor, M. C., Smith, K., Hunter, K. J., and Fairlamb, A. H., Phenotype of recombinant Leishmania donovani and Trypanosoma cruzi which over-express trypanothione reductase: sensitivity towards agents that are thought to induce oxidative stress, Eur. J. Biochem., 218, 29, 1993.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 29
    • Kelly, J.M.1    Taylor, M.C.2    Smith, K.3    Hunter, K.J.4    Fairlamb, A.H.5
  • 66
    • 0022592935 scopus 로고
    • Correlation between enhanced oxidative metabolism and leishmanicidal activity in activated macrophages from healer and non-healer mouse strains
    • Buchmüller-Rouiller, Y. and Mauël, J., Correlation between enhanced oxidative metabolism and leishmanicidal activity in activated macrophages from healer and non-healer mouse strains, J. Immunol., 136, 3884, 1986.
    • (1986) J. Immunol. , vol.136 , pp. 3884
    • Buchmüller-Rouiller, Y.1    Mauël, J.2
  • 67
    • 0023116482 scopus 로고
    • Impairment of the oxidative metabolism of mouse peritoneal macrophages by intracellular Leishmania spp
    • Buchmüller-Rouiller, Y. and Mauël, J., Impairment of the oxidative metabolism of mouse peritoneal macrophages by intracellular Leishmania spp., Infect. Immun., 55, 587, 1987.
    • (1987) Infect. Immun. , vol.55 , pp. 587
    • Buchmüller-Rouiller, Y.1    Mauël, J.2
  • 69
    • 0023853958 scopus 로고
    • Roles of CR3 and mannose receptors in the attachment and ingestion of Leishmania donovani by human mononuclear phagocytes
    • Wilson, M. E. and Pearson, R. D., Roles of CR3 and mannose receptors in the attachment and ingestion of Leishmania donovani by human mononuclear phagocytes, Infect. Immun., 56, 363, 1988.
    • (1988) Infect. Immun. , vol.56 , pp. 363
    • Wilson, M.E.1    Pearson, R.D.2
  • 70
    • 0021080912 scopus 로고
    • Receptors for C3b and C3bi promote phagocytosis but not the release of toxic oxygen from human phagocytes
    • Wright, S. D. and Silverstein, S. C., Receptors for C3b and C3bi promote phagocytosis but not the release of toxic oxygen from human phagocytes, J. Exp. Med., 158, 2016, 1983.
    • (1983) J. Exp. Med. , vol.158 , pp. 2016
    • Wright, S.D.1    Silverstein, S.C.2
  • 71
    • 0023667646 scopus 로고
    • Inhibition of protein kinase C activity by the Leishmania donovani lipophosphoglycan
    • McNeely, T. B. and Turco, S. J., Inhibition of protein kinase C activity by the Leishmania donovani lipophosphoglycan, Biochem. Biophys. Res. Commun., 148, 653, 1987.
    • (1987) Biochem. Biophys. Res. Commun. , vol.148 , pp. 653
    • McNeely, T.B.1    Turco, S.J.2
  • 72
    • 0025849761 scopus 로고
    • Leishmania donovani lipophosphoglycan selectively inhibits signal transduction in macrophages
    • Descoteaux, A., Turco, S. J., Sacks, D. L., and Matlashewski, G., Leishmania donovani lipophosphoglycan selectively inhibits signal transduction in macrophages, J. Immunol., 146, 2747, 1991.
    • (1991) J. Immunol. , vol.146 , pp. 2747
    • Descoteaux, A.1    Turco, S.J.2    Sacks, D.L.3    Matlashewski, G.4
  • 73
    • 0026673841 scopus 로고
    • Inhibition of macrophage protein kinase C-mediated protein phosphorylation by Leishmania donovani lipophosphoglycan
    • Descoteaux, A., Matlashewski, G., and Turco, S. J., Inhibition of macrophage protein kinase C-mediated protein phosphorylation by Leishmania donovani lipophosphoglycan, J. Immunol., 149, 3008, 1992.
    • (1992) J. Immunol. , vol.149 , pp. 3008
    • Descoteaux, A.1    Matlashewski, G.2    Turco, S.J.3
  • 75
    • 0025887577 scopus 로고
    • Hydrogen peroxide-mediated toxicity for Leishmania donovani chagasi promastigotes: Role of hydroxy radical and protection by heat shock
    • Zarley, J. H., Britigan, B. E., and Wilson, M. E., Hydrogen peroxide-mediated toxicity for Leishmania donovani chagasi promastigotes: role of hydroxy radical and protection by heat shock, J. Clin. Invest., 88, 1511, 1991.
    • (1991) J. Clin. Invest. , vol.88 , pp. 1511
    • Zarley, J.H.1    Britigan, B.E.2    Wilson, M.E.3
  • 76
    • 0028114539 scopus 로고
    • Response of Leishmania chagasi promastigotes to oxidant stress
    • Wilson, M. E., Andersen, K. A., and Britigan, B. E., Response of Leishmania chagasi promastigotes to oxidant stress, Infect. Immun., 62, 5133, 1994.
    • (1994) Infect. Immun. , vol.62 , pp. 5133
    • Wilson, M.E.1    Andersen, K.A.2    Britigan, B.E.3
  • 77
    • 0025203611 scopus 로고
    • Oxidative stress and the redox status of malaria-infected erythrocytes
    • Hunt, N. H. and Stocker, R., Oxidative stress and the redox status of malaria-infected erythrocytes, Blood Cells, 16, 499, 1990.
    • (1990) Blood Cells , vol.16 , pp. 499
    • Hunt, N.H.1    Stocker, R.2
  • 79
    • 0018777677 scopus 로고
    • Plasmodium falciparum: Microaerophilic requirements in human blood cells
    • Scheibel, L. W., Ashton, S. H., and Trager, W., Plasmodium falciparum: microaerophilic requirements in human blood cells, Exp. Parasitol., 47, 410, 1979.
    • (1979) Exp. Parasitol. , vol.47 , pp. 410
    • Scheibel, L.W.1    Ashton, S.H.2    Trager, W.3
  • 80
    • 0020681921 scopus 로고
    • Free oxygen radical generators as antimalarial drugs
    • Clark, I. A., Cowden, W. B., and Butcher, G. A., Free oxygen radical generators as antimalarial drugs, Lancet, 1, 234, 1983.
    • (1983) Lancet , vol.1 , pp. 234
    • Clark, I.A.1    Cowden, W.B.2    Butcher, G.A.3
  • 81
    • 0020672571 scopus 로고
    • Killing of blood-stage murine malaria parasites by hydrogen peroxide
    • Dockrell, H. M. and Playfair, J. H. L., Killing of blood-stage murine malaria parasites by hydrogen peroxide, Infect. Immun., 39, 456, 1983.
    • (1983) Infect. Immun. , vol.39 , pp. 456
    • Dockrell, H.M.1    Playfair, J.H.L.2
  • 82
    • 0021367318 scopus 로고
    • Oxidative killing of the intraerythrocytic malaria parasite Plasmodium yoelli by activated macrophages
    • Ockenhouse, C. F. and Shear, H. L., Oxidative killing of the intraerythrocytic malaria parasite Plasmodium yoelli by activated macrophages, J. Immunol., 132, 424, 1984.
    • (1984) J. Immunol. , vol.132 , pp. 424
    • Ockenhouse, C.F.1    Shear, H.L.2
  • 83
    • 0021167145 scopus 로고
    • Induction of crisis forms in the human malaria parasite Plasmodium falcipariun by γ-interferon-activated, monocyte-derived macrophages
    • Ockenhouse, C. F., Schulman, S., and Shear, H. L., Induction of crisis forms in the human malaria parasite Plasmodium falcipariun by γ-interferon-activated, monocyte-derived macrophages, J. Immunol., 133, 1601, 1984.
    • (1984) J. Immunol. , vol.133 , pp. 1601
    • Ockenhouse, C.F.1    Schulman, S.2    Shear, H.L.3
  • 84
    • 0027021116 scopus 로고
    • Correlation between destruction of malarial parasites by polymorphonuclear leucocytes and oxidative stress
    • Golenser, J., Kamyl, M., Tsafack, A., Marva, E., Cohen, A., Kitrossky, N., and Chevion, M., Correlation between destruction of malarial parasites by polymorphonuclear leucocytes and oxidative stress, Free Rad. Res. Commun., 17, 249, 1992.
    • (1992) Free Rad. Res. Commun. , vol.17 , pp. 249
    • Golenser, J.1    Kamyl, M.2    Tsafack, A.3    Marva, E.4    Cohen, A.5    Kitrossky, N.6    Chevion, M.7
  • 86
  • 87
    • 0023058890 scopus 로고
    • Oxygen consumption in Plasmodium berghei-infected murine red cells: A direct spectrophotometric assay in intact erythrocytes
    • Deslauriers, R., Moffatt, D. J., and Smith, I. C. P., Oxygen consumption in Plasmodium berghei-infected murine red cells: a direct spectrophotometric assay in intact erythrocytes, Biochim. Biophys. Acta, 886, 319, 1986.
    • (1986) Biochim. Biophys. Acta , vol.886 , pp. 319
    • Deslauriers, R.1    Moffatt, D.J.2    Smith, I.C.P.3
  • 88
    • 0026099675 scopus 로고
    • Mitochondria of mammalian Plasmodium spp
    • Fry, M. and Beesley, J. E., Mitochondria of mammalian Plasmodium spp., Parasitology, 102, 17, 1991.
    • (1991) Parasitology , vol.102 , pp. 17
    • Fry, M.1    Beesley, J.E.2
  • 89
    • 0023626466 scopus 로고
    • Oxidant stress in malaria as probed by stable nitroxide radicals in erythrocytes infected with Plasmodium berghei: The effects of primaquine and chloroquine
    • Deslauriers, R., Butler, K., and Smith, I. C. P., Oxidant stress in malaria as probed by stable nitroxide radicals in erythrocytes infected with Plasmodium berghei: the effects of primaquine and chloroquine, Biochim. Biophys. Acta, 931, 267, 1987.
    • (1987) Biochim. Biophys. Acta , vol.931 , pp. 267
    • Deslauriers, R.1    Butler, K.2    Smith, I.C.P.3
  • 90
    • 0002664391 scopus 로고
    • Malaria-induced erythrocyte oxidant sensitivity
    • Brewer, G. J., Ed., Alan R. Liss, New York
    • Etkin, N. L. and Eaton, J. W., Malaria-induced erythrocyte oxidant sensitivity, in Erythrocyte Structure and Function, Brewer, G. J., Ed., Alan R. Liss, New York, 1975, 219.
    • (1975) Erythrocyte Structure and Function , pp. 219
    • Etkin, N.L.1    Eaton, J.W.2
  • 91
    • 0023704318 scopus 로고
    • Detection of short-chain carbonyl products of peroxidation from malaria-parasite (Plasmodium vinckei)-infected red blood cells exposed to oxidative stress
    • Buffinton, G. D., Hunt, N. H., Cowden, W. B., and Clark, I. A., Detection of short-chain carbonyl products of peroxidation from malaria-parasite (Plasmodium vinckei)-infected red blood cells exposed to oxidative stress, Biochem. J., 249, 63, 1988.
    • (1988) Biochem. J. , vol.249 , pp. 63
    • Buffinton, G.D.1    Hunt, N.H.2    Cowden, W.B.3    Clark, I.A.4
  • 92
    • 0026786497 scopus 로고
    • Oxidative damage of erythrocytes infected with Plasmodium falciparum: An in vitro study
    • Mohan, K., Ganguly, N. K., Dubey, M. L., and Mahajan, R. C., Oxidative damage of erythrocytes infected with Plasmodium falciparum: an in vitro study, Ann. Hematol., 65, 131, 1992.
    • (1992) Ann. Hematol. , vol.65 , pp. 131
    • Mohan, K.1    Ganguly, N.K.2    Dubey, M.L.3    Mahajan, R.C.4
  • 94
    • 0022503788 scopus 로고
    • Damage to malaria-infected erythrocytes following exposure to oxidant-generating systems
    • Wozencraft, A. O., Damage to malaria-infected erythrocytes following exposure to oxidant-generating systems, Parasitology, 92, 559, 1986.
    • (1986) Parasitology , vol.92 , pp. 559
    • Wozencraft, A.O.1
  • 95
    • 0027430639 scopus 로고
    • Origin of reactive oxygen species in erythrocytes infected with Plasmodium falciparum
    • Ginsburg, H. and Atamna, H., Origin of reactive oxygen species in erythrocytes infected with Plasmodium falciparum, Mol. Biochem. Parasitol., 61, 231, 1993.
    • (1993) Mol. Biochem. Parasitol. , vol.61 , pp. 231
    • Ginsburg, H.1    Atamna, H.2
  • 96
    • 0027218524 scopus 로고
    • Is hemin responsible for the susceptibility of Plasmodia to oxidant stress?
    • Har-El, R., Marva, E., Chevion, M., and Golenser, J., Is hemin responsible for the susceptibility of Plasmodia to oxidant stress?, Free Rad. Res. Commun., 18, 279, 1993.
    • (1993) Free Rad. Res. Commun. , vol.18 , pp. 279
    • Har-El, R.1    Marva, E.2    Chevion, M.3    Golenser, J.4
  • 97
    • 0020552880 scopus 로고
    • Malaria parasites adopt host cell superoxide dismutase
    • Fairfield, A. S., Meshnick, S. R., and Eaton, J. W., Malaria parasites adopt host cell superoxide dismutase, Science, 221, 764, 1983.
    • (1983) Science , vol.221 , pp. 764
    • Fairfield, A.S.1    Meshnick, S.R.2    Eaton, J.W.3
  • 98
    • 0022807565 scopus 로고
    • Superoxide dismutase and catalase in the murine malaria, Plasmodium berghei: Content and sub-cellular distribution
    • Fairfield, A. S., Eaton, J. W., and Meshnick, S. R., Superoxide dismutase and catalase in the murine malaria, Plasmodium berghei: content and sub-cellular distribution, Arch. Biochem. Biophys., 250, 526, 1986.
    • (1986) Arch. Biochem. Biophys. , vol.250 , pp. 526
    • Fairfield, A.S.1    Eaton, J.W.2    Meshnick, S.R.3
  • 99
    • 26844550134 scopus 로고
    • Glutathione metabolism in malaria infected erythrocytes
    • Eaton, J. W. and Brewer, G. J., Eds., Alan R. Liss, New York
    • Eckman, J. R., Glutathione metabolism in malaria infected erythrocytes, in Malaria and the Red Cell, Eaton, J. W. and Brewer, G. J., Eds., Alan R. Liss, New York, 1984, 1.
    • (1984) Malaria and the Red Cell , pp. 1
    • Eckman, J.R.1
  • 100
    • 0022339848 scopus 로고
    • Plasmodium berghei: Oxidant defense system
    • Seth, R. K., Saini, A. S., and Jaswal, T. S., Plasmodium berghei: oxidant defense system, Exp. Parasitol., 60, 414, 1985.
    • (1985) Exp. Parasitol. , vol.60 , pp. 414
    • Seth, R.K.1    Saini, A.S.2    Jaswal, T.S.3
  • 101
    • 0029130017 scopus 로고
    • Plasmodium berghei: Implication of intracellular glutathione and its related enzyme in chloroquine resistance in vivo
    • Dubois, V. L., Platel, D. F. N., Pauly, G., and Tribouley-Duret, J., Plasmodium berghei: implication of intracellular glutathione and its related enzyme in chloroquine resistance in vivo, Exp. Parasitol., 81, 117, 1995.
    • (1995) Exp. Parasitol. , vol.81 , pp. 117
    • Dubois, V.L.1    Platel, D.F.N.2    Pauly, G.3    Tribouley-Duret, J.4
  • 103
    • 0024382247 scopus 로고
    • Plasmodium falciparum: Inhibitor sensitivity of the endogenous superoxide dismutase
    • Ranz, A. and Meshnick, S. R., Plasmodium falciparum: inhibitor sensitivity of the endogenous superoxide dismutase, Exp. Parasitol., 69, 125, 1989.
    • (1989) Exp. Parasitol. , vol.69 , pp. 125
    • Ranz, A.1    Meshnick, S.R.2
  • 104
    • 0025893626 scopus 로고
    • The survival of Plasmodium under oxidant stress
    • Golenser, J., Marva, E., and Chevion, M., The survival of Plasmodium under oxidant stress, Parasitol. Today, 7, 142, 1991.
    • (1991) Parasitol. Today , vol.7 , pp. 142
    • Golenser, J.1    Marva, E.2    Chevion, M.3
  • 105
    • 0027244093 scopus 로고
    • Presence of an endogenous superoxide dismutase activity in three rodent malaria species
    • Becuwe, P., Solmianny, C., Camus, D., and Dive, D., Presence of an endogenous superoxide dismutase activity in three rodent malaria species, Parasitol. Res., 79, 349, 1993.
    • (1993) Parasitol. Res. , vol.79 , pp. 349
    • Becuwe, P.1    Solmianny, C.2    Camus, D.3    Dive, D.4
  • 107
    • 0023152836 scopus 로고
    • Studies on glutathione reductase and methemoglobin from human erythrocytes parasitized with Plasmodium falciparum
    • Hempelmann, E., Schirmer, R. H., Fritsch, G., Hundt, E., and Groschel-Stewart, U., Studies on glutathione reductase and methemoglobin from human erythrocytes parasitized with Plasmodium falciparum, Mol. Biochem. Parasitol., 23, 19, 1987.
    • (1987) Mol. Biochem. Parasitol. , vol.23 , pp. 19
    • Hempelmann, E.1    Schirmer, R.H.2    Fritsch, G.3    Hundt, E.4    Groschel-Stewart, U.5
  • 108
    • 33748233963 scopus 로고
    • Disulfide-reductase inhibitors as chemotherapeutic agents: The design of drugs for trypanosomiasis and malaria
    • Schirmer, R. H., Müller, J. G., and Krauth-Siegel, R. L., Disulfide-reductase inhibitors as chemotherapeutic agents: the design of drugs for trypanosomiasis and malaria, Angew. Chem. Int. Ed. Engl., 34, 141, 1995.
    • (1995) Angew. Chem. Int. Ed. Engl. , vol.34 , pp. 141
    • Schirmer, R.H.1    Müller, J.G.2    Krauth-Siegel, R.L.3
  • 109
    • 0029563798 scopus 로고
    • Plasmodium falciparum glutathione reductase exhibits sequence similarities with the human host enzyme in the core structure but differs at the ligand-binding sites
    • Müller, S., Becker, K., Bergmann, B., Schirmer, R. H., and Walter, R. D., Plasmodium falciparum glutathione reductase exhibits sequence similarities with the human host enzyme in the core structure but differs at the ligand-binding sites, Mol. Biochem. Parasitol., 74, 11, 1995.
    • (1995) Mol. Biochem. Parasitol. , vol.74 , pp. 11
    • Müller, S.1    Becker, K.2    Bergmann, B.3    Schirmer, R.H.4    Walter, R.D.5
  • 110
    • 0025335874 scopus 로고
    • Glucose-6-phosphate dehydrogenase from Plasmodium berghei: Kinetic and electrophoretic characterization
    • Buckwitz, D., Jacobash, G., Kuckelkorn, U., Plonka, A., and Gerth, C., Glucose-6-phosphate dehydrogenase from Plasmodium berghei: kinetic and electrophoretic characterization, Exp. Parasitol., 70, 264, 1990.
    • (1990) Exp. Parasitol. , vol.70 , pp. 264
    • Buckwitz, D.1    Jacobash, G.2    Kuckelkorn, U.3    Plonka, A.4    Gerth, C.5
  • 111
    • 0025309238 scopus 로고
    • Expression and characterization of glucose-6phosphate dehydrogenase of Plasmodium falciparum
    • Kurdi-Haider, B. and Luzzatto, L., Expression and characterization of glucose-6phosphate dehydrogenase of Plasmodium falciparum, Mol. Biochem. Parasitol., 41, 83, 1990.
    • (1990) Mol. Biochem. Parasitol. , vol.41 , pp. 83
    • Kurdi-Haider, B.1    Luzzatto, L.2
  • 112
    • 0025242681 scopus 로고
    • Plasmodium falciparum carbohydrate metabolism: A connection between host cell and parasite
    • Roth, E., Jr., Plasmodium falciparum carbohydrate metabolism: a connection between host cell and parasite, Blood Cells, 16, 453, 1990.
    • (1990) Blood Cells , vol.16 , pp. 453
    • Roth Jr., E.1
  • 113
    • 0028041047 scopus 로고
    • Hexose-monophosphate shunt activity in intact Plasmodium falciparum-infected erythrocytes and in free parasites
    • Atamna, H., Pascarmona, G., and Ginsburg, H., Hexose-monophosphate shunt activity in intact Plasmodium falciparum-infected erythrocytes and in free parasites, Mol. Biochem. Parasitol., 67, 79, 1994.
    • (1994) Mol. Biochem. Parasitol. , vol.67 , pp. 79
    • Atamna, H.1    Pascarmona, G.2    Ginsburg, H.3
  • 114
    • 0021744045 scopus 로고
    • Primary structure and genomic organization of the histidine-rich protein of the malaria parasite Plasmodium lophurae
    • Ravetch, J. V., Feder, R., Pavlovec, A., and Blobel, G., Primary structure and genomic organization of the histidine-rich protein of the malaria parasite Plasmodium lophurae, Nature (London), 312, 616, 1984.
    • (1984) Nature (London) , vol.312 , pp. 616
    • Ravetch, J.V.1    Feder, R.2    Pavlovec, A.3    Blobel, G.4
  • 116
    • 0025013014 scopus 로고
    • Homologous sequences in Plasmodium cynomolgi and the gene of the histidine-rich knob protein of Plasmodium falciparum
    • Kilejian, A., Yang, Y.-F., Cochrane, A. H., and Rashid, M. A., Homologous sequences in Plasmodium cynomolgi and the gene of the histidine-rich knob protein of Plasmodium falciparum, Mol. Biochem. Parasitol., 38, 291, 1990.
    • (1990) Mol. Biochem. Parasitol. , vol.38 , pp. 291
    • Kilejian, A.1    Yang, Y.-F.2    Cochrane, A.H.3    Rashid, M.A.4
  • 117
    • 0022553865 scopus 로고
    • Inhibitory effects of histidine analogues on growth and protein synthesis by Plasmodium falciparum in vitro
    • Howard, R. J., Andrutis, A. T., Leech, J. H., Ellis, W. Y., Cohen, L. A., and Kirk, K. L., Inhibitory effects of histidine analogues on growth and protein synthesis by Plasmodium falciparum in vitro, Biochem. Pharmacol., 35, 1589, 1986.
    • (1986) Biochem. Pharmacol. , vol.35 , pp. 1589
    • Howard, R.J.1    Andrutis, A.T.2    Leech, J.H.3    Ellis, W.Y.4    Cohen, L.A.5    Kirk, K.L.6
  • 119
    • 0023732274 scopus 로고
    • A site-specific mechanism for free radical induced biological damage: The essential role of redox-active transition metals
    • Chevion, M., A site-specific mechanism for free radical induced biological damage: the essential role of redox-active transition metals, Free Rad. Biol. Med., 5, 27, 1988.
    • (1988) Free Rad. Biol. Med. , vol.5 , pp. 27
    • Chevion, M.1
  • 120
    • 0024259939 scopus 로고
    • Evidence for a neutrophil-mediated protective response in malaria
    • Nnalue, N. A. and Friedman, M. J., Evidence for a neutrophil-mediated protective response in malaria, Parasite Immunol., 10, 47, 1988.
    • (1988) Parasite Immunol. , vol.10 , pp. 47
    • Nnalue, N.A.1    Friedman, M.J.2
  • 121
    • 0025225484 scopus 로고
    • Some reflections concerning host erythrocyte-malarial parasite interrelationships
    • Ginsburg, H., Some reflections concerning host erythrocyte-malarial parasite interrelationships, Blood Cells, 16, 225, 1990.
    • (1990) Blood Cells , vol.16 , pp. 225
    • Ginsburg, H.1
  • 122
    • 0026228356 scopus 로고
    • Enhanced uptake and metabolism of riboflavin in erythrocytes infected with Plasmodium falciparum
    • Dutta, P., Enhanced uptake and metabolism of riboflavin in erythrocytes infected with Plasmodium falciparum, J. Protozool., 38, 479, 1991.
    • (1991) J. Protozool. , vol.38 , pp. 479
    • Dutta, P.1
  • 123
    • 0026646561 scopus 로고
    • Plasmodium falciparum-induced perturbations of the erythrocyte anti-oxidant system
    • Mohan, K., Dubey, M. L., Ganguly, N. K., and Mahajan, R. C., Plasmodium falciparum-induced perturbations of the erythrocyte anti-oxidant system, Clin. Chim. Acta, 209, 19, 1992.
    • (1992) Clin. Chim. Acta , vol.209 , pp. 19
    • Mohan, K.1    Dubey, M.L.2    Ganguly, N.K.3    Mahajan, R.C.4
  • 124
    • 0028717713 scopus 로고
    • Increased glutathione cycling and vitamin E of P. falciparum-infected erythrocytes fail to prevent spontaneous haemolysis
    • Mohan, K., Dubey, M. L., Ganguly, N. K., Nain, C. K., and Mahajan, R. C., Increased glutathione cycling and vitamin E of P. falciparum-infected erythrocytes fail to prevent spontaneous haemolysis, Ind. J. Biochem. Biophys., 31, 476, 1994.
    • (1994) Ind. J. Biochem. Biophys. , vol.31 , pp. 476
    • Mohan, K.1    Dubey, M.L.2    Ganguly, N.K.3    Nain, C.K.4    Mahajan, R.C.5
  • 125
    • 0027746361 scopus 로고
    • Oxidative stress and anti-oxidant defence mechanism in Plasmodium vivax malaria before and after chloroquine treatment
    • Sarin, K., Kumar, A., Prakash, A., and Sharma, A., Oxidative stress and anti-oxidant defence mechanism in Plasmodium vivax malaria before and after chloroquine treatment, Ind. J. Malariol., 30, 127, 1993.
    • (1993) Ind. J. Malariol. , vol.30 , pp. 127
    • Sarin, K.1    Kumar, A.2    Prakash, A.3    Sharma, A.4
  • 126
    • 0024599904 scopus 로고
    • An alkyl hydroperoxide reductase from Salmonella typhimurium involved in the defense of DNA against oxidative damage
    • Jacobson, F. S., Morgan, R. W., Christman, M. F., and Ames, B. N., An alkyl hydroperoxide reductase from Salmonella typhimurium involved in the defense of DNA against oxidative damage, J. Biol. Chem., 264, 1488, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1488
    • Jacobson, F.S.1    Morgan, R.W.2    Christman, M.F.3    Ames, B.N.4
  • 127
    • 0025741197 scopus 로고
    • Elimination of hydrogen peroxide by Haemophilus somnus, a catalase-negative pathogen of cattle
    • Sample, A. K. and Czuprynski, C. J., Elimination of hydrogen peroxide by Haemophilus somnus, a catalase-negative pathogen of cattle, Infect. Immun., 59, 2239, 1991.
    • (1991) Infect. Immun. , vol.59 , pp. 2239
    • Sample, A.K.1    Czuprynski, C.J.2
  • 128
    • 33645423200 scopus 로고
    • Scavenging of hydrogen peroxide in prokaryotic and eukaryotic algae: Acquisition of ascorbate peroxidase during the evolution of cyanobacteria
    • Miyake, C., Michihata, F., and Asada, K., Scavenging of hydrogen peroxide in prokaryotic and eukaryotic algae: acquisition of ascorbate peroxidase during the evolution of cyanobacteria, Plant Cell Physiol., 32, 33, 1991.
    • (1991) Plant Cell Physiol. , vol.32 , pp. 33
    • Miyake, C.1    Michihata, F.2    Asada, K.3
  • 129
    • 0030053375 scopus 로고    scopus 로고
    • Tritrichomonas foetus and Trichomonas vaginalis: The pattern of inactivation of hydrogenase activity by oxygen and activities of catalase and ascorbate peroxidase
    • Page-Sharp, M., Behm, C. A., and Smith, G. D., Tritrichomonas foetus and Trichomonas vaginalis: the pattern of inactivation of hydrogenase activity by oxygen and activities of catalase and ascorbate peroxidase, Microbiology, 142, 207, 1996.
    • (1996) Microbiology , vol.142 , pp. 207
    • Page-Sharp, M.1    Behm, C.A.2    Smith, G.D.3
  • 130
    • 0006198640 scopus 로고
    • Hydrogen peroxide-inducible proteins in Salmonella typhimurium overlap with heat shock and other stress proteins
    • Morgan, R. W., Christman, M. F., Jacobson, F. S., Storz, G., and Ames, B. N., Hydrogen peroxide-inducible proteins in Salmonella typhimurium overlap with heat shock and other stress proteins, Proc. Natl. Acad. Sci. U.S.A., 83, 8059, 1986.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 8059
    • Morgan, R.W.1    Christman, M.F.2    Jacobson, F.S.3    Storz, G.4    Ames, B.N.5
  • 131
    • 0024343602 scopus 로고
    • A global response induced in Escherichia coli by redox-cycling agents overlaps with that induced by peroxide stress
    • Greenberg, J. T. and Demple, B., A global response induced in Escherichia coli by redox-cycling agents overlaps with that induced by peroxide stress, J. Bacteriol., 171, 3933, 1989.
    • (1989) J. Bacteriol. , vol.171 , pp. 3933
    • Greenberg, J.T.1    Demple, B.2
  • 132
    • 0025721047 scopus 로고
    • Redox redux: The control of oxidative stress responses
    • Demple, B. and Amabile-Cuevas, C. F., Redox redux: the control of oxidative stress responses, Cell, 67, 837, 1991.
    • (1991) Cell , vol.67 , pp. 837
    • Demple, B.1    Amabile-Cuevas, C.F.2
  • 134
    • 0021199319 scopus 로고
    • Virulence of Entamoeba histolytica trophozoites: Effects of bacteria, microaerobic conditions and metronidazole
    • Bracha, R. and Mirelman, D., Virulence of Entamoeba histolytica trophozoites: effects of bacteria, microaerobic conditions and metronidazole, J. Exp. Med., 160, 353, 1984.
    • (1984) J. Exp. Med. , vol.160 , pp. 353
    • Bracha, R.1    Mirelman, D.2
  • 135
    • 0345422085 scopus 로고
    • Entamoeba histolytica: From intestine to liver
    • Mehlotra, R. K., Entamoeba histolytica: from intestine to liver, Parasitol. Today, 4, 235, 1988.
    • (1988) Parasitol. Today , vol.4 , pp. 235
    • Mehlotra, R.K.1
  • 136
    • 0026700178 scopus 로고
    • Oxido-reductive functions of Entamoeba histolytica in relation to virulence
    • Kumar, S., Tripathi, L. M., and Sagar, P., Oxido-reductive functions of Entamoeba histolytica in relation to virulence, Ann. Trop. Med. Parasitol., 86, 239, 1992.
    • (1992) Ann. Trop. Med. Parasitol. , vol.86 , pp. 239
    • Kumar, S.1    Tripathi, L.M.2    Sagar, P.3
  • 137
    • 0027257177 scopus 로고
    • The structure, biosynthesis and function of glycosylated phosphatidylinositols in the parasitic protozoa and higher eukaryotes
    • McConville, M. J. and Ferguson, M. A. J., The structure, biosynthesis and function of glycosylated phosphatidylinositols in the parasitic protozoa and higher eukaryotes, Biochem. J., 294, 305, 1993.
    • (1993) Biochem. J. , vol.294 , pp. 305
    • McConville, M.J.1    Ferguson, M.A.J.2
  • 139
    • 0026670944 scopus 로고
    • Humoral immune response against a 70-kilodalton heat shock protein of Entamoeba histolytica in a group of patients with invasive amoebiasis
    • Ortner, S., Plaimauer, B., Binder, M., Wiedermann, G., Scheiner, O., and Duchene, M., Humoral immune response against a 70-kilodalton heat shock protein of Entamoeba histolytica in a group of patients with invasive amoebiasis, Mol. Biochem. Parasitol., 54, 175, 1992.
    • (1992) Mol. Biochem. Parasitol. , vol.54 , pp. 175
    • Ortner, S.1    Plaimauer, B.2    Binder, M.3    Wiedermann, G.4    Scheiner, O.5    Duchene, M.6
  • 140
    • 0026644625 scopus 로고
    • An immunodominant antigen of Giardia lamblia is a heat shock protein
    • Char, S., Cevallos, A. M., and Farthing, M. J., An immunodominant antigen of Giardia lamblia is a heat shock protein, Biotechnol. Ther., 3, 151, 1992.
    • (1992) Biotechnol. Ther. , vol.3 , pp. 151
    • Char, S.1    Cevallos, A.M.2    Farthing, M.J.3
  • 143
    • 0027961010 scopus 로고
    • Enhanced expression of Plasmodium falciparum heat shock protein PFHSP70-I at higher temperatures and parasite survival
    • Biswas, S. and Sharma, Y. D., Enhanced expression of Plasmodium falciparum heat shock protein PFHSP70-I at higher temperatures and parasite survival, FEMS Microbiol. Lett., 124, 425, 1994.
    • (1994) FEMS Microbiol. Lett. , vol.124 , pp. 425
    • Biswas, S.1    Sharma, Y.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.