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Volumn 83, Issue 2, 2012, Pages 304-318

Dissecting the role of glutathione biosynthesis in Plasmodium falciparum

Author keywords

[No Author keywords available]

Indexed keywords

BUTHIONINE SULFOXIMINE; GLUTAMATE CYSTEINE LIGASE; GLUTATHIONE; GLUTATHIONE REDUCTASE; GLUTATHIONE SYNTHASE; THIOL;

EID: 84855760118     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2011.07933.x     Document Type: Article
Times cited : (41)

References (66)
  • 1
    • 14944354773 scopus 로고    scopus 로고
    • Characterization of the glyoxalases of the malarial parasite Plasmodium falciparum and comparison with their human counterparts
    • Akoachere, M., Iozef, R., Rahlfs, S., Deponte, M., Mannervik, B., Creighton, D.J., etal. (2005) Characterization of the glyoxalases of the malarial parasite Plasmodium falciparum and comparison with their human counterparts. Biol Chem 386: 41-52.
    • (2005) Biol Chem , vol.386 , pp. 41-52
    • Akoachere, M.1    Iozef, R.2    Rahlfs, S.3    Deponte, M.4    Mannervik, B.5    Creighton, D.J.6
  • 2
    • 0031574219 scopus 로고    scopus 로고
    • The malaria parasite supplies glutathione to its host cell - investigation of glutathione transport and metabolism in human erythrocytes infected with Plasmodium falciparum
    • Atamna, H., and Ginsburg, H. (1997) The malaria parasite supplies glutathione to its host cell - investigation of glutathione transport and metabolism in human erythrocytes infected with Plasmodium falciparum. Eur J Biochem 250: 670-679.
    • (1997) Eur J Biochem , vol.250 , pp. 670-679
    • Atamna, H.1    Ginsburg, H.2
  • 3
    • 0032513245 scopus 로고    scopus 로고
    • Plasmodium falciparum glutathione metabolism and growth are independent of glutathione system of host erythrocyte
    • Ayi, K., Cappadoro, M., Branca, M., Turrini, F., and Arese, P. (1998) Plasmodium falciparum glutathione metabolism and growth are independent of glutathione system of host erythrocyte. FEBS Lett 424: 257-261.
    • (1998) FEBS Lett , vol.424 , pp. 257-261
    • Ayi, K.1    Cappadoro, M.2    Branca, M.3    Turrini, F.4    Arese, P.5
  • 4
    • 0346725043 scopus 로고    scopus 로고
    • Disruption of gamma-glutamylcysteine synthetase results in absolute glutathione auxotrophy and apoptosis in Candida albicans
    • Baek, Y.U., Kim, Y.R., Yim, H.S., and Kang, S.O. (2004) Disruption of gamma-glutamylcysteine synthetase results in absolute glutathione auxotrophy and apoptosis in Candida albicans. FEBS Lett 556: 47-52.
    • (2004) FEBS Lett , vol.556 , pp. 47-52
    • Baek, Y.U.1    Kim, Y.R.2    Yim, H.S.3    Kang, S.O.4
  • 5
    • 0037621507 scopus 로고    scopus 로고
    • Glutathione - functions and metabolism in the malarial parasite Plasmodium falciparum
    • Becker, K., Rahlfs, S., Nickel, C., and Schirmer, R.H. (2003) Glutathione - functions and metabolism in the malarial parasite Plasmodium falciparum. Biol Chem 384: 551-566.
    • (2003) Biol Chem , vol.384 , pp. 551-566
    • Becker, K.1    Rahlfs, S.2    Nickel, C.3    Schirmer, R.H.4
  • 7
    • 27644597015 scopus 로고    scopus 로고
    • Mutations conferring drug resistance in malaria parasite drug transporters Pgh1 and PfCRT do not affect steady-state vacuolar Ca2+
    • Biagini, G.A., Fidock, D.A., Bray, P.G., and Ward, S.A. (2005) Mutations conferring drug resistance in malaria parasite drug transporters Pgh1 and PfCRT do not affect steady-state vacuolar Ca2+. Antimicrob Agents Chemother 49: 4807-4808.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 4807-4808
    • Biagini, G.A.1    Fidock, D.A.2    Bray, P.G.3    Ward, S.A.4
  • 8
    • 0024286857 scopus 로고
    • Biochemical characterization of glutathione-deficient mutants of Escherichia coli K12 and Salmonella strains TA1535 and TA100
    • Bouter, S., Kerklaan, P.R., Zoetemelk, C.E., and Mohn, G.R. (1988) Biochemical characterization of glutathione-deficient mutants of Escherichia coli K12 and Salmonella strains TA1535 and TA100. Biochem Pharmacol 37: 577-581.
    • (1988) Biochem Pharmacol , vol.37 , pp. 577-581
    • Bouter, S.1    Kerklaan, P.R.2    Zoetemelk, C.E.3    Mohn, G.R.4
  • 9
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 10
    • 33645502915 scopus 로고    scopus 로고
    • Development and application of a positive-negative selectable marker system for use in reverse genetics in Plasmodium
    • Braks, J.A., Franke-Fayard, B., Kroeze, H., Janse, C.J., and Waters, A.P. (2006) Development and application of a positive-negative selectable marker system for use in reverse genetics in Plasmodium. Nucleic Acids Res 34: e39.
    • (2006) Nucleic Acids Res , vol.34
    • Braks, J.A.1    Franke-Fayard, B.2    Kroeze, H.3    Janse, C.J.4    Waters, A.P.5
  • 11
    • 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, E.D., Rahlfs, S., Schirmer, R.H., Becker, K., and Matuschewski, K. (2010) 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) 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
  • 12
    • 0029096627 scopus 로고
    • Gcs1, a gene encoding gamma-glutamylcysteine synthetase in the fission yeast Schizosaccharomyces pombe
    • Coblenz, A., and Wolf, K. (1995) Gcs1, a gene encoding gamma-glutamylcysteine synthetase in the fission yeast Schizosaccharomyces pombe. Yeast 11: 1171-1177.
    • (1995) Yeast , vol.11 , pp. 1171-1177
    • Coblenz, A.1    Wolf, K.2
  • 13
    • 0036618855 scopus 로고    scopus 로고
    • Transfection technology and the study of drug resistance in the malaria parasite Plasmodium falciparum
    • Crabb, B.S. (2002) Transfection technology and the study of drug resistance in the malaria parasite Plasmodium falciparum. Drug Resist Updat 5: 126-130.
    • (2002) Drug Resist Updat , vol.5 , pp. 126-130
    • Crabb, B.S.1
  • 14
    • 0030006717 scopus 로고    scopus 로고
    • Characterization of promoters and stable transfection by homologous and nonhomologous recombination in Plasmodium falciparum
    • Crabb, B.S., and Cowman, A.F. (1996) Characterization of promoters and stable transfection by homologous and nonhomologous recombination in Plasmodium falciparum. Proc Natl Acad Sci USA 93: 7289-7294.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 7289-7294
    • Crabb, B.S.1    Cowman, A.F.2
  • 16
    • 0018606732 scopus 로고
    • Quantitative assessment of antimalarial activity in vitro by a semiautomated microdilution technique
    • Desjardins, R.E., Canfield, C.J., Haynes, J.D., and Chulay, J.D. (1979) Quantitative assessment of antimalarial activity in vitro by a semiautomated microdilution technique. Antimicrob Agents Chemother 16: 710-718.
    • (1979) Antimicrob Agents Chemother , vol.16 , pp. 710-718
    • Desjardins, R.E.1    Canfield, C.J.2    Haynes, J.D.3    Chulay, J.D.4
  • 17
    • 22144494182 scopus 로고    scopus 로고
    • Development of the endoplasmic reticulum, mitochondrion and apicoplast during the asexual life cycle of Plasmodium falciparum
    • van Dooren, G.G., Marti, M., Tonkin, C.J., Stimmler, L.M., Cowman, A.F., and McFadden, G.I. (2005) Development of the endoplasmic reticulum, mitochondrion and apicoplast during the asexual life cycle of Plasmodium falciparum. Mol Microbiol 57: 405-419.
    • (2005) Mol Microbiol , vol.57 , pp. 405-419
    • van Dooren, G.G.1    Marti, M.2    Tonkin, C.J.3    Stimmler, L.M.4    Cowman, A.F.5    McFadden, G.I.6
  • 18
    • 41449103202 scopus 로고    scopus 로고
    • Disruption of the PfPK7 gene impairs schizogony and sporogony in the human malaria parasite Plasmodium falciparum
    • Dorin-Semblat, D., Sicard, A., Doerig, C., and Ranford-Cartwright, L. (2008) Disruption of the PfPK7 gene impairs schizogony and sporogony in the human malaria parasite Plasmodium falciparum. Eukaryot Cell 7: 279-285.
    • (2008) Eukaryot Cell , vol.7 , pp. 279-285
    • Dorin-Semblat, D.1    Sicard, A.2    Doerig, C.3    Ranford-Cartwright, L.4
  • 19
    • 0029908565 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a putative glutathione reductase gene, the PfGR2 gene, from Plasmodium falciparum
    • Farber, P.M., Becker, K., Muller, S., Schirmer, R.H., and Franklin, R.M. (1996) Molecular cloning and characterization of a putative glutathione reductase gene, the PfGR2 gene, from Plasmodium falciparum. Eur J Biochem 239: 655-661.
    • (1996) Eur J Biochem , vol.239 , pp. 655-661
    • Farber, P.M.1    Becker, K.2    Muller, S.3    Schirmer, R.H.4    Franklin, R.M.5
  • 20
    • 77951133554 scopus 로고    scopus 로고
    • Present trends in vitamin E research
    • Galli, F., and Azzi, A. (2010) Present trends in vitamin E research. Biofactors 36: 33-42.
    • (2010) Biofactors , vol.36 , pp. 33-42
    • Galli, F.1    Azzi, A.2
  • 21
    • 0030004354 scopus 로고    scopus 로고
    • Glutathione is an essential metabolite required for resistance to oxidative stress in the yeast Saccharomyces cerevisiae
    • Grant, C.M., MacIver, F.H., and Dawes, I.W. (1996) Glutathione is an essential metabolite required for resistance to oxidative stress in the yeast Saccharomyces cerevisiae. Curr Genet 29: 511-515.
    • (1996) Curr Genet , vol.29 , pp. 511-515
    • Grant, C.M.1    MacIver, F.H.2    Dawes, I.W.3
  • 22
    • 0030747207 scopus 로고    scopus 로고
    • Glutathione synthetase is dispensable for growth under both normal and oxidative stress conditions in the yeast Saccharomyces cerevisiae due to an accumulation of the dipeptide gamma-glutamylcysteine
    • Grant, C.M., MacIver, F.H., and Dawes, I.W. (1997) Glutathione synthetase is dispensable for growth under both normal and oxidative stress conditions in the yeast Saccharomyces cerevisiae due to an accumulation of the dipeptide gamma-glutamylcysteine. Mol Biol Cell 8: 1699-1707.
    • (1997) Mol Biol Cell , vol.8 , pp. 1699-1707
    • Grant, C.M.1    MacIver, F.H.2    Dawes, I.W.3
  • 23
    • 0019798176 scopus 로고
    • Glutathione turnover in human erythrocytes. Inhibition by buthionine sulfoximine and incorporation of glycine by exchange
    • Griffith, O.W. (1981) Glutathione turnover in human erythrocytes. Inhibition by buthionine sulfoximine and incorporation of glycine by exchange. J Biol Chem 256: 4900-4904.
    • (1981) J Biol Chem , vol.256 , pp. 4900-4904
    • Griffith, O.W.1
  • 24
    • 0020444895 scopus 로고
    • Mechanism of action, metabolism, and toxicity of buthionine sulfoximine and its higher homologs, potent inhibitors of glutathione synthesis
    • Griffith, O.W. (1982) Mechanism of action, metabolism, and toxicity of buthionine sulfoximine and its higher homologs, potent inhibitors of glutathione synthesis. J Biol Chem 257: 13704-13712.
    • (1982) J Biol Chem , vol.257 , pp. 13704-13712
    • Griffith, O.W.1
  • 25
    • 0032617250 scopus 로고    scopus 로고
    • The enzymes of glutathione synthesis: gamma-glutamylcysteine synthetase
    • xii
    • Griffith, O.W., and Mulcahy, R.T. (1999) The enzymes of glutathione synthesis: gamma-glutamylcysteine synthetase. Adv Enzymol Relat Areas Mol Biol 73: 209-267. xii.
    • (1999) Adv Enzymol Relat Areas Mol Biol , vol.73 , pp. 209-267
    • Griffith, O.W.1    Mulcahy, R.T.2
  • 26
    • 0035985070 scopus 로고    scopus 로고
    • Glutathione S-transferase of the malarial parasite Plasmodium falciparum: characterization of a potential drug target
    • Harwaldt, P., Rahlfs, S., and Becker, K. (2002) Glutathione S-transferase of the malarial parasite Plasmodium falciparum: characterization of a potential drug target. Biol Chem 383: 821-830.
    • (2002) Biol Chem , vol.383 , pp. 821-830
    • Harwaldt, P.1    Rahlfs, S.2    Becker, K.3
  • 27
    • 0027227925 scopus 로고
    • Amino acid sequence and function of the light subunit of rat kidney gamma-glutamylcysteine synthetase
    • Huang, C.S., Anderson, M.E., and Meister, A. (1993a) Amino acid sequence and function of the light subunit of rat kidney gamma-glutamylcysteine synthetase. J Biol Chem 268: 20578-20583.
    • (1993) J Biol Chem , vol.268 , pp. 20578-20583
    • Huang, C.S.1    Anderson, M.E.2    Meister, A.3
  • 28
    • 0027171195 scopus 로고
    • Catalytic and regulatory properties of the heavy subunit of rat kidney gamma-glutamylcysteine synthetase
    • Huang, C.S., Chang, L.S., Anderson, M.E., and Meister, A. (1993b) Catalytic and regulatory properties of the heavy subunit of rat kidney gamma-glutamylcysteine synthetase. J Biol Chem 268: 19675-19680.
    • (1993) J Biol Chem , vol.268 , pp. 19675-19680
    • Huang, C.S.1    Chang, L.S.2    Anderson, M.E.3    Meister, A.4
  • 29
    • 0141994807 scopus 로고    scopus 로고
    • Gene knockdown of gamma-glutamylcysteine synthetase by RNAi in the parasitic protozoa Trypanosoma brucei demonstrates that it is an essential enzyme
    • Huynh, T.T., Huynh, V.T., Harmon, M.A., and Phillips, M.A. (2003) Gene knockdown of gamma-glutamylcysteine synthetase by RNAi in the parasitic protozoa Trypanosoma brucei demonstrates that it is an essential enzyme. J Biol Chem 278: 39794-39800.
    • (2003) J Biol Chem , vol.278 , pp. 39794-39800
    • Huynh, T.T.1    Huynh, V.T.2    Harmon, M.A.3    Phillips, M.A.4
  • 30
    • 0024325611 scopus 로고
    • Host cell specificity and schizogony of Plasmodium berghei under different in vitro conditions
    • Janse, C.J., Boorsma, E.G., Ramesar, J., Grobbee, M.J., and Mons, B. (1989) Host cell specificity and schizogony of Plasmodium berghei under different in vitro conditions. Int J Parasitol 19: 509-514.
    • (1989) Int J Parasitol , vol.19 , pp. 509-514
    • Janse, C.J.1    Boorsma, E.G.2    Ramesar, J.3    Grobbee, M.J.4    Mons, B.5
  • 31
    • 0034006339 scopus 로고    scopus 로고
    • Altered plasma cytokines and total glutathione levels in parenterally fed critically ill trauma patients with adjuvant recombinant human growth hormone (rhGH) therapy
    • Jeevanandam, M., Begay, C.K., Shahbazian, L.M., and Petersen, S.R. (2000) Altered plasma cytokines and total glutathione levels in parenterally fed critically ill trauma patients with adjuvant recombinant human growth hormone (rhGH) therapy. Crit Care Med 28: 324-329.
    • (2000) Crit Care Med , vol.28 , pp. 324-329
    • Jeevanandam, M.1    Begay, C.K.2    Shahbazian, L.M.3    Petersen, S.R.4
  • 32
    • 0034704081 scopus 로고    scopus 로고
    • The thioredoxin system of the malaria parasite Plasmodium falciparum. Glutathione reduction revisited
    • Kanzok, S.M., Schirmer, R.H., Turbachova, I., Iozef, R., and Becker, K. (2000) The thioredoxin system of the malaria parasite Plasmodium falciparum. Glutathione reduction revisited. J Biol Chem 275: 40180-40186.
    • (2000) J Biol Chem , vol.275 , pp. 40180-40186
    • Kanzok, S.M.1    Schirmer, R.H.2    Turbachova, I.3    Iozef, R.4    Becker, K.5
  • 33
    • 0037016697 scopus 로고    scopus 로고
    • Escherichia coli gamma-glutamylcysteine synthetase. Two active site metal ions affect substrate and inhibitor binding
    • Kelly, B.S., Antholine, W.E., and Griffith, O.W. (2002) Escherichia coli gamma-glutamylcysteine synthetase. Two active site metal ions affect substrate and inhibitor binding. J Biol Chem 277: 50-58.
    • (2002) J Biol Chem , vol.277 , pp. 50-58
    • Kelly, B.S.1    Antholine, W.E.2    Griffith, O.W.3
  • 34
    • 0030176163 scopus 로고    scopus 로고
    • Plasmodium falciparum: isolation of large numbers of parasite clones from infected blood samples
    • Kirkman, L.A., Su, X.Z., and Wellems, T.E. (1996) Plasmodium falciparum: isolation of large numbers of parasite clones from infected blood samples. Exp Parasitol 83: 147-149.
    • (1996) Exp Parasitol , vol.83 , pp. 147-149
    • Kirkman, L.A.1    Su, X.Z.2    Wellems, T.E.3
  • 35
    • 0035109514 scopus 로고    scopus 로고
    • The malaria parasite Plasmodium falciparum possesses a functional thioredoxin system
    • Krnajski, Z., Gilberger, T.W., Walter, R.D., and Muller, S. (2001) The malaria parasite Plasmodium falciparum possesses a functional thioredoxin system. Mol Biochem Parasitol 112: 219-228.
    • (2001) Mol Biochem Parasitol , vol.112 , pp. 219-228
    • Krnajski, Z.1    Gilberger, T.W.2    Walter, R.D.3    Muller, S.4
  • 36
    • 0037135586 scopus 로고    scopus 로고
    • Thioredoxin reductase is essential for the survival of Plasmodium falciparum erythrocytic stages
    • Krnajski, Z., Gilberger, T.W., Walter, R.D., Cowman, A.F., and Müller, S. (2002) Thioredoxin reductase is essential for the survival of Plasmodium falciparum erythrocytic stages. J Biol Chem 277: 25970-25975.
    • (2002) J Biol Chem , vol.277 , pp. 25970-25975
    • Krnajski, Z.1    Gilberger, T.W.2    Walter, R.D.3    Cowman, A.F.4    Müller, S.5
  • 37
    • 0018704491 scopus 로고
    • Synchronization of Plasmodium falciparum erythrocytic stages in culture
    • Lambros, C., and Vanderberg, J.P. (1979) Synchronization of Plasmodium falciparum erythrocytic stages in culture. J Parasitol 65: 418-420.
    • (1979) J Parasitol , vol.65 , pp. 418-420
    • Lambros, C.1    Vanderberg, J.P.2
  • 38
    • 33750011601 scopus 로고    scopus 로고
    • Mitochondrial glutathione transport: physiological, pathological and toxicological implications
    • Lash, L.H. (2006) Mitochondrial glutathione transport: physiological, pathological and toxicological implications. Chem Biol Interact 163: 54-67.
    • (2006) Chem Biol Interact , vol.163 , pp. 54-67
    • Lash, L.H.1
  • 39
    • 0035735334 scopus 로고    scopus 로고
    • The essential and ancillary role of glutathione in Saccharomyces cerevisiae analysed using a grande gsh1 disruptant strain
    • Lee, J.C., Straffon, M.J., Jang, T.Y., Higgins, V.J., Grant, C.M., and Dawes, I.W. (2001) The essential and ancillary role of glutathione in Saccharomyces cerevisiae analysed using a grande gsh1 disruptant strain. FEMS Yeast Res 1: 57-65.
    • (2001) FEMS Yeast Res , vol.1 , pp. 57-65
    • Lee, J.C.1    Straffon, M.J.2    Jang, T.Y.3    Higgins, V.J.4    Grant, C.M.5    Dawes, I.W.6
  • 41
    • 33845717875 scopus 로고    scopus 로고
    • Vitamin C. Biosynthesis, recycling and degradation in mammals
    • Linster, C.L., and Van Schaftingen, E. (2007) Vitamin C. Biosynthesis, recycling and degradation in mammals. FEBS J 274: 1-22.
    • (2007) FEBS J , vol.274 , pp. 1-22
    • Linster, C.L.1    Van Schaftingen, E.2
  • 42
    • 0030016346 scopus 로고    scopus 로고
    • Characterization of Trypanosoma brucei gamma-glutamylcysteine synthetase, an essential enzyme in the biosynthesis of trypanothione (diglutathionylspermidine)
    • Lueder, D.V., and Phillips, M.A. (1996) Characterization of Trypanosoma brucei gamma-glutamylcysteine synthetase, an essential enzyme in the biosynthesis of trypanothione (diglutathionylspermidine). J Biol Chem 271: 17485-17490.
    • (1996) J Biol Chem , vol.271 , pp. 17485-17490
    • Lueder, D.V.1    Phillips, M.A.2
  • 43
    • 0040115912 scopus 로고    scopus 로고
    • The putative gamma-glutamylcysteine synthetase from Plasmodium falciparum contains large insertions and a variable tandem repeat
    • Lüersen, K., Walter, R.D., and Müller, S. (1999) The putative gamma-glutamylcysteine synthetase from Plasmodium falciparum contains large insertions and a variable tandem repeat. Mol Biochem Parasitol 98: 131-142.
    • (1999) Mol Biochem Parasitol , vol.98 , pp. 131-142
    • Lüersen, K.1    Walter, R.D.2    Müller, S.3
  • 44
    • 0034161967 scopus 로고    scopus 로고
    • Plasmodium falciparum-infected red blood cells depend on a functional glutathione de novo synthesis attributable to an enhanced loss of glutathione
    • Lüersen, K., Walter, R.D., and Müller, S. (2000) Plasmodium falciparum-infected red blood cells depend on a functional glutathione de novo synthesis attributable to an enhanced loss of glutathione. Biochem J 346: 545-552.
    • (2000) Biochem J , vol.346 , pp. 545-552
    • Lüersen, K.1    Walter, R.D.2    Müller, S.3
  • 45
    • 33748300551 scopus 로고    scopus 로고
    • Negative selection using yeast cytosine deaminase/uracil phosphoribosyl transferase in Plasmodium falciparum for targeted gene deletion by double crossover recombination
    • Maier, A.G., Braks, J.A., Waters, A.P., and Cowman, A.F. (2006) Negative selection using yeast cytosine deaminase/uracil phosphoribosyl transferase in Plasmodium falciparum for targeted gene deletion by double crossover recombination. Mol Biochem Parasitol 150: 118-121.
    • (2006) Mol Biochem Parasitol , vol.150 , pp. 118-121
    • Maier, A.G.1    Braks, J.A.2    Waters, A.P.3    Cowman, A.F.4
  • 46
    • 0010478667 scopus 로고
    • Mitochondrial damage in muscle occurs after marked depletion of glutathione and is prevented by giving glutathione monoester
    • Martensson, J., and Meister, A. (1989) Mitochondrial damage in muscle occurs after marked depletion of glutathione and is prevented by giving glutathione monoester. Proc Natl Acad Sci USA 86: 471-475.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 471-475
    • Martensson, J.1    Meister, A.2
  • 47
    • 0036566055 scopus 로고    scopus 로고
    • Glutathione synthetase from Plasmodium falciparum
    • Meierjohann, S., Walter, R.D., and Müller, S. (2002a) Glutathione synthetase from Plasmodium falciparum. Biochem J 363: 833-838.
    • (2002) Biochem J , vol.363 , pp. 833-838
    • Meierjohann, S.1    Walter, R.D.2    Müller, S.3
  • 48
    • 0037115759 scopus 로고    scopus 로고
    • Regulation of intracellular glutathione levels in erythrocytes infected with chloroquine-sensitive and chloroquine-resistant Plasmodium falciparum
    • Meierjohann, S., Walter, R.D., and Müller, S. (2002b) Regulation of intracellular glutathione levels in erythrocytes infected with chloroquine-sensitive and chloroquine-resistant Plasmodium falciparum. Biochem J 368: 761-768.
    • (2002) Biochem J , vol.368 , pp. 761-768
    • Meierjohann, S.1    Walter, R.D.2    Müller, S.3
  • 49
    • 0020537304 scopus 로고
    • Selective modification of glutathione metabolism
    • Meister, A. (1983) Selective modification of glutathione metabolism. Science 220: 472-477.
    • (1983) Science , vol.220 , pp. 472-477
    • Meister, A.1
  • 50
    • 0024264526 scopus 로고
    • Glutathione metabolism and its selective modification
    • Meister, A. (1988) Glutathione metabolism and its selective modification. J Biol Chem 263: 17205-17208.
    • (1988) J Biol Chem , vol.263 , pp. 17205-17208
    • Meister, A.1
  • 53
    • 4444359792 scopus 로고    scopus 로고
    • Redox and antioxidant systems of the malaria parasite Plasmodium falciparum
    • Müller, S. (2004) Redox and antioxidant systems of the malaria parasite Plasmodium falciparum. Mol Microbiol 53: 1291-1305.
    • (2004) Mol Microbiol , vol.53 , pp. 1291-1305
    • Müller, S.1
  • 56
    • 42449112152 scopus 로고    scopus 로고
    • A comprehensive model of purine uptake by the malaria parasite Plasmodium falciparum: identification of four purine transport activities in intraerythrocytic parasites
    • Quashie, N.B., Dorin-Semblat, D., Bray, P.G., Biagini, G.A., Doerig, C., Ranford-Cartwright, L.C., and De Koning, H.P. (2008) A comprehensive model of purine uptake by the malaria parasite Plasmodium falciparum: identification of four purine transport activities in intraerythrocytic parasites. Biochem J 411: 287-295.
    • (2008) Biochem J , vol.411 , pp. 287-295
    • Quashie, N.B.1    Dorin-Semblat, D.2    Bray, P.G.3    Biagini, G.A.4    Doerig, C.5    Ranford-Cartwright, L.C.6    De Koning, H.P.7
  • 57
    • 0035813229 scopus 로고    scopus 로고
    • Plasmodium falciparum possesses a classical glutaredoxin and a second, glutaredoxin-like protein with a PICOT homology domain
    • Rahlfs, S., Fischer, M., and Becker, K. (2001) Plasmodium falciparum possesses a classical glutaredoxin and a second, glutaredoxin-like protein with a PICOT homology domain. J Biol Chem 276: 37133-37140.
    • (2001) J Biol Chem , vol.276 , pp. 37133-37140
    • Rahlfs, S.1    Fischer, M.2    Becker, K.3
  • 58
    • 65549119262 scopus 로고    scopus 로고
    • Disruption of a Plasmodium falciparum multidrug resistance-associated protein (PfMRP) alters its fitness and transport of antimalarial drugs and glutathione
    • Raj, D.K., Mu, J., Jiang, H., Kabat, J., Singh, S., Sullivan, M., etal. (2009) Disruption of a Plasmodium falciparum multidrug resistance-associated protein (PfMRP) alters its fitness and transport of antimalarial drugs and glutathione. J Biol Chem 284: 7687-7696.
    • (2009) J Biol Chem , vol.284 , pp. 7687-7696
    • Raj, D.K.1    Mu, J.2    Jiang, H.3    Kabat, J.4    Singh, S.5    Sullivan, M.6
  • 59
    • 0034708162 scopus 로고    scopus 로고
    • Pgh1 modulates sensitivity and resistance to multiple antimalarials in Plasmodium falciparum
    • Reed, M.B., Saliba, K.J., Caruana, S.R., Kirk, K., and Cowman, A.F. (2000) Pgh1 modulates sensitivity and resistance to multiple antimalarials in Plasmodium falciparum. Nature 403: 906-909.
    • (2000) Nature , vol.403 , pp. 906-909
    • Reed, M.B.1    Saliba, K.J.2    Caruana, S.R.3    Kirk, K.4    Cowman, A.F.5
  • 60
    • 68949143115 scopus 로고    scopus 로고
    • An essential role for the Plasmodium Nek-2 Nima-related protein kinase in the sexual development of malaria parasites
    • Reininger, L., Tewari, R., Fennell, C., Holland, Z., Goldring, D., Ranford-Cartwright, L., etal. (2009) An essential role for the Plasmodium Nek-2 Nima-related protein kinase in the sexual development of malaria parasites. J Biol Chem 284: 20858-20868.
    • (2009) J Biol Chem , vol.284 , pp. 20858-20868
    • Reininger, L.1    Tewari, R.2    Fennell, C.3    Holland, Z.4    Goldring, D.5    Ranford-Cartwright, L.6
  • 61
    • 46549088004 scopus 로고    scopus 로고
    • Glutathione level and glutathione-dependent enzyme activities in blood serum of patients with gastrointestinal tract tumors
    • Scibior, D., Skrzycki, M., Podsiad, M., and Czeczot, H. (2008) Glutathione level and glutathione-dependent enzyme activities in blood serum of patients with gastrointestinal tract tumors. Clin Biochem 41: 852-858.
    • (2008) Clin Biochem , vol.41 , pp. 852-858
    • Scibior, D.1    Skrzycki, M.2    Podsiad, M.3    Czeczot, H.4
  • 62
    • 0017311840 scopus 로고
    • Human malaria parasites in continuous culture
    • Trager, W., and Jensen, J.B. (1976) Human malaria parasites in continuous culture. Science 193: 673-675.
    • (1976) Science , vol.193 , pp. 673-675
    • Trager, W.1    Jensen, J.B.2
  • 63
    • 0015089766 scopus 로고
    • New thick-film technique for malaria diagnosis. Use of saponin stromatolytic solution for lysis
    • Umlas, J., and Fallon, J.N. (1971) New thick-film technique for malaria diagnosis. Use of saponin stromatolytic solution for lysis. Am J Trop Med Hyg 20: 527-529.
    • (1971) Am J Trop Med Hyg , vol.20 , pp. 527-529
    • Umlas, J.1    Fallon, J.N.2
  • 65
    • 0019125693 scopus 로고
    • The level and half-life of glutathione in human plasma
    • Wendel, A., and Cikryt, P. (1980) The level and half-life of glutathione in human plasma. FEBS Lett 120: 209-211.
    • (1980) FEBS Lett , vol.120 , pp. 209-211
    • Wendel, A.1    Cikryt, P.2
  • 66
    • 66949132549 scopus 로고    scopus 로고
    • Two pathways for cysteine biosynthesis in Leishmania major
    • Williams, R.A., Westrop, G.D., and Coombs, G.H. (2009) Two pathways for cysteine biosynthesis in Leishmania major. Biochem J 420: 451-462.
    • (2009) Biochem J , vol.420 , pp. 451-462
    • Williams, R.A.1    Westrop, G.D.2    Coombs, G.H.3


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