메뉴 건너뛰기




Volumn 44, Issue , 2007, Pages 143-193

Peroxiredoxins in bacterial antioxidant defense

Author keywords

AhpC; Bacteria; Gene regulation; Hydrogen peroxide; HypR; Ohr; OhrR; Organic peroxide; OsmC; Oxidative stress; OxyR; Peroxiredoxin; Peroxynitrite; PerR; Tpx; Virulence

Indexed keywords

ANTIOXIDANT; BACTERIAL PROTEIN; CYSTEINE; PEROXIDE; PEROXIREDOXIN; REPRESSOR PROTEIN;

EID: 38749140290     PISSN: 03060225     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4020-6051-9_7     Document Type: Article
Times cited : (91)

References (213)
  • 1
    • 1842558298 scopus 로고    scopus 로고
    • Control of the alternative sigma factor sigmaE in Escherichia coli
    • Ades, S. E., 2004, Control of the alternative sigma factor sigmaE in Escherichia coli. Curr. Opin. Microbiol. 7: 157-162.
    • (2004) Curr. Opin. Microbiol , vol.7 , pp. 157-162
    • Ades, S.E.1
  • 2
    • 0029855070 scopus 로고    scopus 로고
    • General and oxidative stress responses in Bacillus subtilis: Cloning, expression, and mutation of the alkyl hydroperoxide reductase operon
    • Antelmann, H., Engelmann, S., Schmid, R., and Hecker, M., 1996, General and oxidative stress responses in Bacillus subtilis: cloning, expression, and mutation of the alkyl hydroperoxide reductase operon. J. Bacteriol. 178: 6571-6578.
    • (1996) J. Bacteriol , vol.178 , pp. 6571-6578
    • Antelmann, H.1    Engelmann, S.2    Schmid, R.3    Hecker, M.4
  • 3
    • 0029144017 scopus 로고
    • A homologue to the Escherichia coli alkyl hydroperoxide reductase AhpC is induced by osmotic upshock in Staphylococcus aureus
    • Armstrong-Buisseret, L., Cole, M. B., and Stewart, G. S., 1995, A homologue to the Escherichia coli alkyl hydroperoxide reductase AhpC is induced by osmotic upshock in Staphylococcus aureus. Microbiol. 141: 1655-1661.
    • (1995) Microbiol , vol.141 , pp. 1655-1661
    • Armstrong-Buisseret, L.1    Cole, M.B.2    Stewart, G.S.3
  • 4
    • 0035088098 scopus 로고    scopus 로고
    • Global analysis of Escherichia coli gene expression during the acetate-induced acid tolerance response
    • Arnold, C. N., McElhanon, J., Lee, A., Leonhart, R., and Siegele, D. A., 2001, Global analysis of Escherichia coli gene expression during the acetate-induced acid tolerance response. J. Bacteriol. 183: 2178-2186.
    • (2001) J. Bacteriol , vol.183 , pp. 2178-2186
    • Arnold, C.N.1    McElhanon, J.2    Lee, A.3    Leonhart, R.4    Siegele, D.A.5
  • 5
    • 0034915594 scopus 로고    scopus 로고
    • Bacterial Ohr and OsmC paralogues define two protein families with distinct functions and patterns of expression
    • Atichartpongkul, S., Loprasert, S., Vattanaviboon, P., Whangsuk, W., Helmann John, D., and Mongkolsuk, S., 2001, Bacterial Ohr and OsmC paralogues define two protein families with distinct functions and patterns of expression. Microbiol. 147: 1775-1782.
    • (2001) Microbiol , vol.147 , pp. 1775-1782
    • Atichartpongkul, S.1    Loprasert, S.2    Vattanaviboon, P.3    Whangsuk, W.4    Helmann John, D.5    Mongkolsuk, S.6
  • 6
    • 0032837846 scopus 로고    scopus 로고
    • An ironregulated alkyl hydroperoxide reductase (AhpC) confers aerotolerance and oxidative stress resistance to the microaerophilic pathogen
    • Baillon, M.-L. A., van Vliet, A. H. M., Ketley, J. M., Constantinidou, C., and Penn, C. W., 1999, An ironregulated alkyl hydroperoxide reductase (AhpC) confers aerotolerance and oxidative stress resistance to the microaerophilic pathogen Campylobacter jejuni. J. Bacteriol. 181: 4798-4804.
    • (1999) Campylobacter jejuni. J. Bacteriol , vol.181 , pp. 4798-4804
    • Baillon, M.-L.A.1    van Vliet, A.H.M.2    Ketley, J.M.3    Constantinidou, C.4    Penn, C.W.5
  • 7
    • 0037646517 scopus 로고    scopus 로고
    • Catalytic mechanism of thiol peroxidase from Escherichia coli. Sulfenic acid formation and overoxidation of essential CYS61
    • Baker, L. M., and Poole, L. B., 2003, Catalytic mechanism of thiol peroxidase from Escherichia coli. Sulfenic acid formation and overoxidation of essential CYS61. J. Biol. Chem. 278: 9203-9211.
    • (2003) J. Biol. Chem , vol.278 , pp. 9203-9211
    • Baker, L.M.1    Poole, L.B.2
  • 8
    • 0035108401 scopus 로고    scopus 로고
    • Essential thioredoxin-dependent peroxiredoxin system from Helicobacter pylori: Genetic and kinetic characterization
    • Baker, L. M., Raudonikiene, A., Hoffman, P. S., and Poole, L. B., 2001, Essential thioredoxin-dependent peroxiredoxin system from Helicobacter pylori: genetic and kinetic characterization. J. Bacteriol. 183: 1961-1973.
    • (2001) J. Bacteriol , vol.183 , pp. 1961-1973
    • Baker, L.M.1    Raudonikiene, A.2    Hoffman, P.S.3    Poole, L.B.4
  • 9
    • 17444408182 scopus 로고    scopus 로고
    • Exposure to cadmium elevates expression of genes in the OxyR and OhrR regulons and induces cross-resistance to peroxide killing treatments in Xanthomonas campestris
    • Banjerdkij, P., Vattanaviboon, P., and Mongkolsuk, S., 2005, Exposure to cadmium elevates expression of genes in the OxyR and OhrR regulons and induces cross-resistance to peroxide killing treatments in Xanthomonas campestris. Appl. Environ. Microbiol. 7: 1843-1849.
    • (2005) Appl. Environ. Microbiol , vol.7 , pp. 1843-1849
    • Banjerdkij, P.1    Vattanaviboon, P.2    Mongkolsuk, S.3
  • 10
    • 1842288543 scopus 로고    scopus 로고
    • Specific and general stress proteins in Bacillus subtilis-a two-dimensional protein electrophoresis study
    • Bernhardt, J., Volker, U., Volker, A., Antelmann, H., Schmid, R., Mach, H., and Hecker, M., 1997, Specific and general stress proteins in Bacillus subtilis-a two-dimensional protein electrophoresis study. Microbiol. 143: 999-1017.
    • (1997) Microbiol , vol.143 , pp. 999-1017
    • Bernhardt, J.1    Volker, U.2    Volker, A.3    Antelmann, H.4    Schmid, R.5    Mach, H.6    Hecker, M.7
  • 11
    • 0032932220 scopus 로고    scopus 로고
    • Acid-and base-induced proteins during aerobic and anaerobic growth of Escherichia coli revealed by two-dimensional gel electrophoresis
    • Blankenhorn, D., Phillips, J., and Slonczewski, J. L., 1999, Acid-and base-induced proteins during aerobic and anaerobic growth of Escherichia coli revealed by two-dimensional gel electrophoresis. J. Bacteriol. 181: 2209-2216.
    • (1999) J. Bacteriol , vol.181 , pp. 2209-2216
    • Blankenhorn, D.1    Phillips, J.2    Slonczewski, J.L.3
  • 12
    • 0031863419 scopus 로고    scopus 로고
    • Interplay between global regulators of Escherichia coli: Effect of RpoS, Lrp and H-NS on transcription of the gene osmC
    • Bouvier, J., Gordia, S., Kampmann, G., Lange, R., Hengge-Aronis, R., and Gutierrez, C., 1998, Interplay between global regulators of Escherichia coli: effect of RpoS, Lrp and H-NS on transcription of the gene osmC. Mo. l Microbiol. 28: 971-980.
    • (1998) Mo. l Microbiol , vol.28 , pp. 971-980
    • Bouvier, J.1    Gordia, S.2    Kampmann, G.3    Lange, R.4    Hengge-Aronis, R.5    Gutierrez, C.6
  • 14
    • 25444441531 scopus 로고    scopus 로고
    • The individual and common repertoire of DNA-binding transcriptional regulators of Corynebacterium glutamicum, Corynebacterium efficiens, Corynebacterium diphtheriae and Corynebacterium jeikeium deduced from the complete genome sequences
    • Brune, I., Brinkrolf, K., Kalinowski, J., Puhler, A., and Tauch, A., 2005, The individual and common repertoire of DNA-binding transcriptional regulators of Corynebacterium glutamicum, Corynebacterium efficiens, Corynebacterium diphtheriae and Corynebacterium jeikeium deduced from the complete genome sequences. BMC Genomics 6: 86.
    • (2005) BMC Genomics , vol.6
    • Brune, I.1    Brinkrolf, K.2    Kalinowski, J.3    Puhler, A.4    Tauch, A.5
  • 15
    • 0034648827 scopus 로고    scopus 로고
    • Peroxynitrite reductase activity of bacterial peroxiredoxins
    • Bryk, R., Griffin, P., and Nathan, C., 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
  • 16
    • 0037039818 scopus 로고    scopus 로고
    • Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein
    • Bryk, R., Lima, C. D., Erdjument-Bromage, H., Tempst, P., and Nathan, C., 2002, Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein. Science 295: 1073-1077.
    • (2002) Science , vol.295 , pp. 1073-1077
    • Bryk, R.1    Lima, C.D.2    Erdjument-Bromage, H.3    Tempst, P.4    Nathan, C.5
  • 17
    • 0029854169 scopus 로고    scopus 로고
    • Mutation of the Bacillus subtilis alkyl hydroperoxide reductase (ahpCF) operon reveals compensatory interactions among hydrogen peroxide stress genes
    • Bsat, N., Chen, L., and Helmann, J. D., 1996, Mutation of the Bacillus subtilis alkyl hydroperoxide reductase (ahpCF) operon reveals compensatory interactions among hydrogen peroxide stress genes. J. Bacteriol. 178: 6579-6586.
    • (1996) J. Bacteriol , vol.178 , pp. 6579-6586
    • Bsat, N.1    Chen, L.2    Helmann, J.D.3
  • 18
    • 0031850630 scopus 로고    scopus 로고
    • Bacillus subtilis contains multiple Fur homologues: Identification of the iron uptake (Fur) and peroxide regulon (PerR) repressors
    • Bsat, N., Herbig, A. F., Cassillas-Martinez, L., Setlow, P., and Helmann, J. D., 1998, Bacillus subtilis contains multiple Fur homologues: identification of the iron uptake (Fur) and peroxide regulon (PerR) repressors. Mol. Microbiol. 29: 189-198.
    • (1998) Mol. Microbiol , vol.29 , pp. 189-198
    • Bsat, N.1    Herbig, A.F.2    Cassillas-Martinez, L.3    Setlow, P.4    Helmann, J.D.5
  • 19
    • 0028845858 scopus 로고
    • Thioredoxin-linked "thiol peroxidase" from periplasmic space of
    • Cha, M.-K., Kim, H.-K., and Kim, I.-H., 1995, Thioredoxin-linked "thiol peroxidase" from periplasmic space of Escherichia coli. J. Biol. Chem. 270: 28635-28641.
    • (1995) Escherichia coli. J. Biol. Chem , vol.270 , pp. 28635-28641
    • Cha, M.-K.1    Kim, H.-K.2    Kim, I.-H.3
  • 20
    • 0029839215 scopus 로고    scopus 로고
    • Mutation and Mutagenesis of thiol peroxidase of Escherichia coli and a new type of thiol peroxidase family
    • Cha, M.-K., Kim, H.-K., and Kim, I.-H., 1996, Mutation and Mutagenesis of thiol peroxidase of Escherichia coli and a new type of thiol peroxidase family. J. Bacteriol. 178: 5610-5614.
    • (1996) J. Bacteriol , vol.178 , pp. 5610-5614
    • Cha, M.-K.1    Kim, H.-K.2    Kim, I.-H.3
  • 21
    • 1542335652 scopus 로고    scopus 로고
    • Escherichia coli periplasmic thiol peroxidase acts as lipid hydroperoxide peroxidase and the principal antioxidative function during anaerobic growth
    • Cha, M.-K., Kim, W.-C., Lim, C.-J., Kim, K., and Kim, I.-H., 2004, Escherichia coli periplasmic thiol peroxidase acts as lipid hydroperoxide peroxidase and the principal antioxidative function during anaerobic growth. J. Biol. Chem. 279: 8769-8778.
    • (2004) J. Biol. Chem , vol.279 , pp. 8769-8778
    • Cha, M.-K.1    Kim, W.-C.2    Lim, C.-J.3    Kim, K.4    Kim, I.-H.5
  • 22
    • 0028226006 scopus 로고
    • Cloning and sequencing of thiol-specific antioxidant from mammalian brain: Alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes
    • Chae, H. Z., Robison, K., Poole, L. B., Church, G., Storz, G., and Rhee, S. G., 1994, Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes. Pro. c Nat. l Acad. Sci. USA 91: 7017-7021.
    • (1994) Pro. c Nat. l Acad. Sci. USA , vol.91 , pp. 7017-7021
    • Chae, H.Z.1    Robison, K.2    Poole, L.B.3    Church, G.4    Storz, G.5    Rhee, S.G.6
  • 23
    • 22144475073 scopus 로고    scopus 로고
    • OxyR mediated compensatory expression between ahpC and katA and the significance of ahpC in protection from hydrogen peroxide in Xanthomonas campestris
    • Charoenlap, N., Eiamphungporn, W., Nopmanee, C., Utamapongchai, S., Vattanaviboon, P., and Mongkolsuk, S., 2005, OxyR mediated compensatory expression between ahpC and katA and the significance of ahpC in protection from hydrogen peroxide in Xanthomonas campestris. FEMS Microbiol. Let. t 249: 73-78.
    • (2005) FEMS Microbiol. Let. t , vol.249 , pp. 73-78
    • Charoenlap, N.1    Eiamphungporn, W.2    Nopmanee, C.3    Utamapongchai, S.4    Vattanaviboon, P.5    Mongkolsuk, S.6
  • 24
    • 0029152774 scopus 로고
    • Coordinate regulation of Bacillus subtilis peroxide stress genes by hydrogen peroxide and metal ions
    • Chen, L., Keramati, L., and Helmann, J. D., 1995, Coordinate regulation of Bacillus subtilis peroxide stress genes by hydrogen peroxide and metal ions. Proc. Natl. Acad. Sci. USA 92: 8190-8194.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8190-8194
    • Chen, L.1    Keramati, L.2    Helmann, J.D.3
  • 25
    • 0032060482 scopus 로고    scopus 로고
    • Alkyl hydroperoxide reductase subunit C (AhpC) protects bacterial and human cells against reactive nitrogen intermediates
    • Chen, L., Xie, Q.-W., and Nathan, C., 1998, Alkyl hydroperoxide reductase subunit C (AhpC) protects bacterial and human cells against reactive nitrogen intermediates. Mol. Cell. 1: 795-805.
    • (1998) Mol. Cell , vol.1 , pp. 795-805
    • Chen, L.1    Xie, Q.-W.2    Nathan, C.3
  • 26
    • 1542272169 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli thiol peroxidase in the oxidized state: Insights into intramolecular disulfide formation and substrate binding in atypical 2-Cys peroxiredoxins
    • Choi, J., Choi, S., Choi, J., Cha, M.-K., Kim, I.-H., and Shin, W., 2003, Crystal structure of Escherichia coli thiol peroxidase in the oxidized state: insights into intramolecular disulfide formation and substrate binding in atypical 2-Cys peroxiredoxins. J. Biol. Chem. 278: 49478-49486.
    • (2003) J. Biol. Chem , vol.278 , pp. 49478-49486
    • Choi, J.1    Choi, S.2    Choi, J.3    Cha, M.-K.4    Kim, I.-H.5    Shin, W.6
  • 27
    • 0021930684 scopus 로고
    • Positive control of a regulon for defenses against oxidative stress and some heat-shock proteins in Salmonella typhimurium
    • Christman, M. F., Morgan, R. W., Jacobson, F. S., and Ames, B. M., 1985, Positive control of a regulon for defenses against oxidative stress and some heat-shock proteins in Salmonella typhimurium. Cell 41: 753-762.
    • (1985) Cell , vol.41 , pp. 753-762
    • Christman, M.F.1    Morgan, R.W.2    Jacobson, F.S.3    Ames, B.M.4
  • 28
    • 33644559039 scopus 로고    scopus 로고
    • The antioxidant protein alkylhydroperoxide reductase of Helicobacter pylori switches from a peroxide reductase to a molecular chaperone function
    • Chuang, M.-H., Wu, M.-S., Lo, W.-L., Jaw-Town, L., Wong, C.-H., and Chiou, S.-H., 2006, The antioxidant protein alkylhydroperoxide reductase of Helicobacter pylori switches from a peroxide reductase to a molecular chaperone function. Proc. Natl. Acad. Sci. USA 103: 2552-2557.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 2552-2557
    • Chuang, M.-H.1    Wu, M.-S.2    Lo, W.-L.3    Jaw-Town, L.4    Wong, C.-H.5    Chiou, S.-H.6
  • 29
    • 31344471227 scopus 로고    scopus 로고
    • ohrR and ohr are the primary sensor/regulator and protective genes against organic hydroperoxide stress in Agrobacterium tumefaciens
    • Chuchue, T., Tanboon, W., Prapagdee, B., Dubbs, J. M., Vattanaviboon, P., and Mongkolsuk, S., 2006, ohrR and ohr are the primary sensor/regulator and protective genes against organic hydroperoxide stress in Agrobacterium tumefaciens. J. Bacteriol. 188: 842-851.
    • (2006) J. Bacteriol , vol.188 , pp. 842-851
    • Chuchue, T.1    Tanboon, W.2    Prapagdee, B.3    Dubbs, J.M.4    Vattanaviboon, P.5    Mongkolsuk, S.6
  • 30
    • 0037258943 scopus 로고    scopus 로고
    • Role of the thioredoxin system and the thiolperoxidases Tpx and Bcp in mediating resistance to oxidative and nitrosative stress in Helicobacter pylori
    • Comtois, S. L., Gidley, M. D., and Kelly, D. J., 2003, Role of the thioredoxin system and the thiolperoxidases Tpx and Bcp in mediating resistance to oxidative and nitrosative stress in Helicobacter pylori. Microbiol. 149: 121-129.
    • (2003) Microbiol , vol.149 , pp. 121-129
    • Comtois, S.L.1    Gidley, M.D.2    Kelly, D.J.3
  • 31
    • 0035118225 scopus 로고    scopus 로고
    • Survival of Escherichia coli during long-term starvation: Effects of aeration, NaCl, and the rpoS and osmC gene products
    • Conter, A., Gagneaux, C., Magali, S., and Gutierrez, C., 2001, Survival of Escherichia coli during long-term starvation: effects of aeration, NaCl, and the rpoS and osmC gene products. Res. Microbiol. 152: 17-26.
    • (2001) Res. Microbiol , vol.152 , pp. 17-26
    • Conter, A.1    Gagneaux, C.2    Magali, S.3    Gutierrez, C.4
  • 32
    • 0036236202 scopus 로고    scopus 로고
    • The RcsCB His-Asp phosphorelay system is essential to overcome chlorpromazine-induced stress in Escherichia coli
    • Conter, A., Sturny, R., Gutierrez, C., and Cam, K., 2002, The RcsCB His-Asp phosphorelay system is essential to overcome chlorpromazine-induced stress in Escherichia coli. J. Bacterio. l 10: 2850-2853.
    • (2002) J. Bacterio. l , vol.10 , pp. 2850-2853
    • Conter, A.1    Sturny, R.2    Gutierrez, C.3    Cam, K.4
  • 33
    • 0037500300 scopus 로고    scopus 로고
    • Organic hydroperoxide resistance gene encodes a thiol-dependent peroxidase
    • Cussiol, J. R. R., Alves, S. V., de Oliviera, M. A., and Netto, L. E. S., 2003, Organic hydroperoxide resistance gene encodes a thiol-dependent peroxidase. J. Biol. Chem. 278: 11570-11578.
    • (2003) J. Biol. Chem , vol.278 , pp. 11570-11578
    • Cussiol, J.R.R.1    Alves, S.V.2    de Oliviera, M.A.3    Netto, L.E.S.4
  • 34
    • 0034805870 scopus 로고    scopus 로고
    • Regulation of osmC gene expression by the two-component system rcsB-rcsC in Escherichia coli
    • Davalos-Garcia, M., Conter, A., Toesca, I., Gutierrez, C., and Cam, K., 2001, Regulation of osmC gene expression by the two-component system rcsB-rcsC in Escherichia coli. J. Bacteriol. 183: 5870-5876.
    • (2001) J. Bacteriol , vol.183 , pp. 5870-5876
    • Davalos-Garcia, M.1    Conter, A.2    Toesca, I.3    Gutierrez, C.4    Cam, K.5
  • 36
    • 0028882958 scopus 로고
    • Mycobacterium tuberculosis is a natural mutant with an inactivated oxidative-stress regulatory gene: Implications for sensitivity to isoniazid
    • Deretic, V., Philipp, W., Dhandayuthapani, S., Mudd, M. H., Curcic, R., Garbe, T. R., Heym, B., Via, L. E., and Cole, S. T., 1995, Mycobacterium tuberculosis is a natural mutant with an inactivated oxidative-stress regulatory gene: implications for sensitivity to isoniazid. Mol. Microbiol. 17: 889-900.
    • (1995) Mol. Microbiol , vol.17 , pp. 889-900
    • Deretic, V.1    Philipp, W.2    Dhandayuthapani, S.3    Mudd, M.H.4    Curcic, R.5    Garbe, T.R.6    Heym, B.7    Via, L.E.8    Cole, S.T.9
  • 37
    • 0030910666 scopus 로고    scopus 로고
    • Interactions of OxyR with the promoter region of the oxyR and ahpC genes from Mycobacterium leprae and
    • Dhandayuthapani, S., Mudd, M. H., and Deretic, V., 1997, Interactions of OxyR with the promoter region of the oxyR and ahpC genes from Mycobacterium leprae and Mycobacterium tuberculosis. J. Bacteriol. 179: 2401-2409.
    • (1997) Mycobacterium tuberculosis. J. Bacteriol , vol.179 , pp. 2401-2409
    • Dhandayuthapani, S.1    Mudd, M.H.2    Deretic, V.3
  • 38
    • 0029888258 scopus 로고    scopus 로고
    • Oxidative stress response and its role in sensitivity to isoniazid in mycobacteria: Characterization and inducibility of ahpC by peroxides in Mycobacterium smegmatis and lack of expression in M. aurum and
    • Dhandayuthapani, S., Zhang, Y., Mudd, M. H., and Deretic, V., 1996, Oxidative stress response and its role in sensitivity to isoniazid in mycobacteria: characterization and inducibility of ahpC by peroxides in Mycobacterium smegmatis and lack of expression in M. aurum and M. tuberculosis. J. Bacteriol. 178: 3641-3649.
    • (1996) M. tuberculosis. J. Bacteriol , vol.178 , pp. 3641-3649
    • Dhandayuthapani, S.1    Zhang, Y.2    Mudd, M.H.3    Deretic, V.4
  • 40
    • 0031081208 scopus 로고    scopus 로고
    • The adc locus, which affects competence for genetic transformation in Streptococcus pneumoniae, encodes an ABC transporter with a putative lipoprotein homologous to a family of streptococcal adhesins
    • Dintilhac, A., and Claverys, J. P., 1997, The adc locus, which affects competence for genetic transformation in Streptococcus pneumoniae, encodes an ABC transporter with a putative lipoprotein homologous to a family of streptococcal adhesins. Res. Microbiol. 148: 119-131.
    • (1997) Res. Microbiol , vol.148 , pp. 119-131
    • Dintilhac, A.1    Claverys, J.P.2
  • 41
    • 0001384280 scopus 로고
    • Cytochrome-independent electron transport enzymes of bacteria
    • (Gunsalus, I.C. and Stanier, R.Y., eds), Academic Press Inc., New York, N.Y., USA
    • Dolin, M. I., 1961, Cytochrome-independent electron transport enzymes of bacteria, in The bacteria Vol. 2 (Gunsalus, I. C. and Stanier, R. Y., eds), Academic Press Inc., New York, N. Y., USA, pp. 425-460.
    • (1961) The bacteria Vol. 2 , pp. 425-460
    • Dolin, M.I.1
  • 42
    • 0034902327 scopus 로고    scopus 로고
    • Role of OxyS of Mycobacterium tuberculosis in oxidative stress: Overexpression confers increased sensitivity to organic hydroperoxides
    • Domenech, P., Honore, N., Heym, B., and Cole, S. T., 2001, Role of OxyS of Mycobacterium tuberculosis in oxidative stress: overexpression confers increased sensitivity to organic hydroperoxides. Microbes. Infect. 3: 713-721.
    • (2001) Microbes. Infect , vol.3 , pp. 713-721
    • Domenech, P.1    Honore, N.2    Heym, B.3    Cole, S.T.4
  • 43
    • 2442560235 scopus 로고    scopus 로고
    • H-NS: A universal regulator for a dynamic genome
    • Dorman, C. J., 2004, H-NS: a universal regulator for a dynamic genome. Nat Rev Microbiol 2: 391-400.
    • (2004) Nat Rev Microbiol , vol.2 , pp. 391-400
    • Dorman, C.J.1
  • 44
    • 33746409023 scopus 로고    scopus 로고
    • Sequence and organization of pMAC, an Acinetobacter baumannii plasmid harboring genes involved in organic peroxide resistance
    • Dorsey, C. W., Tomaras, A. P., and Actis, L. A., 2006, Sequence and organization of pMAC, an Acinetobacter baumannii plasmid harboring genes involved in organic peroxide resistance. Plasmid 56: 112-123.
    • (2006) Plasmid , vol.56 , pp. 112-123
    • Dorsey, C.W.1    Tomaras, A.P.2    Actis, L.A.3
  • 45
  • 46
    • 0030822346 scopus 로고    scopus 로고
    • Roles for the two cysteine residues of AhpC in catalysis of peroxide reduction by alkyl hydroperoxide reductase from
    • Ellis, H. R., and Poole, L. B., 1997, Roles for the two cysteine residues of AhpC in catalysis of peroxide reduction by alkyl hydroperoxide reductase from Salmonella typhimurium. Biochemistry 36: 13349-13356.
    • (1997) Salmonella typhimurium. Biochemistry , vol.36 , pp. 13349-13356
    • Ellis, H.R.1    Poole, L.B.2
  • 47
    • 0026650304 scopus 로고
    • Distinctive western blot antibody patterns induced by infection of mice with individual strains of the Mycobacterium avium complex
    • Elsaghier, A., Nolan, A., Allen, B., and Ivanyi, J., 1992, Distinctive western blot antibody patterns induced by infection of mice with individual strains of the Mycobacterium avium complex. Immunol. 76: 355-361.
    • (1992) Immunol , vol.76 , pp. 355-361
    • Elsaghier, A.1    Nolan, A.2    Allen, B.3    Ivanyi, J.4
  • 50
    • 0027402652 scopus 로고
    • Light emission from a Mudlux transcriptional fusion in Salmonella typhimurium is stimulated by hydrogen peroxide and by interaction with the mouse macrophage cell line J774. 2
    • Francis, K. P., and Gallagher, M. P., 1993, Light emission from a Mudlux transcriptional fusion in Salmonella typhimurium is stimulated by hydrogen peroxide and by interaction with the mouse macrophage cell line J774. 2. Infect. Immun. 61: 640-649.
    • (1993) Infect. Immun , vol.61 , pp. 640-649
    • Francis, K.P.1    Gallagher, M.P.2
  • 51
    • 0030974197 scopus 로고    scopus 로고
    • Identification of the ahp operon of Salmonella typhimurium as a macrophage-induced locus
    • Francis, K. P., Taylor, P. D., Inchley, C. J., and Gallagher, M. P., 1997, Identification of the ahp operon of Salmonella typhimurium as a macrophage-induced locus. J. Bacteriol. 179: 4046-4048.
    • (1997) J. Bacteriol , vol.179 , pp. 4046-4048
    • Francis, K.P.1    Taylor, P.D.2    Inchley, C.J.3    Gallagher, M.P.4
  • 52
    • 0034971954 scopus 로고    scopus 로고
    • OhrR is a repressor of ohrA, a key organic hydroperoxide resistance determinant in Bacillus subtilis
    • Fuangthong, M., Atichartpongkun, S., Mongkolsuk, S., and Helmann, D., 2001, OhrR is a repressor of ohrA, a key organic hydroperoxide resistance determinant in Bacillus subtilis. J. Bacteriol. 183: 4134-4141.
    • (2001) J. Bacteriol , vol.183 , pp. 4134-4141
    • Fuangthong, M.1    Atichartpongkun, S.2    Mongkolsuk, S.3    Helmann, D.4
  • 53
    • 0142214661 scopus 로고    scopus 로고
    • Recognition of DNA by three ferric uptake regulator (Fur) homologs in Bacillus subtilis
    • Fuangthong, M., and Helmann, J. D., 2003, Recognition of DNA by three ferric uptake regulator (Fur) homologs in Bacillus subtilis. J. Bacteriol. 185: 6348-6357.
    • (2003) J. Bacteriol , vol.185 , pp. 6348-6357
    • Fuangthong, M.1    Helmann, J.D.2
  • 54
    • 0037076330 scopus 로고    scopus 로고
    • The OhrR repressor senses organic hydroperoxides by reversible formation of a cysteine-sulfenic acid derivative
    • Fuangthong, M., and Helmann, D., 2002a, The OhrR repressor senses organic hydroperoxides by reversible formation of a cysteine-sulfenic acid derivative. Proc. Natl. Acad. Sci. USA 99: 6690-6695.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 6690-6695
    • Fuangthong, M.1    Helmann, D.2
  • 55
    • 0036267391 scopus 로고    scopus 로고
    • Regulation of the Bacillus subtilis fur and perR genes by PerR: Not all members of the PerR regulon are peroxide inducible
    • Fuangthong, M., Herbig, A. F., Bsat, N., and Helmann, D., 2002b, Regulation of the Bacillus subtilis fur and perR genes by PerR: not all members of the PerR regulon are peroxide inducible. J. Bacterio. l 184: 3276-3286.
    • (2002) J. Bacterio. l , vol.184 , pp. 3276-3286
    • Fuangthong, M.1    Herbig, A.F.2    Bsat, N.3    Helmann, D.4
  • 56
    • 0035719919 scopus 로고    scopus 로고
    • Molecular cloning and transcriptional analysis of the alkyl hydroperoxide reductase genes from Pseudomonas putida KT2442
    • Fukumori, F., and Kishii, M., 2001, Molecular cloning and transcriptional analysis of the alkyl hydroperoxide reductase genes from Pseudomonas putida KT2442. J. Gen. Appl. Microbiol. 47: 269-277.
    • (2001) J. Gen. Appl. Microbiol , vol.47 , pp. 269-277
    • Fukumori, F.1    Kishii, M.2
  • 57
    • 29644439241 scopus 로고    scopus 로고
    • Iron and pH homeostasis intersect at the level of Fur regulation in the gastric pathogen
    • Gancz, H., Censini, S., and Merrell, D. S., 2006, Iron and pH homeostasis intersect at the level of Fur regulation in the gastric pathogen Helicobacter pylori. Infect. Immun. 74: 602-614.
    • (2006) Helicobacter pylori. Infect. Immun , vol.74 , pp. 602-614
    • Gancz, H.1    Censini, S.2    Merrell, D.S.3
  • 58
    • 0025976447 scopus 로고
    • Nucleotide sequence of a gene coding for a saliva-binding protein (SsaB) from Streptococcus sanguis 12 and possible role of the protein in coaggregation with actinomyces
    • Ganeshkumar, N., Hannam, P. M., Kolenbrander, P. E., and McBride, B. C., 1991, Nucleotide sequence of a gene coding for a saliva-binding protein (SsaB) from Streptococcus sanguis 12 and possible role of the protein in coaggregation with actinomyces. Infect. Immun. 59: 1093-1099.
    • (1991) Infect. Immun , vol.59 , pp. 1093-1099
    • Ganeshkumar, N.1    Hannam, P.M.2    Kolenbrander, P.E.3    McBride, B.C.4
  • 59
    • 0033978494 scopus 로고    scopus 로고
    • Indole-inducible proteins in bacteria suggest membrane and oxidant toxicity
    • Garbe, T. R., Kobayashi, M., and Yukawa, H., 2000, Indole-inducible proteins in bacteria suggest membrane and oxidant toxicity. Arch. Microbiol. 173: 78-82.
    • (2000) Arch. Microbiol , vol.173 , pp. 78-82
    • Garbe, T.R.1    Kobayashi, M.2    Yukawa, H.3
  • 60
    • 0030050577 scopus 로고    scopus 로고
    • Growth-phase-dependent expression of the osmotically inducible gene osmC of Escherichia coli K-12
    • Gordia, S., and Gutierrez, C., 1996, Growth-phase-dependent expression of the osmotically inducible gene osmC of Escherichia coli K-12. Mol. Microbiol. 19: 729-736.
    • (1996) Mol. Microbiol , vol.19 , pp. 729-736
    • Gordia, S.1    Gutierrez, C.2
  • 61
    • 0024064790 scopus 로고
    • Overproduction of peroxide-scavenging enzymes in Escherichia coli suppresses spontaneous mutagenesis and sensitivity to redox-cycling agents in oxyR-mutants
    • Greenberg, J. T., and Demple, B., 1988, Overproduction of peroxide-scavenging enzymes in Escherichia coli suppresses spontaneous mutagenesis and sensitivity to redox-cycling agents in oxyR-mutants. EMBO J. 7: 2611-2617.
    • (1988) EMBO J , vol.7 , pp. 2611-2617
    • Greenberg, J.T.1    Demple, B.2
  • 62
    • 0023274450 scopus 로고
    • The use of transposon TnphoA to detect genes for cell envelope proteins subject to a common regulatory stimulus. Analysis of osmotically regulated genes in Escherichia coli
    • Gutierrez, C., Barondess, J., Manoil, C., and Beckwith, J., 1987, The use of transposon TnphoA to detect genes for cell envelope proteins subject to a common regulatory stimulus. Analysis of osmotically regulated genes in Escherichia coli. J. Mol. Biol. 195: 289-297.
    • (1987) J. Mol. Biol , vol.195 , pp. 289-297
    • Gutierrez, C.1    Barondess, J.2    Manoil, C.3    Beckwith, J.4
  • 63
    • 0025812628 scopus 로고
    • Osmotic induction of gene osmC expression in Escherichia coli K12
    • Gutierrez, C., and Devedjian, J. C., 1991, Osmotic induction of gene osmC expression in Escherichia coli K12. J. Mol. Biol. 220: 959-973.
    • (1991) J. Mol. Biol , vol.220 , pp. 959-973
    • Gutierrez, C.1    Devedjian, J.C.2
  • 64
    • 0036778158 scopus 로고    scopus 로고
    • Role of OxyR as a peroxide-sensing positive regulator in Streptomyces coelicolor A3(2)
    • Hahn, J.-S., Oh, S.-Y., and Roe, J.-H., 2002, Role of OxyR as a peroxide-sensing positive regulator in Streptomyces coelicolor A3(2). J. Bacteriol. 184: 5214-5222.
    • (2002) J. Bacteriol , vol.184 , pp. 5214-5222
    • Hahn, J.-S.1    Oh, S.-Y.2    Roe, J.-H.3
  • 65
    • 0021351203 scopus 로고
    • Oxygen toxicity, oxygen radicals, transition metals and disease
    • Halliwell, B., and Gutteridge, J. M. C., 1984, Oxygen toxicity, oxygen radicals, transition metals and disease. Biochem. J. 219: 1-14.
    • (1984) Biochem. J , vol.219 , pp. 1-14
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 66
    • 0030572708 scopus 로고    scopus 로고
    • Nitrosative stress: Activation of the transcription factor OxyR
    • Hausladen, A., Privalle, C. T., Keng, T., De Angelo, J., and Stamler, J. S., 1996, Nitrosative stress: activation of the transcription factor OxyR. Cell 86: 719-29.
    • (1996) Cell , vol.86 , pp. 719-729
    • Hausladen, A.1    Privalle, C.T.2    Keng, T.3    De Angelo, J.4    Stamler, J.S.5
  • 67
    • 0034987011 scopus 로고    scopus 로고
    • General stress response of Bacillus subtilis and other bacteria
    • Hecker, M., and Volker, A., 2001, General stress response of Bacillus subtilis and other bacteria. Adv. Microb. Physiol. 44: 35-91.
    • (2001) Adv. Microb. Physiol , vol.44 , pp. 35-91
    • Hecker, M.1    Volker, A.2
  • 68
    • 0037027342 scopus 로고    scopus 로고
    • OxyR: A molecular code for redox sensing
    • Helmann, J. D. (2002). OxyR: A molecular code for redox sensing. Sci STKE 157: PE46.
    • (2002) Sci STKE , vol.157
    • Helmann, J.D.1
  • 69
    • 0037215627 scopus 로고    scopus 로고
    • The global transcriptional response of Bacillus subtilis to peroxide stress is coordinated by three transcription factors
    • Helmann, J. D., Wu, M., Fang, Winston, Gaballa, A., Kobel, P. A., Morshedi, M. M., Fawcett, P., and Paddon, C., 2003, The global transcriptional response of Bacillus subtilis to peroxide stress is coordinated by three transcription factors. J. Bacteriol. 185: 243-253.
    • (2003) J. Bacteriol , vol.185 , pp. 243-253
    • Helmann, J.D.1    Wu, M.2    Fang Winston Gaballa, A.3    Kobel, P.A.4    Morshedi, M.M.5    Fawcett, P.6    Paddon, C.7
  • 71
    • 0035723780 scopus 로고    scopus 로고
    • Roles of metal ions and hydrogen peroxide in modulating the interaction of the Bacillus subtilis PerR peroxide regulon repressor with operator DNA
    • Herbig, A. F., and Helmann, J. D., 2001, Roles of metal ions and hydrogen peroxide in modulating the interaction of the Bacillus subtilis PerR peroxide regulon repressor with operator DNA. Mol. Microbiol. 41: 849-859.
    • (2001) Mol. Microbiol , vol.41 , pp. 849-859
    • Herbig, A.F.1    Helmann, J.D.2
  • 72
    • 0034319185 scopus 로고    scopus 로고
    • Molecular biology of oxygen tolerance in lactic acid bacteria: Functions of NADH oxidases and Dpr in oxidative stress
    • Higuchi, M., Yamamoto, Y., and Kamio, Y., 2000, Molecular biology of oxygen tolerance in lactic acid bacteria: Functions of NADH oxidases and Dpr in oxidative stress. J. Biosci. Bioeng. 90: 484-493.
    • (2000) J. Biosci. Bioeng , vol.90 , pp. 484-493
    • Higuchi, M.1    Yamamoto, Y.2    Kamio, Y.3
  • 75
    • 33645088173 scopus 로고    scopus 로고
    • Salt stress adaptation of Bacillus subtilis: A physiological proteomics approach
    • Hoper, D., Bernhardt, J., and Hecker, M., 2006, Salt stress adaptation of Bacillus subtilis: a physiological proteomics approach. Proteomics 6: 1550-62.
    • (2006) Proteomics , vol.6 , pp. 1550-1562
    • Hoper, D.1    Bernhardt, J.2    Hecker, M.3
  • 76
    • 0035013928 scopus 로고    scopus 로고
    • PerR controls oxidative stress resistance and iron storage proteins and is required for virulence in Staphylococcus aureus
    • Horsburgh, M. J., Clements, M. O., Crossley, H., Ingham, E., and Foster, S. J., 2001, PerR controls oxidative stress resistance and iron storage proteins and is required for virulence in Staphylococcus aureus. Infect. Immun. 69: 3744-3754.
    • (2001) Infect. Immun , vol.69 , pp. 3744-3754
    • Horsburgh, M.J.1    Clements, M.O.2    Crossley, H.3    Ingham, E.4    Foster, S.J.5
  • 77
    • 0242608621 scopus 로고    scopus 로고
    • Pathways of oxidative damage
    • Imlay, J. A., 2003, Pathways of oxidative damage. Annu. Rev. Microbiol. 57: 395-418.
    • (2003) Annu. Rev. Microbiol , vol.57 , pp. 395-418
    • Imlay, J.A.1
  • 78
    • 0024604234 scopus 로고
    • An alkyl hydroperoxide reductase induced by oxidative stress in Salmonella typhimurium and Escherichia coli: Genetic characterization and cloning of ahp
    • Jacobson, F. S., Morgan, R. W., Christman, M. F., and Ames, B. M., 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
    • Jacobson, F.S.1    Morgan, R.W.2    Christman, M.F.3    Ames, B.M.4
  • 79
    • 1042278885 scopus 로고    scopus 로고
    • Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis
    • Jaeger, T., Budde, H., Flohé, L., Menge, U., Singh, M., Trujillo, M., and Radi, R., 2004, Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis. Arch. Biochem. Biophy. s 423: 182-191.
    • (2004) Arch. Biochem. Biophy. s , vol.423 , pp. 182-191
    • Jaeger, T.1    Budde, H.2    Flohé, L.3    Menge, U.4    Singh, M.5    Trujillo, M.6    Radi, R.7
  • 80
    • 0036773537 scopus 로고    scopus 로고
    • Oxidative stress tolerance is manganese Mn2+ regulated in Streptococcus gordonii
    • Jakubovics, N. S., Smith, A. W., and Jenkinson, H. F., 2002, Oxidative stress tolerance is manganese Mn2+ regulated in Streptococcus gordonii. Microbiol. 148: 3255-3263.
    • (2002) Microbiol , vol.148 , pp. 3255-3263
    • Jakubovics, N.S.1    Smith, A.W.2    Jenkinson, H.F.3
  • 81
    • 3142663916 scopus 로고    scopus 로고
    • Alkyl hydroperoxide peroxidase subunit C (ahpC) protects against organic peroxides but does not affect the virulence of Porphyromonas gingivalis W83
    • Johnson, N. A., Liu, Y., and Fletcher, H. M., 2004, Alkyl hydroperoxide peroxidase subunit C (ahpC) protects against organic peroxides but does not affect the virulence of Porphyromonas gingivalis W83. Oral Microbiol. Immunol. 19: 233-239.
    • (2004) Oral Microbiol. Immunol , vol.19 , pp. 233-239
    • Johnson, N.A.1    Liu, Y.2    Fletcher, H.M.3
  • 83
    • 0034519875 scopus 로고    scopus 로고
    • NADPH oxidase, Nramp1 and nitric oxide synthase 2 in the host antimicrobial response
    • Karupiah, G., Hunt, N. H., King, N. J., and Chaudhri, G., 2000, NADPH oxidase, Nramp1 and nitric oxide synthase 2 in the host antimicrobial response. Rev. Immunogenet. 2: 387-415.
    • (2000) Rev. Immunogenet , vol.2 , pp. 387-415
    • Karupiah, G.1    Hunt, N.H.2    King, N.J.3    Chaudhri, G.4
  • 85
  • 86
    • 17644426975 scopus 로고    scopus 로고
    • Novel roles of ohrR-ohr in Xanthomonas sensing, metabolism, and physiological adaptive response to lipid hydroperoxide
    • Klomsiri, C., Panmanee, W., Dharmsthiti, S., Vattanaviboon, P., and Mongkolsuk, S., 2005, Novel roles of ohrR-ohr in Xanthomonas sensing, metabolism, and physiological adaptive response to lipid hydroperoxide. J. Bacteriol. 187: 3277-3281.
    • (2005) J. Bacteriol , vol.187 , pp. 3277-3281
    • Klomsiri, C.1    Panmanee, W.2    Dharmsthiti, S.3    Vattanaviboon, P.4    Mongkolsuk, S.5
  • 87
    • 0031887789 scopus 로고    scopus 로고
    • The adhesion-associated sca operon in Streptococcus gordonii encodes an inducible high-affinity ABC transporter for Mn2+ uptake
    • Kolenbrander, P. E., Andersen, R. N., Baker, R. A., and Jenkinson, H. F., 1998, The adhesion-associated sca operon in Streptococcus gordonii encodes an inducible high-affinity ABC transporter for Mn2+ uptake. J. Bacteriol. 180: 290-295.
    • (1998) J. Bacteriol , vol.180 , pp. 290-295
    • Kolenbrander, P.E.1    Andersen, R.N.2    Baker, R.A.3    Jenkinson, H.F.4
  • 88
    • 0041358749 scopus 로고    scopus 로고
    • Use of proteomics and physiological characteristics to elucidate ecotoxic effects of methyl tert-butyl ether in Pseudomonas putida KT2440
    • Krayl, M., Benndorf, D., Loffhagen, N., and Babel, W., 2003, Use of proteomics and physiological characteristics to elucidate ecotoxic effects of methyl tert-butyl ether in Pseudomonas putida KT2440. Proteomics 3: 1544-1552.
    • (2003) Proteomics , vol.3 , pp. 1544-1552
    • Krayl, M.1    Benndorf, D.2    Loffhagen, N.3    Babel, W.4
  • 89
    • 0028965108 scopus 로고
    • Mutational analysis of the redoxsensitive transcriptional regulator OxyR: Regions important for oxidation and transcriptional activation
    • Kullik, I., Toledano, M. B., Tartaglia, L. A., and Storz, G., 1995, Mutational analysis of the redoxsensitive transcriptional regulator OxyR: regions important for oxidation and transcriptional activation. J. Bacteriol. 177: 1285-1291.
    • (1995) J. Bacteriol , vol.177 , pp. 1285-1291
    • Kullik, I.1    Toledano, M.B.2    Tartaglia, L.A.3    Storz, G.4
  • 91
    • 0038182632 scopus 로고    scopus 로고
    • Comparison between NaCl tolerance response and acclimation to cold temperature in Shewanella putrefaciens
    • Leblanc, L., Leboeuf, C., Leroi, F., Hartke, A., and Yanick, A., 2003, Comparison between NaCl tolerance response and acclimation to cold temperature in Shewanella putrefaciens. Curr. Microbiol. 46: 157-167.
    • (2003) Curr. Microbiol , vol.46 , pp. 157-167
    • Leblanc, L.1    Leboeuf, C.2    Leroi, F.3    Hartke, A.4    Yanick, A.5
  • 93
    • 33645037891 scopus 로고    scopus 로고
    • The PerR transcription factor senses H2O2 by metal-catalysed histidine oxidation
    • Lee, J.-W., and Helmann, J. D., 2006, The PerR transcription factor senses H2O2 by metal-catalysed histidine oxidation. Nature 440: 363-367.
    • (2006) Nature , vol.440 , pp. 363-367
    • Lee, J.-W.1    Helmann, J.D.2
  • 94
    • 12244252764 scopus 로고    scopus 로고
    • Structural and functional characterization of the Pseudomonas hydroperoxide resistance protein Ohr
    • Lesniak, J., Barton, W. A., and Nikolov, D. B., 2002, Structural and functional characterization of the Pseudomonas hydroperoxide resistance protein Ohr. EMBO J. 21: 6649-6659.
    • (2002) EMBO J , vol.21 , pp. 6649-6659
    • Lesniak, J.1    Barton, W.A.2    Nikolov, D.B.3
  • 95
    • 0345708209 scopus 로고    scopus 로고
    • Structural and functional features of the Escherichia coli hydroperoxide resistance protein OsmC
    • Lesniak, J., Barton, W. A., and Nikolov, D. B., 2003, Structural and functional features of the Escherichia coli hydroperoxide resistance protein OsmC. Protein Sci. 12: 2838-2843.
    • (2003) Protein Sci , vol.12 , pp. 2838-2843
    • Lesniak, J.1    Barton, W.A.2    Nikolov, D.B.3
  • 96
    • 0035852735 scopus 로고    scopus 로고
    • Induction of oxyradicals by arsenic: Implication for mechanism of genotoxicity
    • Liu, S. X., Athar, M., Lippai, I., Waldren, C., and Hei, T. K., 2001, Induction of oxyradicals by arsenic: implication for mechanism of genotoxicity. Proc. Natl. Acad. Sci. USA 98: 1643-1648.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 1643-1648
    • Liu, S.X.1    Athar, M.2    Lippai, I.3    Waldren, C.4    Hei, T.K.5
  • 97
    • 10044259795 scopus 로고    scopus 로고
    • Role of a nosX homolog in Streptococcus gordonii in aerobic growth and biofilm formation
    • Loo, C. Y., Mitrakul, K., Jaafar, S., Gyurko, C., Hughes, C. V., and Ganeshkumar, N., 2004, Role of a nosX homolog in Streptococcus gordonii in aerobic growth and biofilm formation. J. Bacteriol. 186: 8183-8206.
    • (2004) J. Bacteriol , vol.186 , pp. 8183-8206
    • Loo, C.Y.1    Mitrakul, K.2    Jaafar, S.3    Gyurko, C.4    Hughes, C.V.5    Ganeshkumar, N.6
  • 98
    • 0031008472 scopus 로고    scopus 로고
    • Isolation and analysis of the Xanthomonas alkyl hydroperoxide reductase and the peroxide sensor regulator genes ahpC and ahpF-oxyR-orfX
    • Loprasert, S., Artichartpongkun, S., Whangsuk, W., and Mongkolsuk, S., 1997, Isolation and analysis of the Xanthomonas alkyl hydroperoxide reductase and the peroxide sensor regulator genes ahpC and ahpF-oxyR-orfX. J. Bacteriol. 179: 3944-3949.
    • (1997) J. Bacteriol , vol.179 , pp. 3944-3949
    • Loprasert, S.1    Artichartpongkun, S.2    Whangsuk, W.3    Mongkolsuk, S.4
  • 99
    • 0033774725 scopus 로고    scopus 로고
    • Molecular and physiological analysis of an OxyR-regulated ahpC promoter in Xanthomonas campestris pv. phaseoli
    • Loprasert, S., Fuangthong, M., Whangsuk, W., Atichartpongkun, S., and Mongkolsuk, S., 2000, Molecular and physiological analysis of an OxyR-regulated ahpC promoter in Xanthomonas campestris pv. phaseoli. Mol. Microbiol. 37: 1504-1514.
    • (2000) Mol. Microbiol , vol.37 , pp. 1504-1514
    • Loprasert, S.1    Fuangthong, M.2    Whangsuk, W.3    Atichartpongkun, S.4    Mongkolsuk, S.5
  • 100
    • 0346364903 scopus 로고    scopus 로고
    • Compensatory increase in ahpC gene expression and its role in protecting Burkholderia pseudomallei against reactive nitrogen intermediates
    • Loprasert, S., Sallabhan, R., Whangsuk, W., and Mongkolsuk, S., 2003, Compensatory increase in ahpC gene expression and its role in protecting Burkholderia pseudomallei against reactive nitrogen intermediates. Arch. Microbiol. 180: 498-502.
    • (2003) Arch. Microbiol , vol.180 , pp. 498-502
    • Loprasert, S.1    Sallabhan, R.2    Whangsuk, W.3    Mongkolsuk, S.4
  • 101
    • 4544379505 scopus 로고    scopus 로고
    • DpsA protects the human pathogen Burkholderia pseudomallei against organic hydroperoxide
    • Loprasert, S., Whangsuk, W., Sallabhan, R., and Mongkolsuk, S., 2004, DpsA protects the human pathogen Burkholderia pseudomallei against organic hydroperoxide. Arch. Microbio. l 182: 96-101.
    • (2004) Arch. Microbio. l , vol.182 , pp. 96-101
    • Loprasert, S.1    Whangsuk, W.2    Sallabhan, R.3    Mongkolsuk, S.4
  • 102
    • 0033679155 scopus 로고    scopus 로고
    • A 26 kDa protein of Helicobacter pylori shows alkyl hydroperoxide reductase (AhpC) activity and the mono-cistronic transcription of the gene is affected by pH
    • Lundström, A. M., and Bolin, I., 2000, A 26 kDa protein of Helicobacter pylori shows alkyl hydroperoxide reductase (AhpC) activity and the mono-cistronic transcription of the gene is affected by pH. Microb. Patho. g 29: 257-266.
    • (2000) Microb. Patho. g , vol.29 , pp. 257-266
    • Lundström, A.M.1    Bolin, I.2
  • 103
    • 0034961878 scopus 로고    scopus 로고
    • The 26-kilodalton, AhpC homologue, of Helicobacter pylori is also produced by other Helicobacter species
    • Lundström, A. M., Sundaeus, V., and Bolin, I., 2001, The 26-kilodalton, AhpC homologue, of Helicobacter pylori is also produced by other Helicobacter species. Helicobacter 6: 44-54.
    • (2001) Helicobacter , vol.6 , pp. 44-54
    • Lundström, A.M.1    Sundaeus, V.2    Bolin, I.3
  • 104
    • 33645109891 scopus 로고    scopus 로고
    • The impairment of superoxide dismutase coordinates the derepression of the PerR regulon in the response of Staphylococcus aureus to HOCl stress
    • Maalej, S., Dammak, I., and Dukan, S., 2006, The impairment of superoxide dismutase coordinates the derepression of the PerR regulon in the response of Staphylococcus aureus to HOCl stress. Microbiol. 152: 855-861.
    • (2006) Microbiol , vol.152 , pp. 855-861
    • Maalej, S.1    Dammak, I.2    Dukan, S.3
  • 105
    • 25144451503 scopus 로고    scopus 로고
    • The Rcs phosphorelay: A complex signal transduction system
    • Majdalani, N., and Gottesman, S., 2005, The Rcs phosphorelay: a complex signal transduction system. Ann. Rev. Microbiol. 59: 379-405.
    • (2005) Ann. Rev. Microbiol , vol.59 , pp. 379-405
    • Majdalani, N.1    Gottesman, S.2
  • 106
    • 0032944213 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis catalase and peroxidase activities and resistance to oxidative killing in human monocytes in vitro
    • Manca, C., Paul, S., Barry, C. E. I., Freedman, V. H., and Kaplan, G., 1999, Mycobacterium tuberculosis catalase and peroxidase activities and resistance to oxidative killing in human monocytes in vitro. Infect. Immun. 67: 74-79.
    • (1999) Infect. Immun , vol.67 , pp. 74-79
    • Manca, C.1    Paul, S.2    Barry, C.E.I.3    Freedman, V.H.4    Kaplan, G.5
  • 107
    • 0032844704 scopus 로고    scopus 로고
    • Bactericidal activity of photocatalytic TiO(2) reaction: Toward an understanding of its killing mechanism
    • Maness, P.-C., Smolinski, S., Blake, D. M., Huang, Z., Wolfrum, E. J., and Jacoby, W. A., 1999, Bactericidal activity of photocatalytic TiO(2) reaction: toward an understanding of its killing mechanism. Appl. Environ. Microbiol. 65: 4094-4098.
    • (1999) Appl. Environ. Microbiol , vol.65 , pp. 4094-4098
    • Maness, P.-C.1    Smolinski, S.2    Blake, D.M.3    Huang, Z.4    Wolfrum, E.J.5    Jacoby, W.A.6
  • 108
    • 0036772990 scopus 로고    scopus 로고
    • Oxidative stress response genes in Mycobacterium tuberculosis: Role of ahpC in resistance to peroxynitrite and stage-specific survival in macrophages
    • Master, S. S., Springer, B., Sander, P., Boettger, E. C., Deretic, V., and Timmins, G. S., 2002, Oxidative stress response genes in Mycobacterium tuberculosis: role of ahpC in resistance to peroxynitrite and stage-specific survival in macrophages. Microbiol. 148: 3139-3144.
    • (2002) Microbiol , vol.148 , pp. 3139-3144
    • Master, S.S.1    Springer, B.2    Sander, P.3    Boettger, E.C.4    Deretic, V.5    Timmins, G.S.6
  • 109
    • 2942588414 scopus 로고    scopus 로고
    • The structure of the organic hydroperoxide resistance protein from Deinococcus radiodurans. Do conformational changes facilitate recycling of the redox disulfide
    • Meunier-Jamin, C., Kapp, U., Leonard, G. A., and McSweeney, S., 2004, The structure of the organic hydroperoxide resistance protein from Deinococcus radiodurans. Do conformational changes facilitate recycling of the redox disulfide. J. Biol. Chem. 279: 25830-25837.
    • (2004) J. Biol. Chem , vol.279 , pp. 25830-25837
    • Meunier-Jamin, C.1    Kapp, U.2    Leonard, G.A.3    McSweeney, S.4
  • 110
    • 0032943524 scopus 로고    scopus 로고
    • In vivo transcription of the Escherichia coli oxyR regulon as a function of growth phase and in response to oxidative stress
    • Michan, C., Manchado, M., Dorado, G., and Pueyo, C., 1999, In vivo transcription of the Escherichia coli oxyR regulon as a function of growth phase and in response to oxidative stress. J. Bacteriol. 181: 2759-2764.
    • (1999) J. Bacteriol , vol.181 , pp. 2759-2764
    • Michan, C.1    Manchado, M.2    Dorado, G.3    Pueyo, C.4
  • 111
    • 0036047508 scopus 로고    scopus 로고
    • Regulation of inducible peroxide stress responses
    • Mongkolsuk, S., and Helmann, J., D., 2002, Regulation of inducible peroxide stress responses. Mol. Microbiol. 45: 9-15.
    • (2002) Mol. Microbiol , vol.45 , pp. 9-15
    • Mongkolsuk, S.1    Helmann, J.D.2
  • 112
    • 0030974196 scopus 로고    scopus 로고
    • Characterization of transcription organization and analysis of unique expression patterns of an alkyl hydroperoxide reductase C gene (ahpC) and the peroxide regulator operon ahpF-oxyR-orfX from Xanthomonas campestris pv. phaseoli
    • Mongkolsuk, S., Loprasert, S., Whangsuk, W., Fuangthong, M., and Atichartpongkun, S., 1997, Characterization of transcription organization and analysis of unique expression patterns of an alkyl hydroperoxide reductase C gene (ahpC) and the peroxide regulator operon ahpF-oxyR-orfX from Xanthomonas campestris pv. phaseoli. J. Bacteriol. 179: 3950-3955.
    • (1997) J. Bacteriol , vol.179 , pp. 3950-3955
    • Mongkolsuk, S.1    Loprasert, S.2    Whangsuk, W.3    Fuangthong, M.4    Atichartpongkun, S.5
  • 113
    • 0031899593 scopus 로고    scopus 로고
    • Identification and characterization of a new organic hydroperoxide resistance (ohr) gene with a novel pattern of oxidative stress regulation from Xanthomonas campestris pv. phaseoli
    • Mongkolsuk, S., Praituan, W., Loprasert, S., Fuangthong, M., and Chamnongpol, S., 1998a, Identification and characterization of a new organic hydroperoxide resistance (ohr) gene with a novel pattern of oxidative stress regulation from Xanthomonas campestris pv. phaseoli. J. Bacteriol. 180: 2636-2643.
    • (1998) J. Bacteriol , vol.180 , pp. 2636-2643
    • Mongkolsuk, S.1    Praituan, W.2    Loprasert, S.3    Fuangthong, M.4    Chamnongpol, S.5
  • 114
    • 0031859324 scopus 로고    scopus 로고
    • Construction and physiological analysis of a Xanthomonas mutant to examine the role of the oxyR gene in oxidantinduced protection against peroxide killing
    • Mongkolsuk, S., Sukchawalit, R., Loprasert, S., Praituan, W., and Upaichit, A., 1998b, Construction and physiological analysis of a Xanthomonas mutant to examine the role of the oxyR gene in oxidantinduced protection against peroxide killing. J. Bacteriol. 180: 3988-3991.
    • (1998) J. Bacteriol , vol.180 , pp. 3988-3991
    • Mongkolsuk, S.1    Sukchawalit, R.2    Loprasert, S.3    Praituan, W.4    Upaichit, A.5
  • 115
    • 0034047382 scopus 로고    scopus 로고
    • Mutations in oxyR resulting in peroxide resistance in Xanthomonas campestris
    • Mongkolsuk, S., Whangsuk, W., Fuangthong, M., and Loprasert, S., 2000a, Mutations in oxyR resulting in peroxide resistance in Xanthomonas campestris. J. Bacteriol. 182: 3846-3849.
    • (2000) J. Bacteriol , vol.182 , pp. 3846-3849
    • Mongkolsuk, S.1    Whangsuk, W.2    Fuangthong, M.3    Loprasert, S.4
  • 116
    • 0034460324 scopus 로고    scopus 로고
    • A Xanthomonas alkyl hydroperoxide reductase subunit C (ahpC) mutant showed an altered peroxide stress response and complex regulation of the compensatory response of peroxide detoxification enzymes
    • Mongkolsuk, S., Whangsuk, W., Vattanaviboon, P., Loprasert, S., and Fuangthong, M., 2000b, A Xanthomonas alkyl hydroperoxide reductase subunit C (ahpC) mutant showed an altered peroxide stress response and complex regulation of the compensatory response of peroxide detoxification enzymes. J. Bacteriol. 182: 6845-6849.
    • (2000) J. Bacteriol , vol.182 , pp. 6845-6849
    • Mongkolsuk, S.1    Whangsuk, W.2    Vattanaviboon, P.3    Loprasert, S.4    Fuangthong, M.5
  • 117
    • 0006198640 scopus 로고
    • Hydrogen peroxideinducible 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. M., 1986, Hydrogen peroxideinducible proteins in Salmonella typhimurium overlap with heat shock and other stress proteins. Proc. Natl. Acad. Sci. USA 83: 8059-8063.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8059-8063
    • Morgan, R.W.1    Christman, M.F.2    Jacobson, F.S.3    Storz, G.4    Ames, B.M.5
  • 118
    • 0842326281 scopus 로고    scopus 로고
    • The staphylococcal ferritins are differentially regulated in response to iron and manganese and via PerR and Fur
    • Morrissey, J. A., Cockayne, A., Brummell, K., and Williams, P., 2004, The staphylococcal ferritins are differentially regulated in response to iron and manganese and via PerR and Fur. Infect. Immun. 72: 972-979.
    • (2004) Infect. Immun , vol.72 , pp. 972-979
    • Morrissey, J.A.1    Cockayne, A.2    Brummell, K.3    Williams, P.4
  • 119
    • 1242318677 scopus 로고    scopus 로고
    • Transcriptome and proteome analysis of Bacillus subtilis gene expression in response to superoxide and peroxide stress
    • Mostertz, J., Scharf, C., Hecker, M., and Homuth, G., 2004, Transcriptome and proteome analysis of Bacillus subtilis gene expression in response to superoxide and peroxide stress. Microbiol. 150: 497-512.
    • (2004) Microbiol , vol.150 , pp. 497-512
    • Mostertz, J.1    Scharf, C.2    Hecker, M.3    Homuth, G.4
  • 120
    • 4444342918 scopus 로고    scopus 로고
    • Analysis of altered protein expression patterns of Chlamydia pneumoniae by an integrated proteome-works system
    • Mukhopadhyay, S., Miller, R. D., and Summersgill, J. T., 2004, Analysis of altered protein expression patterns of Chlamydia pneumoniae by an integrated proteome-works system. J. Proteome Res. 3: 878-883.
    • (2004) J. Proteome Res , vol.3 , pp. 878-883
    • Mukhopadhyay, S.1    Miller, R.D.2    Summersgill, J.T.3
  • 121
    • 0034255209 scopus 로고    scopus 로고
    • Reactive oxygen and nitrogen intermediates in the relationship between mammalian hosts and microbial pathogens
    • Nathan, C., and Shiloh, M. U., 2000, Reactive oxygen and nitrogen intermediates in the relationship between mammalian hosts and microbial pathogens. Proc. Natl. Acad. Sci. USA 97: 8841-8848.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8841-8848
    • Nathan, C.1    Shiloh, M.U.2
  • 122
    • 0028835104 scopus 로고
    • Leucine-responsive regulatory protein: A global regulator of gene expression in E. coli
    • Newman, E. B., and Lin, R., 1995, Leucine-responsive regulatory protein: a global regulator of gene expression in E. coli. Ann. Rev. Microbiol. 49: 747-775.
    • (1995) Ann. Rev. Microbiol , vol.49 , pp. 747-775
    • Newman, E.B.1    Lin, R.2
  • 123
    • 0035157997 scopus 로고    scopus 로고
    • Genetic and physiological characterization of ohr, encoding a protein involved in organic hydroperoxide resistance in Pseudomonas aeruginosa
    • Ochsner, U. A., Hassett, D. J., and Vasil, M. L., 2001, Genetic and physiological characterization of ohr, encoding a protein involved in organic hydroperoxide resistance in Pseudomonas aeruginosa. J. Bacteriol. 183: 773-778.
    • (2001) J. Bacteriol , vol.183 , pp. 773-778
    • Ochsner, U.A.1    Hassett, D.J.2    Vasil, M.L.3
  • 124
    • 0033874090 scopus 로고    scopus 로고
    • Role of the Pseudomonas aeruginosa oxyR-recG operon in oxidative stress defense and DNA repair: OxyR-dependent regulation of katB-ankB, ahpB, and ahpC-ahpF
    • Ochsner, U. A., Vasil, M. L., Eyad, A., Kislay, P., and Hassett, D. J., 2000, Role of the Pseudomonas aeruginosa oxyR-recG operon in oxidative stress defense and DNA repair: OxyR-dependent regulation of katB-ankB, ahpB, and ahpC-ahpF. J. Bacteriol. 182: 4533-44.
    • (2000) J. Bacteriol , vol.182 , pp. 4533-4544
    • Ochsner, U.A.1    Vasil, M.L.2    Eyad, A.3    Kislay, P.4    Hassett, D.J.5
  • 125
    • 33645543011 scopus 로고    scopus 로고
    • Superoxide dismutase-encoding gene of the obligate anaerobe Porphyromonas gingivalis is regulated by the redox-sensing transcription activator OxyR
    • Ohara, N., Kikuchi, Y., Shoji, M., Naito, M., and Nakayama, K., 2006, Superoxide dismutase-encoding gene of the obligate anaerobe Porphyromonas gingivalis is regulated by the redox-sensing transcription activator OxyR. Microbiol. 152: 955-966.
    • (2006) Microbiol , vol.152 , pp. 955-966
    • Ohara, N.1    Kikuchi, Y.2    Shoji, M.3    Naito, M.4    Nakayama, K.5
  • 126
    • 31344481247 scopus 로고    scopus 로고
    • Proteomics-based analysis of a counteroxidative stress system in Porphyromonas gingivalis
    • Okano, S., Shibata, Y., Shiroza, T., and Abiko, Y., 2006, Proteomics-based analysis of a counteroxidative stress system in Porphyromonas gingivalis. Proteomics 6: 251-258.
    • (2006) Proteomics , vol.6 , pp. 251-258
    • Okano, S.1    Shibata, Y.2    Shiroza, T.3    Abiko, Y.4
  • 128
    • 0037220694 scopus 로고    scopus 로고
    • Association of Helicobacter pylori antioxidant activities with host colonization proficiency
    • Olczak, A. A., Seyler, R. W., Olson, J. W., and Maier, R. J., 2003, Association of Helicobacter pylori antioxidant activities with host colonization proficiency. Infect. Immun. 71: 580-583.
    • (2003) Infect. Immun , vol.71 , pp. 580-583
    • Olczak, A.A.1    Seyler, R.W.2    Olson, J.W.3    Maier, R.J.4
  • 130
    • 33646202329 scopus 로고    scopus 로고
    • Structural insights into enzyme-substrate interaction and characterization of enzymatic intermediates of organic hydroperoxide resistance protein from
    • Oliveira, M. A., Guimares, B. G., Cussiol, J. R. R., Medrano, F. J., Gozzo, F. C., and Netto, L. E. S., 2006, Structural insights into enzyme-substrate interaction and characterization of enzymatic intermediates of organic hydroperoxide resistance protein from Xylella fastidiosa. J. Mol. Biol. 359: 433-435.
    • (2006) Xylella fastidiosa. J. Mol. Biol , vol.359 , pp. 433-435
    • Oliveira, M.A.1    Guimares, B.G.2    Cussiol, J.R.R.3    Medrano, F.J.4    Gozzo, F.C.5    Netto, L.E.S.6
  • 131
    • 0033985237 scopus 로고    scopus 로고
    • Alkyl hydroperoxide reductases C and D are major antigens constitutively expressed by Mycobacterium avium subsp. paratuberculosis
    • Olsen, I., Reitan, L. J., Holstad, G., and Wiker, H. G., 2000, Alkyl hydroperoxide reductases C and D are major antigens constitutively expressed by Mycobacterium avium subsp. paratuberculosis. Infect. Immun. 68: 801-808.
    • (2000) Infect. Immun , vol.68 , pp. 801-808
    • Olsen, I.1    Reitan, L.J.2    Holstad, G.3    Wiker, H.G.4
  • 132
    • 0034974390 scopus 로고    scopus 로고
    • AhpC, AhpD, and a secreted 14-kilodalton antigen from Mycobacterium avium subsp. paratuberculosis distinguish between paratuberculosis and bovine tuberculosis in an enzyme-linked immunosorbent assay
    • Olsen, I., Tryland, M., Wiker, H. G., and Reitan, L. J., 2001, AhpC, AhpD, and a secreted 14-kilodalton antigen from Mycobacterium avium subsp. paratuberculosis distinguish between paratuberculosis and bovine tuberculosis in an enzyme-linked immunosorbent assay. Clin. Diagn. Lab. Immunol. 8: 797-801.
    • (2001) Clin. Diagn. Lab. Immunol , vol.8 , pp. 797-801
    • Olsen, I.1    Tryland, M.2    Wiker, H.G.3    Reitan, L.J.4
  • 133
    • 0036786304 scopus 로고    scopus 로고
    • Construction and characterization of transposon insertion mutations in Corynebacterium diphtheriae that affect expression of the diphtheria toxin repressor (DtxR)
    • Oram, D., Marra, Avdalovic, A., and Holmes, R. K., 2002, Construction and characterization of transposon insertion mutations in Corynebacterium diphtheriae that affect expression of the diphtheria toxin repressor (DtxR). J. Bacteriol. 184: 5723-5732.
    • (2002) J. Bacteriol , vol.184 , pp. 5723-5732
    • Oram, D.1    Marra Avdalovic, A.2    Holmes, R.K.3
  • 135
    • 0031660550 scopus 로고    scopus 로고
    • Oxidative stress response and characterization of the oxyR-ahpC and furA-katG loci in Mycobacterium marinum
    • Pagan-Ramos, E., Song, J., McFalone, M., Mudd, M. H., and Deretic, V., 1998, Oxidative stress response and characterization of the oxyR-ahpC and furA-katG loci in Mycobacterium marinum. J. Bacteriol. 180: 4856-4864.
    • (1998) J. Bacteriol , vol.180 , pp. 4856-4864
    • Pagan-Ramos, E.1    Song, J.2    McFalone, M.3    Mudd, M.H.4    Deretic, V.5
  • 136
    • 0141492988 scopus 로고    scopus 로고
    • Thiol-based regulatory switches
    • Paget, M. S., and Buttner, M. J., 2003, Thiol-based regulatory switches. Ann. Rev. Genet. 37: 91-121.
    • (2003) Ann. Rev. Genet , vol.37 , pp. 91-121
    • Paget, M.S.1    Buttner, M.J.2
  • 137
    • 0036032183 scopus 로고    scopus 로고
    • OhrR, a transcription repressor that senses and responds to changes in organic peroxide levels in Xanthomonas campestris pv. phaseoli
    • Panmanee, W., Vattanaviboon, P., Eiamphungporn, W., Whangsuk, W., Sallabhan, R., and Mongkolsuk, S., 2002, OhrR, a transcription repressor that senses and responds to changes in organic peroxide levels in Xanthomonas campestris pv. phaseoli. Mol. Microbiol. 45: 1647-1654.
    • (2002) Mol. Microbiol , vol.45 , pp. 1647-1654
    • Panmanee, W.1    Vattanaviboon, P.2    Eiamphungporn, W.3    Whangsuk, W.4    Sallabhan, R.5    Mongkolsuk, S.6
  • 138
    • 32444439989 scopus 로고    scopus 로고
    • Novel organic hydroperoxidesensing and responding mechanisms for OhrR, a major bacterial sensor and regulator of organic hydroperoxide stress
    • Panmanee, W., Vattanaviboon, P., Poole, L. B., and Mongkolsuk, S., 2006, Novel organic hydroperoxidesensing and responding mechanisms for OhrR, a major bacterial sensor and regulator of organic hydroperoxide stress. J. Bacteriol. 188: 1389-1395.
    • (2006) J. Bacteriol , vol.188 , pp. 1389-1395
    • Panmanee, W.1    Vattanaviboon, P.2    Poole, L.B.3    Mongkolsuk, S.4
  • 139
    • 21544465580 scopus 로고    scopus 로고
    • Substantial DNA damage from submicromolar intracellular hydrogen peroxide detected in Hpx-mutants of
    • Park, S., You, X., and Imlay, J. A., 2005, Substantial DNA damage from submicromolar intracellular hydrogen peroxide detected in Hpx-mutants of Escherichia coli. Proc. Natl. Acad. Sci. USA 102: 9317-9322.
    • (2005) Escherichia coli. Proc. Natl. Acad. Sci. USA , vol.102 , pp. 9317-9322
    • Park, S.1    You, X.2    Imlay, J.A.3
  • 140
    • 23244466487 scopus 로고    scopus 로고
    • Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin
    • Parsonage, D., Youngblood, D. S., Ganapathy, N. S., Wood, Z. A., Karpus, A. P., and Poole, L. B., 2005, Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin. Biochemistry 44: 10583-10592.
    • (2005) Biochemistry , vol.44 , pp. 10583-10592
    • Parsonage, D.1    Youngblood, D.S.2    Ganapathy, N.S.3    Wood, Z.A.4    Karpus, A.P.5    Poole, L.B.6
  • 141
    • 0035985625 scopus 로고    scopus 로고
    • Global adjustment of microbial physiology during free radical stress
    • Pomposiello, P. J., and Demple, B., 2002, Global adjustment of microbial physiology during free radical stress. Adv. Microb. Physiol. 46: 319-341.
    • (2002) Adv. Microb. Physiol , vol.46 , pp. 319-341
    • Pomposiello, P.J.1    Demple, B.2
  • 142
    • 0033621685 scopus 로고    scopus 로고
    • Streptococcus mutans H2O2-forming NADH oxidase is an alkyl hydroperoxide reductase protein
    • Poole, L. B., Higuchi, M., Shimada, M., Calzi, M., Li, and Kamio, Y., 2000a, Streptococcus mutans H2O2-forming NADH oxidase is an alkyl hydroperoxide reductase protein. Free Rad. Biol. Med. 28: 108-120.
    • (2000) Free Rad. Biol. Med , vol.28 , pp. 108-120
    • Poole, L.B.1    Higuchi, M.2    Shimada, M.3    Calzi, M.4    Li5    Kamio, Y.6
  • 143
    • 0033771859 scopus 로고    scopus 로고
    • AhpF and other NADH: Peroxiredoxin oxidoreductases, homologues of low Mr thioredoxin reductase
    • Poole, L. B., Reynolds, C. M., Wood, Z. A., Karpus, A. P., Ellis, H. R., and Li Calzi, M., 2000b, AhpF and other NADH: peroxiredoxin oxidoreductases, homologues of low Mr thioredoxin reductase. Eur. J. Biochem. 267: 6126-6133.
    • (2000) Eur. J. Biochem , vol.267 , pp. 6126-6133
    • Poole, L.B.1    Reynolds, C.M.2    Wood, Z.A.3    Karpus, A.P.4    Ellis, H.R.5    Li Calzi, M.6
  • 145
    • 0026739788 scopus 로고
    • NhaR, a protein homologous to a family of bacterial regulatory proteins (LysR), regulates nhaA, the sodium proton antiporter gene in Escherichia coli
    • Rahav-Manor, O., Carmel, O., Karpel, R., Taglicht, D., Glaser, G., Schuldiner, S., and Padan, E., 1992, NhaR, a protein homologous to a family of bacterial regulatory proteins (LysR), regulates nhaA, the sodium proton antiporter gene in Escherichia coli. J. Biol. Chem. 267: 10433-10438.
    • (1992) J. Biol. Chem , vol.267 , pp. 10433-10438
    • Rahav-Manor, O.1    Carmel, O.2    Karpel, R.3    Taglicht, D.4    Glaser, G.5    Schuldiner, S.6    Padan, E.7
  • 146
    • 0036081333 scopus 로고    scopus 로고
    • Macrophage-induced genes of Legionella pneumophila: Protection from reactive intermediates and solute imbalance during intracellular growth
    • Rankin, S., Li, Z., and Isberg, R. R., 2002, Macrophage-induced genes of Legionella pneumophila: protection from reactive intermediates and solute imbalance during intracellular growth. Infect. Immun. 70: 3637-3648.
    • (2002) Infect. Immun , vol.70 , pp. 3637-3648
    • Rankin, S.1    Li, Z.2    Isberg, R.R.3
  • 147
    • 2142652096 scopus 로고    scopus 로고
    • Crystallographic structure and biochemical analysis of the Thermus thermophilus osmotically inducible protein C
    • Rehse, P. H., Ohshima, N., Nodake, Y., and Tahirov, T. H., 2004, Crystallographic structure and biochemical analysis of the Thermus thermophilus osmotically inducible protein C. J. Mol. Biol. 338: 959-968.
    • (2004) J. Mol. Biol , vol.338 , pp. 959-968
    • Rehse, P.H.1    Ohshima, N.2    Nodake, Y.3    Tahirov, T.H.4
  • 149
    • 19944418509 scopus 로고    scopus 로고
    • A member of the cAMP receptor protein family of transcription regulators in Mycobacterium tuberculosis is required for virulence in mice and controls transcription of the rpfA gene coding for a resuscitation promoting factor
    • Rickman, L., Scott, C., Hunt, D. M., Hutchinson, T., Menendez, M. C., Whalan, R., Hinds, J., Colston, M. J., Green, J., and Buxton, R. S., 2005, A member of the cAMP receptor protein family of transcription regulators in Mycobacterium tuberculosis is required for virulence in mice and controls transcription of the rpfA gene coding for a resuscitation promoting factor. Mol. Microbiol. 56: 1274-1286.
    • (2005) Mol. Microbiol , vol.56 , pp. 1274-1286
    • Rickman, L.1    Scott, C.2    Hunt, D.M.3    Hutchinson, T.4    Menendez, M.C.5    Whalan, R.6    Hinds, J.7    Colston, M.J.8    Green, J.9    Buxton, R.S.10
  • 150
    • 0035142748 scopus 로고    scopus 로고
    • Identification and characterization of gsp65, an organic hydroperoxide resistance (ohr) gene encoding a general stress protein in Enterococcus faecalis
    • Rince, A., Giard, J.-C., Pichereau, V., Flahaut, S., and Auffray, Y., 2001, Identification and characterization of gsp65, an organic hydroperoxide resistance (ohr) gene encoding a general stress protein in Enterococcus faecalis. J. Bacteriol. 183: 1482-1488.
    • (2001) J. Bacteriol , vol.183 , pp. 1482-1488
    • Rince, A.1    Giard, J.-C.2    Pichereau, V.3    Flahaut, S.4    Auffray, Y.5
  • 151
    • 0033816764 scopus 로고    scopus 로고
    • The redox-sensitive transcriptional activator OxyR regulates the peroxide response regulon in the obligate anaerobe
    • Rocha, E. R., Owens, G. J., and Smith, C. J., 2000, The redox-sensitive transcriptional activator OxyR regulates the peroxide response regulon in the obligate anaerobe Bacteroides fragilis. J. Bacteriol. 182: 5059-5069.
    • (2000) Bacteroides fragilis. J. Bacteriol , vol.182 , pp. 5059-5069
    • Rocha, E.R.1    Owens, G.J.2    Smith, C.J.3
  • 152
    • 0031734418 scopus 로고    scopus 로고
    • Characterization of a peroxide-resistant mutant of the anaerobic bacterium
    • Rocha, E. R., and Smith, C. J., 1998, Characterization of a peroxide-resistant mutant of the anaerobic bacterium Bacteroides fragilis. J. Bacteriol. 180: 5906-5912.
    • (1998) Bacteroides fragilis. J. Bacteriol , vol.180 , pp. 5906-5912
    • Rocha, E.R.1    Smith, C.J.2
  • 153
    • 0032851571 scopus 로고    scopus 로고
    • Role of the alkyl hydroperoxide reductase (ahpCF) gene in oxidative stress defense of the obligate anaerobe
    • Rocha, E. R., and Smith, C. J., 1999, Role of the alkyl hydroperoxide reductase (ahpCF) gene in oxidative stress defense of the obligate anaerobe Bacteroides fragilis. J. Bacteriol. 181: 5701-5710.
    • (1999) Bacteroides fragilis. J. Bacteriol , vol.181 , pp. 5701-5710
    • Rocha, E.R.1    Smith, C.J.2
  • 155
    • 0034031272 scopus 로고    scopus 로고
    • Mapping and identification of Mycobacterium tuberculosis proteins by two-dimensional gel electrophoresis, microsequencing and immunodetection
    • Rosenkrands, I., Weldingh, K., Jacobsen, S., Hansen, C. V., Florio, W., Gianetri, I., and Andersen, P., 2000b, Mapping and identification of Mycobacterium tuberculosis proteins by two-dimensional gel electrophoresis, microsequencing and immunodetection. Electrophoresis 21: 935-48.
    • (2000) Electrophoresis , vol.21 , pp. 935-948
    • Rosenkrands, I.1    Weldingh, K.2    Jacobsen, S.3    Hansen, C.V.4    Florio, W.5    Gianetri, I.6    Andersen, P.7
  • 157
    • 0027446708 scopus 로고
    • Molecular biology of the LysR family of transcriptional regulators
    • Schell, M. A., 1993, Molecular biology of the LysR family of transcriptional regulators. Ann. Rev. Microbiol. 47: 597-626.
    • (1993) Ann. Rev. Microbiol , vol.47 , pp. 597-626
    • Schell, M.A.1
  • 158
    • 0035209075 scopus 로고    scopus 로고
    • Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli
    • Seaver, L. C., and Imlay, J. A., 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
  • 159
    • 21144433999 scopus 로고    scopus 로고
    • Hydrogen peroxide increases the activities of soxRS regulon enzymes and the levels of oxidized proteins and lipids in Escherichia coli
    • Semchyshyn, H., Bagnyukova, T., Storey, K., and Storey, V., 2005, Hydrogen peroxide increases the activities of soxRS regulon enzymes and the levels of oxidized proteins and lipids in Escherichia coli. Cell Biol. Int. 70: 424-431.
    • (2005) Cell Biol. Int , vol.70 , pp. 424-431
    • Semchyshyn, H.1    Bagnyukova, T.2    Storey, K.3    Storey, V.4
  • 160
    • 0034607656 scopus 로고    scopus 로고
    • DsbG, a protein disulfide isomerase with chaperone activity
    • Shao, F., Bader, M. W., Jalob, U., and Bardwell, J. C. A., 2000, DsbG, a protein disulfide isomerase with chaperone activity. J. Biol. Chem. 275: 13349-13352.
    • (2000) J. Biol. Chem , vol.275 , pp. 13349-13352
    • Shao, F.1    Bader, M.W.2    Jalob, U.3    Bardwell, J.C.A.4
  • 161
    • 0036156059 scopus 로고    scopus 로고
    • ohr, Encoding an organic hydroperoxide reductase, is an in vivoinduced gene in Actinobacillus pleuropneumoniae
    • Shea, R. J., and Mulks, M. H., 2002, ohr, Encoding an organic hydroperoxide reductase, is an in vivoinduced gene in Actinobacillus pleuropneumoniae. Infect. Immun. 70: 794-802.
    • (2002) Infect. Immun , vol.70 , pp. 794-802
    • Shea, R.J.1    Mulks, M.H.2
  • 163
    • 0032693096 scopus 로고    scopus 로고
    • AhpC, oxidative stress and drug resistance in Mycobacterium tuberculosis
    • Sherman, D. R., Mdhluli, K., Hickey, M. J., Barry, C. E. I., and Stover, C. K., 1999, AhpC, oxidative stress and drug resistance in Mycobacterium tuberculosis. Biofactors 10: 211-217.
    • (1999) Biofactors , vol.10 , pp. 211-217
    • Sherman, D.R.1    Mdhluli, K.2    Hickey, M.J.3    Barry, C.E.I.4    Stover, C.K.5
  • 165
    • 29644437414 scopus 로고    scopus 로고
    • Dihydrolipoamide acyltransferase is critical for Mycobacterium tuberculosis pathogenesis
    • Shi, S., and Ehrt, S., 2006, Dihydrolipoamide acyltransferase is critical for Mycobacterium tuberculosis pathogenesis. Infect. Immun. 74: 56-63.
    • (2006) Infect. Immun , vol.74 , pp. 56-63
    • Shi, S.1    Ehrt, S.2
  • 167
    • 0034583805 scopus 로고    scopus 로고
    • pH-dependent protein profiles of Helicobacter pylori analyzed by two-dimensional gels
    • Slonczewski, J. L., Mcgee, D. J., Phillips, J., Kirkpatrick, C., and Mobley, H. L. T., 2000, pH-dependent protein profiles of Helicobacter pylori analyzed by two-dimensional gels. Helicobacter 5: 240-247.
    • (2000) Helicobacter , vol.5 , pp. 240-247
    • Slonczewski, J.L.1    Mcgee, D.J.2    Phillips, J.3    Kirkpatrick, C.4    Mobley, H.L.T.5
  • 168
    • 0036129504 scopus 로고    scopus 로고
    • Evidence that ORF3 at the Streptococcus parasanguis fimA locus encodes a thiol-specific antioxidant
    • Spatafora, G., Van Hoeven, N., Wagner, K., and Fives-Taylor, P., 2002, Evidence that ORF3 at the Streptococcus parasanguis fimA locus encodes a thiol-specific antioxidant. Microbiol. 148: 755-762.
    • (2002) Microbiol , vol.148 , pp. 755-762
    • Spatafora, G.1    Van Hoeven, N.2    Wagner, K.3    Fives-Taylor, P.4
  • 169
    • 0034826633 scopus 로고    scopus 로고
    • Silencing of oxidative stress response in Mycobacterium tuberculosis: Expression patterns of ahpC in virulent and avirulent strains and effect of ahpC inactivation
    • Springer, B., Sander, P., Zahrt, T., McFalone, M., Song, J., Papavinasasundaram, K. G., Colston, M. J., Boettger, E., and Deretic, V., 2001, Silencing of oxidative stress response in Mycobacterium tuberculosis: expression patterns of ahpC in virulent and avirulent strains and effect of ahpC inactivation. Infect. Immun. 69: 5967-5973.
    • (2001) Infect. Immun , vol.69 , pp. 5967-5973
    • Springer, B.1    Sander, P.2    Zahrt, T.3    McFalone, M.4    Song, J.5    Papavinasasundaram, K.G.6    Colston, M.J.7    Boettger, E.8    Deretic, V.9
  • 170
    • 0036062240 scopus 로고    scopus 로고
    • pH-dependent expression of periplasmic proteins and amino acid catabolism in Escherichia coli
    • Stancik, L. M., Stancik, D. M., Schmidt, B., Barnhart, D. M., Yoncheva, Y., N., and Slonczewski, J. L., 2002, pH-dependent expression of periplasmic proteins and amino acid catabolism in Escherichia coli. J. Bacteriol. 184: 4246-4258.
    • (2002) J. Bacteriol , vol.184 , pp. 4246-4258
    • Stancik, L.M.1    Stancik, D.M.2    Schmidt, B.3    Barnhart, D.M.4    Yoncheva, Y.N.5    Slonczewski, J.L.6
  • 171
    • 0036802316 scopus 로고    scopus 로고
    • mRNA expression profiles for Escherichia coli ingested by normal and phagocyte oxidase-deficient human neutrophils
    • Staudinger, B. J., Oberdoerster, M. A., Lewis, P. J., and Rosen, H., 2002, mRNA expression profiles for Escherichia coli ingested by normal and phagocyte oxidase-deficient human neutrophils. J. Clin. Invest. 110: 1151-1163.
    • (2002) J. Clin. Invest , vol.110 , pp. 1151-1163
    • Staudinger, B.J.1    Oberdoerster, M.A.2    Lewis, P.J.3    Rosen, H.4
  • 172
    • 0023487170 scopus 로고
    • Spontaneous mutagenesis and oxidative damage to DNA in Salmonella typhimurium
    • Storz, G., Christman, M. F., Sies, H., and Ames, B. M., 1987, Spontaneous mutagenesis and oxidative damage to DNA in Salmonella typhimurium. Proc. Natl. Acad. Sci. USA 84: 8917-8921.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 8917-8921
    • Storz, G.1    Christman, M.F.2    Sies, H.3    Ames, B.M.4
  • 173
    • 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., Jacobson, F. S., Tartaglia, L. A., Morgan, R. W., Silveira, L. A., and Ames, B. M., 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.M.6
  • 174
    • 0025214474 scopus 로고
    • Transcriptional regulator of oxidative stress inducible genes: Direct activation by oxidation
    • Storz, G., Tartaglia, L. A., and Ames, B. M., 1990, Transcriptional regulator of oxidative stress inducible genes: direct activation by oxidation. Science 248: 189-194.
    • (1990) Science , vol.248 , pp. 189-194
    • Storz, G.1    Tartaglia, L.A.2    Ames, B.M.3
  • 175
    • 0004268763 scopus 로고    scopus 로고
    • Oxidative stress
    • (Storz, G. and Hengge-Aronis, R., eds.), American Society for Microbiology Press, Washington, DC, USA
    • Storz, G., and Zheng, M., 2000, Oxidative stress, in Bacterial stress responses (Storz, G. and Hengge-Aronis, R., eds.), American Society for Microbiology Press, Washington, DC, USA, pp. 47-59.
    • (2000) Bacterial stress responses , pp. 47-59
    • Storz, G.1    Zheng, M.2
  • 176
    • 0038782375 scopus 로고    scopus 로고
    • NhaR and RcsB independently regulate the osmCp1 promoter of Escherichia coli at overlapping regulatory sites
    • Sturny, R., Cam, K., Gutierrez, C., and Conter, A., 2003, NhaR and RcsB independently regulate the osmCp1 promoter of Escherichia coli at overlapping regulatory sites. J. Bacteriol. 185: 4298-4304.
    • (2003) J. Bacteriol , vol.185 , pp. 4298-4304
    • Sturny, R.1    Cam, K.2    Gutierrez, C.3    Conter, A.4
  • 177
    • 0034944405 scopus 로고    scopus 로고
    • Complex regulation of the organic hydroperoxide resistance gene (ohr) fromXanthomonasinvolvesOhrR, a novel organic peroxideinducible negative regulator, and posttranscriptional modifications
    • Sukchawalit, R., Loprasert, S., Atichartpongkun, S., and Mongkolsuk, S., 2001, Complex regulation of the organic hydroperoxide resistance gene (ohr) fromXanthomonasinvolvesOhrR, a novel organic peroxideinducible negative regulator, and posttranscriptional modifications. J. Bacteriol. 183: 4405-4412.
    • (2001) J. Bacteriol , vol.183 , pp. 4405-4412
    • Sukchawalit, R.1    Loprasert, S.2    Atichartpongkun, S.3    Mongkolsuk, S.4
  • 178
    • 0029034529 scopus 로고
    • Cloning of a Corynebacterium diphtheriae iron-repressible gene that shares sequence homology with the AhpC subunit of alkyl hydroperoxide reductase of
    • Tai, S. S., and Zhu, Y., Yi, 1995, Cloning of a Corynebacterium diphtheriae iron-repressible gene that shares sequence homology with the AhpC subunit of alkyl hydroperoxide reductase of Salmonella typhimurium. J. Bacteriol. 177: 3512-3517.
    • (1995) Salmonella typhimurium. J. Bacteriol , vol.177 , pp. 3512-3517
    • Tai, S.S.1    Zhu, Y.2    Yi3
  • 179
    • 0024785396 scopus 로고
    • Identification and molecular analysis of oxyR-regulated promoters important for the bacterial adaptation to oxidative stress
    • Tartaglia, L. A., Storz, G., and Ames, B. M., 1989, Identification and molecular analysis of oxyR-regulated promoters important for the bacterial adaptation to oxidative stress. J. Mol. Biol. 210: 709-719.
    • (1989) J. Mol. Biol , vol.210 , pp. 709-719
    • Tartaglia, L.A.1    Storz, G.2    Ames, B.M.3
  • 180
    • 0025365949 scopus 로고
    • Alkyl hydroperoxide reductase from Salmonella typhimurium. Sequence and homology to thioredoxin reductase and other flavoprotein disulfide oxidoreductases
    • Tartaglia, L. A., Storz, G., Brodsky, M. H., Lai, A., and Ames, B. M., 1990, Alkyl hydroperoxide reductase from Salmonella typhimurium. Sequence and homology to thioredoxin reductase and other flavoprotein disulfide oxidoreductases. J. Biol. Chem. 265: 10535-10540.
    • (1990) J. Biol. Chem , vol.265 , pp. 10535-10540
    • Tartaglia, L.A.1    Storz, G.2    Brodsky, M.H.3    Lai, A.4    Ames, B.M.5
  • 181
    • 0031814102 scopus 로고    scopus 로고
    • The Salmonella typhimurium AhpC polypeptide is not essential for virulence in BALB/c mice but is recognized as an antigen during infection
    • Taylor, P. D., Inchley, C. J., and Gallagher, M. P., 1998, The Salmonella typhimurium AhpC polypeptide is not essential for virulence in BALB/c mice but is recognized as an antigen during infection. Infect. Immun. 66: 3207-3217.
    • (1998) Infect. Immun , vol.66 , pp. 3207-3217
    • Taylor, P.D.1    Inchley, C.J.2    Gallagher, M.P.3
  • 182
  • 183
    • 0034780281 scopus 로고    scopus 로고
    • The transcriptional activator NhaR is responsible for the osmotic induction of osmC(P1), a promoter of the stress-inducible gene osmC in Escherichia coli
    • Toesca, I., Perard, C., Bouvier, J., Gutierrez, C., and Conter, A., 2001, The transcriptional activator NhaR is responsible for the osmotic induction of osmC(P1), a promoter of the stress-inducible gene osmC in Escherichia coli. Microbiol. 147: 2795-2803.
    • (2001) Microbiol , vol.147 , pp. 2795-2803
    • Toesca, I.1    Perard, C.2    Bouvier, J.3    Gutierrez, C.4    Conter, A.5
  • 184
    • 0028023175 scopus 로고
    • Redox-dependent shift of OxyR-DNA contacts along an extended DNA-binding site: A mechanism for differential promoter selection
    • Toledano, M. B., Kullik, I., Trinh, F., Baird, P. T., Schneider, T. D., and Storz, G., 1994, Redox-dependent shift of OxyR-DNA contacts along an extended DNA-binding site: a mechanism for differential promoter selection. Cell 78: 897-909.
    • (1994) Cell , vol.78 , pp. 897-909
    • Toledano, M.B.1    Kullik, I.2    Trinh, F.3    Baird, P.T.4    Schneider, T.D.5    Storz, G.6
  • 185
    • 0032716842 scopus 로고    scopus 로고
    • Campylobacter jejuni contains two fur homologs: Characterization of iron-responsive regulation of peroxide stress defense genes by the PerR repressor
    • van Vliet, A. H. M., Baillon, M.-L. A., Penn, C. W., and Ketley, J. M., 1999, Campylobacter jejuni contains two fur homologs: characterization of iron-responsive regulation of peroxide stress defense genes by the PerR repressor. J. Bacteriol. 181: 6371-6376.
    • (1999) J. Bacteriol , vol.181 , pp. 6371-6376
    • van Vliet, A.H.M.1    Baillon, M.-L.A.2    Penn, C.W.3    Ketley, J.M.4
  • 186
    • 0036436682 scopus 로고    scopus 로고
    • Evaluation of the roles that alkyl hydroperoxide reductase and Ohr play in organic peroxideinduced gene expression and protection against organic peroxides in Xanthomonas campestris
    • Vattanaviboon, P., Whangsuk, W., Panmanee, W., Klomsiri, C., Dharmsthiti, S., and Mongkolsuk, S., 2002, Evaluation of the roles that alkyl hydroperoxide reductase and Ohr play in organic peroxideinduced gene expression and protection against organic peroxides in Xanthomonas campestris. Biochem. Biophys. Res. Commun. 299: 177-182.
    • (2002) Biochem. Biophys. Res. Commun , vol.299 , pp. 177-182
    • Vattanaviboon, P.1    Whangsuk, W.2    Panmanee, W.3    Klomsiri, C.4    Dharmsthiti, S.5    Mongkolsuk, S.6
  • 187
    • 1342303776 scopus 로고    scopus 로고
    • Identification of a new oxidative stress transcriptional regulator in Enterococcus faecalis
    • Verneuil, N., Le Breton, Y., Hartke, A., Auffray, Y., and Giard, J.-C., 2004a, Identification of a new oxidative stress transcriptional regulator in Enterococcus faecalis. Lait. 84: 69-76.
    • (2004) Lait , vol.84 , pp. 69-76
    • Verneuil, N.1    Le Breton, Y.2    Hartke, A.3    Auffray, Y.4    Giard, J.-C.5
  • 188
    • 3342931121 scopus 로고    scopus 로고
    • Effects of the Enterococcus faecalis hypR gene encoding a new transcriptional regulator on oxidative stress response and intracellular survival within macrophages
    • Verneuil, N., Sanguinetti, M., Le Breton, Y., Posteraro, B., Fadda, G., Auffray, Y., Hartke, A., and Giard, J.-C., 2004b, Effects of the Enterococcus faecalis hypR gene encoding a new transcriptional regulator on oxidative stress response and intracellular survival within macrophages. Infect. Immun. 72: 4424-4431.
    • (2004) Infect. Immun , vol.72 , pp. 4424-4431
    • Verneuil, N.1    Sanguinetti, M.2    Le Breton, Y.3    Posteraro, B.4    Fadda, G.5    Auffray, Y.6    Hartke, A.7    Giard, J.-C.8
  • 190
    • 0031829737 scopus 로고    scopus 로고
    • One of two osmC homologs in Bacillus subtilis is part of the sigmaB-dependent general stress regulon
    • Volker, U., Maul, B., and Hecker, M., 1998, One of two osmC homologs in Bacillus subtilis is part of the sigmaB-dependent general stress regulon. J. Bacteriol. 180: 4212-4218.
    • (1998) J. Bacteriol , vol.180 , pp. 4212-4218
    • Volker, U.1    Maul, B.2    Hecker, M.3
  • 191
    • 0031582202 scopus 로고    scopus 로고
    • Scavengase p20: A novel family of bacterial antioxidant enzymes
    • Wan, X.-Y., Zhou, Y., Yan, Z.-Y., Wang, H.-L., Hou, Y.-D., and Jin, D.-Y., 1997, Scavengase p20: a novel family of bacterial antioxidant enzymes. FEBS Lett. 407: 32-36.
    • (1997) FEBS Lett , vol.407 , pp. 32-36
    • Wan, X.-Y.1    Zhou, Y.2    Yan, Z.-Y.3    Wang, H.-L.4    Hou, Y.-D.5    Jin, D.-Y.6
  • 192
    • 10644290115 scopus 로고    scopus 로고
    • Role of a bacterial organic hydroperoxide detoxification system in preventing catalase inactivation
    • Wang, G., Conover, R. C., Benoit, S., Olczak, A. A., Olson, J. W., Johnson, M. K., and Maier, R. J., 2004, Role of a bacterial organic hydroperoxide detoxification system in preventing catalase inactivation. J. Biol. Chem. 279: 51908-51914.
    • (2004) J. Biol. Chem , vol.279 , pp. 51908-51914
    • Wang, G.1    Conover, R.C.2    Benoit, S.3    Olczak, A.A.4    Olson, J.W.5    Johnson, M.K.6    Maier, R.J.7
  • 193
    • 27744563761 scopus 로고    scopus 로고
    • Oxidative stress defense mechanisms to counter iron-promoted DNA damage in Helicobacter pylori
    • Wang, G., Conover, R. C., Olczak, A. A., Alamuri, P., Johnson, M. K., and Maier, R. J., 2005, Oxidative stress defense mechanisms to counter iron-promoted DNA damage in Helicobacter pylori. Free Rad. Res. 39: 1183-1191.
    • (2005) Free Rad. Res , vol.39 , pp. 1183-1191
    • Wang, G.1    Conover, R.C.2    Olczak, A.A.3    Alamuri, P.4    Johnson, M.K.5    Maier, R.J.6
  • 194
    • 0031884727 scopus 로고    scopus 로고
    • Heat shock response enhances acid tolerance of Escherichia coli O157: H7
    • Wang, G., and P., D. M., 1998, Heat shock response enhances acid tolerance of Escherichia coli O157: H7. Lett Appl Microbiol 26: 31-34.
    • (1998) Lett Appl Microbiol , vol.26 , pp. 31-34
    • Wang, G.P.D.M.1
  • 195
    • 0031825604 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis for analysis of Mycobacterium tuberculosis culture filtrate and purification and characterization of six novel proteins
    • Weldingh, K., Rosenkrands, I., Jacobsen, S., Rasmussen, P. B., Elhay, M. J., and Andersen, P., 1998, Two-dimensional electrophoresis for analysis of Mycobacterium tuberculosis culture filtrate and purification and characterization of six novel proteins. Infect. Immun. 66: 3492-3500.
    • (1998) Infect. Immun , vol.66 , pp. 3492-3500
    • Weldingh, K.1    Rosenkrands, I.2    Jacobsen, S.3    Rasmussen, P.B.4    Elhay, M.J.5    Andersen, P.6
  • 196
    • 31344443334 scopus 로고    scopus 로고
    • Ligand-responsive transcriptional regulation by members of the MarR family of winged helix proteins
    • Wilkinson, S. P., and Grove, A., 2006, Ligand-responsive transcriptional regulation by members of the MarR family of winged helix proteins. Curr. Issues Mol. Biol. 8: 51-62.
    • (2006) Curr. Issues Mol. Biol , vol.8 , pp. 51-62
    • Wilkinson, S.P.1    Grove, A.2
  • 198
    • 0031733825 scopus 로고    scopus 로고
    • Antisense RNA to ahpC, an oxidative stress defence gene involved in isoniazid resistance, indicates that AhpC of Mycobacterium bovis has virulence properties
    • Wilson, T., de lisle, G. W., Marcinkeviciene, J. A., Blanchard, J. S., and Collins, D. M., 1998, Antisense RNA to ahpC, an oxidative stress defence gene involved in isoniazid resistance, indicates that AhpC of Mycobacterium bovis has virulence properties. Microbiol. 144: 2687-2695.
    • (1998) Microbiol , vol.144 , pp. 2687-2695
    • Wilson, T.1    de lisle, G.W.2    Marcinkeviciene, J.A.3    Blanchard, J.S.4    Collins, D.M.5
  • 199
    • 10844248477 scopus 로고    scopus 로고
    • Human peripheral and gastric lymphocyte responses to Helicobacter pylori NapA and AhpC differ in infected and uninfected individuals
    • Windle, H. J., Ang, Y. S., Athie-Morales, V., McManus, R., and Kelleher, D., 2006, Human peripheral and gastric lymphocyte responses to Helicobacter pylori NapA and AhpC differ in infected and uninfected individuals. Gut 54: 25-32.
    • (2006) Gut , vol.54 , pp. 25-32
    • Windle, H.J.1    Ang, Y.S.2    Athie-Morales, V.3    McManus, R.4    Kelleher, D.5
  • 200
    • 0037197672 scopus 로고    scopus 로고
    • Dimers to doughnuts: Redox-sensitive oligomerization of 2-cysteine peroxiredoxins
    • Wood, Z. A., Poole, L. B., Hantgan, R. R., and Karpus, A. P., 2002, Dimers to doughnuts: redox-sensitive oligomerization of 2-cysteine peroxiredoxins. Biochemistry 41: 5493-5504.
    • (2002) Biochemistry , vol.41 , pp. 5493-5504
    • Wood, Z.A.1    Poole, L.B.2    Hantgan, R.R.3    Karpus, A.P.4
  • 202
    • 0026608021 scopus 로고
    • Cloning and expression of the gene for the Avi-3 antigen of Mycobacterium avium and mapping of its epitopes
    • Yamaguchi, R., Matsuo, K., Yamazaki, A., Takahashi, M., Fukasawa, Y., Wada, M., and Abe, C., 1992, Cloning and expression of the gene for the Avi-3 antigen of Mycobacterium avium and mapping of its epitopes. Infect. Immun. 60: 1210-1216.
    • (1992) Infect. Immun , vol.60 , pp. 1210-1216
    • Yamaguchi, R.1    Matsuo, K.2    Yamazaki, A.3    Takahashi, M.4    Fukasawa, Y.5    Wada, M.6    Abe, C.7
  • 203
    • 0034319185 scopus 로고    scopus 로고
    • Molecular biology of oxygen tolerance in lactic acid bacteria: Functions of NADH oxidases and Dpr in oxidative stress
    • Yamamoto, Y., 2000a, Molecular biology of oxygen tolerance in lactic acid bacteria: Functions of NADH oxidases and Dpr in oxidative stress. Biosci Biotech Biochem 90: 484-493.
    • (2000) Biosci Biotech Biochem , vol.90 , pp. 484-493
    • Yamamoto, Y.1
  • 204
    • 0034046747 scopus 로고    scopus 로고
    • Role of the dpr product in oxygen tolerance in Streptococcus mutans
    • Yamamoto, Y., Higuchi, M., Poole, L. B., and Kamio, Y., 2000b, Role of the dpr product in oxygen tolerance in Streptococcus mutans. J. Bacteriol. 182: 3740-3747.
    • (2000) J. Bacteriol , vol.182 , pp. 3740-3747
    • Yamamoto, Y.1    Higuchi, M.2    Poole, L.B.3    Kamio, Y.4
  • 205
    • 0036200214 scopus 로고    scopus 로고
    • Reactive nitrogen and oxygen intermediates and bacterial defenses: Unusual adaptations in Mycobacterium tuberculosis
    • Zarht, T. C., and Deretic, V., 2002, Reactive nitrogen and oxygen intermediates and bacterial defenses: unusual adaptations in Mycobacterium tuberculosis. Antioxid. Redox Signal. 4: 141-159.
    • (2002) Antioxid. Redox Signal , vol.4 , pp. 141-159
    • Zarht, T.C.1    Deretic, V.2
  • 206
    • 0029830769 scopus 로고    scopus 로고
    • Molecular basis for the exquisite sensitivity of Mycobacterium tuberculosis to isoniazid
    • Zhang, Y., Dhandayuthapani, S., and Deretic, V., 1996, Molecular basis for the exquisite sensitivity of Mycobacterium tuberculosis to isoniazid. Proc. Natl. Acad. Sci. USA 93: 13212-13216.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13212-13216
    • Zhang, Y.1    Dhandayuthapani, S.2    Deretic, V.3
  • 208
    • 33645551821 scopus 로고    scopus 로고
    • Hydrogen peroxidemediated isoniazid activation catalyzed by Mycobacterium tuberculosis catalase-peroxidase (KatG) and its S315T mutant
    • Zhao, X., Yu, H., Yu, S., Wang, F., Sacchettini, J. C., and Magliozzo, R. S., 2006, Hydrogen peroxidemediated isoniazid activation catalyzed by Mycobacterium tuberculosis catalase-peroxidase (KatG) and its S315T mutant. Biochemistry 45: 4131-4140.
    • (2006) Biochemistry , vol.45 , pp. 4131-4140
    • Zhao, X.1    Yu, H.2    Yu, S.3    Wang, F.4    Sacchettini, J.C.5    Magliozzo, R.S.6
  • 209
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • Zheng, M., Aslund, F., and Storz, G., 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
  • 210
    • 0033991496 scopus 로고    scopus 로고
    • Redox sensing by prokaryotic transcription factors
    • Zheng, M., and Storz, G., 2000, Redox sensing by prokaryotic transcription factors. Biochem. Pharmacol. 59: 1-6.
    • (2000) Biochem. Pharmacol , vol.59 , pp. 1-6
    • Zheng, M.1    Storz, G.2
  • 211
    • 0034943657 scopus 로고    scopus 로고
    • Computation-directed identification of OxyR DNA binding sites in Escherichia coli
    • Zheng, M., Wang, X., Doan, B., Lewis, K. A., and Schneider, T. D., 2001a, Computation-directed identification of OxyR DNA binding sites in Escherichia coli. J. Bacteriol. 183: 4571-4591.
    • (2001) J. Bacteriol , vol.183 , pp. 4571-4591
    • Zheng, M.1    Wang, X.2    Doan, B.3    Lewis, K.A.4    Schneider, T.D.5
  • 212
    • 0034932337 scopus 로고    scopus 로고
    • DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide
    • Zheng, M., Wang, X., Templeton, L. J., Smulski, D. R., LaRossa, R. A., and Storz, G., 2001b, DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide. J. Bacteriol. 183: 4562-4570.
    • (2001) J. Bacteriol , vol.183 , pp. 4562-4570
    • Zheng, M.1    Wang, X.2    Templeton, L.J.3    Smulski, D.R.4    LaRossa, R.A.5    Storz, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.