메뉴 건너뛰기




Volumn 56, Issue 4, 2012, Pages 262-272

Superoxide dismutase activity of Helicobacter pylori per se from 158 clinical isolates and the characteristics

Author keywords

Bacterial superoxide dismutase (SOD); Characteristic of high SOD activity strains; Gastroduodenal disease; Helicobacter pylori clinical isolates

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; IRON SUPEROXIDE DISMUTASE; MANGANESE SUPEROXIDE DISMUTASE; PARAQUAT; SUPEROXIDE DISMUTASE;

EID: 84859865402     PISSN: 03855600     EISSN: 13480421     Source Type: Journal    
DOI: 10.1111/j.1348-0421.2012.00433.x     Document Type: Article
Times cited : (17)

References (57)
  • 1
    • 0034691065 scopus 로고    scopus 로고
    • A M(r) 34,000 proinflammatory outer membrane protein (oipA) of Helicobacter pylori
    • Yamaoka Y., Kwon D.H., Graham D.Y. (2000) A M(r) 34, 000 proinflammatory outer membrane protein (oipA) of Helicobacter pylori. Proc Natl Acad Sci USA 97: 7533-8.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 7533-7538
    • Yamaoka, Y.1    Kwon, D.H.2    Graham, D.Y.3
  • 2
    • 78649368029 scopus 로고    scopus 로고
    • Molecular pathogenesis of Helicobacter pylori infection: the role of bacterial virulence factors
    • Molnar B., Galamb O., Sipos F., Leiszter K., Tulassay Z. (2010) Molecular pathogenesis of Helicobacter pylori infection: the role of bacterial virulence factors. Dig Dis 28: 604-8.
    • (2010) Dig Dis , vol.28 , pp. 604-608
    • Molnar, B.1    Galamb, O.2    Sipos, F.3    Leiszter, K.4    Tulassay, Z.5
  • 5
    • 79958024656 scopus 로고    scopus 로고
    • Helicobacter pylori neutrophil activating protein as target for new drugs against H. pylori inflammation
    • Choli-Papadopoulou T., Kottakis F., Papadopoulos G., Pendas S. (2011) Helicobacter pylori neutrophil activating protein as target for new drugs against H. pylori inflammation. World J Gastroenterol 17: 2585-91.
    • (2011) World J Gastroenterol , vol.17 , pp. 2585-2591
    • Choli-Papadopoulou, T.1    Kottakis, F.2    Papadopoulos, G.3    Pendas, S.4
  • 6
    • 34248196148 scopus 로고    scopus 로고
    • VacA and HP-NAP, Ying and Yang of Helicobacter pylori-associated gastric inflammation
    • D' Elios M.M., Montecucco C., de Bernard M. (2007) VacA and HP-NAP, Ying and Yang of Helicobacter pylori-associated gastric inflammation. Clin Chim Acta 381: 32-8.
    • (2007) Clin Chim Acta , vol.381 , pp. 32-38
    • D' Elios, M.M.1    Montecucco, C.2    de Bernard, M.3
  • 7
    • 77954565540 scopus 로고    scopus 로고
    • Helicobacter pylori dupA is polymorphic, and its active form induces proinflammatory cytokine secretion by mononuclear cells
    • Hussein N.R., Argent R.H., Marx C.K., Patel S.R., Robinson K., Atherton J.C. (2010) Helicobacter pylori dupA is polymorphic, and its active form induces proinflammatory cytokine secretion by mononuclear cells. J Infect Dis 202: 261-9.
    • (2010) J Infect Dis , vol.202 , pp. 261-269
    • Hussein, N.R.1    Argent, R.H.2    Marx, C.K.3    Patel, S.R.4    Robinson, K.5    Atherton, J.C.6
  • 8
    • 0030037316 scopus 로고    scopus 로고
    • Helicobacter pylori urease is a potent stimulus of mononuclear phagocyte activation and inflammatory cytokine production
    • Harris P.R., Mobley H.L., Perez-Perez G.I., Blaser M.J., Smith P.D. (1996) Helicobacter pylori urease is a potent stimulus of mononuclear phagocyte activation and inflammatory cytokine production. Gastroenterology 111: 419-25.
    • (1996) Gastroenterology , vol.111 , pp. 419-425
    • Harris, P.R.1    Mobley, H.L.2    Perez-Perez, G.I.3    Blaser, M.J.4    Smith, P.D.5
  • 10
    • 0037087337 scopus 로고    scopus 로고
    • The Helicobacter pylori blood group antigen-binding adhesin facilitates bacterial colonization and augments a nonspecific immune response
    • Rad R., Gerhard M., Lang R., Schoniger M., Rosch T., Schepp W., Becker I., Wagner H., Prinz C. (2002) The Helicobacter pylori blood group antigen-binding adhesin facilitates bacterial colonization and augments a nonspecific immune response. J Immunol 168: 3033-41.
    • (2002) J Immunol , vol.168 , pp. 3033-3041
    • Rad, R.1    Gerhard, M.2    Lang, R.3    Schoniger, M.4    Rosch, T.5    Schepp, W.6    Becker, I.7    Wagner, H.8    Prinz, C.9
  • 12
    • 33750198309 scopus 로고    scopus 로고
    • Helicobacter pylori SabA adhesin evokes a strong inflammatory response in human neutrophils which is down-regulated by the neutrophil-activating protein
    • Petersson C., Forsberg M., Aspholm M., Olfat F.O., Forslund T., Boren T., Magnusson K.E. (2006) Helicobacter pylori SabA adhesin evokes a strong inflammatory response in human neutrophils which is down-regulated by the neutrophil-activating protein. Med Microbiol Immunol 195: 195-206.
    • (2006) Med Microbiol Immunol , vol.195 , pp. 195-206
    • Petersson, C.1    Forsberg, M.2    Aspholm, M.3    Olfat, F.O.4    Forslund, T.5    Boren, T.6    Magnusson, K.E.7
  • 13
    • 0024811787 scopus 로고
    • Bacterial adaptation to oxidative stress: implications for pathogenesis and interaction with phagocytic cells
    • Hassett D.J., Cohen M.S. (1989) Bacterial adaptation to oxidative stress: implications for pathogenesis and interaction with phagocytic cells. FASEB J 14: 2574-82.
    • (1989) FASEB J , vol.14 , pp. 2574-2582
    • Hassett, D.J.1    Cohen, M.S.2
  • 14
    • 0031029702 scopus 로고    scopus 로고
    • Role of oxidants in microbial pathophysiology
    • Miller R.A., Britigan B.E. (1997) Role of oxidants in microbial pathophysiology. Clin Microbiol Rev 10: 1-18.
    • (1997) Clin Microbiol Rev , vol.10 , pp. 1-18
    • Miller, R.A.1    Britigan, B.E.2
  • 15
    • 0025786078 scopus 로고
    • Oxidative stress responses in Escherichia coli and Salmonella typhimurium
    • Farr S.B., Kogoma T. (1991) Oxidative stress responses in Escherichia coli and Salmonella typhimurium. Microbiol Rev 55: 561-85.
    • (1991) Microbiol Rev , vol.55 , pp. 561-585
    • Farr, S.B.1    Kogoma, T.2
  • 16
    • 0030777042 scopus 로고    scopus 로고
    • Contribution of the Mn-cofactored superoxide dismutase (SodA) to the virulence of Yersinia enterocolitica serotype O8
    • Roggenkamp A., Bittner T., Leitritz L., Sing A., Heesemann J. (1997) Contribution of the Mn-cofactored superoxide dismutase (SodA) to the virulence of Yersinia enterocolitica serotype O8. Infect Immun 65: 4705-10.
    • (1997) Infect Immun , vol.65 , pp. 4705-4710
    • Roggenkamp, A.1    Bittner, T.2    Leitritz, L.3    Sing, A.4    Heesemann, J.5
  • 17
    • 0028247113 scopus 로고
    • The iron superoxide dismutase of Legionella pneumophila is essential for viability
    • Sadosky A.B., Wilson J.W., Steinman H.M., Shuman H.A. (1994) The iron superoxide dismutase of Legionella pneumophila is essential for viability. J Bacteriol 176: 3790-9.
    • (1994) J Bacteriol , vol.176 , pp. 3790-3799
    • Sadosky, A.B.1    Wilson, J.W.2    Steinman, H.M.3    Shuman, H.A.4
  • 18
    • 0027366226 scopus 로고
    • Purification of Helicobacter pylori superoxide dismutase and cloning and sequencing of the gene
    • Spiegelhalder C., Gerstenecker B., Kersten A., Schiltz E., Kist M. (1993) Purification of Helicobacter pylori superoxide dismutase and cloning and sequencing of the gene. Infect Immun 61: 5315-25.
    • (1993) Infect Immun , vol.61 , pp. 5315-5325
    • Spiegelhalder, C.1    Gerstenecker, B.2    Kersten, A.3    Schiltz, E.4    Kist, M.5
  • 19
    • 0028933323 scopus 로고
    • Structure-function in Escherichia coli iron superoxide dismutase: comparisons with the manganese enzyme from Thermus thermophilus
    • Lah M.S., Dixon M.M., Pattridge K.A., Stallings W.C., Fee J.A., Ludwig M.L. (1995) Structure-function in Escherichia coli iron superoxide dismutase: comparisons with the manganese enzyme from Thermus thermophilus. Biochemistry 34: 1646-60.
    • (1995) Biochemistry , vol.34 , pp. 1646-1660
    • Lah, M.S.1    Dixon, M.M.2    Pattridge, K.A.3    Stallings, W.C.4    Fee, J.A.5    Ludwig, M.L.6
  • 20
    • 0030748521 scopus 로고    scopus 로고
    • The crystal structure of an Fe-superoxide dismutase from the hyperthermophile Aquifex pyrophilus at 1.9 A resolution: structural basis for thermostability
    • Lim J.H., Yu Y.G., Han Y.S., Cho S., Ahn B.Y., Kim S.H., Cho Y. (1997) The crystal structure of an Fe-superoxide dismutase from the hyperthermophile Aquifex pyrophilus at 1.9 A resolution: structural basis for thermostability. J Mol Biol 270: 259-74.
    • (1997) J Mol Biol , vol.270 , pp. 259-274
    • Lim, J.H.1    Yu, Y.G.2    Han, Y.S.3    Cho, S.4    Ahn, B.Y.5    Kim, S.H.6    Cho, Y.7
  • 21
    • 0028932184 scopus 로고
    • X-ray structure analysis of the iron-dependent superoxide dismutase from Mycobacterium tuberculosis at 2.0 Angstroms resolution reveals novel dimer-dimer interactions
    • Cooper J.B., Mclntyre K., Badasso M.O., Wood S.P., Zhang Y., Garbe T.R., Young D. (1995) X-ray structure analysis of the iron-dependent superoxide dismutase from Mycobacterium tuberculosis at 2.0 Angstroms resolution reveals novel dimer-dimer interactions. J Mol Biol 246: 531-44.
    • (1995) J Mol Biol , vol.246 , pp. 531-544
    • Cooper, J.B.1    Mclntyre, K.2    Badasso, M.O.3    Wood, S.P.4    Zhang, Y.5    Garbe, T.R.6    Young, D.7
  • 22
    • 0025196784 scopus 로고
    • The 2.1-A resolution structure of iron superoxide dismutase from Pseudomonas ovalis
    • Stoddard B.L., Howell P.L., Ringe D., Petsko G.A. (1990) The 2.1-A resolution structure of iron superoxide dismutase from Pseudomonas ovalis. Biochemistry 29: 8885-93.
    • (1990) Biochemistry , vol.29 , pp. 8885-8893
    • Stoddard, B.L.1    Howell, P.L.2    Ringe, D.3    Petsko, G.A.4
  • 23
    • 54049115084 scopus 로고    scopus 로고
    • The crystal structure of the superoxide dismutase from Helicobacter pylori reveals a structured C-terminal extension
    • Esposito L., Seydel A., Aiello R., Sorrentino G., Cendron L., Zanotti G., Zagari A. (2008) The crystal structure of the superoxide dismutase from Helicobacter pylori reveals a structured C-terminal extension. Biochim Biophys Acta 1784: 1601-6.
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 1601-1606
    • Esposito, L.1    Seydel, A.2    Aiello, R.3    Sorrentino, G.4    Cendron, L.5    Zanotti, G.6    Zagari, A.7
  • 24
    • 33746541640 scopus 로고    scopus 로고
    • The diverse antioxidant systems of Helicobacter pylori
    • Wang G., Alamuri P., Maier R.J. (2006) The diverse antioxidant systems of Helicobacter pylori. Mol Microbiol 61: 847-60.
    • (2006) Mol Microbiol , vol.61 , pp. 847-860
    • Wang, G.1    Alamuri, P.2    Maier, R.J.3
  • 25
    • 0035001195 scopus 로고    scopus 로고
    • Superoxide dismutase-deficient mutants of Helicobacter pylori are hypersensitive to oxidative stress and defective in host colonization
    • Seyler R.W. Jr., Olson J.W., Maier R.J. (2001) Superoxide dismutase-deficient mutants of Helicobacter pylori are hypersensitive to oxidative stress and defective in host colonization. Infect Immun 69: 4034-40.
    • (2001) Infect Immun , vol.69 , pp. 4034-4040
    • Seyler Jr, R.W.1    Olson, J.W.2    Maier, R.J.3
  • 27
    • 0344440862 scopus 로고    scopus 로고
    • Superoxide-dismutase activity of the gastric mucosa in patients with Helicobacter pylori infection
    • Farkas R., Selmeci L., Tulassay Z., Pronai L. (2003) Superoxide-dismutase activity of the gastric mucosa in patients with Helicobacter pylori infection. Anticancer Res 23: 4309-12.
    • (2003) Anticancer Res , vol.23 , pp. 4309-4312
    • Farkas, R.1    Selmeci, L.2    Tulassay, Z.3    Pronai, L.4
  • 29
    • 0031657583 scopus 로고    scopus 로고
    • Nucleotide sequence and characterization of cdrA, a cell division-related gene of Helicobacter pylori
    • Takeuchi H., Shirai M., Akada J.K., Tsuda M., Nakazawa T. (1998) Nucleotide sequence and characterization of cdrA, a cell division-related gene of Helicobacter pylori. J Bacteriol 180: 5263-8.
    • (1998) J Bacteriol , vol.180 , pp. 5263-5268
    • Takeuchi, H.1    Shirai, M.2    Akada, J.K.3    Tsuda, M.4    Nakazawa, T.5
  • 31
    • 77954966370 scopus 로고    scopus 로고
    • The mechanical binding strengths of Helicobacter pylori BabA and SabA adhesins using an adhesion binding assay-ELISA, and its clinical relevance in Japan
    • Nishioka M., Takeuchi H., Con S.A., Uehara Y., Nishimori I., Okumiya T., Kumon Y., Sugiura T. (2010) The mechanical binding strengths of Helicobacter pylori BabA and SabA adhesins using an adhesion binding assay-ELISA, and its clinical relevance in Japan. Microbiol Immunol 54: 442-51.
    • (2010) Microbiol Immunol , vol.54 , pp. 442-451
    • Nishioka, M.1    Takeuchi, H.2    Con, S.A.3    Uehara, Y.4    Nishimori, I.5    Okumiya, T.6    Kumon, Y.7    Sugiura, T.8
  • 32
    • 61849108169 scopus 로고    scopus 로고
    • Relationship of IL-8 production and the CagA status in AGS cells infected with Helicobacter pylori exposed to low pH and activating transcription factor 3 (ATF3)
    • Zhang Y., Takeuchi H., Nishioka M., Morimoto N., Kamioka M., Kumon Y., Sugiura T. (2009) Relationship of IL-8 production and the CagA status in AGS cells infected with Helicobacter pylori exposed to low pH and activating transcription factor 3 (ATF3). Microbiol Res 164: 180-90.
    • (2009) Microbiol Res , vol.164 , pp. 180-190
    • Zhang, Y.1    Takeuchi, H.2    Nishioka, M.3    Morimoto, N.4    Kamioka, M.5    Kumon, Y.6    Sugiura, T.7
  • 35
    • 0001754396 scopus 로고    scopus 로고
    • Spectrophotometric assay for superoxide dismutase based on the reduction of highly water-soluble tetrazolium salts by xanthine-xanthine oxidase
    • Ukeda H., Kawana D., Maeda S., Sawamura M. (1999) Spectrophotometric assay for superoxide dismutase based on the reduction of highly water-soluble tetrazolium salts by xanthine-xanthine oxidase. Biosci Biotechnol Biochem 63: 485-8.
    • (1999) Biosci Biotechnol Biochem , vol.63 , pp. 485-488
    • Ukeda, H.1    Kawana, D.2    Maeda, S.3    Sawamura, M.4
  • 36
    • 0035156332 scopus 로고    scopus 로고
    • In vitro resistance of Burkholderia cepacia complex isolates to reactive oxygen species in relation to catalase and superoxide dismutase production
    • Lefebre M., Valvano M. (2001) In vitro resistance of Burkholderia cepacia complex isolates to reactive oxygen species in relation to catalase and superoxide dismutase production. Microbiology 147: 97-109.
    • (2001) Microbiology , vol.147 , pp. 97-109
    • Lefebre, M.1    Valvano, M.2
  • 37
    • 0031685512 scopus 로고    scopus 로고
    • Structural, functional and mutational analysis of the pfr gene encoding a ferritin from Helicobacter pylori
    • Bereswill S., Waidner U., Odenbreit S., Lichte F., Fassbinder F., Bode G., Kist M. (1998) Structural, functional and mutational analysis of the pfr gene encoding a ferritin from Helicobacter pylori. Microbiology 144: 2505-16.
    • (1998) Microbiology , vol.144 , pp. 2505-2516
    • Bereswill, S.1    Waidner, U.2    Odenbreit, S.3    Lichte, F.4    Fassbinder, F.5    Bode, G.6    Kist, M.7
  • 38
    • 0033973782 scopus 로고    scopus 로고
    • Identification and molecular analysis of superoxide dismutase isoforms in Helicobacter pylori
    • Bereswill S., Neuner O., Strobel S., Kist M. (2000) Identification and molecular analysis of superoxide dismutase isoforms in Helicobacter pylori. FEMS Microbiol Lett 183: 241-5.
    • (2000) FEMS Microbiol Lett , vol.183 , pp. 241-245
    • Bereswill, S.1    Neuner, O.2    Strobel, S.3    Kist, M.4
  • 39
    • 0033759351 scopus 로고    scopus 로고
    • Regulation of ferritin-mediated cytoplasmic iron storage by the ferric uptake regulator homolog (Fur) of Helicobacter pylori
    • Bereswill S., Greiner S., van Vliet A.H., Waidner B., Fassbinder F., Schiltz E., Kusters J.G., Kist M. (2000) Regulation of ferritin-mediated cytoplasmic iron storage by the ferric uptake regulator homolog (Fur) of Helicobacter pylori. J Bacteriol 182: 5948-53.
    • (2000) J Bacteriol , vol.182 , pp. 5948-5953
    • Bereswill, S.1    Greiner, S.2    van Vliet, A.H.3    Waidner, B.4    Fassbinder, F.5    Schiltz, E.6    Kusters, J.G.7    Kist, M.8
  • 41
    • 48549084063 scopus 로고    scopus 로고
    • Mechanism for gastric cancer development by Helicobacter pylori infection
    • Chiba T., Marusawa H., Seno H., Watanabe N. (2008) Mechanism for gastric cancer development by Helicobacter pylori infection. J Gastroenterol Hepatol 23: 1175-81.
    • (2008) J Gastroenterol Hepatol , vol.23 , pp. 1175-1181
    • Chiba, T.1    Marusawa, H.2    Seno, H.3    Watanabe, N.4
  • 42
  • 43
  • 45
    • 0029952225 scopus 로고    scopus 로고
    • Production of reactive oxygen species by gastric cells in association with Helicobacter pylori
    • Bagchi D., Bhattacharya G., Stohs S.J. (1996) Production of reactive oxygen species by gastric cells in association with Helicobacter pylori. Free Radic Res 24: 439-50.
    • (1996) Free Radic Res , vol.24 , pp. 439-450
    • Bagchi, D.1    Bhattacharya, G.2    Stohs, S.J.3
  • 46
    • 0025972738 scopus 로고
    • DNA damage by oxygen-derived species. Its mechanism and measurement in mammalian systems
    • Halliwell B., Aruoma O.I. (1991) DNA damage by oxygen-derived species. Its mechanism and measurement in mammalian systems. FEBS Lett 281: 9-19.
    • (1991) FEBS Lett , vol.281 , pp. 9-19
    • Halliwell, B.1    Aruoma, O.I.2
  • 47
    • 0028918334 scopus 로고
    • Superoxide and hydrogen peroxide in relation to mammalian cell proliferation
    • Burdon R.H. (1995) Superoxide and hydrogen peroxide in relation to mammalian cell proliferation. Free Radic Biol Med 18: 775-94.
    • (1995) Free Radic Biol Med , vol.18 , pp. 775-794
    • Burdon, R.H.1
  • 48
    • 0042820012 scopus 로고    scopus 로고
    • Pronounced conversion of the metal-specific activity of superoxide dismutase from Porphyromonas gingivalis by the mutation of a single amino acid (Gly 155Thr) located apart from the active site
    • Yamakura F., Sugio S., Hiraoka B.Y., Ohmori D., Yokota T. (2003) Pronounced conversion of the metal-specific activity of superoxide dismutase from Porphyromonas gingivalis by the mutation of a single amino acid (Gly 155Thr) located apart from the active site. Biochemistry 42: 10790-9.
    • (2003) Biochemistry , vol.42 , pp. 10790-10799
    • Yamakura, F.1    Sugio, S.2    Hiraoka, B.Y.3    Ohmori, D.4    Yokota, T.5
  • 49
    • 0002696602 scopus 로고
    • Oxygen stress and superoxide dismutases
    • Scandalios J.G. (1993) Oxygen stress and superoxide dismutases. Plant Physiol 101: 7-12.
    • (1993) Plant Physiol , vol.101 , pp. 7-12
    • Scandalios, J.G.1
  • 50
    • 0026734136 scopus 로고
    • High levels of reactive oxygen metabolites in colon cancer tissue: Analysis by chemiluminescence probe
    • Keshavarzian A., Zapeda D., List T., Mobarhan S. (1992) High levels of reactive oxygen metabolites in colon cancer tissue: Analysis by chemiluminescence probe. Nutr Cancer 17: 243-9.
    • (1992) Nutr Cancer , vol.17 , pp. 243-249
    • Keshavarzian, A.1    Zapeda, D.2    List, T.3    Mobarhan, S.4
  • 52
    • 0028236403 scopus 로고
    • Genetic, enzymatic, and pathogenic studies of the iron superoxide dismutase of Campylobacter jejuni
    • Pesci E.C., Cottle D.L., Pickett C.L. (1994) Genetic, enzymatic, and pathogenic studies of the iron superoxide dismutase of Campylobacter jejuni. Infect Immun 62: 2687-94.
    • (1994) Infect Immun , vol.62 , pp. 2687-2694
    • Pesci, E.C.1    Cottle, D.L.2    Pickett, C.L.3
  • 53
    • 0028364560 scopus 로고
    • Cloning, nucleotide sequence and characterization of a gene encoding superoxide dismutase from Campylobacter jejuni and Campylobacter coli
    • Purdy D., Park S.F. (1994) Cloning, nucleotide sequence and characterization of a gene encoding superoxide dismutase from Campylobacter jejuni and Campylobacter coli. Microbiology 140: 1203-8.
    • (1994) Microbiology , vol.140 , pp. 1203-1208
    • Purdy, D.1    Park, S.F.2
  • 54
    • 0028337813 scopus 로고
    • Expression of superoxide dismutase in Listeria monocytogenes
    • Vasconcelos J.A., Deneer H.G. (1994) Expression of superoxide dismutase in Listeria monocytogenes. Appl Environ Microbiol 60: 2360-6.
    • (1994) Appl Environ Microbiol , vol.60 , pp. 2360-2366
    • Vasconcelos, J.A.1    Deneer, H.G.2
  • 55
    • 0021689682 scopus 로고
    • An electrophoretic analysis of superoxide dismutase in Campylobacter spp
    • Kikuchi H.E., Suzuki T. (1984) An electrophoretic analysis of superoxide dismutase in Campylobacter spp. J Gen Microbiol 130: 2791-6.
    • (1984) J Gen Microbiol , vol.130 , pp. 2791-2796
    • Kikuchi, H.E.1    Suzuki, T.2
  • 56
    • 63749127709 scopus 로고    scopus 로고
    • Mutation of cytotoxin-associated gene A affects expressions of antioxidant proteins of Helicobacter pylori
    • Huang Z.G., Duan G.C., Fan Q.T., Zhang W.D., Song C.H., Huang X.Y., Zhang R.G. (2009) Mutation of cytotoxin-associated gene A affects expressions of antioxidant proteins of Helicobacter pylori. World J Gastroenterol 15: 599-606.
    • (2009) World J Gastroenterol , vol.15 , pp. 599-606
    • Huang, Z.G.1    Duan, G.C.2    Fan, Q.T.3    Zhang, W.D.4    Song, C.H.5    Huang, X.Y.6    Zhang, R.G.7
  • 57
    • 79957605851 scopus 로고    scopus 로고
    • Biochemical and pathophysiological characterization of Helicobacter pylori asparaginase
    • Shibayama K., Takeuchi H., Wachino J., Mori S., Arakawa Y. (2011) Biochemical and pathophysiological characterization of Helicobacter pylori asparaginase. Microbiol Immunol 55: 408-17.
    • (2011) Microbiol Immunol , vol.55 , pp. 408-417
    • Shibayama, K.1    Takeuchi, H.2    Wachino, J.3    Mori, S.4    Arakawa, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.