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Volumn 95, Issue 6, 2013, Pages 1136-1145

Up-regulation of neutrophil activating protein in Helicobacter pylori under high-salt stress: Structural and phylogenetic comparison with bacterial iron-binding ferritins

Author keywords

Analytical ultracentrifugation; Helicobacter pylori; High salt stress; Iron binding protein; Isothermal titration calorimetry; Neutrophil activating protein

Indexed keywords

BACTERIAL PROTEIN; CERULOPLASMIN; FERRITIN; NEUTROPHIL ACTIVATING PROTEIN; UNCLASSIFIED DRUG;

EID: 84877755275     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2012.12.017     Document Type: Article
Times cited : (6)

References (59)
  • 1
    • 22344438694 scopus 로고    scopus 로고
    • Epidemiology of gastric cancer in Japan
    • DOI 10.1136/pgmj.2004.029330
    • M. Inoue, and S. Tsugane Epidemiology of gastric cancer in Japan Postgrad. Med. J. 81 2005 419 424 (Pubitemid 41002579)
    • (2005) Postgraduate Medical Journal , vol.81 , Issue.957 , pp. 419-424
    • Inoue, M.1    Tsugane, S.2
  • 2
    • 14144249629 scopus 로고    scopus 로고
    • Salt, salted food intake, and risk of gastric cancer: Epidemiologic evidence
    • DOI 10.1111/j.1349-7006.2005.00006.x
    • S. Tsugane Salt, salted food intake, and risk of gastric cancer: epidemiologic evidence Cancer Sci. 96 2005 1 6 (Pubitemid 40310017)
    • (2005) Cancer Science , vol.96 , Issue.1 , pp. 1-6
    • Tsugane, S.1
  • 4
    • 0027065034 scopus 로고
    • Human gastric carcinogenesis: A multistep and multifactorial process - First American Cancer Society Award lecture on cancer epidemiology and prevention
    • P. Correa Human gastric carcinogenesis: A multistep and multifactorial process-first American cancer society award lecture on cancer epidemiology and prevention Cancer Res. 52 1992 6735 6740 (Pubitemid 23006271)
    • (1992) Cancer Research , vol.52 , Issue.24 , pp. 6735-6740
    • Correa, P.1
  • 5
    • 0037266696 scopus 로고    scopus 로고
    • Helicobacter pylori infection and gastric carcinogenesis in animal models
    • DOI 10.1007/s101200300000
    • M. Tatematsu, K. Nozaki, and T. Tsukamoto Helicobacter pylori infection and gastric carcinogenesis in animal models Gastric Cancer 6 2003 1 7 (Pubitemid 36460550)
    • (2003) Gastric Cancer , vol.6 , Issue.1 , pp. 1-7
    • Tatemaisu, M.1    Nozaki, K.2    Tsukamoto, T.3
  • 6
    • 67650137086 scopus 로고    scopus 로고
    • Review of salt consumption and stomach cancer risk: Epidemiological and biological evidence
    • X.Q. Wang, P.D. Terry, and H. Yan Review of salt consumption and stomach cancer risk: epidemiological and biological evidence World J. Gastroenterol. 15 2009 2204 2213
    • (2009) World J. Gastroenterol. , vol.15 , pp. 2204-2213
    • Wang, X.Q.1    Terry, P.D.2    Yan, H.3
  • 7
    • 68149166570 scopus 로고    scopus 로고
    • Helicobacter pylori and gastric cancer
    • H. Suzuki, E. Iwasaki, and T. Hibi Helicobacter pylori and gastric cancer Gastric Cancer 12 2009 79 87
    • (2009) Gastric Cancer , vol.12 , pp. 79-87
    • Suzuki, H.1    Iwasaki, E.2    Hibi, T.3
  • 8
    • 65049086892 scopus 로고    scopus 로고
    • Helicobacter pylori and gastric carcinogenesis
    • M. Hatakeyama Helicobacter pylori and gastric carcinogenesis J. Gastroenterol. 44 2009 239 248
    • (2009) J. Gastroenterol. , vol.44 , pp. 239-248
    • Hatakeyama, M.1
  • 9
    • 0029911619 scopus 로고    scopus 로고
    • Relationship between Helicobacter pylori eradication and reduced duodenal and gastric ulcer recurrence: A review
    • DOI 10.1053/gast.1996.v110.pm8613015
    • R.J. Hopkins, L.S. Girardi, and E.A. Turney Relationship between Helicobacter pylori eradication and reduced duodenal and gastric ulcer recurrence: A review Gastroenterology 110 1996 1244 1252 (Pubitemid 26113765)
    • (1996) Gastroenterology , vol.110 , Issue.4 , pp. 1244-1252
    • Hopkins, R.J.1    Girardi, L.S.2    Turney, E.A.3
  • 10
    • 0032420217 scopus 로고    scopus 로고
    • Helicobacter pylori infection and the pathogenesis of duodenal ulceration
    • DOI 10.1111/j.1749-6632.1998.tb11114.x
    • M.M. Walker, and J.E. Crabtree Helicobacter pylori infection and the pathogenesis of duodenal ulceration Ann. N. Y Acad. Sci. 859 1998 96 111 (Pubitemid 29021009)
    • (1998) Annals of the New York Academy of Sciences , vol.859 , pp. 96-111
    • Walker, M.M.1    Crabtree, J.E.2
  • 11
    • 0025885785 scopus 로고
    • Mucosal tumour necrosis factor alpha and interleukin-6 in patients with Helicobacter pylori associated gastritis
    • J.E. Crabtree, T.M. Shallcross, R.V. Heatley, and J.I. Wyatt Mucosal tumour necrosis factor alpha and interleukin-6 in patients with Helicobacter pylori associated gastritis Gut 32 1991 1473 1477
    • (1991) Gut , vol.32 , pp. 1473-1477
    • Crabtree, J.E.1    Shallcross, T.M.2    Heatley, R.V.3    Wyatt, J.I.4
  • 12
    • 0026680231 scopus 로고
    • Helicobacter pylori secretes a chemotactic factor for monocytes and neutrophils
    • P.M. Craig, M.C. Territo, W.E. Karnes, and J.H. Walsh Helicobacter pylori secretes a chemotactic factor for monocytes and neutrophils Gut 33 1992 1020 1023
    • (1992) Gut , vol.33 , pp. 1020-1023
    • Craig, P.M.1    Territo, M.C.2    Karnes, W.E.3    Walsh, J.H.4
  • 14
    • 34247161416 scopus 로고    scopus 로고
    • CagA protein of Helicobacter pylori: A hijacker of gastric epithelial cell signaling
    • DOI 10.1016/j.bcp.2006.10.022, PII S0006295206006708
    • O. Handa, Y. Naito, and T. Yoshikawa CagA protein of Helicobacter pylori: A hijacker of gastric epithelial cell signaling Biochem. Pharmacol. 73 2007 1697 1702 (Pubitemid 46601402)
    • (2007) Biochemical Pharmacology , vol.73 , Issue.11 , pp. 1697-1702
    • Handa, O.1    Naito, Y.2    Yoshikawa, T.3
  • 15
    • 78651282637 scopus 로고    scopus 로고
    • Helicobacter pylori: A ROS-inducing bacterial species in the stomach
    • O. Handa, Y. Naito, and T. Yoshikawa Helicobacter pylori: A ROS-inducing bacterial species in the stomach Inflamm. Res. 59 2010 997 1003
    • (2010) Inflamm. Res. , vol.59 , pp. 997-1003
    • Handa, O.1    Naito, Y.2    Yoshikawa, T.3
  • 16
    • 0025865390 scopus 로고
    • Soluble surface proteins from Helicobacter pylori activate monocytes/macrophages by lipopolysaccharide-independent mechanism
    • U.E. Mai, G.I. Perez-Perez, L.M. Wahl, S.M. Wahl, M.J. Blaser, and P.D. Smith Soluble surface proteins from Helicobacter pylori activate monocytes/macrophages by lipopolysaccharide-independent mechanism J. Clin. Invest. 87 1991 894 900
    • (1991) J. Clin. Invest. , vol.87 , pp. 894-900
    • Mai, U.E.1    Perez-Perez, G.I.2    Wahl, L.M.3    Wahl, S.M.4    Blaser, M.J.5    Smith, P.D.6
  • 17
    • 0026570302 scopus 로고
    • Surface proteins from Helicobacter pylori exhibit chemotactic activity for human leukocytes and are present in gastric mucosa
    • U.E. Mai, G.I. Perez-Perez, J.B. Allen, S.M. Wahl, M.J. Blaser, and P.D. Smith Surface proteins from Helicobacter pylori exhibit chemotactic activity for human leukocytes and are present in gastric mucosa J. Exp. Med. 175 1992 517 525
    • (1992) J. Exp. Med. , vol.175 , pp. 517-525
    • Mai, U.E.1    Perez-Perez, G.I.2    Allen, J.B.3    Wahl, S.M.4    Blaser, M.J.5    Smith, P.D.6
  • 18
    • 0027397858 scopus 로고
    • A neutrophil chemotactic factor present in H. pylori but absent in H. mustelae
    • DOI 10.1007/BF01296786
    • R. Kozol, B. McCurdy, and R. Czanko A neutrophil chemotactic factor present in H. pylori but absent in H. mustelae Dig. Dis. Sci. 38 1993 137 141 (Pubitemid 23039465)
    • (1993) Digestive Diseases and Sciences , vol.38 , Issue.1 , pp. 137-141
    • Kozol, R.1    McCurdy, B.2    Czanko, R.3
  • 23
    • 0031883873 scopus 로고    scopus 로고
    • Neutrophil-activating protein mediates adhesion of Helicobacter pylori to sulfated carbohydrates on high-molecular-weight salivary mucin
    • F. Namavar, M. Sparrius, E.C. Veerman, B.J. Appelmelk, and C.M. Vandenbroucke-Grauls Neutrophil-activating protein mediates adhesion of Helicobacter pylori to sulfated carbohydrates on high-molecular-weight salivary mucin Infect. Immun. 66 1998 444 447 (Pubitemid 28074179)
    • (1998) Infection and Immunity , vol.66 , Issue.2 , pp. 444-447
    • Namavar, F.1    Sparrius, M.2    Veerman, E.C.I.3    Appelmelk, B.J.4    Vandenbroucke-Grauls, C.M.5
  • 27
    • 33845511105 scopus 로고    scopus 로고
    • Dual roles of Helicobacter pylori NapA in inducing and combating oxidative stress
    • DOI 10.1128/IAI.00991-06
    • G. Wang, Y. Hong, A. Olczak, S.E. Maier, and R.J. Maier Dual roles of Helicobacter pylori NapA in inducing and combating oxidative stress Infect. Immun. 74 2006 6839 6846 (Pubitemid 44913159)
    • (2006) Infection and Immunity , vol.74 , Issue.12 , pp. 6839-6846
    • Wang, G.1    Hong, Y.2    Olczak, A.3    Maier, S.E.4    Maier, R.J.5
  • 28
    • 27144493317 scopus 로고    scopus 로고
    • Proteomic analysis of proteins expressed by Helicobacter pylori under oxidative stress
    • M.H. Chuang, M.S. Wu, J.T. Lin, and S.H. Chiou Proteomic analysis of proteins expressed by Helicobacter pylori under oxidative stress Proteomics 5 2005 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
  • 29
    • 33644559039 scopus 로고    scopus 로고
    • The antioxidant protein alkylhydroperoxide reductase of Helicobacter pylori switches from a peroxide reductase to a molecular chaperone function
    • M.H. Chuang, M.S. Wu, W.L. Lo, J.T. Lin, C.H. Wong, and S.H. Chiou The antioxidant protein alkylhydroperoxide reductase of Helicobacter pylori switches from a peroxide reductase to a molecular chaperone function Proc. Natl. Acad. Sci. U. S. A. 103 2006 2552 2557
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 2552-2557
    • Chuang, M.H.1    Wu, M.S.2    Lo, W.L.3    Lin, J.T.4    Wong, C.H.5    Chiou, S.H.6
  • 30
    • 77950610038 scopus 로고    scopus 로고
    • Upregulation of a non-heme iron-containing ferritin with dual ferroxidase and DNA-binding activities in Helicobacter pylori under acid stress
    • C.H. Huang, I.L. Lee, I.J. Yeh, J.H. Liao, C.L. Ni, S.H. Wu, and S.H. Chiou Upregulation of a non-heme iron-containing ferritin with dual ferroxidase and DNA-binding activities in Helicobacter pylori under acid stress J. Biochem. 147 2010 535 543
    • (2010) J. Biochem. , vol.147 , pp. 535-543
    • Huang, C.H.1    Lee, I.L.2    Yeh, I.J.3    Liao, J.H.4    Ni, C.L.5    Wu, S.H.6    Chiou, S.H.7
  • 31
    • 77953711968 scopus 로고    scopus 로고
    • Characterization of site-specific mutants of alkylhydroperoxide reductase with dual functionality from Helicobacter pylori
    • C.H. Huang, M.H. Chuang, Y.H. Wu, W.C. Chuang, P.J. Jhuang, and S.H. Chiou Characterization of site-specific mutants of alkylhydroperoxide reductase with dual functionality from Helicobacter pylori J. Biochem. 147 2010 661 669
    • (2010) J. Biochem. , vol.147 , pp. 661-669
    • Huang, C.H.1    Chuang, M.H.2    Wu, Y.H.3    Chuang, W.C.4    Jhuang, P.J.5    Chiou, S.H.6
  • 32
    • 79958027313 scopus 로고    scopus 로고
    • Alkylhydroperoxide reductase of Helicobacter pylori as a biomarker for gastric patients with different pathological manifestations
    • C.H. Huang, M.H. Chuang, W.L. Lo, M.S. Wu, Y.H. Wu, D.C. Wu, and S.H. Chiou Alkylhydroperoxide reductase of Helicobacter pylori as a biomarker for gastric patients with different pathological manifestations Biochimie 93 2011 1115 1123
    • (2011) Biochimie , vol.93 , pp. 1115-1123
    • Huang, C.H.1    Chuang, M.H.2    Lo, W.L.3    Wu, M.S.4    Wu, Y.H.5    Wu, D.C.6    Chiou, S.H.7
  • 33
    • 84855238338 scopus 로고    scopus 로고
    • Proteomic analysis of upregulated proteins in Helicobacter pylori under oxidative stress induced by hydrogen peroxide
    • C.H. Huang, and S.H. Chiou Proteomic analysis of upregulated proteins in Helicobacter pylori under oxidative stress induced by hydrogen peroxide Kaohsiung J. Med. Sci. 27 2011 544 553
    • (2011) Kaohsiung J. Med. Sci. , vol.27 , pp. 544-553
    • Huang, C.H.1    Chiou, S.H.2
  • 34
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • P. Schuck Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling Biophys. J. 78 2000 1606 1619 (Pubitemid 30141584)
    • (2000) Biophysical Journal , vol.78 , Issue.3 , pp. 1606-1619
    • Schuck, P.1
  • 35
    • 0034672122 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Inclusion of denatured proteins with native proteins in the analysis
    • DOI 10.1006/abio.2000.4879
    • N. Sreerama, S.Y. Venyaminov, and R.W. Woody Estimation of protein secondary structure from circular dichroism spectra: inclusion of denatured proteins with native proteins in the analysis Anal. Biochem. 287 2000 243 251 (Pubitemid 32006233)
    • (2000) Analytical Biochemistry , vol.287 , Issue.2 , pp. 243-251
    • Sreerama, N.1    Venyaminov, S.Yu.2    Woody, R.W.3
  • 36
    • 0025342577 scopus 로고
    • Unified approach to alignment and phylogenies
    • J. Hein Unified approach to alignment and phylogenies Methods Enzymol. 183 1990 626 645 (Pubitemid 20148846)
    • (1990) Methods in Enzymology , vol.183 , pp. 626-645
    • Hein, J.1
  • 37
    • 0028843199 scopus 로고
    • Identification of four new prokaryotic bacterioferritins, from Helicobacter pylori, Anabaena variabilis, Bacillus subtilis and Treponema pallidum, by analysis of gene sequences
    • D.J. Evans Jr., D.G. Evans, H.C. Lampert, and H. Nakano Identification of four new prokaryotic bacterioferritins, from Helicobacter pylori, Anabaena variabilis, Bacillus subtilis and Treponema pallidum, by analysis of gene sequences Gene 153 1995 123 127
    • (1995) Gene , vol.153 , pp. 123-127
    • Evans Jr., D.J.1    Evans, D.G.2    Lampert, H.C.3    Nakano, H.4
  • 38
    • 0029901047 scopus 로고    scopus 로고
    • Dietary salt, nitrate and stomach cancer mortality in 24 countries. European Cancer Prevention (ECP) and the INTERSALT cooperative research group
    • J.V. Joossens, M.J. Hill, P. Elliott, R. Stamler, E. Lesaffre, A. Dyer, R. Nichols, and H. Kesteloot Dietary salt, nitrate and stomach cancer mortality in 24 countries. European Cancer Prevention (ECP) and the INTERSALT cooperative research group Int. J. Epidemiol. 25 1996 494 504
    • (1996) Int. J. Epidemiol. , vol.25 , pp. 494-504
    • Joossens, J.V.1    Hill, M.J.2    Elliott, P.3    Stamler, R.4    Lesaffre, E.5    Dyer, A.6    Nichols, R.7    Kesteloot, H.8
  • 40
    • 0031014275 scopus 로고    scopus 로고
    • Food consumption and gastric cancer mortality in five regions of Japan
    • Y. Tsubono, M. Kobayashi, and S. Tsugane Food consumption and gastric cancer mortality in five regions of Japan Nutr. Cancer 27 1997 60 64 (Pubitemid 26424317)
    • (1997) Nutrition and Cancer , vol.27 , Issue.1 , pp. 60-64
    • Tsubono, Y.1    Kobayashi, M.2    Tsugane, S.3
  • 43
    • 33746130269 scopus 로고    scopus 로고
    • High salt diets dose-dependently promote gastric chemical carcinogenesis in Helicobacter pylori-infected Mongolian gerbils associated with a shift in mucin production from glandular to surface mucous cells
    • DOI 10.1002/ijc.21810
    • S. Kato, T. Tsukamoto, T. Mizoshita, H. Tanaka, T. Kumagai, H. Ota, T. Katsuyama, M. Asaka, and M. Tatematsu High salt diets dose-dependently promote gastric chemical carcinogenesis in Helicobacter pylori-infected Mongolian gerbils associated with a shift in mucin production from glandular to surface mucous cells Int. J. Cancer 119 2006 1558 1566 (Pubitemid 44258761)
    • (2006) International Journal of Cancer , vol.119 , Issue.7 , pp. 1558-1566
    • Kato, S.1    Tsukamoto, T.2    Mizoshita, T.3    Tanaka, H.4    Kumagai, T.5    Ota, H.6    Katsuyama, T.7    Asaka, M.8    Tatematsu, M.9
  • 45
    • 0033214456 scopus 로고    scopus 로고
    • High-salt diet induces gastric epithelial hyperplasia and parietal cell loss, and enhances Helicobacter pylori colonization in C57BL/6 mice
    • J.G. Fox, C.A. Dangler, N.S. Taylor, A. King, T.J. Koh, and T.C. Wang High-salt diet induces gastric epithelial hyperplasia and parietal cell loss, and enhances Helicobacter pylori colonization in C57BL/6 mice Cancer Res. 59 1999 4823 4828 (Pubitemid 29472883)
    • (1999) Cancer Research , vol.59 , Issue.19 , pp. 4823-4828
    • Fox, J.G.1    Dangler, C.A.2    Taylor, N.S.3    King, A.4    Koh, T.J.5    Wang, T.C.6
  • 46
    • 34250372426 scopus 로고    scopus 로고
    • Regulation of Helicobacter pylori cagA expression in response to salt
    • DOI 10.1158/0008-5472.CAN-06-4746
    • J.T. Loh, V.J. Torres, and T.L. Cover Regulation of Helicobacter pylori cagA expression in response to salt Cancer Res. 67 2007 4709 4715 (Pubitemid 46910177)
    • (2007) Cancer Research , vol.67 , Issue.10 , pp. 4709-4715
    • Loh, J.T.1    Torres, V.J.2    Cover, T.L.3
  • 47
    • 44349155407 scopus 로고    scopus 로고
    • Sodium chloride affects Helicobacter pylori growth and gene expression
    • DOI 10.1128/JB.01728-07
    • H. Gancz, K.R. Jones, and D.S. Merrell Sodium chloride affects Helicobacter pylori growth and gene expression J. Bacteriol. 190 2008 4100 4105 (Pubitemid 351732893)
    • (2008) Journal of Bacteriology , vol.190 , Issue.11 , pp. 4100-4105
    • Gancz, H.1    Jones, K.R.2    Merrell, D.S.3
  • 49
    • 34249846924 scopus 로고    scopus 로고
    • The neutrophil-activating Dps protein of Helicobacter pylori, HP-NAP, adopts a mechanism different from Escherichia coli Dps to bind and condense DNA
    • DOI 10.1093/nar/gkm077
    • P. Ceci, L. Mangiarotti, C. Rivetti, and E. Chiancone The neutrophil-activating Dps protein of Helicobacter pylori, HP-NAP, adopts a mechanism different from Escherichia coli Dps to bind and condense DNA Nucleic Acids Res. 35 2007 2247 2256 (Pubitemid 47073712)
    • (2007) Nucleic Acids Research , vol.35 , Issue.7 , pp. 2247-2256
    • Ceci, P.1    Mangiarotti, L.2    Rivetti, C.3    Chiancone, E.4
  • 50
    • 0037125958 scopus 로고    scopus 로고
    • Ferrous ion binding to recombinant human H-chain ferritin. An isothermal titration calorimetry study
    • DOI 10.1021/bi020215g
    • F. Bou-Abdallah, P. Arosio, P. Santambrogio, X. Yang, C. Janus-Chandler, and N.D. Chasteen Ferrous ion binding to recombinant human H-chain ferritin. An isothermal titration calorimetry study Biochemistry 41 2002 11184 11191 (Pubitemid 35034020)
    • (2002) Biochemistry , vol.41 , Issue.37 , pp. 11184-11191
    • Bou-Abdallah, F.1    Arosio, P.2    Santambrogio, P.3    Yang, X.4    Janus-Chandler, C.5    Chasteen, N.D.6
  • 51
    • 17144402211 scopus 로고    scopus 로고
    • The so-called Listeria innocua ferritin is a Dps protein. Iron incorporation, detoxification, and DNA protection properties
    • DOI 10.1021/bi0472705
    • M. Su, S. Cavallo, S. Stefanini, E. Chiancone, and N.D. Chasteen The so-called Listeria innocua ferritin is a Dps protein. Iron incorporation, detoxification, and DNA protection properties Biochemistry 44 2005 5572 5578 (Pubitemid 40525094)
    • (2005) Biochemistry , vol.44 , Issue.15 , pp. 5572-5578
    • Su, M.1    Cavallo, S.2    Stefanini, S.3    Chiancone, E.4    Chasteen, N.D.5
  • 52
    • 21244482459 scopus 로고    scopus 로고
    • 6 unfoldase: Allosteric control of a protein machine
    • DOI 10.1016/j.cell.2005.05.024, PII S0092867405005039
    • G.L. Hersch, R.E. Burton, D.N. Bolon, T.A. Baker, and R.T. Sauer Asymmetric interactions of ATP with the AAA+ ClpX6 unfoldase: Allosteric control of a protein machine Cell 121 2005 1017 1027 (Pubitemid 40884394)
    • (2005) Cell , vol.121 , Issue.7 , pp. 1017-1027
    • Hersch, G.L.1    Burton, R.E.2    Bolon, D.N.3    Baker, T.A.4    Sauer, R.T.5
  • 53
    • 0035873182 scopus 로고    scopus 로고
    • Neutrophil-activating protein (HP-NAP) versus ferritin (Pfr): Comparison of synthesis in Helicobacter pylori
    • DOI 10.1016/S0378-1097(01)00174-4, PII S0378109701001744
    • W.G. Dundon, A. Polenghi, G. Del Guidice, R. Rappuoli, and C. Montecucco Neutrophil-activating protein (HP-NAP) versus ferritin (Pfr): comparison of synthesis in Helicobacter pylori FEMS Microbiol. Lett. 199 2001 143 149 (Pubitemid 32455478)
    • (2001) FEMS Microbiology Letters , vol.199 , Issue.1 , pp. 143-149
    • Dundon, W.G.1    Polenghi, A.2    Del Guidice, G.3    Rappuoli, R.4    Montecucco, C.5
  • 54
    • 54449100093 scopus 로고    scopus 로고
    • Helicobacter pylori neutrophil-activating protein promotes myeloperoxidase release from human neutrophils
    • C.A. Wang, Y.C. Liu, S.Y. Du, C.W. Lin, and H.W. Fu Helicobacter pylori neutrophil-activating protein promotes myeloperoxidase release from human neutrophils Biochem. Biophys. Res. Commun. 377 2008 52 56
    • (2008) Biochem. Biophys. Res. Commun. , vol.377 , pp. 52-56
    • Wang, C.A.1    Liu, Y.C.2    Du, S.Y.3    Lin, C.W.4    Fu, H.W.5
  • 56
    • 77957905503 scopus 로고    scopus 로고
    • The immune modulating activity of the Helicobacter pylori HP-NAP: Friend or foe?
    • M. de Bernard, and M.M. D'Elios The immune modulating activity of the Helicobacter pylori HP-NAP: friend or foe? Toxicon 56 2010 1186 1192
    • (2010) Toxicon , vol.56 , pp. 1186-1192
    • De Bernard, M.1    D'Elios, M.M.2
  • 57
    • 54149084001 scopus 로고    scopus 로고
    • The neutrophil-activating protein of Helicobacter pylori down-modulates Th2 inflammation in ovalbumin-induced allergic asthma
    • G. Codolo, P. Mazzi, A. Amedei, G. Del Prete, G. Berton, M.M. D'Elios, and M. de Bernard The neutrophil-activating protein of Helicobacter pylori down-modulates Th2 inflammation in ovalbumin-induced allergic asthma Cell. Microbiol. 10 2008 2355 2363
    • (2008) Cell. Microbiol. , vol.10 , pp. 2355-2363
    • Codolo, G.1    Mazzi, P.2    Amedei, A.3    Del Prete, G.4    Berton, G.5    D'Elios, M.M.6    De Bernard, M.7
  • 59
    • 77955506941 scopus 로고    scopus 로고
    • Helicobacter pylori gamma-glutamyl transpeptidase is a pathogenic factor in the development of peptic ulcer disease
    • M. Gong, S.S. Ling, S.Y. Lui, K.G. Yeoh, B. Ho, Helicobacter pylori gamma-glutamyl transpeptidase is a pathogenic factor in the development of peptic ulcer disease, Gastroenterology 139 564-573.
    • Gastroenterology , vol.139 , pp. 564-573
    • Gong, M.1    Ling, S.S.2    Lui, S.Y.3    Yeoh, K.G.4    Ho, B.5


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