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Volumn 288, Issue 38, 2013, Pages 27456-27468

Ebsulfur is a benzisothiazolone cytocidal inhibitor targeting the trypanothione reductase of Trypanosoma brucei

Author keywords

[No Author keywords available]

Indexed keywords

NON-PROTEIN THIOLS; POTENT INHIBITOR; REACTIVE OXYGEN SPECIES; SELECTIVITY INDEX; SULFUR ANALOGUES; TRYPANOSOMA BRUCEI; TRYPANOSOMA CRUZI; TRYPANOTHIONE REDUCTASE;

EID: 84884583041     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.495101     Document Type: Article
Times cited : (50)

References (52)
  • 2
    • 33644982177 scopus 로고    scopus 로고
    • Drugresistance of Trypanosoma b. Rhodesiense isolates from Tanzania
    • Kibona, S. N., Matemba, L., Kaboya, J. S., and Lubega, G. W. (2006) Drugresistance of Trypanosoma b. rhodesiense isolates from Tanzania. Trop. Med. Int. Health 11, 144-155
    • (2006) Trop. Med. Int. Health , vol.11 , pp. 144-155
    • Kibona, S.N.1    Matemba, L.2    Kaboya, J.S.3    Lubega, G.W.4
  • 3
    • 0036126805 scopus 로고    scopus 로고
    • Parasites and the brain: Neuroinvasion, immunopathogenesis and neuronal dysfunctions
    • Kristensson, K., Mhlanga, J. D., and Bentivoglio, M. (2002) Parasites and the brain: neuroinvasion, immunopathogenesis and neuronal dysfunctions. Curr. Top. Microbiol. Immunol. 265, 227-257
    • (2002) Curr. Top. Microbiol. Immunol. , vol.265 , pp. 227-257
    • Kristensson, K.1    Mhlanga, J.D.2    Bentivoglio, M.3
  • 4
    • 85047690580 scopus 로고    scopus 로고
    • Cerebral vessel laminins and IFN-γ define Trypanosoma brucei brucei penetration of the blood-brain barrier
    • Masocha, W., Robertson, B., Rottenberg, M. E., Mhlanga, J., Sorokin, L., and Kristensson, K. (2004) Cerebral vessel laminins and IFN-γ define Trypanosoma brucei brucei penetration of the blood-brain barrier. J. Clin. Invest. 114, 689-694
    • (2004) J. Clin. Invest. , vol.114 , pp. 689-694
    • Masocha, W.1    Robertson, B.2    Rottenberg, M.E.3    Mhlanga, J.4    Sorokin, L.5    Kristensson, K.6
  • 5
    • 0026793462 scopus 로고
    • Metabolism and functions of trypanothione in the Kinetoplastida
    • Fairlamb, A. H., and Cerami, A. (1992) Metabolism and functions of trypanothione in the Kinetoplastida. Annu. Rev. Microbiol. 46, 695-729
    • (1992) Annu. Rev. Microbiol. , vol.46 , pp. 695-729
    • Fairlamb, A.H.1    Cerami, A.2
  • 6
    • 0022002912 scopus 로고
    • Trypanothione: A novel bis (glutathionyl) spermidine cofactor for glutathione reductase in trypanosomatids
    • Fairlamb, A. H., Blackburn, P., Ulrich, P., Chait, B. T., and Cerami, A. (1985) Trypanothione: a novel bis (glutathionyl) spermidine cofactor for glutathione reductase in trypanosomatids. Science 227, 1485-1487
    • (1985) Science , vol.227 , pp. 1485-1487
    • Fairlamb, A.H.1    Blackburn, P.2    Ulrich, P.3    Chait, B.T.4    Cerami, A.5
  • 8
    • 0033977079 scopus 로고    scopus 로고
    • Trypanosomes lacking trypanothione reductase are avirulent and show increased sensitivity to oxidative stress
    • Krieger, S., Schwarz, W., Ariyanayagam, M. R., Fairlamb, A. H., Krauth-Siegel, R. L., and Clayton, C. (2000) Trypanosomes lacking trypanothione reductase are avirulent and show increased sensitivity to oxidative stress. Mol. Microbiol. 35, 542-552
    • (2000) Mol. Microbiol. , vol.35 , pp. 542-552
    • Krieger, S.1    Schwarz, W.2    Ariyanayagam, M.R.3    Fairlamb, A.H.4    Krauth-Siegel, R.L.5    Clayton, C.6
  • 9
    • 33846963220 scopus 로고    scopus 로고
    • Depletion of the thioredoxin homologue tryparedoxin impairs antioxidative defence in African trypanosomes
    • Comini, M. A., Krauth-Siegel, R. L., and Flohé, L. (2007) Depletion of the thioredoxin homologue tryparedoxin impairs antioxidative defence in African trypanosomes. Biochem. J. 402, 43-49
    • (2007) Biochem. J. , vol.402 , pp. 43-49
    • Comini, M.A.1    Krauth-Siegel, R.L.2    Flohé, L.3
  • 10
    • 49349112856 scopus 로고    scopus 로고
    • Redox control in trypanosomatids, parasitic protozoa with trypanothione-based thiol metabolism
    • Krauth-Siegel, R. L., and Comini, M. A. (2008) Redox control in trypanosomatids, parasitic protozoa with trypanothione-based thiol metabolism. Biochim. Biophys. Acta 1780, 1236-1248
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 1236-1248
    • Krauth-Siegel, R.L.1    Comini, M.A.2
  • 11
    • 78049356626 scopus 로고    scopus 로고
    • The dithiol glutaredoxins of African trypanosomes have distinct roles and are closely linked to the unique trypanothione metabolism
    • Ceylan, S., Seidel, V., Ziebart, N., Berndt, C., Dirdjaja, N., and Krauth-Siegel, R. L. (2010) The dithiol glutaredoxins of African trypanosomes have distinct roles and are closely linked to the unique trypanothione metabolism. J. Biol. Chem. 285, 35224-35237
    • (2010) J. Biol. Chem. , vol.285 , pp. 35224-35237
    • Ceylan, S.1    Seidel, V.2    Ziebart, N.3    Berndt, C.4    Dirdjaja, N.5    Krauth-Siegel, R.L.6
  • 12
    • 0036833868 scopus 로고    scopus 로고
    • Enzymes of the trypanothione metabolism as targets for antitrypanosomal drug development
    • Schmidt, A., and Krauth-Siegel, R. L. (2002) Enzymes of the trypanothione metabolism as targets for antitrypanosomal drug development. Curr. Top. Med. Chem. 2, 1239-1259
    • (2002) Curr. Top. Med. Chem. , vol.2 , pp. 1239-1259
    • Schmidt, A.1    Krauth-Siegel, R.L.2
  • 13
    • 79952277996 scopus 로고    scopus 로고
    • Targeting trypanothione metabolism in trypanosomatid human parasites
    • Olin-Sandoval, V., Moreno-Sánchez, R., and Saavedra, E. (2010) Targeting trypanothione metabolism in trypanosomatid human parasites. Curr. Drug. Targets 11, 1614-1630
    • (2010) Curr. Drug. Targets , vol.11 , pp. 1614-1630
    • Olin-Sandoval, V.1    Moreno-Sánchez, R.2    Saavedra, E.3
  • 15
    • 0000385699 scopus 로고
    • Trypanothione is the primary target for arsenical drugs against African trypanosomes
    • Fairlamb, A. H., Henderson, G. B., and Cerami, A. (1989) Trypanothione is the primary target for arsenical drugs against African trypanosomes. Proc. Natl. Acad. Sci. U. S. A. 86, 2607-2611
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 2607-2611
    • Fairlamb, A.H.1    Henderson, G.B.2    Cerami, A.3
  • 16
    • 4544289321 scopus 로고    scopus 로고
    • Dual action of antimonial drugs on thiol redox metabolism in the human pathogen Leishmania donovani
    • Wyllie, S., Cunningham, M. L., and Fairlamb, A. H. (2004) Dual action of antimonial drugs on thiol redox metabolism in the human pathogen Leishmania donovani. J. Biol. Chem. 279, 39925-39932
    • (2004) J. Biol. Chem. , vol.279 , pp. 39925-39932
    • Wyllie, S.1    Cunningham, M.L.2    Fairlamb, A.H.3
  • 17
  • 19
    • 80053920610 scopus 로고    scopus 로고
    • Dihydroquinazolines as a novel class of Trypanosoma brucei trypanothione reductase inhibitors: Discovery, synthesis, and characterization of their binding mode by protein crystallography
    • Patterson, S., Alphey, M. S., Jones, D. C., Shanks, E. J., Street, I. P., Frearson, J. A., Wyatt, P. G., Gilbert, I. H., and Fairlamb, A. H. (2011) Dihydroquinazolines as a novel class of Trypanosoma brucei trypanothione reductase inhibitors: discovery, synthesis, and characterization of their binding mode by protein crystallography. J. Med. Chem. 54, 6514-6530
    • (2011) J. Med. Chem. , vol.54 , pp. 6514-6530
    • Patterson, S.1    Alphey, M.S.2    Jones, D.C.3    Shanks, E.J.4    Street, I.P.5    Frearson, J.A.6    Wyatt, P.G.7    Gilbert, I.H.8    Fairlamb, A.H.9
  • 20
    • 3142719178 scopus 로고    scopus 로고
    • Two interacting binding sites for quinacrine derivatives in the active site of trypanothione reductase: A template for drug design
    • Saravanamuthu, A., Vickers, T. J., Bond, C. S., Peterson, M. R., Hunter, W. N., and Fairlamb, A. H. (2004) Two interacting binding sites for quinacrine derivatives in the active site of trypanothione reductase: a template for drug design. J. Biol. Chem. 279, 29493-29500
    • (2004) J. Biol. Chem. , vol.279 , pp. 29493-29500
    • Saravanamuthu, A.1    Vickers, T.J.2    Bond, C.S.3    Peterson, M.R.4    Hunter, W.N.5    Fairlamb, A.H.6
  • 21
    • 0033619994 scopus 로고    scopus 로고
    • Inhibition of Trypanosoma cruzi trypanothione reductase by acridines: Kinetic studies and structure-activity relationships
    • Bonse, S., Santelli-Rouvier, C., Barbe, J., and Krauth-Siegel, R. L. (1999) Inhibition of Trypanosoma cruzi trypanothione reductase by acridines: kinetic studies and structure-activity relationships. J. Med. Chem. 42, 5448-5454
    • (1999) J. Med. Chem. , vol.42 , pp. 5448-5454
    • Bonse, S.1    Santelli-Rouvier, C.2    Barbe, J.3    Krauth-Siegel, R.L.4
  • 22
    • 22744459375 scopus 로고    scopus 로고
    • Inhibitors of Trypanosoma cruzi trypanothione reductase revealed by virtual screening and parallel synthesis
    • Meiering, S., Inhoff, O., Mies, J., Vincek, A., Garcia, G., Kramer, B., Dormeyer, M., and Krauth-Siegel, R. L. (2005) Inhibitors of Trypanosoma cruzi trypanothione reductase revealed by virtual screening and parallel synthesis. J. Med. Chem. 48, 4793-4802
    • (2005) J. Med. Chem. , vol.48 , pp. 4793-4802
    • Meiering, S.1    Inhoff, O.2    Mies, J.3    Vincek, A.4    Garcia, G.5    Kramer, B.6    Dormeyer, M.7    Krauth-Siegel, R.L.8
  • 23
    • 0029114721 scopus 로고
    • Molecular actions of ebselen-an antiinflammatory antioxidant
    • Schewe, T. (1995) Molecular actions of ebselen-an antiinflammatory antioxidant. Gen. Pharmacol. 26, 1153-1169
    • (1995) Gen. Pharmacol. , vol.26 , pp. 1153-1169
    • Schewe, T.1
  • 24
    • 0037172997 scopus 로고    scopus 로고
    • Ebselen: A substrate for human thioredoxin reductase strongly stimulating its hydroperoxide reductase activity and a superfast thioredoxin oxidant
    • Zhao, R., Masayasu, H., and Holmgren, A. (2002) Ebselen: A substrate for human thioredoxin reductase strongly stimulating its hydroperoxide reductase activity and a superfast thioredoxin oxidant. Proc. Natl Acad. Sci. U. S. A. 99, 8579-8584
    • (2002) Proc. Natl Acad. Sci. U. S. A. , vol.99 , pp. 8579-8584
    • Zhao, R.1    Masayasu, H.2    Holmgren, A.3
  • 25
    • 0037131424 scopus 로고    scopus 로고
    • A novel antioxidant mechanism of ebselen involving ebselen diselenide, a substrate of mammalian thioredoxin and thioredoxin reductase
    • Zhao, R., and Holmgren, A. (2002) A novel antioxidant mechanism of ebselen involving ebselen diselenide, a substrate of mammalian thioredoxin and thioredoxin reductase. J. Biol. Chem. 277, 39456-39462
    • (2002) J. Biol. Chem. , vol.277 , pp. 39456-39462
    • Zhao, R.1    Holmgren, A.2
  • 26
    • 0024316299 scopus 로고
    • Susceptibility of methicillinresistant Staphylococcus aureus to the selenium-containing compound 2-phenyl-1, 2-benzoisoselenazol-3 (2H)-one (PZ51)
    • Nozawa, R., Yokota, T., and Fujimoto, T. (1989) Susceptibility of methicillinresistant Staphylococcus aureus to the selenium-containing compound 2-phenyl-1, 2-benzoisoselenazol-3 (2H)-one (PZ51). Antimicrob. Agents Chemother. 33, 1388-1390
    • (1989) Antimicrob. Agents Chemother. , vol.33 , pp. 1388-1390
    • Nozawa, R.1    Yokota, T.2    Fujimoto, T.3
  • 28
    • 84869211845 scopus 로고    scopus 로고
    • Bacillus anthracis thioredoxin systems, characterization and role as electron donors for ribonucleotide reductase
    • Gustafsson, T. N., Sahlin, M., Lu, J., Sjöberg, B. M., and Holmgren, A. (2012) Bacillus anthracis thioredoxin systems, characterization and role as electron donors for ribonucleotide reductase. J. Biol. Chem. 287, 39686-39697
    • (2012) J. Biol. Chem. , vol.287 , pp. 39686-39697
    • Gustafsson, T.N.1    Sahlin, M.2    Lu, J.3    Sjöberg, B.M.4    Holmgren, A.5
  • 30
    • 0024412233 scopus 로고
    • Expedient synthesis of ebselen and related-compounds
    • Engman, L., and Hallberg, A. (1989) Expedient synthesis of ebselen and related-compounds. J. Org. Chem. 54, 2964-2966
    • (1989) J. Org. Chem. , vol.54 , pp. 2964-2966
    • Engman, L.1    Hallberg, A.2
  • 31
    • 84986684913 scopus 로고
    • Aromatic and azaaromatic diselenides, benzisoselenazolones, and relatedcompounds as immunomodulators active in humans-Synthesis and properties
    • Mlochowski, J., Kloc, K., Syper, L., Inglot, A. D., and Piasecki, E. (1993) Aromatic and azaaromatic diselenides, benzisoselenazolones, and relatedcompounds as immunomodulators active in humans-Synthesis and properties. Liebigs Annalen Der. Chemie, 1239-1244
    • (1993) Liebigs Annalen Der. Chemie , pp. 1239-1244
    • Mlochowski, J.1    Kloc, K.2    Syper, L.3    Inglot, A.D.4    Piasecki, E.5
  • 32
    • 8444247959 scopus 로고    scopus 로고
    • Azaanalogues of ebselen as antimicrobial and antiviral agents: Synthesis and properties
    • Wójtowicz, H., Kloc, K., Maliszewska, I., Mlóchowski, J., Pietka, M., and Piasecki, E. (2004) Azaanalogues of ebselen as antimicrobial and antiviral agents: synthesis and properties. Farmaco 59, 863-868
    • (2004) Farmaco , vol.59 , pp. 863-868
    • Wójtowicz, H.1    Kloc, K.2    Maliszewska, I.3    Mlóchowski, J.4    Pietka, M.5    Piasecki, E.6
  • 34
    • 84861576185 scopus 로고    scopus 로고
    • Inhibition of thioredoxin reductase by a novel series of bis-1, 2-benzisoselenazol-3 (2H)-ones: Organoselenium compounds for cancer therapy
    • He, J., Li, D., Xiong, K., Ge, Y., Jin, H., Zhang, G., Hong, M., Tian, Y., Yin, J., and Zeng, H. (2012) Inhibition of thioredoxin reductase by a novel series of bis-1, 2-benzisoselenazol-3 (2H)-ones: Organoselenium compounds for cancer therapy. Bioorg. Med. Chem. 20, 3816-3827
    • (2012) Bioorg. Med. Chem. , vol.20 , pp. 3816-3827
    • He, J.1    Li, D.2    Xiong, K.3    Ge, Y.4    Jin, H.5    Zhang, G.6    Hong, M.7    Tian, Y.8    Yin, J.9    Zeng, H.10
  • 35
    • 0036532463 scopus 로고    scopus 로고
    • The design and synthesis of redox core-α amino acid composites based on thiol-disulfide exchange mechanism and a comparative study of their zinc abstraction potential from [CCXX] boxes in proteins
    • Ranganathan, S., Muraleedharan, K. M., Bharadwaj, P., Chatterji, D., and Karle, I. (2002) The design and synthesis of redox core-α amino acid composites based on thiol-disulfide exchange mechanism and a comparative study of their zinc abstraction potential from [CCXX] boxes in proteins. Tetrahedron 58, 2861-2874
    • (2002) Tetrahedron , vol.58 , pp. 2861-2874
    • Ranganathan, S.1    Muraleedharan, K.M.2    Bharadwaj, P.3    Chatterji, D.4    Karle, I.5
  • 36
    • 84862777796 scopus 로고    scopus 로고
    • An efficient copper-mediated synthetic methodology for benzo[d]isothiazol-3 (2H)-ones and related sulfur-nitrogen heterocycles
    • Bhakuni, B. S., Balkrishna, S. J., Kumar, A., and Kumar, S. (2012) An efficient copper-mediated synthetic methodology for benzo[d]isothiazol-3 (2H)-ones and related sulfur-nitrogen heterocycles. Tetrahedron Lett. 53, 1354-1357
    • (2012) Tetrahedron Lett. , vol.53 , pp. 1354-1357
    • Bhakuni, B.S.1    Balkrishna, S.J.2    Kumar, A.3    Kumar, S.4
  • 37
    • 0028942106 scopus 로고
    • Human neutrophils lose their surface Fcγ RIII and acquire annexin V-binding sites during apoptosis in vitro
    • Homburg, C. H., De Haas, M., Von Dem Borne, A. E., Verhoeven, A. J., Reutelingsperger, C. P., and Roos, D. (1995) Human neutrophils lose their surface Fcγ RIII and acquire annexin V-binding sites during apoptosis in vitro. Blood 85, 532-540
    • (1995) Blood , vol.85 , pp. 532-540
    • Homburg, C.H.1    De Haas, M.2    Von Dem Borne, A.E.3    Verhoeven, A.J.4    Reutelingsperger, C.P.5    Roos, D.6
  • 38
    • 33646020662 scopus 로고    scopus 로고
    • The effect of TAO expression on PCD-like phenomenon development and drug resistance in Trypanosoma brucei
    • Tsuda, A., Witola, W. H., Konnai, S., Ohashi, K., and Onuma, M. (2006) The effect of TAO expression on PCD-like phenomenon development and drug resistance in Trypanosoma brucei. Parasitol. Int. 55, 135-142
    • (2006) Parasitol. Int. , vol.55 , pp. 135-142
    • Tsuda, A.1    Witola, W.H.2    Konnai, S.3    Ohashi, K.4    Onuma, M.5
  • 40
    • 71549158851 scopus 로고    scopus 로고
    • Comparative structural, kinetic and inhibitor studies of Trypanosoma brucei trypanothione reductase with T
    • Jones, D. C., Ariza, A., Chow, W. H., Oza, S. L., and Fairlamb, A. H. (2010) Comparative structural, kinetic and inhibitor studies of Trypanosoma brucei trypanothione reductase with T. cruzi. Mol. Biochem. Parasitol. 169, 12-19
    • (2010) Cruzi. Mol. Biochem. Parasitol. , vol.169 , pp. 12-19
    • Jones, D.C.1    Ariza, A.2    Chow, W.H.3    Oza, S.L.4    Fairlamb, A.H.5
  • 41
    • 73649151319 scopus 로고
    • Esters of methanesulfonic acid as irreversible inhibitors of acetylcholinesterase
    • Kitz, R., and Wilson, I. B. (1962) Esters of methanesulfonic acid as irreversible inhibitors of acetylcholinesterase. J. Biol. Chem. 237, 3245-3249
    • (1962) J. Biol. Chem. , vol.237 , pp. 3245-3249
    • Kitz, R.1    Wilson, I.B.2
  • 42
    • 0142227145 scopus 로고    scopus 로고
    • Specific chemotherapy of Chagas disease: Controversies and advances
    • Urbina, J. A., and Docampo, R. (2003) Specific chemotherapy of Chagas disease: controversies and advances. Trends Parasitol. 19, 495-501
    • (2003) Trends Parasitol. , vol.19 , pp. 495-501
    • Urbina, J.A.1    Docampo, R.2
  • 43
    • 84555196640 scopus 로고    scopus 로고
    • Antiparasitic prodrug nifurtimox: Revisiting its activation mechanism
    • Cerecetto, H., and González, M. (2011) Antiparasitic prodrug nifurtimox: revisiting its activation mechanism. Future Microbiol. 6, 847-850
    • (2011) Future Microbiol. , vol.6 , pp. 847-850
    • Cerecetto, H.1    González, M.2
  • 47
    • 0041355353 scopus 로고    scopus 로고
    • RNA interference identifies two hydroperoxide metabolizing enzymes that are essential to the blood stream form of the African trypanosome
    • Wilkinson, S. R., Horn, D., Prathalingam, S. R., and Kelly, J. M. (2003) RNA interference identifies two hydroperoxide metabolizing enzymes that are essential to the blood stream form of the African trypanosome. J. Biol. Chem. 278, 31640-31646
    • (2003) J. Biol. Chem. , vol.278 , pp. 31640-31646
    • Wilkinson, S.R.1    Horn, D.2    Prathalingam, S.R.3    Kelly, J.M.4
  • 48
    • 17644393919 scopus 로고    scopus 로고
    • Substrate specificity, localization, and essential role of the glutathione peroxidase-type tryparedoxin peroxidases in Trypanosoma brucei
    • Schlecker, T., Schmidt, A., Dirdjaja, N., Voncken, F., Clayton, C., and Krauth-Siegel, R. L. (2005) Substrate specificity, localization, and essential role of the glutathione peroxidase-type tryparedoxin peroxidases in Trypanosoma brucei. J. Biol. Chem. 280, 14385-14394
    • (2005) J. Biol. Chem. , vol.280 , pp. 14385-14394
    • Schlecker, T.1    Schmidt, A.2    Dirdjaja, N.3    Voncken, F.4    Clayton, C.5    Krauth-Siegel, R.L.6
  • 49
    • 0029360570 scopus 로고
    • Flavoprotein structure and mechanism. 5. Trypanothione reductase and lipoamide dehydrogenase as targets for a structure-based drug design
    • Krauth-Siegel, R. L., and Schöneck, R. (1995) Flavoprotein structure and mechanism. 5. Trypanothione reductase and lipoamide dehydrogenase as targets for a structure-based drug design. FASEB J. 9, 1138-1146
    • (1995) FASEB J. , vol.9 , pp. 1138-1146
    • Krauth-Siegel, R.L.1    Schöneck, R.2
  • 50
    • 0019512549 scopus 로고
    • Inhibition of glutathione synthesis as a chemotherapeutic strategy for trypanosomiasis
    • Arrick, B. A., Griffith, O. W., and Cerami, A. (1981) Inhibition of glutathione synthesis as a chemotherapeutic strategy for trypanosomiasis. J. Exp. Med. 153, 720-725
    • (1981) J. Exp. Med. , vol.153 , pp. 720-725
    • Arrick, B.A.1    Griffith, O.W.2    Cerami, A.3
  • 51
    • 0032574808 scopus 로고    scopus 로고
    • Down-regulation of Leishmania donovani trypanothione reductase by heterologous expression of a trans-dominant mutant homologue: Effect on parasite intracellular survival
    • Tovar, J., Cunningham, M. L., Smith, A. C., Croft, S. L., and Fairlamb, A. H. (1998) Down-regulation of Leishmania donovani trypanothione reductase by heterologous expression of a trans-dominant mutant homologue: effect on parasite intracellular survival. Proc. Natl. Acad. Sci. U. S. A. 95, 5311-5316
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 5311-5316
    • Tovar, J.1    Cunningham, M.L.2    Smith, A.C.3    Croft, S.L.4    Fairlamb, A.H.5
  • 52
    • 0030926411 scopus 로고    scopus 로고
    • Disruption of the trypanothione reductase gene of Leishmania decreases its ability to survive oxidative stress in macrophages
    • Dumas, C., Ouellette, M., Tovar, J., Cunningham, M. L., Fairlamb, A. H., Tamar, S., Olivier, M., and Papadopoulou, B. (1997) Disruption of the trypanothione reductase gene of Leishmania decreases its ability to survive oxidative stress in macrophages. EMBO J. 16, 2590-2598
    • (1997) EMBO J. , vol.16 , pp. 2590-2598
    • Dumas, C.1    Ouellette, M.2    Tovar, J.3    Cunningham, M.L.4    Fairlamb, A.H.5    Tamar, S.6    Olivier, M.7    Papadopoulou, B.8


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