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Volumn 49, Issue 2, 2011, Pages 251-256

Identification of S-nitrosylation of proteins of Helicobacter pylori in response to nitric oxide stress

Author keywords

biotin switch; Helicobacter pylori; nitric oxide; S nitrosylation

Indexed keywords

BACTERIAL PROTEIN; NITRIC OXIDE; NITROPRUSSIDE SODIUM; S NITROSOGLUTATHIONE;

EID: 79955704725     PISSN: 12258873     EISSN: 12258873     Source Type: Journal    
DOI: 10.1007/s12275-011-0262-7     Document Type: Article
Times cited : (10)

References (42)
  • 1
    • 0035108401 scopus 로고    scopus 로고
    • Essential thioredoxin-dependent peroxiredoxin system from Helicobacter pylori: genetic and kinetic characterization
    • Baker, L. M., A. Raudonikiene, P. S. Hoffman, and L. B. Poole. 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
  • 2
    • 24344459117 scopus 로고    scopus 로고
    • Identification of a new sialic acid-binding protein in Helicobacter pylori
    • Bennett, H. J. and I. S. Roberts. 2005. Identification of a new sialic acid-binding protein in Helicobacter pylori. FEMS. Immunol. Med. Microbiol. 44, 163-169.
    • (2005) FEMS. Immunol. Med. Microbiol. , vol.44 , pp. 163-169
    • Bennett, H.J.1    Roberts, I.S.2
  • 3
    • 0034648827 scopus 로고    scopus 로고
    • Peroxynitrite reductase activity of bacterial peroxiredoxins
    • Bryk, R., P. Griffin, and C. Nathan. 2000. Peroxynitrite reductase activity of bacterial peroxiredoxins. Nature 407, 211-215.
    • (2000) Nature , vol.407 , pp. 211-215
    • Bryk, R.1    Griffin, P.2    Nathan, C.3
  • 4
    • 47249142931 scopus 로고    scopus 로고
    • Analysis of growth phase-dependent proteome profiles reveals differential regulation of mRNA and protein in Helicobacter pylori
    • Choi, Y. W., S. A. Park, H. W. Lee, D. S. Kim, and N. G. Lee. 2008. Analysis of growth phase-dependent proteome profiles reveals differential regulation of mRNA and protein in Helicobacter pylori. Proteomics 8, 2665-2675.
    • (2008) Proteomics , vol.8 , pp. 2665-2675
    • Choi, Y.W.1    Park, S.A.2    Lee, H.W.3    Kim, D.S.4    Lee, N.G.5
  • 5
    • 27144493317 scopus 로고    scopus 로고
    • Proteomic analysis of proteins expressed by Helicobacter pylori under oxidative stress
    • Chuang, M. H., M. S. Wu, J. T. Lin, and S. H. Chiou. 2005. Proteomic analysis of proteins expressed by Helicobacter pylori under oxidative stress. Proteomics 5, 3895-3901.
    • (2005) Proteomics , vol.5 , pp. 3895-3901
    • Chuang, M.H.1    Wu, M.S.2    Lin, J.T.3    Chiou, S.H.4
  • 6
    • 0032724005 scopus 로고    scopus 로고
    • Effect of nitric oxide on Helicobacter pylori morphology
    • Cole, S. P., V. F. Kharitonov, and D. G. Guiney. 1999. Effect of nitric oxide on Helicobacter pylori morphology. J. Infect. Dis. 180, 1713-1717.
    • (1999) J. Infect. Dis. , vol.180 , pp. 1713-1717
    • Cole, S.P.1    Kharitonov, V.F.2    Guiney, D.G.3
  • 7
    • 0030822346 scopus 로고    scopus 로고
    • Roles for the two cysteine residues of AhpC in catalysis of peroxide reduction by alkyl hydroperoxide reductase from Salmonella typhimurium
    • Ellis, H. R. and L. B. Poole. 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) Biochemistry , vol.36 , pp. 13349-13356
    • Ellis, H.R.1    Poole, L.B.2
  • 8
    • 32244449093 scopus 로고    scopus 로고
    • Influence of culture medium on the resistance and response of Mycobacterium bovis BCG to reactive nitrogen intermediates
    • Florio, W., G. Batoni, S. Esin, D. Bottai, G. Maisetta, F. Favilli, F. L. Brancatisano, and M. Campa. 2004. Influence of culture medium on the resistance and response of Mycobacterium bovis BCG to reactive nitrogen intermediates. Microbes Infect. 8, 434-441.
    • (2004) Microbes Infect. , vol.8 , pp. 434-441
    • Florio, W.1    Batoni, G.2    Esin, S.3    Bottai, D.4    Maisetta, G.5    Favilli, F.6    Brancatisano, F.L.7    Campa, M.8
  • 9
    • 58049124883 scopus 로고    scopus 로고
    • Detection of protein S-nitrosylation with the biotin-switch technique
    • Forrester, M. T., M. W. Foster, M. Benhar, and J. S. Stamler. 2009. Detection of protein S-nitrosylation with the biotin-switch technique. Free Radic. Biol. Med. 46, 119-126.
    • (2009) Free Radic. Biol. Med. , vol.46 , pp. 119-126
    • Forrester, M.T.1    Foster, M.W.2    Benhar, M.3    Stamler, J.S.4
  • 10
    • 34347268109 scopus 로고    scopus 로고
    • Assessment and application of the biotin switch technique for examining protein S-nitrosylation under conditions of pharmacologically induced oxidative stress
    • Forrester, M. T., M. W. Foster, and J. S. Stamler. 2007. Assessment and application of the biotin switch technique for examining protein S-nitrosylation under conditions of pharmacologically induced oxidative stress. J. Biol. Chem. 282, 13977-13983.
    • (2007) J. Biol. Chem. , vol.282 , pp. 13977-13983
    • Forrester, M.T.1    Foster, M.W.2    Stamler, J.S.3
  • 11
    • 33646907087 scopus 로고    scopus 로고
    • GroEL-GroESmediated protein folding
    • Horwich, A. L., G. W. Farr, and W. A. Fenton. 2006. GroEL-GroESmediated protein folding. Chem. Rev. 106, 1917-1930.
    • (2006) Chem. Rev. , vol.106 , pp. 1917-1930
    • Horwich, A.L.1    Farr, G.W.2    Fenton, W.A.3
  • 12
    • 33746070773 scopus 로고    scopus 로고
    • An ascorbate-dependent artifact that interferes with the interpretation of the biotin switch assay
    • Huang, B. and C. Chen. 2006. An ascorbate-dependent artifact that interferes with the interpretation of the biotin switch assay. Free Radic Biol. Med. 15, 562-567.
    • (2006) Free Radic Biol. Med. , vol.15 , pp. 562-567
    • Huang, B.1    Chen, C.2
  • 13
    • 0035849715 scopus 로고    scopus 로고
    • The biotin switch method for the detection of S-nitrosylated proteins
    • Jaffrey, S. R. and S. H. Snyder. 2001. The biotin switch method for the detection of S-nitrosylated proteins. Sci. STKE. 86, pl1.
    • (2001) Sci. STKE. , vol.86
    • Jaffrey, S.R.1    Snyder, S.H.2
  • 15
    • 0033929063 scopus 로고    scopus 로고
    • Helicobacter pylori urease suppresses bactericidal activity of peroxynitrite via carbon dioxide production
    • Kuwahara, H., Y. Miyamoto, T. Akaike, T. Kubota, T. Sawa, S. Okamoto, and H. Maeda. 2000. Helicobacter pylori urease suppresses bactericidal activity of peroxynitrite via carbon dioxide production. Infect. Immun. 68, 4378-4383.
    • (2000) Infect. Immun. , vol.68 , pp. 4378-4383
    • Kuwahara, H.1    Miyamoto, Y.2    Akaike, T.3    Kubota, T.4    Sawa, T.5    Okamoto, S.6    Maeda, H.7
  • 17
    • 62449084925 scopus 로고    scopus 로고
    • Expression of recombinant human FADD, preparation of its polyclonal antiserum and the application in immunoassays
    • Marikar, F. M., D. Ma, J. Ye, B. Tang, W. Zheng, J. Zhang, M. Lu, and Z. Hua. 2008. Expression of recombinant human FADD, preparation of its polyclonal antiserum and the application in immunoassays. Cell. Mol. Immunol. 5, 471-474.
    • (2008) Cell. Mol. Immunol. , vol.5 , pp. 471-474
    • Marikar, F.M.1    Ma, D.2    Ye, J.3    Tang, B.4    Zheng, W.5    Zhang, J.6    Lu, M.7    Hua, Z.8
  • 18
    • 0026701685 scopus 로고
    • Site-directed mutagenesis of the active site cysteine in Klebsiella aerogenes urease
    • Martin, P. R. and R. P. Hausinger. 1992. Site-directed mutagenesis of the active site cysteine in Klebsiella aerogenes urease. J. Biol. Chem. 267, 20024-20027.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20024-20027
    • Martin, P.R.1    Hausinger, R.P.2
  • 19
    • 1042267391 scopus 로고    scopus 로고
    • Detection and proteomic identification of S-nitrosylated proteins in endothelial cells
    • Martínez-Ruiz, A. and S. Lamas. 2004. Detection and proteomic identification of S-nitrosylated proteins in endothelial cells. Arch. Biochem. Biophys. 423, 192-199.
    • (2004) Arch. Biochem. Biophys. , vol.423 , pp. 192-199
    • Martínez-Ruiz, A.1    Lamas, S.2
  • 20
    • 0034053637 scopus 로고    scopus 로고
    • Pathogenesis of Helicobacter pylori infection
    • McGee, D. J. and H. L. Mobley. 2000. Pathogenesis of Helicobacter pylori infection. Curr. Opin. Gastroenterol. 16, 24-31.
    • (2000) Curr. Opin. Gastroenterol. , vol.16 , pp. 24-31
    • McGee, D.J.1    Mobley, H.L.2
  • 21
    • 0031707478 scopus 로고    scopus 로고
    • Urease plays an important role in the chemotactic motility of Helicobacter pylori in a viscous environment
    • Nakamura, H., H. Yoshiyama, H. Takeuchi, T. Mizote, K. Okita, and T. Nakazawa. 1998. Urease plays an important role in the chemotactic motility of Helicobacter pylori in a viscous environment. Infect. Immun. 66, 4832-4837.
    • (1998) Infect. Immun. , vol.66 , pp. 4832-4837
    • Nakamura, H.1    Yoshiyama, H.2    Takeuchi, H.3    Mizote, T.4    Okita, K.5    Nakazawa, T.6
  • 22
    • 4344691283 scopus 로고    scopus 로고
    • Decreased Helicobacter pylori associated gastric carcinogenesis in mice lacking inducible nitric oxide synthase
    • Nam, K. T., S. Y. Oh, B. Ahn, Y. B. Kim, D. D. Jang, K. H. Yang, K. B. Hahm, and D. Y. Kim. 2004. Decreased Helicobacter pylori associated gastric carcinogenesis in mice lacking inducible nitric oxide synthase. Gut 53, 1250-1255.
    • (2004) Gut , vol.53 , pp. 1250-1255
    • Nam, K.T.1    Oh, S.Y.2    Ahn, B.3    Kim, Y.B.4    Jang, D.D.5    Yang, K.H.6    Hahm, K.B.7    Kim, D.Y.8
  • 24
    • 14644387541 scopus 로고    scopus 로고
    • Nitric oxide and nitrosative stress tolerance in bacteria
    • Poole, R. K. 2005. Nitric oxide and nitrosative stress tolerance in bacteria. Biochem. Soc. Trans. 33, 176-180.
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 176-180
    • Poole, R.K.1
  • 25
    • 70350179633 scopus 로고    scopus 로고
    • Helicobacter pylori protein response to nitric oxide stress
    • Qu, W., Y. Zhou, C. Shao, Y. Sun, Q. Zhang, C. Chen, and J. Jia. 2009. Helicobacter pylori protein response to nitric oxide stress. J. Microbiol. 47, 486-493.
    • (2009) J. Microbiol. , vol.47 , pp. 486-493
    • Qu, W.1    Zhou, Y.2    Shao, C.3    Sun, Y.4    Zhang, Q.5    Chen, C.6    Jia, J.7
  • 26
    • 0035424542 scopus 로고    scopus 로고
    • Immune responses to intracellular bacteria
    • Raupach, B. and S. H. Kaufmann. 2001. Immune responses to intracellular bacteria. Curr. Opin. Immunol. 13, 417-428.
    • (2001) Curr. Opin. Immunol. , vol.13 , pp. 417-428
    • Raupach, B.1    Kaufmann, S.H.2
  • 27
    • 12244293660 scopus 로고    scopus 로고
    • S-nitroso proteome of Mycobacterium tuberculosis enzymes of intermediary metabolism and antioxidant defense
    • Rhee, K. Y., H. Erdjument-Bromage, P. Tempst, and C. F. Nathan. 2005. S-nitroso proteome of Mycobacterium tuberculosis enzymes of intermediary metabolism and antioxidant defense. Proc. Natl. Acad. Sci. USA 102, 467-472.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 467-472
    • Rhee, K.Y.1    Erdjument-Bromage, H.2    Tempst, P.3    Nathan, C.F.4
  • 28
    • 0037008715 scopus 로고    scopus 로고
    • Identification of surface proteins of Helicobacter pylori by selective biotinylation, affinity purification, and two-dimensional gel electrophoresis
    • Sabarth, N., S. Lamer, U. Zimny-Arndt, P. R. Jungblut, T. F. Meyer, and D. Bumann. 2002. Identification of surface proteins of Helicobacter pylori by selective biotinylation, affinity purification, and two-dimensional gel electrophoresis. J. Biol. Chem. 277, 27896-27902.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27896-27902
    • Sabarth, N.1    Lamer, S.2    Zimny-Arndt, U.3    Jungblut, P.R.4    Meyer, T.F.5    Bumann, D.6
  • 30
    • 0037477786 scopus 로고    scopus 로고
    • Inhibition of bacterial DNA replication by zinc mobilization during nitrosative stress
    • Schapiro, J. M., S. J. Libby, and F. C. Fang. 2003. Inhibition of bacterial DNA replication by zinc mobilization during nitrosative stress. Proc. Natl. Acad. Sci. USA 100, 8496-8501.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 8496-8501
    • Schapiro, J.M.1    Libby, S.J.2    Fang, F.C.3
  • 31
    • 0037834629 scopus 로고    scopus 로고
    • Evidence that peroxiredoxins are novel members of the thioredoxin fold superfamily
    • Schröder, E. and C. P. Ponting. 1998. Evidence that peroxiredoxins are novel members of the thioredoxin fold superfamily. Protein Sci. 7, 2465-2468.
    • (1998) Protein Sci. , vol.7 , pp. 2465-2468
    • Schröder, E.1    Ponting, C.P.2
  • 32
    • 0033958917 scopus 로고    scopus 로고
    • Expression of the Helicobacter pylori ureI gene is required for acidic pH activation of cytoplasmic urease
    • Scott, D. R., E. A. Marcus, D. L. Weeks, A. Lee, K. Melchers, and G. Sachs. 2000. Expression of the Helicobacter pylori ureI gene is required for acidic pH activation of cytoplasmic urease. Infect. Immun. 68, 470-477.
    • (2000) Infect. Immun. , vol.68 , pp. 470-477
    • Scott, D.R.1    Marcus, E.A.2    Weeks, D.L.3    Lee, A.4    Melchers, K.5    Sachs, G.6
  • 33
    • 0035209075 scopus 로고    scopus 로고
    • Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli
    • Seaver, L. C. and J. A. Imlay. 2001. Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli. J. Bacteriol. 183, 7173-7181.
    • (2001) J. Bacteriol. , vol.183 , pp. 7173-7181
    • Seaver, L.C.1    Imlay, J.A.2
  • 34
    • 46749099880 scopus 로고    scopus 로고
    • The changes of proteomes components of Helicobacter pylori in response to acid stress without urea
    • Shao, C., Q. Zhang, W. Tang, W. Qu, Y. Zhou, Y. Sun, H. Yu, and J. Jia. 2008a. The changes of proteomes components of Helicobacter pylori in response to acid stress without urea. J. Microbiol. 46, 331-337.
    • (2008) J. Microbiol. , vol.46 , pp. 331-337
    • Shao, C.1    Zhang, Q.2    Tang, W.3    Qu, W.4    Zhou, Y.5    Sun, Y.6    Yu, H.7    Jia, J.8
  • 36
    • 0026355724 scopus 로고
    • Identification of the essential cysteine residue in Klebsiella aerogenes urease
    • Todd, M. J. and R. P. Hausinger. 1991. Identification of the essential cysteine residue in Klebsiella aerogenes urease. J. Biol. Chem. 266, 24327-24331.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24327-24331
    • Todd, M.J.1    Hausinger, R.P.2
  • 37
    • 55849097315 scopus 로고    scopus 로고
    • Proteomic analysis of protein S-nitrosylation
    • Torta, F., V. Usuelli, A. Malgaroli, and A. Bachi. 2008. Proteomic analysis of protein S-nitrosylation. Proteomics 8, 4484-4494.
    • (2008) Proteomics , vol.8 , pp. 4484-4494
    • Torta, F.1    Usuelli, V.2    Malgaroli, A.3    Bachi, A.4
  • 38
    • 0028925321 scopus 로고
    • Essential role of Helicobacter pylori urease in gastric colonization: definite proof using a urease-negative mutant constructed by gene replacement
    • Tsuda, M., M. Karita, T. Mizote, M. G. Morshed, K. Okita, and T. Nakazawa. 1994. Essential role of Helicobacter pylori urease in gastric colonization: definite proof using a urease-negative mutant constructed by gene replacement. Eur. J. Gastroenterol. Hepatol. 6, S49-52.
    • (1994) Eur. J. Gastroenterol. Hepatol. , vol.6 , pp. 49-52
    • Tsuda, M.1    Karita, M.2    Mizote, T.3    Morshed, M.G.4    Okita, K.5    Nakazawa, T.6
  • 40
    • 0036185045 scopus 로고    scopus 로고
    • Specific identification of three low molecular weight membraneassociated antigens of Helicobacter pylori
    • Voland, P., D. L. Weeks, D. Vaira, C. Prinz, and G. Sachs. 2002. Specific identification of three low molecular weight membraneassociated antigens of Helicobacter pylori. Aliment. Pharmacol. Ther. 16, 533-544.
    • (2002) Aliment. Pharmacol. Ther. , vol.16 , pp. 533-544
    • Voland, P.1    Weeks, D.L.2    Vaira, D.3    Prinz, C.4    Sachs, G.5
  • 41
    • 21744434507 scopus 로고    scopus 로고
    • Nitric oxide-induced nitrative stress involved in microbial pathogenesis
    • Zaki, M. H., T. Akuta, and T. Akaike. 2005. Nitric oxide-induced nitrative stress involved in microbial pathogenesis. J. Pharmacol. Sci. 98, 117-129.
    • (2005) J. Pharmacol. Sci. , vol.98 , pp. 117-129
    • Zaki, M.H.1    Akuta, T.2    Akaike, T.3
  • 42
    • 33747885475 scopus 로고    scopus 로고
    • Inhibition of urease by bismuth (III): implications for the mechanism of action of bismuth drugs
    • Zhang, L., S. B. Mulrooney, A. F. Leung, Y. Zeng, B. B. Ko, R. P. Hausinger, and H. Sun. 2006. Inhibition of urease by bismuth (III): implications for the mechanism of action of bismuth drugs. Biometals 19, 503-511.
    • (2006) Biometals , vol.19 , pp. 503-511
    • Zhang, L.1    Mulrooney, S.B.2    Leung, A.F.3    Zeng, Y.4    Ko, B.B.5    Hausinger, R.P.6    Sun, H.7


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