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Volumn 97, Issue 6, 2013, Pages 2563-2573

Effect of combined oxidative and nitrosative stresses on Staphylococcus aureus transcriptome

Author keywords

Nitrosative stress; Oxidative stress; Staphylococcus aureus; Transcriptome

Indexed keywords

INNATE IMMUNE SYSTEMS; NITROSATIVE STRESS; REGULATORY FUNCTIONS; S-NITROSOGLUTATHIONE; STAPHYLOCOCCUS AUREUS; TRANSCRIPTIONAL LEVELS; TRANSCRIPTIONAL RESPONSE; TRANSCRIPTOMES;

EID: 84878846133     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-013-4730-3     Document Type: Article
Times cited : (33)

References (50)
  • 1
    • 0034725724 scopus 로고    scopus 로고
    • Phagocytes and oxidative stress
    • 10.1016/S0002-9343(00)00481-2 1:CAS:528:DC%2BD3cXlsFChsLg%3D
    • Babior BM (2000) Phagocytes and oxidative stress. Am J Med 109(1):33-44
    • (2000) Am J Med , vol.109 , Issue.1 , pp. 33-44
    • Babior, B.M.1
  • 2
    • 84863993865 scopus 로고    scopus 로고
    • Oxidative stress modulates the nitric oxide defense promoted by Escherichia coli flavorubredoxin
    • 10.1128/JB.00140-12 1:CAS:528:DC%2BC38XhtVGnsLvP
    • Baptista JM, Justino MC, Melo AM, Teixeira M, Saraiva LM (2012) Oxidative stress modulates the nitric oxide defense promoted by Escherichia coli flavorubredoxin. J Bacteriol 194(14):3611-3617
    • (2012) J Bacteriol , vol.194 , Issue.14 , pp. 3611-3617
    • Baptista, J.M.1    Justino, M.C.2    Melo, A.M.3    Teixeira, M.4    Saraiva, L.M.5
  • 3
    • 54249096108 scopus 로고    scopus 로고
    • Pathogenomics of the staphylococci: Insights into niche adaptation and the emergence of new virulent strains
    • 10.1111/j.1574-6968.2008.01384.x 1:CAS:528:DC%2BD1cXhsVOhu7bJ
    • Ben Zakour NL, Guinane CM, Fitzgerald JR (2008) Pathogenomics of the staphylococci: insights into niche adaptation and the emergence of new virulent strains. FEMS Microbiol Lett 289(1):1-12
    • (2008) FEMS Microbiol Lett , vol.289 , Issue.1 , pp. 1-12
    • Ben Zakour, N.L.1    Guinane, C.M.2    Fitzgerald, J.R.3
  • 4
    • 0037316303 scopus 로고    scopus 로고
    • A comparison of normalization methods for high density oligonucleotide array data based on variance and bias
    • 10.1093/bioinformatics/19.2.185 1:CAS:528:DC%2BD3sXitlCnsL4%3D
    • Bolstad BM, Irizarry RA, Astrand M, Speed TP (2003) A comparison of normalization methods for high density oligonucleotide array data based on variance and bias. Bioinformatics 19(2):185-193
    • (2003) Bioinformatics , vol.19 , Issue.2 , pp. 185-193
    • Bolstad, B.M.1    Irizarry, R.A.2    Astrand, M.3    Speed, T.P.4
  • 5
    • 0037565104 scopus 로고    scopus 로고
    • The SmtB/ArsR family of metalloregulatory transcriptional repressors: Structural insights into prokaryotic metal resistance
    • 10.1016/S0168-6445(03)00054-8 1:CAS:528:DC%2BD3sXksVOltrY%3D
    • Busenlehner LS, Pennella MA, Giedroc DP (2003) The SmtB/ArsR family of metalloregulatory transcriptional repressors: structural insights into prokaryotic metal resistance. FEMS Microbiol Rev 27(2-3):131-143
    • (2003) FEMS Microbiol Rev , vol.27 , Issue.2-3 , pp. 131-143
    • Busenlehner, L.S.1    Pennella, M.A.2    Giedroc, D.P.3
  • 6
    • 32444433730 scopus 로고    scopus 로고
    • Global transcriptome analysis of Staphylococcus aureus response to hydrogen peroxide
    • 10.1128/JB.188.4.1648-1659.2006 1:CAS:528:DC%2BD28Xhs1Glsbs%3D
    • Chang W, Small DA, Toghrol F, Bentley WE (2006) Global transcriptome analysis of Staphylococcus aureus response to hydrogen peroxide. J Bacteriol 188(4):1648-1659
    • (2006) J Bacteriol , vol.188 , Issue.4 , pp. 1648-1659
    • Chang, W.1    Small, D.A.2    Toghrol, F.3    Bentley, W.E.4
  • 7
    • 33846252282 scopus 로고    scopus 로고
    • Complete and SOS-mediated response of Staphylococcus aureus to the antibiotic ciprofloxacin
    • 10.1128/JB.01464-06 1:CAS:528:DC%2BD2sXpt1WrsQ%3D%3D
    • Cirz RT, Jones MB, Gingles NA, Minogue TD, Jarrahi B, Peterson SN, Romesberg FE (2007) Complete and SOS-mediated response of Staphylococcus aureus to the antibiotic ciprofloxacin. J Bacteriol 189(2):531-539
    • (2007) J Bacteriol , vol.189 , Issue.2 , pp. 531-539
    • Cirz, R.T.1    Jones, M.B.2    Gingles, N.A.3    Minogue, T.D.4    Jarrahi, B.5    Peterson, S.N.6    Romesberg, F.E.7
  • 8
    • 0033056490 scopus 로고    scopus 로고
    • Characterization of the major superoxide dismutase of Staphylococcus aureus and its role in starvation survival, stress resistance, and pathogenicity
    • 1:CAS:528:DyaK1MXktFCisro%3D
    • Clements MO, Watson SP, Foster SJ (1999) Characterization of the major superoxide dismutase of Staphylococcus aureus and its role in starvation survival, stress resistance, and pathogenicity. J Bacteriol 181(13):3898-3903
    • (1999) J Bacteriol , vol.181 , Issue.13 , pp. 3898-3903
    • Clements, M.O.1    Watson, S.P.2    Foster, S.J.3
  • 9
    • 33846561089 scopus 로고    scopus 로고
    • Catalase (KatA) and alkyl hydroperoxide reductase (AhpC) have compensatory roles in peroxide stress resistance and are required for survival, persistence, and nasal colonization in Staphylococcus aureus
    • 10.1128/JB.01524-06 1:CAS:528:DC%2BD2sXht1ehtbs%3D
    • Cosgrove K, Coutts G, Jonsson IM, Tarkowski A, Kokai-Kun JF, Mond JJ, Foster SJ (2007) Catalase (KatA) and alkyl hydroperoxide reductase (AhpC) have compensatory roles in peroxide stress resistance and are required for survival, persistence, and nasal colonization in Staphylococcus aureus. J Bacteriol 189(3):1025-1035
    • (2007) J Bacteriol , vol.189 , Issue.3 , pp. 1025-1035
    • Cosgrove, K.1    Coutts, G.2    Jonsson, I.M.3    Tarkowski, A.4    Kokai-Kun, J.F.5    Mond, J.J.6    Foster, S.J.7
  • 10
    • 0030969403 scopus 로고    scopus 로고
    • Siderophore production by Staphylococcus aureus and identification of iron-regulated proteins
    • 1:CAS:528:DyaK2sXjtVKqu7c%3D
    • Courcol RJ, Trivier D, Bissinger MC, Martin GR, Brown MR (1997) Siderophore production by Staphylococcus aureus and identification of iron-regulated proteins. Infect Immun 65(5):1944-1948
    • (1997) Infect Immun , vol.65 , Issue.5 , pp. 1944-1948
    • Courcol, R.J.1    Trivier, D.2    Bissinger, M.C.3    Martin, G.R.4    Brown, M.R.5
  • 11
    • 84858001273 scopus 로고    scopus 로고
    • When oxygen runs short: The microenvironment drives host-pathogen interactions
    • 10.1016/j.micinf.2011.11.003
    • Dietza I, Jerchela S, Szaszáka M, Shimaa K, Rupp J (2012) When oxygen runs short: the microenvironment drives host-pathogen interactions. Microbes Infect 14(4):311-316
    • (2012) Microbes Infect , vol.14 , Issue.4 , pp. 311-316
    • Dietza, I.1    Jerchela, S.2    Szaszáka, M.3    Shimaa, K.4    Rupp, J.5
  • 12
    • 0027661433 scopus 로고
    • Purification and chemical characterization of staphyloferrin B, a hydrophilic siderophore from staphylococci
    • 10.1007/BF00205858 1:CAS:528:DyaK2cXhvVKrt7w%3D
    • Drechsel H, Freund S, Nicholson G, Haag H, Jung O, Zahner H, Jung G (1993) Purification and chemical characterization of staphyloferrin B, a hydrophilic siderophore from staphylococci. Biometals 6(3):185-192
    • (1993) Biometals , vol.6 , Issue.3 , pp. 185-192
    • Drechsel, H.1    Freund, S.2    Nicholson, G.3    Haag, H.4    Jung, O.5    Zahner, H.6    Jung, G.7
  • 13
    • 32544450859 scopus 로고    scopus 로고
    • Effect of combined oxidative and nitrosative stress on Neisseria meningitidis
    • 1:CAS:528:DC%2BD28Xmtlygug%3D%3D
    • Dyet K, Moir J (2006) Effect of combined oxidative and nitrosative stress on Neisseria meningitidis. Biochem Soc Trans 34(Pt 1):197-199
    • (2006) Biochem Soc Trans , vol.34 , Issue.PART 1 , pp. 197-199
    • Dyet, K.1    Moir, J.2
  • 14
    • 15444363634 scopus 로고    scopus 로고
    • Transcriptional responses of Escherichia coli to S-nitrosoglutathione under defined chemostat conditions reveal major changes in methionine biosynthesis
    • 10.1074/jbc.M410393200 1:CAS:528:DC%2BD2MXit1ektb8%3D
    • Flatley J, Barrett J, Pullan ST, Hughes MN, Green J, Poole RK (2005) Transcriptional responses of Escherichia coli to S-nitrosoglutathione under defined chemostat conditions reveal major changes in methionine biosynthesis. J Biol Chem 280(11):10065-10072
    • (2005) J Biol Chem , vol.280 , Issue.11 , pp. 10065-10072
    • Flatley, J.1    Barrett, J.2    Pullan, S.T.3    Hughes, M.N.4    Green, J.5    Poole, R.K.6
  • 15
    • 0018263443 scopus 로고
    • The biology of oxygen radicals
    • 10.1126/science.210504 1:CAS:528:DyaE1cXlvFart7g%3D
    • Fridovich I (1978) The biology of oxygen radicals. Science 201(4359):875-880
    • (1978) Science , vol.201 , Issue.4359 , pp. 875-880
    • Fridovich, I.1
  • 16
    • 0032921250 scopus 로고    scopus 로고
    • Nitric oxide and thiol groups
    • 1:CAS:528:DyaK1MXjsF2qtrg%3D
    • Gaston B (1999) Nitric oxide and thiol groups. Biochim Biophys Acta 1411(2-3):323-333
    • (1999) Biochim Biophys Acta , vol.1411 , Issue.2-3 , pp. 323-333
    • Gaston, B.1
  • 18
    • 33644895690 scopus 로고    scopus 로고
    • Flavohemoglobin requires microaerophilic conditions for nitrosative protection of Staphylococcus aureus
    • 10.1016/j.febslet.2006.02.039
    • Gonçalves VL, Nobre LS, Vicente JB, Teixeira M, Saraiva LM (2006) Flavohemoglobin requires microaerophilic conditions for nitrosative protection of Staphylococcus aureus. FEBS Lett 580(7):1817-1821
    • (2006) FEBS Lett , vol.580 , Issue.7 , pp. 1817-1821
    • Gonçalves, V.L.1    Nobre, L.S.2    Vicente, J.B.3    Teixeira, M.4    Saraiva, L.M.5
  • 19
    • 78049400552 scopus 로고    scopus 로고
    • Specificity of Staphyloferrin B recognition by the SirA receptor from Staphylococcus aureus
    • 10.1074/jbc.M110.172924 1:CAS:528:DC%2BC3cXhtlGktbzE
    • Grigg JC, Cheung J, Heinrichs DE, Murphy ME (2010) Specificity of Staphyloferrin B recognition by the SirA receptor from Staphylococcus aureus. J Biol Chem 285(45):34579-34588
    • (2010) J Biol Chem , vol.285 , Issue.45 , pp. 34579-34588
    • Grigg, J.C.1    Cheung, J.2    Heinrichs, D.E.3    Murphy, M.E.4
  • 20
    • 25444434412 scopus 로고    scopus 로고
    • NO-mediated cytoprotection: Instant adaptation to oxidative stress in bacteria
    • 10.1073/pnas.0504307102 1:CAS:528:DC%2BD2MXhtVOqsbvN
    • Gusarov I, Nudler E (2005) NO-mediated cytoprotection: instant adaptation to oxidative stress in bacteria. Proc Natl Acad Sci USA 102(39):13855-13860
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.39 , pp. 13855-13860
    • Gusarov, I.1    Nudler, E.2
  • 21
    • 0032985815 scopus 로고    scopus 로고
    • Identification and characterization of SirA, an iron-regulated protein from Staphylococcus aureus
    • 1:CAS:528:DyaK1MXhslWrtrk%3D
    • Heinrichs JH, Gatlin LE, Kunsch C, Choi GH, Hanson MS (1999) Identification and characterization of SirA, an iron-regulated protein from Staphylococcus aureus. J Bacteriol 181(5):1436-1443
    • (1999) J Bacteriol , vol.181 , Issue.5 , pp. 1436-1443
    • Heinrichs, J.H.1    Gatlin, L.E.2    Kunsch, C.3    Choi, G.H.4    Hanson, M.S.5
  • 22
    • 0035013928 scopus 로고    scopus 로고
    • PerR controls oxidative stress resistance and iron storage proteins and is required for virulence in Staphylococcus aureus
    • 10.1128/IAI.69.6.3744-3754.2001 1:CAS:528:DC%2BD3MXjvFyrtbc%3D
    • Horsburgh MJ, Clements MO, Crossley H, Ingham E, Foster SJ (2001a) PerR controls oxidative stress resistance and iron storage proteins and is required for virulence in Staphylococcus aureus. Infect Immun 69(6):3744-3754
    • (2001) Infect Immun , vol.69 , Issue.6 , pp. 3744-3754
    • Horsburgh, M.J.1    Clements, M.O.2    Crossley, H.3    Ingham, E.4    Foster, S.J.5
  • 23
    • 0035150765 scopus 로고    scopus 로고
    • In Staphylococcus aureus, fur is an interactive regulator with PerR, contributes to virulence, and is necessary for oxidative stress resistance through positive regulation of catalase and iron homeostasis
    • 10.1128/JB.183.2.468-475.2001 1:CAS:528:DC%2BD3MXktVOltg%3D%3D
    • Horsburgh MJ, Ingham E, Foster SJ (2001b) In Staphylococcus aureus, Fur is an interactive regulator with PerR, contributes to virulence, and is necessary for oxidative stress resistance through positive regulation of catalase and iron homeostasis. J Bacteriol 183(2):468-475
    • (2001) J Bacteriol , vol.183 , Issue.2 , pp. 468-475
    • Horsburgh, M.J.1    Ingham, E.2    Foster, S.J.3
  • 24
    • 0027481965 scopus 로고
    • The reaction of NO with superoxide
    • 10.3109/10715769309145868 1:CAS:528:DyaK3sXmsVeit74%3D
    • Huie RE, Padmaja S (1993) The reaction of NO with superoxide. Free Radic Res Commun 18(4):195-199
    • (1993) Free Radic Res Commun , vol.18 , Issue.4 , pp. 195-199
    • Huie, R.E.1    Padmaja, S.2
  • 26
    • 33847753939 scopus 로고    scopus 로고
    • Micromolar intracellular hydrogen peroxide disrupts metabolism by damaging iron-sulfur enzymes
    • 10.1074/jbc.M607646200 1:CAS:528:DC%2BD2sXit1Oitw%3D%3D
    • Jang S, Imlay JA (2007) Micromolar intracellular hydrogen peroxide disrupts metabolism by damaging iron-sulfur enzymes. J Biol Chem 282(2):929-937
    • (2007) J Biol Chem , vol.282 , Issue.2 , pp. 929-937
    • Jang, S.1    Imlay, J.A.2
  • 27
    • 13244299310 scopus 로고    scopus 로고
    • New genes implicated in the protection of anaerobically grown Escherichia coli against nitric oxide
    • Justino MC, Vicente JB, Teixeira M, Saraiva LM (2005) New genes implicated in the protection of anaerobically grown Escherichia coli against nitric oxide. J Biol Chem 280(4):2636-2643
    • (2005) J Biol Chem , vol.280 , Issue.4 , pp. 2636-2643
    • Justino, M.C.1    Vicente, J.B.2    Teixeira, M.3    Saraiva, L.M.4
  • 28
    • 0021924031 scopus 로고
    • Catalase and superoxide dismutase activities in virulent and nonvirulent Staphylococcus aureus isolates
    • 1:CAS:528:DyaL2MXhvVajtLs%3D
    • Kanafani H, Martin SE (1985) Catalase and superoxide dismutase activities in virulent and nonvirulent Staphylococcus aureus isolates. J Clin Microbiol 21(4):607-610
    • (1985) J Clin Microbiol , vol.21 , Issue.4 , pp. 607-610
    • Kanafani, H.1    Martin, S.E.2
  • 29
    • 0030052434 scopus 로고    scopus 로고
    • Effect of nitric oxide on staphylococcal killing and interactive effect with superoxide
    • 1:CAS:528:DyaK28XhtlyhtA%3D%3D
    • Kaplan SS, Lancaster JR Jr, Basford RE, Simmons RL (1996) Effect of nitric oxide on staphylococcal killing and interactive effect with superoxide. Infect Immun 64(1):69-76
    • (1996) Infect Immun , vol.64 , Issue.1 , pp. 69-76
    • Kaplan, S.S.1    Lancaster Jr., J.R.2    Basford, R.E.3    Simmons, R.L.4
  • 30
    • 0033037505 scopus 로고    scopus 로고
    • Chromosome-determined zinc-responsible operon czr in Staphylococcus aureus strain 912
    • 1:CAS:528:DyaK1MXitlejur0%3D
    • Kuroda M, Hayashi H, Ohta T (1999) Chromosome-determined zinc-responsible operon czr in Staphylococcus aureus strain 912. Microbiol Immunol 43(2):115-125
    • (1999) Microbiol Immunol , vol.43 , Issue.2 , pp. 115-125
    • Kuroda, M.1    Hayashi, H.2    Ohta, T.3
  • 31
    • 0016660853 scopus 로고
    • Catalase, superoxide dismutase, and virulence of Staphylococcus aureus. in vitro and in vivo studies with emphasis on staphylococcal-leukocyte interaction
    • 10.1172/JCI107963 1:CAS:528:DyaE2MXht1alurc%3D
    • Mandell GL (1975) Catalase, superoxide dismutase, and virulence of Staphylococcus aureus. In vitro and in vivo studies with emphasis on staphylococcal-leukocyte interaction. J Clin Invest 55(3):561-566
    • (1975) J Clin Invest , vol.55 , Issue.3 , pp. 561-566
    • Mandell, G.L.1
  • 32
    • 78650038011 scopus 로고    scopus 로고
    • Peroxynitrite stress is exacerbated by flavohaemoglobin-derived oxidative stress in Salmonella typhimurium and is relieved by nitric oxide
    • 10.1099/mic.0.044214-0 1:CAS:528:DC%2BC3cXhs1arsb7L
    • McLean S, Bowman LA, Poole RK (2010) Peroxynitrite stress is exacerbated by flavohaemoglobin-derived oxidative stress in Salmonella typhimurium and is relieved by nitric oxide. Microbiology 156(Pt 12):3556-3565
    • (2010) Microbiology , vol.156 , Issue.PART 12 , pp. 3556-3565
    • McLean, S.1    Bowman, L.A.2    Poole, R.K.3
  • 33
    • 0025707185 scopus 로고
    • Isolation and characterization of staphyloferrin A, a compound with siderophore activity from Staphylococcus hyicus DSM 20459
    • 10.1111/j.1574-6968.1990.tb13863.x 1:STN:280:DyaK3c3ivVOrsQ%3D%3D
    • Meiwes J, Fiedler HP, Haag H, Zahner H, Konetschny-Rapp S, Jung G (1990) Isolation and characterization of staphyloferrin A, a compound with siderophore activity from Staphylococcus hyicus DSM 20459. FEMS Microbiol Lett 55(1-2):201-205
    • (1990) FEMS Microbiol Lett , vol.55 , Issue.1-2 , pp. 201-205
    • Meiwes, J.1    Fiedler, H.P.2    Haag, H.3    Zahner, H.4    Konetschny-Rapp, S.5    Jung, G.6
  • 36
    • 1842558966 scopus 로고    scopus 로고
    • Characterization of virulence factor regulation by SrrAB, a two-component system in Staphylococcus aureus
    • 10.1128/JB.186.8.2430-2438.2004 1:CAS:528:DC%2BD2cXjsV2isr4%3D
    • Pragman AA, Yarwood JM, Tripp TJ, Schlievert PM (2004) Characterization of virulence factor regulation by SrrAB, a two-component system in Staphylococcus aureus. J Bacteriol 186(8):2430-2438
    • (2004) J Bacteriol , vol.186 , Issue.8 , pp. 2430-2438
    • Pragman, A.A.1    Yarwood, J.M.2    Tripp, T.J.3    Schlievert, P.M.4
  • 37
    • 33749572203 scopus 로고    scopus 로고
    • Intracellular innate resistance to bacterial pathogens
    • 10.1111/j.1462-5822.2006.00795.x 1:CAS:528:DC%2BD28XhtFOkurbO
    • Radtke AL, O'Riordan MX (2006) Intracellular innate resistance to bacterial pathogens. Cell Microbiol 8(11):1720-1729
    • (2006) Cell Microbiol , vol.8 , Issue.11 , pp. 1720-1729
    • Radtke, A.L.1    O'Riordan, M.X.2
  • 38
    • 33746482772 scopus 로고    scopus 로고
    • The nitrosative stress response of Staphylococcus aureus is required for resistance to innate immunity
    • 10.1111/j.1365-2958.2006.05290.x 1:CAS:528:DC%2BD28XovVWmt7o%3D
    • Richardson AR, Dunman PM, Fang FC (2006) The nitrosative stress response of Staphylococcus aureus is required for resistance to innate immunity. Mol Microbiol 61(4):927-939
    • (2006) Mol Microbiol , vol.61 , Issue.4 , pp. 927-939
    • Richardson, A.R.1    Dunman, P.M.2    Fang, F.C.3
  • 39
    • 41149096672 scopus 로고    scopus 로고
    • A nitric oxide-inducible lactate dehydrogenase enables Staphylococcus aureus to resist innate immunity
    • 10.1126/science.1155207 1:CAS:528:DC%2BD1cXjsVamtbs%3D
    • Richardson AR, Libby SJ, Fang FC (2008) A nitric oxide-inducible lactate dehydrogenase enables Staphylococcus aureus to resist innate immunity. Science 319(5870):1672-1676
    • (2008) Science , vol.319 , Issue.5870 , pp. 1672-1676
    • Richardson, A.R.1    Libby, S.J.2    Fang, F.C.3
  • 40
    • 7244262073 scopus 로고    scopus 로고
    • The role of the flavodiiron proteins in microbial nitric oxide detoxification
    • 10.1016/S0065-2911(04)49002-X 1:CAS:528:DC%2BD2cXhtVaksrrO
    • Saraiva LM, Vicente JB, Teixeira M (2004) The role of the flavodiiron proteins in microbial nitric oxide detoxification. Adv Microb Physiol 49:77-129
    • (2004) Adv Microb Physiol , vol.49 , pp. 77-129
    • Saraiva, L.M.1    Vicente, J.B.2    Teixeira, M.3
  • 41
    • 0023127806 scopus 로고
    • Universal chemical assay for the detection and determination of siderophores
    • 10.1016/0003-2697(87)90612-9 1:CAS:528:DyaL2sXhtFKjurs%3D
    • Schwyn B, Neilands JB (1987) Universal chemical assay for the detection and determination of siderophores. Anal Biochem 160(1):47-56
    • (1987) Anal Biochem , vol.160 , Issue.1 , pp. 47-56
    • Schwyn, B.1    Neilands, J.B.2
  • 42
    • 65549146791 scopus 로고    scopus 로고
    • A novel nitroreductase of Staphylococcus aureus with S-nitrosoglutathione reductase activity
    • 10.1128/JB.00022-09 1:CAS:528:DC%2BD1MXmt1Cksbo%3D
    • Tavares AF, Nobre LS, Melo AM, Saraiva LM (2009) A novel nitroreductase of Staphylococcus aureus with S-nitrosoglutathione reductase activity. J Bacteriol 191(10):3403-3406
    • (2009) J Bacteriol , vol.191 , Issue.10 , pp. 3403-3406
    • Tavares, A.F.1    Nobre, L.S.2    Melo, A.M.3    Saraiva, L.M.4
  • 43
    • 33847658682 scopus 로고    scopus 로고
    • Mitochondrial aconitase reaction with nitric oxide, S-nitrosoglutathione, and peroxynitrite: Mechanisms and relative contributions to aconitase inactivation
    • 10.1016/j.freeradbiomed.2007.01.007 1:CAS:528:DC%2BD2sXivVantLs%3D
    • Tortora V, Quijano C, Freeman B, Radi R, Castro L (2007) Mitochondrial aconitase reaction with nitric oxide, S-nitrosoglutathione, and peroxynitrite: mechanisms and relative contributions to aconitase inactivation. Free Radic Biol Med 42(7):1075-1088
    • (2007) Free Radic Biol Med , vol.42 , Issue.7 , pp. 1075-1088
    • Tortora, V.1    Quijano, C.2    Freeman, B.3    Radi, R.4    Castro, L.5
  • 44
    • 0040731249 scopus 로고    scopus 로고
    • Construction of a ferritin-deficient mutant of Campylobacter jejuni: Contribution of ferritin to iron storage and protection against oxidative stress
    • 10.1111/j.1365-2958.1996.tb02633.x 1:CAS:528:DyaK28XktFWht70%3D
    • Wai SN, Nakayama K, Umene K, Moriya T, Amako K (1996) Construction of a ferritin-deficient mutant of Campylobacter jejuni: contribution of ferritin to iron storage and protection against oxidative stress. Mol Microbiol 20(6):1127-1134
    • (1996) Mol Microbiol , vol.20 , Issue.6 , pp. 1127-1134
    • Wai, S.N.1    Nakayama, K.2    Umene, K.3    Moriya, T.4    Amako, K.5
  • 45
    • 84863812853 scopus 로고    scopus 로고
    • PerR-mediated oxidative stress response in Staphylococcus aureus
    • 10.5812/jjm.2460
    • Wakabayashi JYI, Cheng DW (2012) PerR-mediated oxidative stress response in Staphylococcus aureus. Jundishapur J Microbiol 5(4):443-449
    • (2012) Jundishapur J Microbiol , vol.5 , Issue.4 , pp. 443-449
    • Wakabayashi, J.Y.I.1    Cheng, D.W.2
  • 46
    • 0026544871 scopus 로고
    • KdpD and KdpE, proteins that control expression of the kdpABC operon, are members of the two-component sensor-effector class of regulators
    • 1:CAS:528:DyaK3sXhvVKjtL4%3D
    • Walderhaug MO, Polarek JW, Voelkner P, Daniel JM, Hesse JE, Altendorf K, Epstein W (1992) KdpD and KdpE, proteins that control expression of the kdpABC operon, are members of the two-component sensor-effector class of regulators. J Bacteriol 174(7):2152-2159
    • (1992) J Bacteriol , vol.174 , Issue.7 , pp. 2152-2159
    • Walderhaug, M.O.1    Polarek, J.W.2    Voelkner, P.3    Daniel, J.M.4    Hesse, J.E.5    Altendorf, K.6    Epstein, W.7
  • 47
    • 0027381424 scopus 로고
    • Nitric oxide protects against cellular damage and cytotoxicity from reactive oxygen species
    • 10.1073/pnas.90.21.9813 1:CAS:528:DyaK2cXivVOnug%3D%3D
    • Wink DA, Hanbauer I, Krishna MC, DeGraff W, Gamson J, Mitchell JB (1993) Nitric oxide protects against cellular damage and cytotoxicity from reactive oxygen species. Proc Natl Acad Sci USA 90(21):9813-9817
    • (1993) Proc Natl Acad Sci USA , vol.90 , Issue.21 , pp. 9813-9817
    • Wink, D.A.1    Hanbauer, I.2    Krishna, M.C.3    Degraff, W.4    Gamson, J.5    Mitchell, J.B.6
  • 48
    • 49749101196 scopus 로고    scopus 로고
    • Proteomic analysis of antioxidant strategies of Staphylococcus aureus: Diverse responses to different oxidants
    • 10.1002/pmic.200701062 1:CAS:528:DC%2BD1cXhtVehsbjI
    • Wolf C, Hochgräfe F, Kusch H, Albrecht D, Hecker M, Engelmann S (2008) Proteomic analysis of antioxidant strategies of Staphylococcus aureus: diverse responses to different oxidants. Proteomics 8(15):3139-3153
    • (2008) Proteomics , vol.8 , Issue.15 , pp. 3139-3153
    • Wolf, C.1    Hochgräfe, F.2    Kusch, H.3    Albrecht, D.4    Hecker, M.5    Engelmann, S.6
  • 49
    • 0038046842 scopus 로고    scopus 로고
    • A mechanism by which nitric oxide accelerates the rate of oxidative DNA damage in Escherichia coli
    • 10.1046/j.1365-2958.2003.03530.x 1:CAS:528:DC%2BD3sXlsVersLk%3D
    • Woodmansee AN, Imlay JA (2003) A mechanism by which nitric oxide accelerates the rate of oxidative DNA damage in Escherichia coli. Mol Microbiol 49(1):11-22
    • (2003) Mol Microbiol , vol.49 , Issue.1 , pp. 11-22
    • Woodmansee, A.N.1    Imlay, J.A.2
  • 50
    • 0034932337 scopus 로고    scopus 로고
    • DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide
    • 10.1128/JB.183.15.4562-4570.2001 1:CAS:528:DC%2BD3MXlsVens7s%3D
    • Zheng M, Wang X, Templeton LJ, Smulski DR, LaRossa RA, Storz G (2001) DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide. J Bacteriol 183(15):4562-4570
    • (2001) J Bacteriol , vol.183 , Issue.15 , pp. 4562-4570
    • Zheng, M.1    Wang, X.2    Templeton, L.J.3    Smulski, D.R.4    Larossa, R.A.5    Storz, G.6


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