메뉴 건너뛰기




Volumn 56, Issue 3, 2008, Pages 279-286

Tip-α (hp0596 gene product) is a highly immunogenic Helicobacter pylori protein involved in colonization of mouse gastric mucosa

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL DNA; BACTERIAL PROTEIN; GENE PRODUCT; INTERLEUKIN 1ALPHA; TIP ALPHA PROTEIN; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 39149119270     PISSN: 03438651     EISSN: 14320991     Source Type: Journal    
DOI: 10.1007/s00284-007-9083-7     Document Type: Article
Times cited : (24)

References (57)
  • 1
    • 4043052866 scopus 로고    scopus 로고
    • Accurate prediction of solvent accessibility using neural networks-based regression
    • Adamczak R, Porollo A, Meller J (2004) Accurate prediction of solvent accessibility using neural networks-based regression. Proteins 56:753-767
    • (2004) Proteins , vol.56 , pp. 753-767
    • Adamczak, R.1    Porollo, A.2    Meller, J.3
  • 2
    • 33750075748 scopus 로고    scopus 로고
    • Helicobacter pylori persistence: An overview of interactions between H. pylori and host immune defenses
    • Algood HM, Cover TL (2006) Helicobacter pylori persistence: an overview of interactions between H. pylori and host immune defenses. Clin Microbiol Rev 19:597-613
    • (2006) Clin Microbiol Rev , vol.19 , pp. 597-613
    • Algood, H.M.1    Cover, T.L.2
  • 3
    • 0033552961 scopus 로고    scopus 로고
    • Genomic-sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori
    • Alm RA, Ling LS, Moir DT et al. (1999) Genomic-sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori. Nature 397:176-180
    • (1999) Nature , vol.397 , pp. 176-180
    • Alm, R.A.1    Ling, L.S.2    Moir, D.T.3
  • 4
    • 0021711731 scopus 로고
    • Simple, rapid, and quantitative release of periplasmic proteins by chloroform
    • Ames GF, Prody C, Kustu S (1984) Simple, rapid, and quantitative release of periplasmic proteins by chloroform. J Bacteriol 160:1181-1183
    • (1984) J Bacteriol , vol.160 , pp. 1181-1183
    • Ames, G.F.1    Prody, C.2    Kustu, S.3
  • 5
    • 10744232629 scopus 로고    scopus 로고
    • Proteomic analysis of the sarcosine-insoluble outer membrane fraction of Helicobacter pylori strain 26695
    • Baik SC, Kim KM, Song SM et al. (2004) Proteomic analysis of the sarcosine-insoluble outer membrane fraction of Helicobacter pylori strain 26695. J Bacteriol 186:949-955
    • (2004) J Bacteriol , vol.186 , pp. 949-955
    • Baik, S.C.1    Kim, K.M.2    Song, S.M.3
  • 6
    • 18744390550 scopus 로고    scopus 로고
    • Effect of interlukin-1beta on proliferation of gastric epithelial cells in culture
    • Beales IL (2002) Effect of interlukin-1beta on proliferation of gastric epithelial cells in culture. BMC Gastroenterol 2:7
    • (2002) BMC Gastroenterol , vol.2 , pp. 7
    • Beales, I.L.1
  • 7
    • 0020604645 scopus 로고
    • Identification and characterization of Campylobacter jejuni outer membrane proteins
    • Blaser MJ, Hopkins JA, Berka RM et al. (1983) Identification and characterization of Campylobacter jejuni outer membrane proteins. Infect Immun 42:276-284
    • (1983) Infect Immun , vol.42 , pp. 276-284
    • Blaser, M.J.1    Hopkins, J.A.2    Berka, R.M.3
  • 8
    • 0036089516 scopus 로고    scopus 로고
    • Proteome analysis of secreted proteins of the gastric pathogen Helicobacter pylori
    • Bumann D, Aksu S, Wendland M et al. (2002) Proteome analysis of secreted proteins of the gastric pathogen Helicobacter pylori. Infect Immun 70:3396-3403
    • (2002) Infect Immun , vol.70 , pp. 3396-3403
    • Bumann, D.1    Aksu, S.2    Wendland, M.3
  • 9
    • 15944418287 scopus 로고    scopus 로고
    • Helicobacter pylori VacA, a paradigm for toxin multifunctionality
    • Cover TL, Blanke SR (2005) Helicobacter pylori VacA, a paradigm for toxin multifunctionality. Nat Rev Microbiol 3:320-332
    • (2005) Nat Rev Microbiol , vol.3 , pp. 320-332
    • Cover, T.L.1    Blanke, S.R.2
  • 10
    • 0034663597 scopus 로고    scopus 로고
    • Application of multiple sequence alignment profiles to improve protein secondary structure prediction
    • Cuff JA, Barton GJ (2000) Application of multiple sequence alignment profiles to improve protein secondary structure prediction. Proteins 40:502-511
    • (2000) Proteins , vol.40 , pp. 502-511
    • Cuff, J.A.1    Barton, G.J.2
  • 11
    • 4744350150 scopus 로고    scopus 로고
    • Protective effect of vaccination with DNA of the H. pylori genomic library in experimentally infected mice
    • Dzwonek A, Mikula M, Woszczynski M et al. (2004) Protective effect of vaccination with DNA of the H. pylori genomic library in experimentally infected mice. Cell Mol Biol Lett 9:483-495
    • (2004) Cell Mol Biol Lett , vol.9 , pp. 483-495
    • Dzwonek, A.1    Mikula, M.2    Woszczynski, M.3
  • 12
    • 0010050956 scopus 로고
    • Solubilization of the cytoplasmic membrane of Escherichia coli by the ionic detergent sodium-lauryl sarcosinate
    • Filip C, Fletcher G, L. Wulff JL, et al. (1973) Solubilization of the cytoplasmic membrane of Escherichia coli by the ionic detergent sodium-lauryl sarcosinate. J Bacteriol 175:966-972
    • (1973) J Bacteriol , vol.175 , pp. 966-972
    • Filip, C.1    Fletcher, G.2    L. Wulff, J.L.3
  • 13
    • 0033654768 scopus 로고    scopus 로고
    • Hybrid fold recognition:combining sequence derived properties with evolutionary information
    • World Scientific Singapore
    • Fischer D (2000) Hybrid fold recognition:combining sequence derived properties with evolutionary information. In: Altman RB (ed) Pacific Symposium on Biocomputing. World Scientific, Singapore, pp 119-130
    • (2000) Pacific Symposium on Biocomputing , pp. 119-130
    • Fischer, D.1    Altman, R.B.2
  • 14
    • 33745755200 scopus 로고    scopus 로고
    • Helicobacter pylori protein oxidation influences the colonization process
    • Godlewska R, Dzwonek A, Mikula M et al. (2006) Helicobacter pylori protein oxidation influences the colonization process. Int J Med Microbiol 296:321-324
    • (2006) Int J Med Microbiol , vol.296 , pp. 321-324
    • Godlewska, R.1    Dzwonek, A.2    Mikula, M.3
  • 15
    • 24344498726 scopus 로고    scopus 로고
    • Restriction of DNA encoding selectable markers decreases the transformation efficiency of Helicobacter pylori
    • Gorrell RJ, Yang J, Kusters JG et al. (2005) Restriction of DNA encoding selectable markers decreases the transformation efficiency of Helicobacter pylori. FEMS Immunol Med Microbiol 44:213-219
    • (2005) FEMS Immunol Med Microbiol , vol.44 , pp. 213-219
    • Gorrell, R.J.1    Yang, J.2    Kusters, J.G.3
  • 16
    • 0036205858 scopus 로고    scopus 로고
    • Immunoproteomics of Helicobacter pylori infection and relation to gastric disease
    • Haas G, Karaali G, Ebermayer K et al. (2002) Immunoproteomics of Helicobacter pylori infection and relation to gastric disease. Proteomics 2:313-324
    • (2002) Proteomics , vol.2 , pp. 313-324
    • Haas, G.1    Karaali, G.2    Ebermayer, K.3
  • 17
    • 0030886291 scopus 로고    scopus 로고
    • A flagellar sheath protein of Helicobacter pylori is identical to HpaA, a putative N-acetylneuraminyllactose-binding hemagglutinin, but is not an adhesin for AGS cells
    • Jones AC, Logan RP, Foynes S et al. (1997) A flagellar sheath protein of Helicobacter pylori is identical to HpaA, a putative N-acetylneuraminyllactose- binding hemagglutinin, but is not an adhesin for AGS cells. J Bacteriol 179:5643-5647
    • (1997) J Bacteriol , vol.179 , pp. 5643-5647
    • Jones, A.C.1    Logan, R.P.2    Foynes, S.3
  • 18
    • 0033537993 scopus 로고    scopus 로고
    • GenTHREADER: An efficient and reliable protein fold recognition method for genomic sequences
    • Jones DT (1999) GenTHREADER: an efficient and reliable protein fold recognition method for genomic sequences. J Mol Biol 287:797-815
    • (1999) J Mol Biol , vol.287 , pp. 797-815
    • Jones, D.T.1
  • 19
    • 0042319306 scopus 로고    scopus 로고
    • Comparative proteome analysis of Helicobacter pylori
    • Jungblut PR, Bumann D, Haas G et al. (2000) Comparative proteome analysis of Helicobacter pylori. Mol Microbiol 36:710-725
    • (2000) Mol Microbiol , vol.36 , pp. 710-725
    • Jungblut, P.R.1    Bumann, D.2    Haas, G.3
  • 20
    • 0242362161 scopus 로고    scopus 로고
    • Combining local-structure, fold-recognition, and new fold methods for protein structure prediction
    • Karplus K, Karchin R, Draper J et al. (2003) Combining local-structure, fold-recognition, and new fold methods for protein structure prediction. Proteins 53:491-496
    • (2003) Proteins , vol.53 , pp. 491-496
    • Karplus, K.1    Karchin, R.2    Draper, J.3
  • 21
    • 0034087259 scopus 로고    scopus 로고
    • Immune response to an 18-kilodalton outer membrane antigen identifies lipoprotein 20 as a Helicobacter pylori vaccine candidate
    • Keenan J, Oliaro J, Domigan N et al. (2000) Immune response to an 18-kilodalton outer membrane antigen identifies lipoprotein 20 as a Helicobacter pylori vaccine candidate. Infect Immun 68:3337-3343
    • (2000) Infect Immun , vol.68 , pp. 3337-3343
    • Keenan, J.1    Oliaro, J.2    Domigan, N.3
  • 22
    • 0034595501 scopus 로고    scopus 로고
    • Enhanced genome annotation using structural profiles in the program 3D-PSSM
    • Kelley LA, MacCallum RM, Sternberg MJ (2000) Enhanced genome annotation using structural profiles in the program 3D-PSSM. J Mol Biol 299:499-520
    • (2000) J Mol Biol , vol.299 , pp. 499-520
    • Kelley, L.A.1    MacCallum, R.M.2    Sternberg, M.J.3
  • 23
    • 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
    • Kimmel B, Bosserhoff A, Frank R et al. (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
    • (2000) Infect Immun , vol.68 , pp. 915-920
    • Kimmel, B.1    Bosserhoff, A.2    Frank, R.3
  • 24
    • 0242362160 scopus 로고    scopus 로고
    • A "fRankenstein's monster" approach to comparative modeling: Merging the finest fragments of fold-recognition models and iterative model refinement aided by 3D structure evaluation
    • Suppl 6
    • Kosinski J, Cymerman IA, Feder M et al. (2003) A "FRankenstein's monster" approach to comparative modeling: merging the finest fragments of fold-recognition models and iterative model refinement aided by 3D structure evaluation. Proteins 53(Suppl 6):369-379
    • (2003) Proteins , vol.53 , pp. 369-379
    • Kosinski, J.1    Cymerman, I.A.2    Feder, M.3
  • 25
    • 0028111910 scopus 로고
    • Molecular characterization of a conserved 20-kilodalton membrane-associated lipoprotein antigen of Helicobacter pylori
    • Kostrzynska M, PW OT, Taylor DE et al. (1994) Molecular characterization of a conserved 20-kilodalton membrane-associated lipoprotein antigen of Helicobacter pylori. J Bacteriol 176:5938-5948
    • (1994) J Bacteriol , vol.176 , pp. 5938-5948
    • Kostrzynska, M.1    PW, O.T.2    Taylor, D.E.3
  • 26
    • 0043123216 scopus 로고    scopus 로고
    • GeneSilico protein structure prediction meta-server
    • Kurowski MA, Bujnicki JM (2003) GeneSilico protein structure prediction meta-server. Nucleic Acids Res 31:3305-3307
    • (2003) Nucleic Acids Res , vol.31 , pp. 3305-3307
    • Kurowski, M.A.1    Bujnicki, J.M.2
  • 28
    • 34248182034 scopus 로고    scopus 로고
    • Helicobacter pylori-secreting protein Tipalpha is a potent inducer of chemokine gene expressions in stomach cancer cells
    • Kuzuhara T, Suganuma M, Kurusu M et al. (2007) Helicobacter pylori-secreting protein Tipalpha is a potent inducer of chemokine gene expressions in stomach cancer cells. J Cancer Res Clin Oncol 133:287-296
    • (2007) J Cancer Res Clin Oncol , vol.133 , pp. 287-296
    • Kuzuhara, T.1    Suganuma, M.2    Kurusu, M.3
  • 29
    • 27744605665 scopus 로고    scopus 로고
    • Presence of a motif conserved between Helicobacter pylori TNF-alpha inducing protein (Tipalpha) and penicillin-binding proteins
    • Kuzuhara T, Suganuma M, Tsuge H et al. (2005) Presence of a motif conserved between Helicobacter pylori TNF-alpha inducing protein (Tipalpha) and penicillin-binding proteins. Biol Pharm Bull 28:2133-2137
    • (2005) Biol Pharm Bull , vol.28 , pp. 2133-2137
    • Kuzuhara, T.1    Suganuma, M.2    Tsuge, H.3
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-695
    • (1970) Nature , vol.227 , pp. 680-695
    • Laemmli, U.K.1
  • 31
    • 0033970290 scopus 로고    scopus 로고
    • In search of immunogenic Helicobacter pylori proteins by screening of expression library
    • Lazowska I, Trzeciak L, Godlewska R et al. (2000) In search of immunogenic Helicobacter pylori proteins by screening of expression library. Digestion 61:14-21
    • (2000) Digestion , vol.61 , pp. 14-21
    • Lazowska, I.1    Trzeciak, L.2    Godlewska, R.3
  • 32
    • 0030941212 scopus 로고    scopus 로고
    • A standardized mouse model of Helicobacter pylori infection: Introducing the Sydney strain
    • Lee A, O'Rourke J, De Uungria MC et al. (1997) A standardized mouse model of Helicobacter pylori infection: introducing the Sydney strain. Gastroenterology 112:1386-1397
    • (1997) Gastroenterology , vol.112 , pp. 1386-1397
    • Lee, A.1    O'Rourke, J.2    De Uungria, M.C.3
  • 33
    • 0034780030 scopus 로고    scopus 로고
    • Pcons: A neural-network-based consensus predictor that improves fold recognition
    • Lundstrom J, Rychlewski L, Bujnicki JM et al. (2001) Pcons: a neural-network-based consensus predictor that improves fold recognition. Protein Sci 10:2354-2362
    • (2001) Protein Sci , vol.10 , pp. 2354-2362
    • Lundstrom, J.1    Rychlewski, L.2    Bujnicki, J.M.3
  • 34
    • 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 CP, Lim MY, Fung K et al. (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
  • 35
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin LJ, Bryson K, Jones DT (2000) The PSIPRED protein structure prediction server. Bioinformatics 16:404-405
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 36
    • 0142027795 scopus 로고    scopus 로고
    • Coupled prediction of protein secondary and tertiary structure
    • Meiler J, Baker D (2003) Coupled prediction of protein secondary and tertiary structure. Proc Natl Acad Sci USA 100:12105-12110
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 12105-12110
    • Meiler, J.1    Baker, D.2
  • 37
    • 0141643390 scopus 로고    scopus 로고
    • Quantitative detection for low levels of Helicobacter pylori infection in experimentally infected mice by real-time PCR
    • Mikula M, Dzwonek A, Jagusztyn-Krynicka EK et al. (2003) Quantitative detection for low levels of Helicobacter pylori infection in experimentally infected mice by real-time PCR. J Microbiol Methods 55:351-359
    • (2003) J Microbiol Methods , vol.55 , pp. 351-359
    • Mikula, M.1    Dzwonek, A.2    Jagusztyn-Krynicka, E.K.3
  • 38
    • 33644931335 scopus 로고    scopus 로고
    • Comparative proteomics and immunoproteomics of Helicobacter pylori related to different gastric pathologies
    • Mini R, Bernardini G, Salzano AM et al. (2006) Comparative proteomics and immunoproteomics of Helicobacter pylori related to different gastric pathologies. J Chromatogr B Anal Technol Biomed Life Sci 833:63-79
    • (2006) J Chromatogr B Anal Technol Biomed Life Sci , vol.833 , pp. 63-79
    • Mini, R.1    Bernardini, G.2    Salzano, A.M.3
  • 39
    • 34250351484 scopus 로고    scopus 로고
    • Amino acids at positions 3 and 4 determine the membrane specificity of Pseudomonas aeruginosa lipoproteins
    • Narita S, Tokuda H (2007) Amino acids at positions 3 and 4 determine the membrane specificity of Pseudomonas aeruginosa lipoproteins. J Biol Chem 282:13372-13378
    • (2007) J Biol Chem , vol.282 , pp. 13372-13378
    • Narita, S.1    Tokuda, H.2
  • 40
    • 0028875018 scopus 로고
    • The putative neuraminyllactose-binding hemagglutinin HpaA of Helicobacter pylori CCUG 17874 is a lipoprotein
    • O'Toole P, Janzon L, Doig P et al. (1995) The putative neuraminyllactose-binding hemagglutinin HpaA of Helicobacter pylori CCUG 17874 is a lipoprotein. J Bacteriol 177:6049-6057
    • (1995) J Bacteriol , vol.177 , pp. 6049-6057
    • O'Toole, P.1    Janzon, L.2    Doig, P.3
  • 41
    • 0033933636 scopus 로고    scopus 로고
    • Cascaded multiple classifiers for secondary structure prediction
    • Ouali M, King RD (2000) Cascaded multiple classifiers for secondary structure prediction. Protein Sci 9:1162-1176
    • (2000) Protein Sci , vol.9 , pp. 1162-1176
    • Ouali, M.1    King, R.D.2
  • 44
    • 0033997036 scopus 로고    scopus 로고
    • Comparison of sequence profiles. Strategies for structural predictions using sequence information
    • Rychlewski L, Jaroszewski L, Li W et al. (2000) Comparison of sequence profiles. Strategies for structural predictions using sequence information. Protein Sci 9:232-241
    • (2000) Protein Sci , vol.9 , pp. 232-241
    • Rychlewski, L.1    Jaroszewski, L.2    Li, W.3
  • 45
    • 0036841283 scopus 로고    scopus 로고
    • Multiparameter selection of Helicobacter pylori antigens identifies two novel antigens with high protective efficacy
    • Sabarth N, Hurwitz R, Meyer TF et al. (2002) Multiparameter selection of Helicobacter pylori antigens identifies two novel antigens with high protective efficacy. Infect Immun 70:6499-6503
    • (2002) Infect Immun , vol.70 , pp. 6499-6503
    • Sabarth, N.1    Hurwitz, R.2    Meyer, T.F.3
  • 47
    • 0032701349 scopus 로고    scopus 로고
    • Testing the '+2 rule' for lipoprotein sorting in the Escherichia coli cell envelope with a new genetic selection
    • Seydel A, Gounon P, Pugsley AP (1999) Testing the '+2 rule' for lipoprotein sorting in the Escherichia coli cell envelope with a new genetic selection. Mol Microbiol 34:810-821
    • (1999) Mol Microbiol , vol.34 , pp. 810-821
    • Seydel, A.1    Gounon, P.2    Pugsley, A.P.3
  • 48
    • 0035967880 scopus 로고    scopus 로고
    • FUGUE: Sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties
    • Shi J, Blundell TL, Mizuguchi K (2001) FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. J Mol Biol 310:243-257
    • (2001) J Mol Biol , vol.310 , pp. 243-257
    • Shi, J.1    Blundell, T.L.2    Mizuguchi, K.3
  • 49
    • 0031585984 scopus 로고    scopus 로고
    • Assembly of protein tertiary structures from fragments with similar local sequences using simulated annealing and Bayesian scoring functions
    • Simons KT, Kooperberg C, Huang E et al. (1997) Assembly of protein tertiary structures from fragments with similar local sequences using simulated annealing and Bayesian scoring functions. J Mol Biol 268:209-225
    • (1997) J Mol Biol , vol.268 , pp. 209-225
    • Simons, K.T.1    Kooperberg, C.2    Huang, E.3
  • 50
    • 16344373015 scopus 로고    scopus 로고
    • Protein homology detection by HMM-HMM comparison
    • Soding J (2005) Protein homology detection by HMM-HMM comparison. Bioinformatics 21:951-960
    • (2005) Bioinformatics , vol.21 , pp. 951-960
    • Soding, J.1
  • 51
    • 17644369266 scopus 로고    scopus 로고
    • New tumor necrosis factor-alpha-inducing protein released from Helicobacter pylori for gastric cancer progression
    • Suganuma M, Kurusu M, Suzuki K et al. (2005) New tumor necrosis factor-alpha-inducing protein released from Helicobacter pylori for gastric cancer progression. J Cancer Res Clin Oncol 131:305-313
    • (2005) J Cancer Res Clin Oncol , vol.131 , pp. 305-313
    • Suganuma, M.1    Kurusu, M.2    Suzuki, K.3
  • 52
    • 32544442311 scopus 로고    scopus 로고
    • Carcinogenic role of tumor necrosis factor-alpha inducing protein of Helicobacter pylori in human stomach
    • Suganuma M, Kuzuhara T, Yamaguchi K et al. (2006) Carcinogenic role of tumor necrosis factor-alpha inducing protein of Helicobacter pylori in human stomach. J Biochem Mol Biol 39:1-8
    • (2006) J Biochem Mol Biol , vol.39 , pp. 1-8
    • Suganuma, M.1    Kuzuhara, T.2    Yamaguchi, K.3
  • 53
    • 0030835739 scopus 로고    scopus 로고
    • The complete genome sequence of the gastric pathogen Helicobacter pylori
    • Tomb JF, White O, Kerlavage AR et al. (1997) The complete genome sequence of the gastric pathogen Helicobacter pylori. Nature 388:539-547
    • (1997) Nature , vol.388 , pp. 539-547
    • Tomb, J.F.1    White, O.2    Kerlavage, A.R.3
  • 54
    • 0034708338 scopus 로고    scopus 로고
    • Inferring regulatory elements from a whole genome. An analysis of Helicobacter pylori sigma(80) family of promoter signals
    • Vanet A, Marsan L, Labigne A et al. (2000) Inferring regulatory elements from a whole genome. An analysis of Helicobacter pylori sigma(80) family of promoter signals. J Mol Biol 297:335-353
    • (2000) J Mol Biol , vol.297 , pp. 335-353
    • Vanet, A.1    Marsan, L.2    Labigne, A.3
  • 55
    • 0032892242 scopus 로고    scopus 로고
    • Cloning and characterization of a novel membrane-associated antigenic protein of Helicobacter pylori
    • Yoshida M, Wakatsuki Y, Kobayashi Y et al. (1999) Cloning and characterization of a novel membrane-associated antigenic protein of Helicobacter pylori. Infect Immun 67:286-293
    • (1999) Infect Immun , vol.67 , pp. 286-293
    • Yoshida, M.1    Wakatsuki, Y.2    Kobayashi, Y.3
  • 56
    • 0032438163 scopus 로고    scopus 로고
    • Lipoprotein release by bacteria: Potential factor in bacterial pathogenesis
    • Zhang Z, H., Niesel DW, Peterson JW et al. (1998) Lipoprotein release by bacteria: potential factor in bacterial pathogenesis. Infect Immun 66:5196-5201
    • (1998) Infect Immun , vol.66 , pp. 5196-5201
    • Zhang, Z.1    Niesel, D.W.2    Peterson, J.W.3
  • 57
    • 2542631929 scopus 로고    scopus 로고
    • Single-body residue-level knowledge-based energy score combined with sequence-profile and secondary structure information for fold recognition
    • Zhou H, Zhou Y (2004) Single-body residue-level knowledge-based energy score combined with sequence-profile and secondary structure information for fold recognition. Proteins 55:1005-1013
    • (2004) Proteins , vol.55 , pp. 1005-1013
    • Zhou, H.1    Zhou, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.