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Volumn 9, Issue 12, 2010, Pages 2796-2826

Complexomics study of two Helicobacter pylori strains of two pathological origins: Potential targets for vaccine development and new insight in bacteria metabolism

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN; BACTERIAL PROTEIN; MEMBRANE PROTEIN; ORPHAN PROTEIN; OUTER MEMBRANE PROTEIN; PROTEIN BABA; PROTEIN HOR; PROTEIN JHP 0119; PROTEIN SABA; UNCLASSIFIED DRUG;

EID: 78650083653     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M110.001065     Document Type: Article
Times cited : (16)

References (186)
  • 1
    • 0037057683 scopus 로고    scopus 로고
    • Helicobacter pylori infection
    • Suerbaum, S., and Michetti, P. (2002) Helicobacter pylori infection. N. Engl. J. Med. 347, 1175-1186
    • (2002) N. Engl. J. Med. , vol.347 , pp. 1175-1186
    • Suerbaum, S.1    Michetti, P.2
  • 4
    • 0027972480 scopus 로고
    • H. pylori and gastric cancer
    • Forman, D., Webb, P., and Parsonnet, J. (1994) H. pylori and gastric cancer. Lancet 343, 243-244
    • (1994) Lancet , vol.343 , pp. 243-244
    • Forman, D.1    Webb, P.2    Parsonnet, J.3
  • 6
    • 0028221115 scopus 로고
    • Gastric lymphoma and Helicobacter pylori
    • Isaacson, P. G. (1994) Gastric lymphoma and Helicobacter pylori. N. Engl. J. Med. 330, 1310-1311
    • (1994) N. Engl. J. Med. , vol.330 , pp. 1310-1311
    • Isaacson, P.G.1
  • 7
    • 0027213922 scopus 로고
    • Regression of primary low-grade B-cell gastric lymphoma of mucosa-associated lymphoid tissue type after eradication of Helicobacter pylori
    • Wotherspoon, A. C., Doglioni, C., Diss, T. C., Pan, L., Moschini, A., de Boni, M., and Isaacson, P. G. (1993) Regression of primary low-grade B-cell gastric lymphoma of mucosa-associated lymphoid tissue type after eradication of Helicobacter pylori. Lancet 342, 575-577
    • (1993) Lancet , vol.342 , pp. 575-577
    • Wotherspoon, A.C.1    Doglioni, C.2    Diss, T.C.3    Pan, L.4    Moschini, A.5    De Boni, M.6    Isaacson, P.G.7
  • 10
    • 0141959129 scopus 로고    scopus 로고
    • Helicobacter pylori genotyping in gastric adenocarcinoma and MALT lymphoma by multiplex PCR analyses of paraffin wax embedded tissues
    • Koehler, C. I., Mues, M. B., Dienes, H. P., Kriegsmann, J., Schirmacher, P., and Odenthal, M. (2003) Helicobacter pylori genotyping in gastric adenocarcinoma and MALT lymphoma by multiplex PCR analyses of paraffin wax embedded tissues. Mol. Pathol. 56, 36-42
    • (2003) Mol. Pathol. , vol.56 , pp. 36-42
    • Koehler, C.I.1    Mues, M.B.2    Dienes, H.P.3    Kriegsmann, J.4    Schirmacher, P.5    Odenthal, M.6
  • 11
    • 0842326287 scopus 로고    scopus 로고
    • Evaluation of the Association of Nine Helicobacter pylori Virulence Factors with Strains Involved in Low-Grade Gastric Mucosa-Associated Lymphoid Tissue Lymphoma
    • DOI 10.1128/IAI.72.2.880-888.2004
    • Lehours, P., Ménard, A., Dupouy, S., Bergey, B., Richy, F., Zerbib, F., Ruskoné-Fourmestraux, A., Delchier, J. C., and Mégraud, F. (2004) Evaluation of the association of nine Helicobacter pylori virulence factors with strains involved in low-grade gastric mucosa-associated lymphoid tissue lymphoma. Infect. Immun. 72, 880-888 (Pubitemid 38166667)
    • (2004) Infection and Immunity , vol.72 , Issue.2 , pp. 880-888
    • Lehours, P.1    Menard, A.2    Dupouy, S.3    Bergey, B.4    Richy, F.5    Zerbib, F.6    Ruskone-Fourmestraux, A.7    Delchier, J.C.8    Megraud, F.9
  • 14
    • 0030892896 scopus 로고    scopus 로고
    • MALT-type lymphoma of the stomach is associated with Helicobacter pylori strains expressing the CagA protein
    • Eck, M., Schmausser, B., Haas, R., Greiner, A., Czub, S., and Müller-Hermelink, H. K. (1997) MALT-type lymphoma of the stomach is associated with Helicobacter pylori strains expressing the CagA protein. Gastroenterology 112, 1482-1486
    • (1997) Gastroenterology , vol.112 , pp. 1482-1486
    • Eck, M.1    Schmausser, B.2    Haas, R.3    Greiner, A.4    Czub, S.5    Müller-Hermelink, H.K.6
  • 18
    • 0032489015 scopus 로고    scopus 로고
    • The cell as a collection of protein machines: Preparing the next generation of molecular biologists
    • Alberts, B. (1998) The cell as a collection of protein machines: preparing the next generation of molecular biologists. Cell 92, 291-294
    • (1998) Cell , vol.92 , pp. 291-294
    • Alberts, B.1
  • 19
    • 42249088081 scopus 로고    scopus 로고
    • How to analyze protein complexes by 2D blue native SDS-PAGE
    • Reisinger, V., and Eichacker, L. A. (2007) How to analyze protein complexes by 2D blue native SDS-PAGE. Proteomics 7, Suppl. 1, 6-16
    • (2007) Proteomics , vol.7 , Issue.SUPPL. 1 , pp. 6-16
    • Reisinger, V.1    Eichacker, L.A.2
  • 20
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schägger, H., and von Jagow, G. (1991) Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal. Biochem. 199, 223-231
    • (1991) Anal. Biochem. , vol.199 , pp. 223-231
    • Schägger, H.1    Von Jagow, G.2
  • 21
    • 0033574964 scopus 로고    scopus 로고
    • Purification of multisubunit membrane protein complexes: Isolation of chloroplast FoF1-ATP synthase, CFo and CF1 by blue native electrophoresis
    • Neff, D., and Dencher, N. A. (1999) Purification of multisubunit membrane protein complexes: isolation of chloroplast FoF1-ATP synthase, CFo and CF1 by blue native electrophoresis. Biochem. Biophys. Res. Commun. 259, 569-575
    • (1999) Biochem. Biophys. Res. Commun. , vol.259 , pp. 569-575
    • Neff, D.1    Dencher, N.A.2
  • 22
    • 1042278126 scopus 로고    scopus 로고
    • Assembly of respiratory complexes I, III, and IV into NADH oxidase supercomplex stabilizes complex I in Paracoccus denitrificans
    • Stroh, A., Anderka, O., Pfeiffer, K., Yagi, T., Finel, M., Ludwig, B., and Schägger, H. (2004) Assembly of respiratory complexes I, III, and IV into NADH oxidase supercomplex stabilizes complex I in Paracoccus denitrificans. J. Biol. Chem. 279, 5000-5007
    • (2004) J. Biol. Chem. , vol.279 , pp. 5000-5007
    • Stroh, A.1    Anderka, O.2    Pfeiffer, K.3    Yagi, T.4    Finel, M.5    Ludwig, B.6    Schägger, H.7
  • 23
    • 13244281728 scopus 로고    scopus 로고
    • Identification of NdhL and Ssl1690 (NdhO) in NDH-1L and NDH-1M complexes of Synechocystis sp. PCC 6803
    • Battchikova, N., Zhang, P., Rudd, S., Ogawa, T., and Aro, E. M. (2005) Identification of NdhL and Ssl1690 (NdhO) in NDH-1L and NDH-1M complexes of Synechocystis sp. PCC 6803. J. Biol. Chem. 280, 2587-2595
    • (2005) J. Biol. Chem. , vol.280 , pp. 2587-2595
    • Battchikova, N.1    Zhang, P.2    Rudd, S.3    Ogawa, T.4    Aro, E.M.5
  • 25
    • 2642529334 scopus 로고    scopus 로고
    • Two-dimensional Blue native/SDS gel electrophoresis of multi-protein complexes from whole cellular lysates: A proteomics approach
    • Camacho-Carvajal, M. M., Wollscheid, B., Aebersold, R., Steimle, V., and Schamel, W. W. (2004) Two-dimensional Blue native/SDS gel electrophoresis of multi-protein complexes from whole cellular lysates: a proteomics approach. Mol. Cell. Proteomics 3, 176-182
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 176-182
    • Camacho-Carvajal, M.M.1    Wollscheid, B.2    Aebersold, R.3    Steimle, V.4    Schamel, W.W.5
  • 26
    • 17144376352 scopus 로고    scopus 로고
    • Two-dimensional Blue Native/sodium dodecyl sulfate gel electrophoresis for analysis of multimeric proteins in platelets
    • Claeys, D., Geering, K., and Meyer, B. J. (2005) Two-dimensional Blue Native/sodium dodecyl sulfate gel electrophoresis for analysis of multimeric proteins in platelets. Electrophoresis 26, 1189-1199
    • (2005) Electrophoresis , vol.26 , pp. 1189-1199
    • Claeys, D.1    Geering, K.2    Meyer, B.J.3
  • 27
    • 33748346853 scopus 로고    scopus 로고
    • A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis
    • Lasserre, J. P., Beyne, E., Pyndiah, S., Lapaillerie, D., Claverol, S., and Bonneu, M. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27, 3306-3321
    • (2006) Electrophoresis , vol.27 , pp. 3306-3321
    • Lasserre, J.P.1    Beyne, E.2    Pyndiah, S.3    Lapaillerie, D.4    Claverol, S.5    Bonneu, M.6
  • 31
    • 0037443871 scopus 로고    scopus 로고
    • A revised annotation and comparative analysis of Helicobacter pylori genomes
    • DOI 10.1093/nar/gkg250
    • Boneca, I. G., de Reuse, H., Epinat, J. C., Pupin, M., Labigne, A., and Moszer, I. (2003) A revised annotation and comparative analysis of Helicobacter pylori genomes. Nucleic Acids Res. 31, 1704-1714 (Pubitemid 36336572)
    • (2003) Nucleic Acids Research , vol.31 , Issue.6 , pp. 1704-1714
    • Boneca, I.G.1    De Reuse, H.2    Epinat, J.-C.3    Pupin, M.4    Labigne, A.5    Moszer, I.6
  • 32
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • DOI 10.1093/nar/25.17.3389
    • Altschul, S. F., Madden, T. L., Schäffer, A. A., Zhang, J., Zhang, Z., Miller, W., and Lipman, D. J. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25, 3389-3402 (Pubitemid 27359211)
    • (1997) Nucleic Acids Research , vol.25 , Issue.17 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5    Miller, W.6    Lipman, D.J.7
  • 33
    • 38549130733 scopus 로고    scopus 로고
    • STITCH: Interaction networks of chemicals and proteins
    • DOI 10.1093/nar/gkm795
    • Kuhn, M., von Mering, C., Campillos, M., Jensen, L. J., and Bork, P. (2008) STITCH: interaction networks of chemicals and proteins. Nucleic Acids Res. 36, D684-D688 (Pubitemid 351149807)
    • (2008) Nucleic Acids Research , vol.36 , Issue.SUPPL. 1
    • Kuhn, M.1    Von Mering, C.2    Campillos, M.3    Jensen, L.J.4    Bork, P.5
  • 34
    • 0028214450 scopus 로고
    • Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis
    • DOI 10.1006/abio.1994.1112
    • Schägger, H., Cramer, W. A., and von Jagow, G. (1994) Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis. Anal. Biochem. 217, 220-230 (Pubitemid 24080754)
    • (1994) Analytical Biochemistry , vol.217 , Issue.2 , pp. 220-230
    • Schagger, H.1    Cramer, W.A.2    Von Jagow, G.3
  • 36
    • 0031578724 scopus 로고    scopus 로고
    • Cloning and functional characterization of Helicobacter pylori fumarate reductase operon comprising three structural genes coding for subunits C, A and B
    • Ge, Z., Jiang, Q., Kalisiak, M. S., and Taylor, D. E. (1997) Cloning and functional characterization of Helicobacter pylori fumarate reductase operon comprising three structural genes coding for subunits C, A and B. Gene 204, 227-234
    • (1997) Gene , vol.204 , pp. 227-234
    • Ge, Z.1    Jiang, Q.2    Kalisiak, M.S.3    Taylor, D.E.4
  • 38
    • 0036249007 scopus 로고    scopus 로고
    • Potential of fumarate reductase as a novel therapeutic target in Helicobacter pylori infection
    • Ge, Z. (2002) Potential of fumarate reductase as a novel therapeutic target in Helicobacter pylori infection. Expert Opin. Ther. Targets 6, 135-146
    • (2002) Expert Opin. Ther. Targets , vol.6 , pp. 135-146
    • Ge, Z.1
  • 39
    • 0034910352 scopus 로고    scopus 로고
    • Proteome analysis of Helicobacter pylori: Major proteins of type strain NCTC 11637
    • Lock, R. A., Cordwell, S. J., Coombs, G. W., Walsh, B. J., and Forbes, G. M. (2001) Proteome analysis of Helicobacter pylori: major proteins of type strain NCTC 11637. Pathology 33, 365-374
    • (2001) Pathology , vol.33 , pp. 365-374
    • Lock, R.A.1    Cordwell, S.J.2    Coombs, G.W.3    Walsh, B.J.4    Forbes, G.M.5
  • 40
    • 1642581485 scopus 로고    scopus 로고
    • The RecA Protein of Helicobacter pylori Requires a Posttranslational Modification for Full Activity
    • DOI 10.1128/JB.186.3.777-784.2004
    • Fischer, W., and Haas, R. (2004) The RecA protein of Helicobacter pylori requires a posttranslational modification for full activity. J. Bacteriol. 186, 777-784 (Pubitemid 38129656)
    • (2004) Journal of Bacteriology , vol.186 , Issue.3 , pp. 777-784
    • Fischer, W.1    Haas, R.2
  • 41
    • 0034739860 scopus 로고    scopus 로고
    • Cloning and characterization of a 22 kDa outer-membrane protein (Omp22) from Helicobacter pylori
    • Kim, J. S., Chang, J. H., Seo, W. Y., Yu, G. J., Chung, S. I., and Yum, J. S. (2000) Cloning and characterization of a 22 kDa outer-membrane protein (Omp22) from Helicobacter pylori. Mol. Cells 10, 633-641
    • (2000) Mol. Cells , vol.10 , pp. 633-641
    • Kim, J.S.1    Chang, J.H.2    Seo, W.Y.3    Yu, G.J.4    Chung, S.I.5    Yum, J.S.6
  • 43
    • 0022374615 scopus 로고
    • The beta subunit of the Escherichia coli ATP synthase exhibits a tight membrane binding property
    • Aris, J. P., and Simoni, R. D. (1985) The beta subunit of the Escherichia coli ATP synthase exhibits a tight membrane binding property. Biochem. Biophys. Res. Commun. 128, 155-162
    • (1985) Biochem. Biophys. Res. Commun. , vol.128 , pp. 155-162
    • Aris, J.P.1    Simoni, R.D.2
  • 45
    • 0029916337 scopus 로고    scopus 로고
    • Capacity of Helicobacter pylori to generate ionic gradients at low pH is similar to that of bacteria which grow under strongly acidic conditions
    • Matin, A., Zychlinsky, E., Keyhan, M., and Sachs, G. (1996) Capacity of Helicobacter pylori to generate ionic gradients at low pH is similar to that of bacteria which grow under strongly acidic conditions. Infect. Immun. 64, 1434-1436 (Pubitemid 26102413)
    • (1996) Infection and Immunity , vol.64 , Issue.4 , pp. 1434-1436
    • Matin, A.1    Zychlinsky, E.2    Keyhan, M.3    Sachs, G.4
  • 46
    • 0030611407 scopus 로고    scopus 로고
    • Analysis of F1F0-ATPase from Helicobacter pylori
    • McGowan, C. C., Cover, T. L., and Blaser, M. J. (1997) Analysis of F1F0-ATPase from Helicobacter pylori. Infect. Immun. 65, 2640-2647
    • (1997) Infect. Immun. , vol.65 , pp. 2640-2647
    • McGowan, C.C.1    Cover, T.L.2    Blaser, M.J.3
  • 47
    • 33748300901 scopus 로고    scopus 로고
    • Comparative immunoproteomics of identification and characterization of virulence factors from Helicobacter pylori related to gastric cancer
    • Lin, Y. F., Wu, M. S., Chang, C. C., Lin, S. W., Lin, J. T., Sun, Y. J., Chen, D. S., and Chow, L. P. (2006) Comparative immunoproteomics of identification and characterization of virulence factors from Helicobacter pylori related to gastric cancer. Mol. Cell. Proteomics 5, 1484-1496
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 1484-1496
    • Lin, Y.F.1    Wu, M.S.2    Chang, C.C.3    Lin, S.W.4    Lin, J.T.5    Sun, Y.J.6    Chen, D.S.7    Chow, L.P.8
  • 48
    • 0033978078 scopus 로고    scopus 로고
    • Identification of immunodominant antigens from Helicobacter pylori and evaluation of their reactivities with sera from patients with different gastroduodenal pathologies
    • DOI 10.1128/IAI.68.2.915-920.2000
    • Kimmel, B., Bosserhoff, A., Frank, R., Gross, R., Goebel, W., and Beier, D. (2000) Identification of immunodominant antigens from Helicobacter pylori and evaluation of their reactivities with sera from patients with different gastroduodenal pathologies. Infect. Immun. 68, 915-920 (Pubitemid 30056553)
    • (2000) Infection and Immunity , vol.68 , Issue.2 , pp. 915-920
    • Kimmel, B.1    Bosserhoff, A.2    Frank, R.3    Gross, R.4    Goebel, W.5    Beier, D.6
  • 49
    • 0034806355 scopus 로고    scopus 로고
    • Novel macrolide-specific ABC-type efflux transporter in Escherichia coli
    • Kobayashi, N., Nishino, K., and Yamaguchi, A. (2001) Novel macrolide-specific ABC-type efflux transporter in Escherichia coli. J. Bacteriol. 183, 5639-5644
    • (2001) J. Bacteriol. , vol.183 , pp. 5639-5644
    • Kobayashi, N.1    Nishino, K.2    Yamaguchi, A.3
  • 50
    • 33846263341 scopus 로고    scopus 로고
    • Reconstitution of the Escherichia coli macrolide transporter: The periplasmic membrane fusion protein MacA stimulates the ATPase activity of MacB
    • Tikhonova, E. B., Devroy, V. K., Lau, S. Y., and Zgurskaya, H. I. (2007) Reconstitution of the Escherichia coli macrolide transporter: the periplasmic membrane fusion protein MacA stimulates the ATPase activity of MacB. Mol. Microbiol. 63, 895-910
    • (2007) Mol. Microbiol. , vol.63 , pp. 895-910
    • Tikhonova, E.B.1    Devroy, V.K.2    Lau, S.Y.3    Zgurskaya, H.I.4
  • 51
    • 0028926676 scopus 로고
    • Genes acrA and acrB encode a stress-induced efflux system of Escherichia coli
    • Ma, D., Cook, D. N., Alberti, M., Pon, N. G., Nikaido, H., and Hearst, J. E. (1995) Genes acrA and acrB encode a stress-induced efflux system of Escherichia coli. Mol. Microbiol. 16, 45-55
    • (1995) Mol. Microbiol. , vol.16 , pp. 45-55
    • Ma, D.1    Cook, D.N.2    Alberti, M.3    Pon, N.G.4    Nikaido, H.5    Hearst, J.E.6
  • 52
    • 0033858392 scopus 로고    scopus 로고
    • Molecular construction of a multidrug exporter system, AcrAB: Molecular interaction between AcrA and AcrB, and cleavage of the N-terminal signal sequence of AcrA
    • Kawabe, T., Fujihira, E., and Yamaguchi, A. (2000) Molecular construction of a multidrug exporter system, AcrAB: molecular interaction between AcrA and AcrB, and cleavage of the N-terminal signal sequence of AcrA. J. Biochem. 128, 195-200
    • (2000) J. Biochem. , vol.128 , pp. 195-200
    • Kawabe, T.1    Fujihira, E.2    Yamaguchi, A.3
  • 53
    • 3542998054 scopus 로고    scopus 로고
    • AcrA, AcrB, and TolC of Escherichia coli form a stable intermembrane multidrug efflux complex
    • DOI 10.1074/jbc.M402230200
    • Tikhonova, E. B., and Zgurskaya, H. I. (2004) AcrA, AcrB, and TolC of Escherichia coli form a stable intermembrane multidrug efflux complex. J. Biol. Chem. 279, 32116-32124 (Pubitemid 39014658)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.31 , pp. 32116-32124
    • Tikhonova, E.B.1    Zgurskaya, H.I.2
  • 54
  • 56
    • 0033515434 scopus 로고    scopus 로고
    • Alignment and structure prediction of divergent protein families: Periplasmic and outer membrane proteins of bacterial efflux pumps
    • Johnson, J. M., and Church, G. M. (1999) Alignment and structure prediction of divergent protein families: periplasmic and outer membrane proteins of bacterial efflux pumps. J. Mol. Biol. 287, 695-715
    • (1999) J. Mol. Biol. , vol.287 , pp. 695-715
    • Johnson, J.M.1    Church, G.M.2
  • 57
    • 16244385589 scopus 로고    scopus 로고
    • A Helicobacter pylori TolC efflux pump confers resistance to metronidazole
    • DOI 10.1128/AAC.49.4.1477-1482.2005
    • van Amsterdam, K., Bart, A., and van der Ende, A. (2005) A Helicobacter pylori TolC efflux pump confers resistance to metronidazole. Antimicrob. Agents Chemother. 49, 1477-1482 (Pubitemid 40463379)
    • (2005) Antimicrobial Agents and Chemotherapy , vol.49 , Issue.4 , pp. 1477-1482
    • Van Amsterdam, K.1    Bart, A.2    Van Der Ende, A.3
  • 58
    • 58149235373 scopus 로고    scopus 로고
    • Efflux pump gene hefA of Helicobacter pylori plays an important role in multidrug resistance
    • Liu, Z. Q., Zheng, P. Y., and Yang, P. C. (2008) Efflux pump gene hefA of Helicobacter pylori plays an important role in multidrug resistance. World J. Gastroenterol. 14, 5217-5222
    • (2008) World J. Gastroenterol. , vol.14 , pp. 5217-5222
    • Liu, Z.Q.1    Zheng, P.Y.2    Yang, P.C.3
  • 59
    • 65449155090 scopus 로고    scopus 로고
    • Crystal structure of the multidrug exporter MexB from Pseudomonas aeruginosa
    • Sennhauser, G., Bukowska, M. A., Briand, C., and Grütter, M. G. (2009) Crystal structure of the multidrug exporter MexB from Pseudomonas aeruginosa. J. Mol. Biol. 389, 134-145
    • (2009) J. Mol. Biol. , vol.389 , pp. 134-145
    • Sennhauser, G.1    Bukowska, M.A.2    Briand, C.3    Grütter, M.G.4
  • 60
    • 34447545490 scopus 로고    scopus 로고
    • Direct analysis of the extracellular proteome from two strains of Helicobacter pylori
    • Smith, T. G., Lim, J. M., Weinberg, M. V., Wells, L., and Hoover, T. R. (2007) Direct analysis of the extracellular proteome from two strains of Helicobacter pylori. Proteomics 7, 2240-2245
    • (2007) Proteomics , vol.7 , pp. 2240-2245
    • Smith, T.G.1    Lim, J.M.2    Weinberg, M.V.3    Wells, L.4    Hoover, T.R.5
  • 61
    • 0031039252 scopus 로고    scopus 로고
    • Cloning and characterization of the Helicobacter pylori flbA gene, which codes for a membrane protein involved in coordinated expression of flagellar genes
    • Schmitz, A., Josenhans, C., and Suerbaum, S. (1997) Cloning and characterization of the Helicobacter pylori flbA gene, which codes for a membrane protein involved in coordinated expression of flagellar genes. J. Bacteriol. 179, 987-997 (Pubitemid 27076556)
    • (1997) Journal of Bacteriology , vol.179 , Issue.4 , pp. 987-997
    • Schmitz, A.1    Josenhans, C.2    Suerbaum, S.3
  • 62
    • 0030027155 scopus 로고    scopus 로고
    • Axonemal dyneins: Assembly, organization, and regulation
    • Porter, M. E. (1996) Axonemal dyneins: assembly, organization, and regulation. Curr. Opin. Cell Biol. 8, 10-17
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 10-17
    • Porter, M.E.1
  • 64
    • 0033918170 scopus 로고    scopus 로고
    • Comparative genomics of Helicobacter pylori: Analysis of the outer membrane protein families
    • DOI 10.1128/IAI.68.7.4155-4168.2000
    • Alm, R. A., Bina, J., Andrews, B. M., Doig, P., Hancock, R. E., and Trust, T. J. (2000) Comparative genomics of Helicobacter pylori: analysis of the outer membrane protein families. Infect. Immun. 68, 4155-4168 (Pubitemid 30434570)
    • (2000) Infection and Immunity , vol.68 , Issue.7 , pp. 4155-4168
    • Alm, R.A.1    Bina, J.2    Andrews, B.M.3    Doig, P.4    Hancock, R.E.W.5    Trust, T.J.6
  • 66
    • 0035015690 scopus 로고    scopus 로고
    • Characterization of four members of a multigene family encoding outer membrane proteins of Helicobacter pylori and their potential for vaccination
    • Peck, B., Ortkamp, M., Nau, U., Niederweis, M., Hundt, E., and Knapp, B. (2001) Characterization of four members of a multigene family encoding outer membrane proteins of Helicobacter pylori and their potential for vaccination. Microbes Infect. 3, 171-179
    • (2001) Microbes Infect. , vol.3 , pp. 171-179
    • Peck, B.1    Ortkamp, M.2    Nau, U.3    Niederweis, M.4    Hundt, E.5    Knapp, B.6
  • 68
    • 0029591597 scopus 로고
    • Isolation and characterization of a conserved porin protein from Helicobacter pylori
    • Doig, P., Exner, M. M., Hancock, R. E., and Trust, T. J. (1995) Isolation and characterization of a conserved porin protein from Helicobacter pylori. J. Bacteriol. 177, 5447-5452
    • (1995) J. Bacteriol. , vol.177 , pp. 5447-5452
    • Doig, P.1    Exner, M.M.2    Hancock, R.E.3    Trust, T.J.4
  • 70
    • 0032983194 scopus 로고    scopus 로고
    • Genetic and functional characterization of the alpAB gene locus essential for the adhesion of Helicobacter pylori to human gastric tissue
    • Odenbreit, S., Till, M., Hofreuter, D., Faller, G., and Haas, R. (1999) Genetic and functional characterization of the alpAB gene locus essential for the adhesion of Helicobacter pylori to human gastric tissue. Mol. Microbiol. 31, 1537-1548
    • (1999) Mol. Microbiol. , vol.31 , pp. 1537-1548
    • Odenbreit, S.1    Till, M.2    Hofreuter, D.3    Faller, G.4    Haas, R.5
  • 71
    • 0036745347 scopus 로고    scopus 로고
    • Role of the alpAB proteins and lipopolysaccharide in adhesion of Helicobacter pylori to human gastric tissue
    • Odenbreit, S., Faller, G., and Haas, R. (2002) Role of the alpAB proteins and lipopolysaccharide in adhesion of Helicobacter pylori to human gastric tissue. Int. J. Med. Microbiol. 292, 247-256
    • (2002) Int. J. Med. Microbiol. , vol.292 , pp. 247-256
    • Odenbreit, S.1    Faller, G.2    Haas, R.3
  • 72
    • 2342479097 scopus 로고    scopus 로고
    • Role of the Helicobacter pylori outer-membrane proteins AlpA and AlpB in colonization of the guinea pig stomach
    • de Jonge, R., Durrani, Z., Rijpkema, S. G., Kuipers, E. J., van Vliet, A. H., and Kusters, J. G. (2004) Role of the Helicobacter pylori outer-membrane proteins AlpA and AlpB in colonization of the guinea pig stomach. J. Med. Microbiol. 53, 375-379
    • (2004) J. Med. Microbiol. , vol.53 , pp. 375-379
    • De Jonge, R.1    Durrani, Z.2    Rijpkema, S.G.3    Kuipers, E.J.4    Van Vliet, A.H.5    Kusters, J.G.6
  • 73
    • 34250309216 scopus 로고    scopus 로고
    • Functional and intracellular signaling differences associated with the Helicobacter pylori AlpAB adhesin from Western and East Asian strains
    • Lu, H., Wu, J. Y., Beswick, E. J., Ohno, T., Odenbreit, S., Haas, R., Reyes, V. E., Kita, M., Graham, D. Y., and Yamaoka, Y. (2007) Functional and intracellular signaling differences associated with the Helicobacter pylori AlpAB adhesin from Western and East Asian strains. J. Biol. Chem. 282, 6242-6254
    • (2007) J. Biol. Chem. , vol.282 , pp. 6242-6254
    • Lu, H.1    Wu, J.Y.2    Beswick, E.J.3    Ohno, T.4    Odenbreit, S.5    Haas, R.6    Reyes, V.E.7    Kita, M.8    Graham, D.Y.9    Yamaoka, Y.10
  • 75
    • 0034691065 scopus 로고    scopus 로고
    • A M(r) 34,000 proinflammatory outer membrane protein (oipA) of Helicobacter pylori
    • Yamaoka, Y., Kwon, D. H., and Graham, D. Y. (2000) A M(r) 34,000 proinflammatory outer membrane protein (oipA) of Helicobacter pylori. Proc. Natl. Acad. Sci. U.S.A. 97, 7533-7538
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 7533-7538
    • Yamaoka, Y.1    Kwon, D.H.2    Graham, D.Y.3
  • 76
    • 40749136361 scopus 로고    scopus 로고
    • OipA plays a role in Helicobacter pylori-induced focal adhesion kinase activation and cytoskeletal re-organization
    • Tabassam, F. H., Graham, D. Y., and Yamaoka, Y. (2008) OipA plays a role in Helicobacter pylori-induced focal adhesion kinase activation and cytoskeletal re-organization. Cell. Microbiol. 10, 1008-1020
    • (2008) Cell. Microbiol. , vol.10 , pp. 1008-1020
    • Tabassam, F.H.1    Graham, D.Y.2    Yamaoka, Y.3
  • 78
    • 1242319255 scopus 로고    scopus 로고
    • Modification of Helicobacter pylori outer membrane protein expression during experimental infection of rhesus macaques
    • Solnick, J. V., Hansen, L. M., Salama, N. R., Boonjakuakul, J. K., and Syvanen, M. (2004) Modification of Helicobacter pylori outer membrane protein expression during experimental infection of rhesus macaques. Proc. Natl. Acad. Sci. U.S.A. 101, 2106-2111
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 2106-2111
    • Solnick, J.V.1    Hansen, L.M.2    Salama, N.R.3    Boonjakuakul, J.K.4    Syvanen, M.5
  • 85
    • 21744446057 scopus 로고    scopus 로고
    • Events at the host-microbial interface of the gastrointestinal tract: IV. The pathogenesis of Helicobacter pylori persistence
    • DOI 10.1152/ajpgi.00086.2005
    • Peek, R. M., Jr. (2005) Events at the host-microbial interface of the gastrointestinal tract IV. The pathogenesis of Helicobacter pylori persistence. Am. J. Physiol. Gastrointest. Liver Physiol. 289, G8-G12 (Pubitemid 40944218)
    • (2005) American Journal of Physiology - Gastrointestinal and Liver Physiology , vol.289 , Issue.1
    • Peek Jr., R.M.1
  • 86
    • 0035266309 scopus 로고    scopus 로고
    • Key importance of the Helicobacter pylori adherence factor blood group antigen binding adhesin during chronic gastric inflammation
    • Prinz, C., Schöniger, M., Rad, R., Becker, I., Keiditsch, E., Wagenpfeil, S., Classen, M., Rösch, T., Schepp, W., and Gerhard, M. (2001) Key importance of the Helicobacter pylori adherence factor blood group antigen binding adhesin during chronic gastric inflammation. Cancer Res. 61, 1903-1909 (Pubitemid 32692006)
    • (2001) Cancer Research , vol.61 , Issue.5 , pp. 1903-1909
    • Prinz, C.1    Schoniger, M.2    Rad, R.3    Becker, I.4    Keiditsch, E.5    Wagenpfeil, S.6    Classen, M.7    Rosch, T.8    Schepp, W.9    Gerhard, M.10
  • 87
    • 0019423084 scopus 로고
    • A monosialoganglioside is a monoclonal antibody-defined antigen of colon carcinoma
    • Magnani, J. L., Brockhaus, M., Smith, D. F., Ginsburg, V., Blaszczyk, M., Mitchell, K. F., Steplewski, Z., and Koprowski, H. (1981) A monosialoganglioside is a monoclonal antibody-defined antigen of colon carcinoma. Science 212, 55-56 (Pubitemid 11114677)
    • (1981) Science , vol.212 , Issue.4490 , pp. 55-56
    • Magnani, J.L.1    Brockhaus, M.2    Smith, D.F.3
  • 90
    • 25444513414 scopus 로고    scopus 로고
    • Inter-species horizontal transfer resulting in core-genome and nicheadaptive variation within Helicobacter pylori
    • Saunders, N. J., Boonmee, P., Peden, J. F., and Jarvis, S. A. (2005) Inter-species horizontal transfer resulting in core-genome and nicheadaptive variation within Helicobacter pylori. BMC Genomics 6, 9
    • (2005) BMC Genomics , vol.6 , pp. 9
    • Saunders, N.J.1    Boonmee, P.2    Peden, J.F.3    Jarvis, S.A.4
  • 91
    • 33644864421 scopus 로고    scopus 로고
    • Interaction between host gastric sialyl-Lewis x and H. pylori SabA enhances H. pylori density in patients lacking gastric Lewis B antigen
    • DOI 10.1111/j.1572-0241.2006.00358.x
    • Sheu, B. S., Odenbreit, S., Hung, K. H., Liu, C. P., Sheu, S. M., Yang, H. B., and Wu, J. J. (2006) Interaction between host gastric Sialyl-Lewis X and H. pylori SabA enhances H. pylori density in patients lacking gastric Lewis B antigen. Am. J. Gastroenterol. 101, 36-44 (Pubitemid 43381706)
    • (2006) American Journal of Gastroenterology , vol.101 , Issue.1 , pp. 36-44
    • Sheu, B.-S.1    Odenbreit, S.2    Hung, K.-H.3    Liu, C.-P.4    Sheu, S.-M.5    Yang, H.-B.6    Wu, J.-J.7
  • 92
    • 12344321439 scopus 로고    scopus 로고
    • Frequencies of the expression of main protein antigens from Helicobacter pylori isolates and production of specific serum antibodies in infected patients
    • Yan, J., Mao, Y. F., and Shao, Z. X. (2005) Frequencies of the expression of main protein antigens from Helicobacter pylori isolates and production of specific serum antibodies in infected patients. World J. Gastroenterol. 11, 421-425
    • (2005) World J. Gastroenterol. , vol.11 , pp. 421-425
    • Yan, J.1    Mao, Y.F.2    Shao, Z.X.3
  • 93
    • 0000088667 scopus 로고    scopus 로고
    • Nucleotide metabolism
    • Mobley, H. L. T., Mendz, G. L., and Hazell, S. L., eds ASM Press, Washington D. C. Chapter 13
    • Mendz, G. L. (2001) Nucleotide metabolism, in Helicobacter pylori: Physiology and Genetics (Mobley, H. L. T., Mendz, G. L., and Hazell, S. L., eds) ASM Press, Washington D. C. Chapter 13, pp. 147-158
    • (2001) Helicobacter Pylori: Physiology and Genetics , pp. 147-158
    • Mendz, G.L.1
  • 95
    • 0029046363 scopus 로고
    • Identification of carboxylation enzymes and characterization of a novel four-subunit pyruvate:flavodoxin oxidoreductase from Helicobacter pylori
    • Hughes, N. J., Chalk, P. A., Clayton, C. L., and Kelly, D. J. (1995) Identification of carboxylation enzymes and characterization of a novel four-subunit pyruvate:flavodoxin oxidoreductase from Helicobacter pylori. J. Bacteriol. 177, 3953-3959
    • (1995) J. Bacteriol. , vol.177 , pp. 3953-3959
    • Hughes, N.J.1    Chalk, P.A.2    Clayton, C.L.3    Kelly, D.J.4
  • 96
    • 0031885642 scopus 로고    scopus 로고
    • Helicobacter pylori porCDAB and oorDABC genes encode distinct pyruvate: Flavodoxin and 2-oxoglutarate:acceptor oxidoreductases which mediate electron transport to NADP
    • Hughes, N. J., Clayton, C. L., Chalk, P. A., and Kelly, D. J. (1998) Helicobacter pylori porCDAB and oorDABC genes encode distinct pyruvate: flavodoxin and 2-oxoglutarate:acceptor oxidoreductases which mediate electron transport to NADP. J. Bacteriol. 180, 1119-1128
    • (1998) J. Bacteriol. , vol.180 , pp. 1119-1128
    • Hughes, N.J.1    Clayton, C.L.2    Chalk, P.A.3    Kelly, D.J.4
  • 97
    • 0029741586 scopus 로고    scopus 로고
    • Metabolic activities of metronidazole-sensitive and -resistant strains of Helicobacter pylori: Repression of pyruvate oxidoreductase and expression of isocitrate lyase activity correlate with resistance
    • Hoffman, P. S., Goodwin, A., Johnsen, J., Magee, K., and Veldhuyzen van Zanten, S. J. (1996) Metabolic activities of metronidazole-sensitive and -resistant strains of Helicobacter pylori: repression of pyruvate oxidoreductase and expression of isocitrate lyase activity correlate with resistance. J. Bacteriol. 178, 4822-4829 (Pubitemid 26321281)
    • (1996) Journal of Bacteriology , vol.178 , Issue.16 , pp. 4822-4829
    • Hoffman, P.S.1    Goodwin, A.2    Johnsen, J.3    Magee, K.4    Van Zanten, S.J.O.V.5
  • 99
    • 35748965549 scopus 로고    scopus 로고
    • Antibacterial targets in fatty acid biosynthesis
    • Wright, H. T., and Reynolds, K. A. (2007) Antibacterial targets in fatty acid biosynthesis. Curr. Opin. Microbiol. 10, 447-453
    • (2007) Curr. Opin. Microbiol. , vol.10 , pp. 447-453
    • Wright, H.T.1    Reynolds, K.A.2
  • 100
    • 38949097460 scopus 로고    scopus 로고
    • Inhibitors of FabI, an enzyme drug target in the bacterial fatty acid biosynthesis pathway
    • Lu, H., and Tonge, P. J. (2008) Inhibitors of FabI, an enzyme drug target in the bacterial fatty acid biosynthesis pathway. Acc. Chem. Res. 41, 11-20
    • (2008) Acc. Chem. Res. , vol.41 , pp. 11-20
    • Lu, H.1    Tonge, P.J.2
  • 101
    • 0032488897 scopus 로고    scopus 로고
    • IDP3 encodes a peroxisomal NADP-dependent isocitrate dehydrogenase required for the beta-oxidation of unsaturated fatty acids
    • DOI 10.1074/jbc.273.6.3702
    • Henke, B., Girzalsky, W., Berteaux-Lecellier, V., and Erdmann, R. (1998) IDP3 encodes a peroxisomal NADP-dependent isocitrate dehydrogenase required for the beta-oxidation of unsaturated fatty acids. J. Biol. Chem. 273, 3702-3711 (Pubitemid 28109798)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.6 , pp. 3702-3711
    • Henke, B.1    Girzalsky, W.2    Berteaux-Lecellier, V.3    Erdmann, R.4
  • 102
    • 0032472937 scopus 로고    scopus 로고
    • Peroxisomal beta-oxidation of polyunsaturated fatty acids in Saccharomyces cerevisiae: Isocitrate dehydrogenase provides NADPH for reduction of double bonds at even positions
    • van Roermund, C. W., Hettema, E. H., Kal, A. J., van den Berg, M., Tabak, H. F., and Wanders, R. J. (1998) Peroxisomal beta-oxidation of polyunsaturated fatty acids in Saccharomyces cerevisiae: isocitrate dehydrogenase provides NADPH for reduction of double bonds at even positions. EMBO J. 17, 677-687
    • (1998) EMBO J. , vol.17 , pp. 677-687
    • Van Roermund, C.W.1    Hettema, E.H.2    Kal, A.J.3    Van Den Berg, M.4    Tabak, H.F.5    Wanders, R.J.6
  • 103
    • 41949086428 scopus 로고    scopus 로고
    • Structural basis for catalytic and inhibitory mechanisms of beta-hydroxyacyl-acyl carrier protein dehydratase (FabZ)
    • Zhang, L., Liu, W., Hu, T., Du, L., Luo, C., Chen, K., Shen, X., and Jiang, H. (2008) Structural basis for catalytic and inhibitory mechanisms of beta-hydroxyacyl-acyl carrier protein dehydratase (FabZ). J. Biol. Chem. 283, 5370-5379
    • (2008) J. Biol. Chem. , vol.283 , pp. 5370-5379
    • Zhang, L.1    Liu, W.2    Hu, T.3    Du, L.4    Luo, C.5    Chen, K.6    Shen, X.7    Jiang, H.8
  • 104
    • 0030431493 scopus 로고    scopus 로고
    • The enoyl-[acyl-carrier-protein] reductase (FabI) of Escherichia coli, which catalyzes a key regulatory step in fatty acid biosynthesis, accepts NADH and NADPH as cofactors and is inhibited by palmitoyl-CoA
    • Bergler, H., Fuchsbichler, S., Högenauer, G., and Turnowsky, F. (1996) The enoyl-[acyl-carrier-protein] reductase (FabI) of Escherichia coli, which catalyzes a key regulatory step in fatty acid biosynthesis, accepts NADH and NADPH as cofactors and is inhibited by palmitoyl-CoA. Eur. J. Biochem. 242, 689-694
    • (1996) Eur. J. Biochem. , vol.242 , pp. 689-694
    • Bergler, H.1    Fuchsbichler, S.2    Högenauer, G.3    Turnowsky, F.4
  • 105
    • 0032492647 scopus 로고    scopus 로고
    • Syntheses and evaluation of benzodiazaborine compounds against M. tuberculosis H37Rv in vitro
    • Davis, M. C., Franzblau, S. G., and Martin, A. R. (1998) Syntheses and evaluation of benzodiazaborine compounds against M. tuberculosis H37Rv in vitro. Bioorg. Med. Chem. Lett. 8, 843-846
    • (1998) Bioorg. Med. Chem. Lett. , vol.8 , pp. 843-846
    • Davis, M.C.1    Franzblau, S.G.2    Martin, A.R.3
  • 106
    • 0033709606 scopus 로고    scopus 로고
    • Isoniazid affects multiple components of the type II fatty acid synthase system of Mycobacterium tuberculosis
    • Slayden, R. A., Lee, R. E., and Barry, C. E., 3rd (2000) Isoniazid affects multiple components of the type II fatty acid synthase system of Mycobacterium tuberculosis. Mol. Microbiol. 38, 514-525
    • (2000) Mol. Microbiol. , vol.38 , pp. 514-525
    • Slayden, R.A.1    Lee, R.E.2    Barry III, C.E.3
  • 108
    • 27744530740 scopus 로고    scopus 로고
    • Up-expression of NapA and other oxidative stress proteins is a compensatory response to loss of major Helicobacter pylori stress resistance factors
    • DOI 10.1080/10715760500306729
    • Olczak, A. A., Wang, G., and Maier, R. J. (2005) Up-expression of NapA and other oxidative stress proteins is a compensatory response to loss of major Helicobacter pylori stress resistance factors. Free Radic. Res. 39, 1173-1182 (Pubitemid 41601419)
    • (2005) Free Radical Research , vol.39 , Issue.11 , pp. 1173-1182
    • Olczak, A.A.1    Wang, G.2    Maier, R.J.3
  • 109
  • 110
    • 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
  • 112
    • 34347386473 scopus 로고    scopus 로고
    • Flavodoxin:quinone reductase (FqrB): A redox partner of pyruvate:ferredoxin oxidoreductase that reversibly couples pyruvate oxidation to NADPH production in Helicobacter pylori and Campylobacter jejuni
    • St Maurice, M., Cremades, N., Croxen, M. A., Sisson, G., Sancho, J., and Hoffman, P. S. (2007) Flavodoxin:quinone reductase (FqrB): a redox partner of pyruvate:ferredoxin oxidoreductase that reversibly couples pyruvate oxidation to NADPH production in Helicobacter pylori and Campylobacter jejuni. J. Bacteriol. 189, 4764-4773
    • (2007) J. Bacteriol. , vol.189 , pp. 4764-4773
    • St Maurice, M.1    Cremades, N.2    Croxen, M.A.3    Sisson, G.4    Sancho, J.5    Hoffman, P.S.6
  • 113
    • 0031946770 scopus 로고    scopus 로고
    • How chaperones fold proteins
    • Beissinger, M., and Buchner, J. (1998) How chaperones fold proteins. Biol. Chem. 379, 245-259
    • (1998) Biol. Chem. , vol.379 , pp. 245-259
    • Beissinger, M.1    Buchner, J.2
  • 115
    • 0027300506 scopus 로고
    • Heat shock proteins: Molecular chaperones of protein biogenesis
    • Craig, E. A., Gambill, B. D., and Nelson, R. J. (1993) Heat shock proteins: molecular chaperones of protein biogenesis. Microbiol. Rev. 57, 402-414
    • (1993) Microbiol. Rev. , vol.57 , pp. 402-414
    • Craig, E.A.1    Gambill, B.D.2    Nelson, R.J.3
  • 116
    • 0027333423 scopus 로고
    • Role of the major heat shock proteins as molecular chaperones
    • Georgopoulos, C., and Welch, W. J. (1993) Role of the major heat shock proteins as molecular chaperones. Annu. Rev. Cell Biol. 9, 601-634
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 601-634
    • Georgopoulos, C.1    Welch, W.J.2
  • 117
    • 0028117314 scopus 로고
    • Molecular chaperones in protein folding: The art of avoiding sticky situations
    • Hartl, F. U., Hlodan, R., and Langer, T. (1994) Molecular chaperones in protein folding: the art of avoiding sticky situations. Trends Biochem. Sci. 19, 20-25
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 20-25
    • Hartl, F.U.1    Hlodan, R.2    Langer, T.3
  • 118
    • 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., Lin, J. T., 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. U.S.A. 103, 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
  • 120
    • 17044389822 scopus 로고    scopus 로고
    • Subproteomes of soluble and structure-bound Helicobacter pylori proteins analyzed by two-dimensional gel electrophoresis and mass spectrometry
    • Backert, S., Kwok, T., Schmid, M., Selbach, M., Moese, S., Peek, R. M., Jr., König, W., Meyer, T. F., and Jungblut, P. R. (2005) Subproteomes of soluble and structure-bound Helicobacter pylori proteins analyzed by two-dimensional gel electrophoresis and mass spectrometry. Proteomics 5, 1331-1345
    • (2005) Proteomics , vol.5 , pp. 1331-1345
    • Backert, S.1    Kwok, T.2    Schmid, M.3    Selbach, M.4    Moese, S.5    Peek Jr., R.M.6    König, W.7    Meyer, T.F.8    Jungblut, P.R.9
  • 122
    • 33750452313 scopus 로고    scopus 로고
    • Effects of cadmium stress on growth, morphology, and protein expression in Rhodobacter capsulatus B10
    • Mohamed Fahmy Gad El-Rab, S., Abdel-Fattah Shoreit, A., and Fukumori, Y. (2006) Effects of cadmium stress on growth, morphology, and protein expression in Rhodobacter capsulatus B10. Biosci. Biotechnol. Biochem. 70, 2394-2402
    • (2006) Biosci. Biotechnol. Biochem. , vol.70 , pp. 2394-2402
    • Mohamed Fahmy Gad El-Rab, S.1    Abdel-Fattah Shoreit, A.2    Fukumori, Y.3
  • 123
    • 0025375220 scopus 로고
    • Heat-shock proteins DnaK and GroEL facilitate export of LacZ hybrid proteins GroEL and DnaK
    • Phillips, G. J., and Silhavy, T. J. (1990) Heat-shock proteins DnaK and GroEL facilitate export of LacZ hybrid proteins GroEL and DnaK. Nature 344, 882-884
    • (1990) Nature , vol.344 , pp. 882-884
    • Phillips, G.J.1    Silhavy, T.J.2
  • 124
    • 0032730207 scopus 로고    scopus 로고
    • The autoregulatory HspR repressor protein governs chaperone gene transcription in Helicobacter pylori
    • Spohn, G., and Scarlato, V. (1999) The autoregulatory HspR repressor protein governs chaperone gene transcription in Helicobacter pylori. Mol. Microbiol. 34, 663-674
    • (1999) Mol. Microbiol. , vol.34 , pp. 663-674
    • Spohn, G.1    Scarlato, V.2
  • 125
    • 39149136478 scopus 로고    scopus 로고
    • The human gastric pathogen Helicobacter pylori has a potential acetone carboxylase that enhances its ability to colonize mice
    • Brahmachary, P., Wang, G., Benoit, S. L., Weinberg, M. V., Maier, R. J., and Hoover, T. R. (2008) The human gastric pathogen Helicobacter pylori has a potential acetone carboxylase that enhances its ability to colonize mice. BMC Microbiol. 8, 14
    • (2008) BMC Microbiol. , vol.8 , pp. 14
    • Brahmachary, P.1    Wang, G.2    Benoit, S.L.3    Weinberg, M.V.4    Maier, R.J.5    Hoover, T.R.6
  • 126
    • 4644324511 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of an acetone carboxylase from Xanthobacter autotrophicus strain Py2
    • Nocek, B., Boyd, J., Ensign, S. A., and Peters, J. W. (2004) Crystallization and preliminary X-ray analysis of an acetone carboxylase from Xanthobacter autotrophicus strain Py2. Acta. Crystallogr. D Biol. Crystallogr. 60, 385-387
    • (2004) Acta. Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 385-387
    • Nocek, B.1    Boyd, J.2    Ensign, S.A.3    Peters, J.W.4
  • 127
    • 33947154219 scopus 로고    scopus 로고
    • The orphan response regulator HP1021 of Helicobacter pylori regulates transcription of a gene cluster presumably involved in acetone metabolism
    • DOI 10.1128/JB.01827-06
    • Pflock, M., Bathon, M., Schär, J., Müller, S., Mollenkopf, H., Meyer, T. F., and Beier, D. (2007) The orphan response regulator HP1021 of Helicobacter pylori regulates transcription of a gene cluster presumably involved in acetone metabolism. J. Bacteriol. 189, 2339-2349 (Pubitemid 46411348)
    • (2007) Journal of Bacteriology , vol.189 , Issue.6 , pp. 2339-2349
    • Pflock, M.1    Bathon, M.2    Schar, J.3    Muller, S.4    Mollenkopf, H.5    Meyer, T.F.6    Beier, D.7
  • 128
    • 5644298311 scopus 로고    scopus 로고
    • Helicobacter pylori vaccine development based on combined subproteome analysis
    • Bumann, D., Jungblut, P. R., and Meyer, T. F. (2004) Helicobacter pylori vaccine development based on combined subproteome analysis. Proteomics 4, 2843-2848
    • (2004) Proteomics , vol.4 , pp. 2843-2848
    • Bumann, D.1    Jungblut, P.R.2    Meyer, T.F.3
  • 130
    • 0036185045 scopus 로고    scopus 로고
    • Specific identification of three low molecular weight membrane-associated antigens of Helicobacter pylori
    • DOI 10.1046/j.1365-2036.2002.01221.x
    • Voland, P., Weeks, D. L., Vaira, D., Prinz, C., and Sachs, G. (2002) Specific identification of three low molecular weight membrane-associated antigens of Helicobacter pylori. Aliment. Pharmacol. Ther. 16, 533-544 (Pubitemid 34214534)
    • (2002) Alimentary Pharmacology and Therapeutics , vol.16 , Issue.3 , pp. 533-544
    • Voland, P.1    Weeks, D.L.2    Vaira, D.3    Prinz, C.4    Sachs, G.5
  • 131
    • 33845879606 scopus 로고    scopus 로고
    • Difference analysis on proteome of Helicobacter pylori in patients with peptic ulcer, gastritis, and gastric cancer
    • Zhang, J., Ding, S. G., Zhong, L. J., Lin, S. R., Yang, B., Peng, J. R., and Lou, Y. X. (2006) Difference analysis on proteome of Helicobacter pylori in patients with peptic ulcer, gastritis, and gastric cancer. Zhonghua Yi Xue Za Zhi 86, 2690-2694
    • (2006) Zhonghua Yi Xue Za Zhi , vol.86 , pp. 2690-2694
    • Zhang, J.1    Ding, S.G.2    Zhong, L.J.3    Lin, S.R.4    Yang, B.5    Peng, J.R.6    Lou, Y.X.7
  • 133
    • 67651246985 scopus 로고    scopus 로고
    • Detection and evaluation of antibodies against neutrophil-activating protein of Helicobacter pylori in patients with gastric cancer
    • Long, M., Luo, J., Li, Y., Zeng, F. Y., and Li, M. (2009) Detection and evaluation of antibodies against neutrophil-activating protein of Helicobacter pylori in patients with gastric cancer. World J. Gastroenterol. 15, 2381-2388
    • (2009) World J. Gastroenterol. , vol.15 , pp. 2381-2388
    • Long, M.1    Luo, J.2    Li, Y.3    Zeng, F.Y.4    Li, M.5
  • 136
    • 4444378917 scopus 로고    scopus 로고
    • Biochemical characterization of protein complexes from the Helicobacter pylori protein interaction map: Strategies for complex formation and evidence for novel interactions within type IV secretion systems
    • DOI 10.1074/mcp.M400048-MCP200
    • Terradot, L., Durnell, N., Li, M., Li, M., Ory, J., Labigne, A., Legrain, P., Colland, F., and Waksman, G. (2004) Biochemical characterization of protein complexes from the Helicobacter pylori protein interaction map: strategies for complex formation and evidence for novel interactions within type IV secretion systems. Mol. Cell. Proteomics 3, 809-819 (Pubitemid 39206262)
    • (2004) Molecular and Cellular Proteomics , vol.3 , Issue.8 , pp. 809-819
    • Terradot, L.1    Durnell, N.2    Li, M.3    Li, M.4    Ory, J.5    Labigne, A.6    Legrain, P.7    Colland, F.8    Waksman, G.9
  • 138
    • 40449098575 scopus 로고    scopus 로고
    • Protein subassemblies of the Helicobacter pylori cag type IV secretion system revealed by localization and interaction studies
    • DOI 10.1128/JB.01341-07
    • Kutter, S., Buhrdorf, R., Haas, J., Schneider-Brachert, W., Haas, R., and Fischer, W. (2008) Protein subassemblies of the Helicobacter pylori Cag type IV secretion system revealed by localization and interaction studies. J. Bacteriol. 190, 2161-2171 (Pubitemid 351355339)
    • (2008) Journal of Bacteriology , vol.190 , Issue.6 , pp. 2161-2171
    • Kutter, S.1    Buhrdorf, R.2    Haas, J.3    Schneider-Brachert, W.4    Haas, R.5    Fischer, W.6
  • 139
    • 0037008715 scopus 로고    scopus 로고
    • Identification of surface proteins of Helicobacter pylori by selective biotinylation, affinity purification, and two-dimensional gel electrophoresis
    • DOI 10.1074/jbc.M204473200
    • Sabarth, N., Lamer, S., Zimny-Arndt, U., Jungblut, P. R., Meyer, T. F., and Bumann, D. (2002) Identification of surface proteins of Helicobacter pylori by selective biotinylation, affinity purification, and two-dimensional gel electrophoresis. J. Biol. Chem. 277, 27896-27902 (Pubitemid 34966736)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.31 , pp. 27896-27902
    • Sabarth, N.1    Lamer, S.2    Zimny-Arndt, U.3    Jungblut, P.R.4    Meyer, T.F.5    Bumann, D.6
  • 140
    • 0035319960 scopus 로고    scopus 로고
    • Proteome analysis of the common human pathogen Helicobacter pylori
    • Bumann, D., Meyer, T. F., and Jungblut, P. R. (2001) Proteome analysis of the common human pathogen Helicobacter pylori. Proteomics 1, 473-479
    • (2001) Proteomics , vol.1 , pp. 473-479
    • Bumann, D.1    Meyer, T.F.2    Jungblut, P.R.3
  • 141
    • 5644272061 scopus 로고    scopus 로고
    • Analysis of automatically generated peptide mass fingerprints of cellular proteins and antigens from Helicobacter pylori 26695 separated by two-dimensional electrophoresis
    • Krah, A., Schmidt, F., Becher, D., Schmid, M., Albrecht, D., Rack, A., Büttner, K., and Jungblut, P. R. (2003) Analysis of automatically generated peptide mass fingerprints of cellular proteins and antigens from Helicobacter pylori 26695 separated by two-dimensional electrophoresis. Mol. Cell. Proteomics 2, 1271-1283
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 1271-1283
    • Krah, A.1    Schmidt, F.2    Becher, D.3    Schmid, M.4    Albrecht, D.5    Rack, A.6    Büttner, K.7    Jungblut, P.R.8
  • 142
    • 23744476040 scopus 로고    scopus 로고
    • Identification of Helicobacter pylori surface proteins by selective proteinase K digestion and antibody phage display
    • DOI 10.1016/j.mimet.2005.04.030, PII S0167701205001429
    • Sabarth, N., Hurvitz, R., Schmidt, M., Zimny-Arndt, U., Jungblut, P. R., Meyer, T. F., and Bumann, D. (2005) Identification of Helicobacter pylori surface proteins by selective proteinase K digestion and antibody phage display. J. Microbiol. Methods 62, 345-349 (Pubitemid 41140124)
    • (2005) Journal of Microbiological Methods , vol.62 , Issue.3 SPEC. ISSUE , pp. 345-349
    • Sabarth, N.1    Hurvitz, R.2    Schmidt, M.3    Zimny-Arndt, U.4    Jungblut, P.R.5    Meyer, T.F.6    Bumann, D.7
  • 143
    • 33644556825 scopus 로고    scopus 로고
    • Comparative proteomic analysis of Helicobacter pylori strains associated with iron deficiency anemia
    • Park, S. A., Lee, H. W., Hong, M. H., Choi, Y. W., Choe, Y. H., Ahn, B. Y., Cho, Y. J., Kim, D. S., and Lee, N. G. (2006) Comparative proteomic analysis of Helicobacter pylori strains associated with iron deficiency anemia. Proteomics 6, 1319-1328
    • (2006) Proteomics , vol.6 , pp. 1319-1328
    • Park, S.A.1    Lee, H.W.2    Hong, M.H.3    Choi, Y.W.4    Choe, Y.H.5    Ahn, B.Y.6    Cho, Y.J.7    Kim, D.S.8    Lee, N.G.9
  • 147
    • 13444262436 scopus 로고    scopus 로고
    • Predicting protein-protein interactions using signature products
    • Martin, S., Roe, D., and Faulon, J. L. (2005) Predicting protein-protein interactions using signature products. Bioinformatics 21, 218-226
    • (2005) Bioinformatics , vol.21 , pp. 218-226
    • Martin, S.1    Roe, D.2    Faulon, J.L.3
  • 148
    • 23844447959 scopus 로고    scopus 로고
    • Identification of protein complexes by comparative analysis of yeast and bacterial protein interaction data
    • Sharan, R., Ideker, T., Kelley, B., Shamir, R., and Karp, R. M. (2005) Identification of protein complexes by comparative analysis of yeast and bacterial protein interaction data. J. Comput. Biol. 12, 835-846
    • (2005) J. Comput. Biol. , vol.12 , pp. 835-846
    • Sharan, R.1    Ideker, T.2    Kelley, B.3    Shamir, R.4    Karp, R.M.5
  • 149
    • 33748661458 scopus 로고    scopus 로고
    • NetAlign: A web-based tool for comparison of protein interaction networks
    • DOI 10.1093/bioinformatics/btl287
    • Liang, Z., Xu, M., Teng, M., and Niu, L. (2006) NetAlign: a web-based tool for comparison of protein interaction networks. Bioinformatics 22, 2175-2177 (Pubitemid 44390916)
    • (2006) Bioinformatics , vol.22 , Issue.17 , pp. 2175-2177
    • Liang, Z.1    Xu, M.2    Teng, M.3    Niu, L.4
  • 150
    • 33745202607 scopus 로고    scopus 로고
    • In silico identification of potential therapeutic targets in the human pathogen Helicobacter pylori
    • Dutta, A., Singh, S. K., Ghosh, P., Mukherjee, R., Mitter, S., and Bandyopadhyay, D. (2006) In silico identification of potential therapeutic targets in the human pathogen Helicobacter pylori. In Silico Biol. 6, 43-47
    • (2006) In Silico Biol. , vol.6 , pp. 43-47
    • Dutta, A.1    Singh, S.K.2    Ghosh, P.3    Mukherjee, R.4    Mitter, S.5    Bandyopadhyay, D.6
  • 152
    • 0031858042 scopus 로고    scopus 로고
    • Identification of potential diagnostic and vaccine candidates of Helicobacter pylori by two-dimensional gel electrophoresis, sequence analysis, and serum profiling
    • McAtee, C. P., Lim, M. Y., Fung, K., Velligan, M., Fry, K., Chow, T., and Berg, D. E. (1998) Identification of potential diagnostic and vaccine candidates of Helicobacter pylori by two-dimensional gel electrophoresis, sequence analysis, and serum profiling. Clin. Diagn. Lab. Immunol. 5, 537-542
    • (1998) Clin. Diagn. Lab. Immunol. , vol.5 , pp. 537-542
    • McAtee, C.P.1    Lim, M.Y.2    Fung, K.3    Velligan, M.4    Fry, K.5    Chow, T.6    Berg, D.E.7
  • 159
    • 33645865541 scopus 로고    scopus 로고
    • Type IV secretion systems and their effectors in bacterial pathogenesis
    • Backert, S., and Meyer, T. F. (2006) Type IV secretion systems and their effectors in bacterial pathogenesis. Curr. Opin. Microbiol. 9, 207-217
    • (2006) Curr. Opin. Microbiol. , vol.9 , pp. 207-217
    • Backert, S.1    Meyer, T.F.2
  • 161
    • 17344379177 scopus 로고    scopus 로고
    • Translocation of Helicobacter pylori CagA into gastric epithelial cells by type IV secretion
    • DOI 10.1126/science.287.5457.1497
    • Odenbreit, S., Püls, J., Sedlmaier, B., Gerland, E., Fischer, W., and Haas, R. (2000) Translocation of Helicobacter pylori CagA into gastric epithelial cells by type IV secretion. Science 287, 1497-1500 (Pubitemid 30127145)
    • (2000) Science , vol.287 , Issue.5457 , pp. 1497-1500
    • Odenbreit, S.1    Puls, J.2    Sedlmaier, B.3    Gerland, E.4    Fischer, W.5    Haas, R.6
  • 162
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh, A., Larsson, B., von Heijne, G., and Sonnhammer, E. L. (2001) Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 305, 567-580
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.4
  • 163
    • 0033767941 scopus 로고    scopus 로고
    • New roles for structure in biology and drug discovery
    • Russell, R. B., and Eggleston, D. S. (2000) New roles for structure in biology and drug discovery. Nat. Struct. Biol. 7, (suppl.) 928-930
    • (2000) Nat. Struct. Biol. , vol.7 , Issue.SUPPL. , pp. 928-930
    • Russell, R.B.1    Eggleston, D.S.2
  • 165
    • 18944379249 scopus 로고    scopus 로고
    • High-resolution crystallography and drug design
    • Cachau, R. E., and Podjarny, A. D. (2005) High-resolution crystallography and drug design. J. Mol. Recognit. 18, 196-202
    • (2005) J. Mol. Recognit. , vol.18 , pp. 196-202
    • Cachau, R.E.1    Podjarny, A.D.2
  • 166
    • 33645377497 scopus 로고    scopus 로고
    • Structure-based development of target-specific compound libraries
    • Orry, A. J., Abagyan, R. A., and Cavasotto, C. N. (2006) Structure-based development of target-specific compound libraries. Drug Discov. Today 11, 261-266
    • (2006) Drug Discov. Today , vol.11 , pp. 261-266
    • Orry, A.J.1    Abagyan, R.A.2    Cavasotto, C.N.3
  • 167
    • 3042621274 scopus 로고    scopus 로고
    • The progress of membrane protein structure determination
    • DOI 10.1110/ps.04712004
    • White, S. H. (2004) The progress of membrane protein structure determination. Protein Sci. 13, 1948-1949 (Pubitemid 38822136)
    • (2004) Protein Science , vol.13 , Issue.7 , pp. 1948-1949
    • White, S.H.1
  • 168
    • 19744376674 scopus 로고    scopus 로고
    • Biochemistry: Global topology analysis of the Escherichia coli inner membrane proteome
    • DOI 10.1126/science.1109730
    • Daley, D. O., Rapp, M., Granseth, E., Melén, K., Drew, D., and von Heijne, G. (2005) Global topology analysis of the Escherichia coli inner membrane proteome. Science 308, 1321-1323 (Pubitemid 40746130)
    • (2005) Science , vol.308 , Issue.5726 , pp. 1321-1323
    • Daley, D.O.1    Rapp, M.2    Granseth, E.3    Melen, K.4    Drew, D.5    Von Heijne, G.6
  • 169
    • 0025823864 scopus 로고
    • Essential role of urease in pathogenesis of gastritis induced by Helicobacter pylori in gnotobiotic piglets
    • Eaton, K. A., Brooks, C. L., Morgan, D. R., and Krakowka, S. (1991) Essential role of urease in pathogenesis of gastritis induced by Helicobacter pylori in gnotobiotic piglets. Infect. Immun. 59, 2470-2475
    • (1991) Infect. Immun. , vol.59 , pp. 2470-2475
    • Eaton, K.A.1    Brooks, C.L.2    Morgan, D.R.3    Krakowka, S.4
  • 170
    • 0025301120 scopus 로고
    • Urea protects Helicobacter (Campylobacter) pylori from the bactericidal effect of acid
    • Marshall, B. J., Barrett, L. J., Prakash, C., McCallum, R. W., and Guerrant, R. L. (1990) Urea protects Helicobacter (Campylobacter) pylori from the bactericidal effect of acid. Gastroenterology 99, 697-702
    • (1990) Gastroenterology , vol.99 , pp. 697-702
    • Marshall, B.J.1    Barrett, L.J.2    Prakash, C.3    McCallum, R.W.4    Guerrant, R.L.5
  • 174
    • 0025369322 scopus 로고
    • Purification and characterization of urease from Helicobacter pylori
    • Dunn, B. E., Campbell, G. P., Perez-Perez, G. I., and Blaser, M. J. (1990) Purification and characterization of urease from Helicobacter pylori. J. Biol. Chem. 265, 9464-9469
    • (1990) J. Biol. Chem. , vol.265 , pp. 9464-9469
    • Dunn, B.E.1    Campbell, G.P.2    Perez-Perez, G.I.3    Blaser, M.J.4
  • 175
    • 0026716505 scopus 로고
    • Urease-associated heat shock protein of Helicobacter pylori
    • Evans, D. J., Jr., Evans, D. G., Engstrand, L., and Graham, D. Y. (1992) Urease-associated heat shock protein of Helicobacter pylori. Infect. Immun. 60, 2125-2127
    • (1992) Infect. Immun. , vol.60 , pp. 2125-2127
    • Evans Jr., D.J.1    Evans, D.G.2    Engstrand, L.3    Graham, D.Y.4
  • 176
    • 36549011754 scopus 로고    scopus 로고
    • Identification, structure and mode of action of a new regulator of the Helicobacter pylori HP0525 ATPase
    • DOI 10.1038/sj.emboj.7601904, PII 7601904
    • Hare, S., Fischer, W., Williams, R., Terradot, L., Bayliss, R., Haas, R., and Waksman, G. (2007) Identification, structure and mode of action of a new regulator of the Helicobacter pylori HP0525 ATPase. EMBO J. 26, 4926-4934 (Pubitemid 350191302)
    • (2007) EMBO Journal , vol.26 , Issue.23 , pp. 4926-4934
    • Hare, S.1    Fischer, W.2    Williams, R.3    Terradot, L.4    Bayliss, R.5    Haas, R.6    Waksman, G.7
  • 177
    • 37049016054 scopus 로고    scopus 로고
    • Functional assembly of the Na+/H+ antiporter of Helicobacter pylori from partial fragments in vivo
    • Karasawa, A., Mitsui, K., Matsushita, M., and Kanazawa, H. (2007) Functional assembly of the Na+/H+ antiporter of Helicobacter pylori from partial fragments in vivo. Biochemistry 46, 14272-14283
    • (2007) Biochemistry , vol.46 , pp. 14272-14283
    • Karasawa, A.1    Mitsui, K.2    Matsushita, M.3    Kanazawa, H.4
  • 178
    • 0037432528 scopus 로고    scopus 로고
    • How reliable are experimental protein-protein interaction data?
    • DOI 10.1016/S0022-2836(03)00239-0
    • Sprinzak, E., Sattath, S., and Margalit, H. (2003) How reliable are experimental protein-protein interaction data? J. Mol. Biol. 327, 919-923 (Pubitemid 36363701)
    • (2003) Journal of Molecular Biology , vol.327 , Issue.5 , pp. 919-923
    • Sprinzak, E.1    Sattath, S.2    Margalit, H.3
  • 179
    • 0033566727 scopus 로고    scopus 로고
    • Conservation, localization and expression of HopZ, a protein involved in adhesion of Helicobacter pylori
    • DOI 10.1093/nar/27.16.3325
    • Peck, B., Ortkamp, M., Diehl, K. D., Hundt, E., and Knapp, B. (1999) Conservation, localization and expression of HopZ, a protein involved in adhesion of Helicobacter pylori. Nucleic Acids Res. 27, 3325-3333 (Pubitemid 29381326)
    • (1999) Nucleic Acids Research , vol.27 , Issue.16 , pp. 3325-3333
    • Peck, B.1    Ortkamp, M.2    Diehl, K.D.3    Hundt, E.4    Knapp, B.5
  • 180
    • 0032161919 scopus 로고    scopus 로고
    • Identification of potential diagnostic and vaccine candidates of Helicobacter pylori by "proteome" technologies
    • McAtee, C. P., Fry, K. E., and Berg, D. E. (1998) Identification of potential diagnostic and vaccine candidates of Helicobacter pylori by "proteome" technologies. Helicobacter 3, 163-169
    • (1998) Helicobacter , vol.3 , pp. 163-169
    • McAtee, C.P.1    Fry, K.E.2    Berg, D.E.3
  • 181
    • 2942590493 scopus 로고    scopus 로고
    • Recombinant antigen from Helicobacter pylori urease as vaccine against H. pylori-associated disease
    • DOI 10.1002/bit.20047
    • Fujii, R., Morihara, F., Fukushima, K., Oku, T., Hifumi, E., and Uda, T. (2004) Recombinant antigen from Helicobacter pylori urease as vaccine against H. pylori-associated disease. Biotechnol. Bioeng. 86, 737-746 (Pubitemid 38745691)
    • (2004) Biotechnology and Bioengineering , vol.86 , Issue.7 , pp. 737-746
    • Fujii, R.1    Morihara, F.2    Fukushima, K.3    Oku, T.4    Hifumi, E.5    Uda, T.6
  • 184
    • 0036777086 scopus 로고    scopus 로고
    • Conservative region of the genes encoding four adhesins of Helicobacter pylori: Cloning, sequence analysis and biological information analysis
    • Bai, Y., Zhang, Y. L., Wang, J. D., Lin, H. J., Zhang, Z. S., and Zhou, D. Y. (2002) Conservative region of the genes encoding four adhesins of Helicobacter pylori: cloning, sequence analysis and biological information analysis. Di Yi Jun Yi Da Xue Xue Bao 22, 869-871
    • (2002) Di Yi Jun Yi Da Xue Xue Bao , vol.22 , pp. 869-871
    • Bai, Y.1    Zhang, Y.L.2    Wang, J.D.3    Lin, H.J.4    Zhang, Z.S.5    Zhou, D.Y.6
  • 185
    • 0346793599 scopus 로고    scopus 로고
    • Cloning and immunogenicity of conservative region of adhesin gene of Helicobacter pylori
    • Bai, Y., Zhang, Y. L., Wang, J. D., Zhang, Z. S., and Zhou, D. Y. (2003) Cloning and immunogenicity of conservative region of adhesin gene of Helicobacter pylori. Zhonghua Yi Xue Za Zhi 83, 736-739
    • (2003) Zhonghua Yi Xue Za Zhi , vol.83 , pp. 736-739
    • Bai, Y.1    Zhang, Y.L.2    Wang, J.D.3    Zhang, Z.S.4    Zhou, D.Y.5
  • 186
    • 0034004724 scopus 로고    scopus 로고
    • Functional expression in Escherichia coli and membrane topology of porin HopE, a member of a large family of conserved proteins in Helicobacter pylori
    • Bina, J., Bains, M., and Hancock, R. E. (2000) Functional expression in Escherichia coli and membrane topology of porin HopE, a member of a large family of conserved proteins in Helicobacter pylori. J. Bacteriol. 182, 2370-2375
    • (2000) J. Bacteriol. , vol.182 , pp. 2370-2375
    • Bina, J.1    Bains, M.2    Hancock, R.E.3


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