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Volumn 185, Issue 5, 2003, Pages 1572-1581

Exogenous glutathione completes the defense against oxidative stress in Haemophilus influenzae

Author keywords

[No Author keywords available]

Indexed keywords

ANTIOXIDANT; CYSTEINE; CYSTEINYLGLYCINE; GENOMIC DNA; GLUTATHIONE; GLUTATHIONE DERIVATIVE; HYDROPEROXIDE; METHYLGLYOXAL; NITROSOGLUTATHIONE; PEROXIDASE; TERT BUTYL HYDROPEROXIDE; TRIPEPTIDE; UNCLASSIFIED DRUG;

EID: 0037369926     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.5.1572-1581.2003     Document Type: Article
Times cited : (47)

References (74)
  • 2
    • 0016688679 scopus 로고
    • Isolation and initial characterization of glutathione-deficient mutants of Escherichia coli K 12
    • Apontoweil, P., and W. Berends. 1975. Isolation and initial characterization of glutathione-deficient mutants of Escherichia coli K 12. Biochim. Biophys. Acta 399:10-22.
    • (1975) Biochim. Biophys. Acta , vol.399 , pp. 10-22
    • Apontoweil, P.1    Berends, W.2
  • 4
    • 0028043692 scopus 로고
    • Characterization and virulence analysis of catalase mutants of Haemophilus influenzae
    • Bishai, W. R., N. S. Howard, J. A. Winkelstein, and H. O. Smith. 1994. Characterization and virulence analysis of catalase mutants of Haemophilus influenzae. Infect. Immun. 62:4855-4860.
    • (1994) Infect. Immun. , vol.62 , pp. 4855-4860
    • Bishai, W.R.1    Howard, N.S.2    Winkelstein, J.A.3    Smith, H.O.4
  • 5
    • 0028272385 scopus 로고
    • A peroxide/ascorbate-inducible catalase from Haemophilus influenzae is homologous to the Escherichia coli katE gene product
    • Bishai, W. R., H. O. Smith, and G. J. Barcak. 1994. A peroxide/ascorbate-inducible catalase from Haemophilus influenzae is homologous to the Escherichia coli katE gene product. J. Bacteriol. 176:2914-2921.
    • (1994) J. Bacteriol. , vol.176 , pp. 2914-2921
    • Bishai, W.R.1    Smith, H.O.2    Barcak, G.J.3
  • 6
    • 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
  • 7
    • 0034648827 scopus 로고    scopus 로고
    • Peroxynitrite reductase activity of bacterial peroxiredoxins
    • Bryk, R., P. Griffin, and C. Nathan. 2000. Peroxynitrite reductase activity of bacterial peroxiredoxins. Nature 407:211-215.
    • (2000) Nature , vol.407 , pp. 211-215
    • Bryk, R.1    Griffin, P.2    Nathan, C.3
  • 8
    • 0027547437 scopus 로고
    • Peptostreptococcus micros has a uniquely high capacity to form hydrogen sulfide from glutathione
    • Carlsson, J., J. T. Larsen, and M. B. Edlund. 1993. Peptostreptococcus micros has a uniquely high capacity to form hydrogen sulfide from glutathione. Oral Microbiol. Immunol. 8:42-45.
    • (1993) Oral Microbiol. Immunol. , vol.8 , pp. 42-45
    • Carlsson, J.1    Larsen, J.T.2    Edlund, M.B.3
  • 9
    • 0029926905 scopus 로고    scopus 로고
    • Bacterial glutathione: A sacrificial defense against chlorine compounds
    • Chesney, J. A., J. W. Eaton, and J. R. Mahoney, Jr. 1996. Bacterial glutathione: a sacrificial defense against chlorine compounds. J. Bacteriol. 178: 2131-2135.
    • (1996) J. Bacteriol. , vol.178 , pp. 2131-2135
    • Chesney, J.A.1    Eaton, J.W.2    Mahoney J.R., Jr.3
  • 10
    • 0035845592 scopus 로고    scopus 로고
    • Survival of nontypeable Haemophilus influenzae in macrophages
    • Craig, J. E., A. Cliffe, K. Garnett, and N. J. High. 2001. Survival of nontypeable Haemophilus influenzae in macrophages. FEMS Microbiol. Lett. 203:55-61.
    • (2001) FEMS Microbiol. Lett. , vol.203 , pp. 55-61
    • Craig, J.E.1    Cliffe, A.2    Garnett, K.3    High, N.J.4
  • 13
    • 0030954101 scopus 로고    scopus 로고
    • Role of bacterial Mn-cofactored superoxide dismutase in oxidative stress responses, nasopharyngeal colonization, and sustained bacteremia caused by Haemophilus influenzae type b
    • D'Mello, R. A., P. R. Langford, and J. S. Kroll. 1997. Role of bacterial Mn-cofactored superoxide dismutase in oxidative stress responses, nasopharyngeal colonization, and sustained bacteremia caused by Haemophilus influenzae type b. Infect. Immun. 65:2700-2706.
    • (1997) Infect. Immun. , vol.65 , pp. 2700-2706
    • D'Mello, R.A.1    Langford, P.R.2    Kroll, J.S.3
  • 16
    • 0028908084 scopus 로고
    • Genetic definition of the Escherichia coli zwf "soxbox," the DNA binding site for SoxS-mediated induction of glucose 6-phosphate dehydrogenase in response to superoxide
    • Fawcett, W. P., and R. E. Wolf, Jr. 1995. Genetic definition of the Escherichia coli zwf "soxbox," the DNA binding site for SoxS-mediated induction of glucose 6-phosphate dehydrogenase in response to superoxide. J. Bacteriol. 177:1742-1750.
    • (1995) J. Bacteriol. , vol.177 , pp. 1742-1750
    • Fawcett, W.P.1    Wolf R.E., Jr.2
  • 18
    • 0028786475 scopus 로고
    • Potassium channel activation by glutathione-S-conjugates in Escherichia coli: Protection against methylglyoxal is mediated by cytoplasmic acidification
    • Ferguson, G. P., D. McLaggan, and I. R. Booth. 1995. Potassium channel activation by glutathione-S-conjugates in Escherichia coli: protection against methylglyoxal is mediated by cytoplasmic acidification. Mol. Microbiol. 17:1025-1033.
    • (1995) Mol. Microbiol. , vol.17 , pp. 1025-1033
    • Ferguson, G.P.1    McLaggan, D.2    Booth, I.R.3
  • 19
    • 0027491161 scopus 로고
    • Activation of potassium channels during metabolite detoxification in Escherichia coli
    • Ferguson, G. P., A. W. Munro, R. M. Douglas, D. McLaggan, and I. R. Booth. 1993. Activation of potassium channels during metabolite detoxification in Escherichia coli. Mol. Microbiol. 9:1297-1303.
    • (1993) Mol. Microbiol. , vol.9 , pp. 1297-1303
    • Ferguson, G.P.1    Munro, A.W.2    Douglas, R.M.3    McLaggan, D.4    Booth, I.R.5
  • 22
    • 0035205673 scopus 로고    scopus 로고
    • The functions of interand intracellular glutathione transport systems in plants
    • Foyer, C. H., F. L. Theodoulou, and S. Delrot. 2001. The functions of interand intracellular glutathione transport systems in plants. Trends Plant Sci. 6:486-492.
    • (2001) Trends Plant Sci. , vol.6 , pp. 486-492
    • Foyer, C.H.1    Theodoulou, F.L.2    Delrot, S.3
  • 23
    • 0035875939 scopus 로고    scopus 로고
    • NADPH-dependent glutathione peroxidase-like proteins (Gpx-1, Gpx-2) reduce unsaturated fatty acid hydroperoxides in Synechocystis PCC 6803
    • Gaber, A., M. Tamoi, T. Takeda, Y. Nakano, and S. Shigeoka. 2001. NADPH-dependent glutathione peroxidase-like proteins (Gpx-1, Gpx-2) reduce unsaturated fatty acid hydroperoxides in Synechocystis PCC 6803. FEBS Lett. 499:32-36.
    • (2001) FEBS Lett. , vol.499 , pp. 32-36
    • Gaber, A.1    Tamoi, M.2    Takeda, T.3    Nakano, Y.4    Shigeoka, S.5
  • 24
    • 0032540947 scopus 로고    scopus 로고
    • In vivo transcription of nrdAB operon and of grxA and fpg genes is triggered in Escherichia coli lacking both thioredoxin and glutaredoxin 1 or thioredoxin and glutathione, respectively
    • Gallardo-Madueno, R., J. F. Leal, G. Dorado, A. Holmgren, J. Lopez-Barea, and C. Pueyo. 1998. In vivo transcription of nrdAB operon and of grxA and fpg genes is triggered in Escherichia coli lacking both thioredoxin and glutaredoxin 1 or thioredoxin and glutathione, respectively. J. Biol. Chem. 273:18382-18388.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18382-18388
    • Gallardo-Madueno, R.1    Leal, J.F.2    Dorado, G.3    Holmgren, A.4    Lopez-Barea, J.5    Pueyo, C.6
  • 25
    • 0033956380 scopus 로고    scopus 로고
    • Differential regulation of glutaredoxin gene expression in response to stress conditions in the yeast Saccharomyces cerevisiae
    • Grant, C. M., S. Luikenhuis, A. Beckhouse, M. Soderbergh, and I. W. Dawes. 2000. Differential regulation of glutaredoxin gene expression in response to stress conditions in the yeast Saccharomyces cerevisiae. Biochim. Biophys. Acta 1490:33-42.
    • (2000) Biochim. Biophys. Acta , vol.1490 , pp. 33-42
    • Grant, C.M.1    Luikenhuis, S.2    Beckhouse, A.3    Soderbergh, M.4    Dawes, I.W.5
  • 26
    • 0030004354 scopus 로고    scopus 로고
    • Glutathione is an essential metabolite required for resistance to oxidative stress in the yeast Saccharomyces cerevisiae
    • Grant, C. M., F. H. MacIver, and I. W. Dawes. 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
  • 28
    • 0022337175 scopus 로고
    • Therapeutic benefits of oxygen radical scavenger treatments remain unproven
    • Greenwald, R. A. 1985, Therapeutic benefits of oxygen radical scavenger treatments remain unproven. J. Free Radic. Biol. Med. 1:173-177.
    • (1985) J. Free Radic. Biol. Med. , vol.1 , pp. 173-177
    • Greenwald, R.A.1
  • 29
    • 0030823068 scopus 로고    scopus 로고
    • Induction of glutathione-dependent formaldehyde dehydrogenase activity in Escherichia coli and Haemophilus influenzae
    • Gutheil, W. G., E. Kasimoglu, and P. C. Nicholson. 1997. Induction of glutathione-dependent formaldehyde dehydrogenase activity in Escherichia coli and Haemophilus influenzae. Biochem. Biophys. Res. Commun. 238:693-696.
    • (1997) Biochem. Biophys. Res. Commun. , vol.238 , pp. 693-696
    • Gutheil, W.G.1    Kasimoglu, E.2    Nicholson, P.C.3
  • 30
    • 0014738279 scopus 로고
    • Defined medium for growth of Haemophilus influenzae
    • Herriott, R. M., E. Y. Meyer, M. Vogt, and M. Modan. 1970. Defined medium for growth of Haemophilus influenzae. J. Bacteriol. 101:513-516.
    • (1970) J. Bacteriol. , vol.101 , pp. 513-516
    • Herriott, R.M.1    Meyer, E.Y.2    Vogt, M.3    Modan, M.4
  • 32
    • 0033578750 scopus 로고    scopus 로고
    • Genetic analysis of glutathione peroxidase in oxidative stress response of Saccharomyces cerevisiae
    • Inoue, Y., T. Matsuda, K. Sugiyama, S. Izawa, and A. Kimura. 1999. Genetic analysis of glutathione peroxidase in oxidative stress response of Saccharomyces cerevisiae. J. Biol. Chem. 274:27002-27009.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27002-27009
    • Inoue, Y.1    Matsuda, T.2    Sugiyama, K.3    Izawa, S.4    Kimura, A.5
  • 33
    • 0029844594 scopus 로고    scopus 로고
    • Importance of catalase in the adaptive response to hydrogen peroxide: Analysis of acatalasaemic Saccharomyces cerevisiae
    • Izawa, S., Y. Inoue, and A. Kimura. 1996. Importance of catalase in the adaptive response to hydrogen peroxide: analysis of acatalasaemic Saccharomyces cerevisiae. Biochem. J. 320:61-67.
    • (1996) Biochem. J. , vol.320 , pp. 61-67
    • Izawa, S.1    Inoue, Y.2    Kimura, A.3
  • 34
    • 0029042565 scopus 로고
    • Oxidative stress response in yeast: Effect of glutathione on adaptation to hydrogen peroxide stress in Saccharomyces cerevisiae
    • Izawa, S., Y. Inoue, and A. Kimura. 1995. Oxidative stress response in yeast: effect of glutathione on adaptation to hydrogen peroxide stress in Saccharomyces cerevisiae. FEBS Lett. 368:73-76.
    • (1995) FEBS Lett. , vol.368 , pp. 73-76
    • Izawa, S.1    Inoue, Y.2    Kimura, A.3
  • 35
    • 0032030784 scopus 로고    scopus 로고
    • Importance of glucose-6-phosphate dehydrogenase in the adaptive response to hydrogen peroxide in Saccharomyces cerevisiae
    • Izawa, S., K. Maeda, T. Miki, J. Mano, Y. Inoue, and A. Kimura. 1998. Importance of glucose-6-phosphate dehydrogenase in the adaptive response to hydrogen peroxide in Saccharomyces cerevisiae. Biochem. J. 330:811-817.
    • (1998) Biochem. J. , vol.330 , pp. 811-817
    • Izawa, S.1    Maeda, K.2    Miki, T.3    Mano, J.4    Inoue, Y.5    Kimura, A.6
  • 36
    • 0029030751 scopus 로고
    • Lethal and mutagenic actions of N-methyl-N′-nitro-N-nitrosoguanidine potentiated by oxidized glutathione, a seemingly harmless substance in the cellular environment
    • Kumaresan, K. R., S. S. Springhorn, and S. A. Lacks. 1995. Lethal and mutagenic actions of N-methyl-N′-nitro-N-nitrosoguanidine potentiated by oxidized glutathione, a seemingly harmless substance in the cellular environment. J. Bacteriol. 177:3641-3646.
    • (1995) J. Bacteriol. , vol.177 , pp. 3641-3646
    • Kumaresan, K.R.1    Springhorn, S.S.2    Lacks, S.A.3
  • 37
    • 0025768952 scopus 로고
    • Effects of overproduction of superoxide dismutase on the toxicity of paraquat toward Escherichia coli
    • Liochev, S. I., and I. Fridovich. 1991. Effects of overproduction of superoxide dismutase on the toxicity of paraquat toward Escherichia coli. J. Biol. Chem. 266:8747-8750.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8747-8750
    • Liochev, S.I.1    Fridovich, I.2
  • 38
    • 0035932413 scopus 로고    scopus 로고
    • A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans
    • Liu, L., A. Hausladen, M. Zeng, L. Que, J. Heitman, and J. S. Stamler. 2001. A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans. Nature 410:490-494.
    • (2001) Nature , vol.410 , pp. 490-494
    • Liu, L.1    Hausladen, A.2    Zeng, M.3    Que, L.4    Heitman, J.5    Stamler, J.S.6
  • 39
    • 0021719208 scopus 로고
    • Genetic mapping of katF, a locus that with katE affects the synthesis of a second catalase species in Escherichia coli
    • Loewen, P. C., and B. L. Triggs. 1984. Genetic mapping of katF, a locus that with katE affects the synthesis of a second catalase species in Escherichia coli. J. Bacteriol. 160:668-675.
    • (1984) J. Bacteriol. , vol.160 , pp. 668-675
    • Loewen, P.C.1    Triggs, B.L.2
  • 40
    • 0032952196 scopus 로고    scopus 로고
    • Glucose 6-phosphate dehydrogenase is required for Salmonella typhimurium virulence and resistance to reactive oxygen and nitrogen intermediates
    • Lundberg, B. E., R. E. Wolf, Jr., M. C. Dinauer, Y. Xu, and F. C. Fang. 1999. Glucose 6-phosphate dehydrogenase is required for Salmonella typhimurium virulence and resistance to reactive oxygen and nitrogen intermediates. Infect. Immun. 67:436-438.
    • (1999) Infect. Immun. , vol.67 , pp. 436-438
    • Lundberg, B.E.1    Wolf R.E., Jr.2    Dinauer, M.C.3    Xu, Y.4    Fang, F.C.5
  • 41
    • 0029907767 scopus 로고    scopus 로고
    • Lack of expression of the global regulator OxyR in Haemophilus influenzae has a profound effect on growth phenotype
    • Maciver, I., and E. J. Hansen. 1996. Lack of expression of the global regulator OxyR in Haemophilus influenzae has a profound effect on growth phenotype. Infect. Immun. 64:4618-4629.
    • (1996) Infect. Immun. , vol.64 , pp. 4618-4629
    • Maciver, I.1    Hansen, E.J.2
  • 43
    • 0028308730 scopus 로고
    • Kinetics and equilibria of S-nitrosothiol-thiol exchange between glutathione, cysteine, penicillamines and serum albumin
    • Meyer, D. J., H. Kramer, N. Ozer, B. Coles, and B. Ketterer. 1994. Kinetics and equilibria of S-nitrosothiol-thiol exchange between glutathione, cysteine, penicillamines and serum albumin. FEBS Lett. 345:177-180.
    • (1994) FEBS Lett. , vol.345 , pp. 177-180
    • Meyer, D.J.1    Kramer, H.2    Ozer, N.3    Coles, B.4    Ketterer, B.5
  • 45
    • 8944258926 scopus 로고    scopus 로고
    • Interruption of the gpxA gene increases the sensitivity of Neisseria meningitidis to paraquat
    • Moore, T. D., and P. F. Sparling. 1996. Interruption of the gpxA gene increases the sensitivity of Neisseria meningitidis to paraquat. J. Bacteriol. 178:4301-4305.
    • (1996) J. Bacteriol. , vol.178 , pp. 4301-4305
    • Moore, T.D.1    Sparling, P.F.2
  • 46
    • 0033013334 scopus 로고    scopus 로고
    • Deficient nucleotide excision repair increases base-pair substitutions but decreases TGGC frameshifts induced by methylglyoxal in Escherichia coli
    • Murata-Kamiya, N., H. Kaji, and H. Kasai. 1999. Deficient nucleotide excision repair increases base-pair substitutions but decreases TGGC frameshifts induced by methylglyoxal in Escherichia coli. Mutat. Res. 442:19-28.
    • (1999) Mutat. Res. , vol.442 , pp. 19-28
    • Murata-Kamiya, N.1    Kaji, H.2    Kasai, H.3
  • 47
    • 0003655628 scopus 로고    scopus 로고
    • Approved standard M2-A6. National Committee for Clinical Laboratory Standards, Wayne, Pa
    • National Committee for Clinical Laboratory Standards. 1997. Performance standards for antimicrobial disk susceptibility tests, 6th ed. Approved standard M2-A6. National Committee for Clinical Laboratory Standards, Wayne, Pa.
    • (1997) Performance Standards for Antimicrobial Disk Susceptibility Tests, 6th Ed.
  • 49
    • 0035879763 scopus 로고    scopus 로고
    • Role of glutathione in regulation of hydroperoxidase I in growing Escherichia coli
    • Oktyabrsky, O. N., G. V. Smirnovam, and N. G. Muzyka. 2001. Role of glutathione in regulation of hydroperoxidase I in growing Escherichia coli. Free Radic. Biol. Med. 31:250-255.
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 250-255
    • Oktyabrsky, O.N.1    Smirnovam, G.V.2    Muzyka, N.G.3
  • 50
    • 0029098024 scopus 로고
    • S-nitrosoglutathione reversibly inhibits GAPDH by S-nitrosylation
    • Padgett, C. M., and A. R. Whorton. 1995. S-nitrosoglutathione reversibly inhibits GAPDH by S-nitrosylation. Am. J. Physiol. 269:C739-C749.
    • (1995) Am. J. Physiol. , vol.269
    • Padgett, C.M.1    Whorton, A.R.2
  • 51
    • 0028988415 scopus 로고
    • Identification of N2-(1-carboxyethyl)guanine (CEG) as a guanine advanced glycosylation end product
    • Papoulis, A., Y. al-Abed, and R. Bucala. 1995. Identification of N2-(1-carboxyethyl)guanine (CEG) as a guanine advanced glycosylation end product. Biochemistry 34:648-655.
    • (1995) Biochemistry , vol.34 , pp. 648-655
    • Papoulis, A.1    Al-Abed, Y.2    Bucala, R.3
  • 53
    • 0034213330 scopus 로고    scopus 로고
    • A short review on the role of glutathione in the response of yeasts to nutritional, environmental, and oxidative stresses
    • Penninckx, M. 2000. A short review on the role of glutathione in the response of yeasts to nutritional, environmental, and oxidative stresses. Enzyme Microb. Technol. 26:737-742.
    • (2000) Enzyme Microb. Technol. , vol.26 , pp. 737-742
    • Penninckx, M.1
  • 54
    • 0027412924 scopus 로고
    • Metabolism and functions of glutathione in micro-organisms
    • Penninckx, M. J., and M. T. Elskens. 1993. Metabolism and functions of glutathione in micro-organisms. Adv. Microb. Physiol. 34:239-301.
    • (1993) Adv. Microb. Physiol. , vol.34 , pp. 239-301
    • Penninckx, M.J.1    Elskens, M.T.2
  • 55
    • 0038957365 scopus 로고    scopus 로고
    • Transcriptional regulation of glutaredoxin and thioredoxin pathways and related enzymes in response to oxidative stress
    • Prieto-Alamo, M. J., J. Jurado, R. Gallardo-Madueno, F. Monje-Casas, A. Holmgren, and C. Pueyo. 2000. Transcriptional regulation of glutaredoxin and thioredoxin pathways and related enzymes in response to oxidative stress. J. Biol. Chem. 275:13398-13405.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13398-13405
    • Prieto-Alamo, M.J.1    Jurado, J.2    Gallardo-Madueno, R.3    Monje-Casas, F.4    Holmgren, A.5    Pueyo, C.6
  • 56
    • 0034102305 scopus 로고    scopus 로고
    • Glutathione is involved in environmental stress responses in Rhizobium tropici, including acid tolerance
    • Riccillo, P. M., C. I. Muglia, F. J. de Bruijn, A. J. Roe, I. R. Booth, and O. M. Aguilar. 2000. Glutathione is involved in environmental stress responses in Rhizobium tropici, including acid tolerance. J. Bacteriol. 182:1748-1753.
    • (2000) J. Bacteriol. , vol.182 , pp. 1748-1753
    • Riccillo, P.M.1    Muglia, C.I.2    De Bruijn, F.J.3    Roe, A.J.4    Booth, I.R.5    Aguilar, O.M.6
  • 57
    • 0025741197 scopus 로고
    • Elimination of hydrogen peroxide by Haemophilus somnus, a catalase-negative pathogen of cattle
    • Sample, A. K., and C. J. Czuprynski. 1991. Elimination of hydrogen peroxide by Haemophilus somnus, a catalase-negative pathogen of cattle. Infect. Immun. 59:2239-2244.
    • (1991) Infect. Immun. , vol.59 , pp. 2239-2244
    • Sample, A.K.1    Czuprynski, C.J.2
  • 58
    • 0035209075 scopus 로고    scopus 로고
    • Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli
    • Seaver, L. C., and J. A. Imlay. 2001. Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli. J. Bacteriol. 183:7173-7181.
    • (2001) J. Bacteriol. , vol.183 , pp. 7173-7181
    • Seaver, L.C.1    Imlay, J.A.2
  • 59
    • 0031894921 scopus 로고    scopus 로고
    • Import and metabolism of glutathione by Streptococcus mutans
    • Sherrill, C., and R. C. Fahey. 1998. Import and metabolism of glutathione by Streptococcus mutans. J. Bacteriol. 180:1454-1459.
    • (1998) J. Bacteriol. , vol.180 , pp. 1454-1459
    • Sherrill, C.1    Fahey, R.C.2
  • 60
    • 0034067665 scopus 로고    scopus 로고
    • Effects of menadione and hydrogen peroxide on glutathione status in growing Escherichia coli
    • Smirnova, G. V., N. G. Muzyka, M. N. Glukhovchenko, and O. N. Oktyabrsky. 2000. Effects of menadione and hydrogen peroxide on glutathione status in growing Escherichia coli. Free Radic. Biol. Med. 28:1009-1016.
    • (2000) Free Radic. Biol. Med. , vol.28 , pp. 1009-1016
    • Smirnova, G.V.1    Muzyka, N.G.2    Glukhovchenko, M.N.3    Oktyabrsky, O.N.4
  • 61
    • 0030222083 scopus 로고    scopus 로고
    • Glutathione is an important antioxidant molecule in the yeast Saccharomyces cerevisiae
    • Stephen, D. W., and D. J. Jamieson. 1996. Glutathione is an important antioxidant molecule in the yeast Saccharomyces cerevisiae. FEMS Microbiol. Lett. 141:207-212.
    • (1996) FEMS Microbiol. Lett. , vol.141 , pp. 207-212
    • Stephen, D.W.1    Jamieson, D.J.2
  • 62
    • 0034680875 scopus 로고    scopus 로고
    • Flavohemoglobin Hmp affords inducible protection for Escherichia coli respiration, catalyzed by cytochromes bo' or bd, from nitric oxide
    • Stevanin, T. M., N. Ioannidis, C. E. Mills, S. O. Kim, M. N. Hughes, and R. K. Poole. 2000. Flavohemoglobin Hmp affords inducible protection for Escherichia coli respiration, catalyzed by cytochromes bo' or bd, from nitric oxide. J. Biol. Chem. 275:35868-35875.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35868-35875
    • Stevanin, T.M.1    Ioannidis, N.2    Mills, C.E.3    Kim, S.O.4    Hughes, M.N.5    Poole, R.K.6
  • 63
    • 0035859807 scopus 로고    scopus 로고
    • Peptide methionine sulfoxide reductase from Escherichia coli and Mycobacterium tuberculosis protects bacteria against oxidative damage from reactive nitrogen intermediates
    • St. John, G., N. Brot, J. Ruan, H. Erdjument-Bromage, P. Tempst, H. Weissbach, and C. Nathan. 2001. Peptide methionine sulfoxide reductase from Escherichia coli and Mycobacterium tuberculosis protects bacteria against oxidative damage from reactive nitrogen intermediates. Proc. Natl. Acad. Sci. USA 98:9901-9906.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9901-9906
    • St. John, G.1    Brot, N.2    Ruan, J.3    Erdjument-Bromage, H.4    Tempst, P.5    Weissbach, H.6    Nathan, C.7
  • 65
    • 0024604234 scopus 로고
    • An alkyl hydroperoxide reductase induced by oxidative stress in Salmonella typhimurium and Escherichia coli: Genetic characterization and cloning of ahp
    • Storz, G., F. S. Jacobson, L. A. Tartaglia, R. W. Morgan, L. A. Silveira, and B. N. Ames. 1989. An alkyl hydroperoxide reductase induced by oxidative stress in Salmonella typhimurium and Escherichia coli: genetic characterization and cloning of ahp. J. Bacteriol. 171:2049-2055.
    • (1989) J. Bacteriol. , vol.171 , pp. 2049-2055
    • Storz, G.1    Jacobson, F.S.2    Tartaglia, L.A.3    Morgan, R.W.4    Silveira, L.A.5    Ames, B.N.6
  • 66
    • 0024446668 scopus 로고
    • Evolution of antioxidant mechanisms: Thiol-dependent peroxidases and thioltransferase among procaryotes
    • Sundquist, A. R., and R. C. Fahey. 1989. Evolution of antioxidant mechanisms: thiol-dependent peroxidases and thioltransferase among procaryotes. J. Mol. Evol. 29:429-435.
    • (1989) J. Mol. Evol. , vol.29 , pp. 429-435
    • Sundquist, A.R.1    Fahey, R.C.2
  • 67
    • 0030930252 scopus 로고    scopus 로고
    • OxyR-dependent induction of Escherichia coli grx gene expression by peroxide stress
    • Tao, K. 1997. OxyR-dependent induction of Escherichia coli grx gene expression by peroxide stress. J. Bacteriol. 179:5967-5970.
    • (1997) J. Bacteriol. , vol.179 , pp. 5967-5970
    • Tao, K.1
  • 68
    • 0021334514 scopus 로고
    • Disulfide reduction and sulfhydryl uptake by Streptococcus mutans
    • Thomas, E. L. 1984. Disulfide reduction and sulfhydryl uptake by Streptococcus mutans. J. Bacteriol. 157:240-246.
    • (1984) J. Bacteriol. , vol.157 , pp. 240-246
    • Thomas, E.L.1
  • 69
    • 0014481378 scopus 로고
    • Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: Applications to mammalian blood and other tissues
    • Tietze, F. 1969. Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues. Anal. Biochem. 27:502-522.
    • (1969) Anal. Biochem. , vol.27 , pp. 502-522
    • Tietze, F.1
  • 70
    • 0015791813 scopus 로고
    • Purification and characterization of S-2-hydroxyaclglutathione hydrolase (glyoxalase II) from human liver
    • Uotila, L. 1973. Purification and characterization of S-2-hydroxyaclglutathione hydrolase (glyoxalase II) from human liver. Biochemistry 12:3944-3951.
    • (1973) Biochemistry , vol.12 , pp. 3944-3951
    • Uotila, L.1
  • 71
    • 0030957038 scopus 로고    scopus 로고
    • Enhanced expression of glucose-6-phosphate dehydrogenase in human cells sustaining oxidative stress
    • Ursini, M. V., A. Parrella, G. Rosa, S. Salzano, and G. Martini. 1997. Enhanced expression of glucose-6-phosphate dehydrogenase in human cells sustaining oxidative stress. Biochem. J. 323:801-806.
    • (1997) Biochem. J. , vol.323 , pp. 801-806
    • Ursini, M.V.1    Parrella, A.2    Rosa, G.3    Salzano, S.4    Martini, G.5
  • 72
    • 0035877729 scopus 로고    scopus 로고
    • Characterization of glutathione amide reductase from Chromatium gracile. Identification of a novel thiol peroxidase (Prx/Grx) fueled by glutathione amide redox cycling
    • Vergauwen, B., F. Pauwels, F. Jacquemotte, T. E. Meyer, M. A. Cusanovich, R. G. Bartsch, and J. J. Van Beeumen. 2001. Characterization of glutathione amide reductase from Chromatium gracile. Identification of a novel thiol peroxidase (Prx/Grx) fueled by glutathione amide redox cycling. J. Biol. Chem. 276:20890-20897.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20890-20897
    • Vergauwen, B.1    Pauwels, F.2    Jacquemotte, F.3    Meyer, T.E.4    Cusanovich, M.A.5    Bartsch, R.G.6    Van Beeumen, J.J.7
  • 73
    • 0030895581 scopus 로고    scopus 로고
    • Cloning, overexpression, and characterization of glutaredoxin 2, an atypical glutaredoxin from Escherichia coli
    • Vlamis-Gardikas, A., F. Aslund, G. Spyrou, T. Bergman, and A. Holmgren. 1997. Cloning, overexpression, and characterization of glutaredoxin 2, an atypical glutaredoxin from Escherichia coli. J. Biol. Chem. 272:11236-11243.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11236-11243
    • Vlamis-Gardikas, A.1    Aslund, F.2    Spyrou, G.3    Bergman, T.4    Holmgren, A.5
  • 74
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • Zheng, M., F. Aslund, and G. Storz. 1998. Activation of the OxyR transcription factor by reversible disulfide bond formation. Science 279:1718-1721.
    • (1998) Science , vol.279 , pp. 1718-1721
    • Zheng, M.1    Aslund, F.2    Storz, G.3


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