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Volumn 7, Issue 7, 2009, Pages 835-867

Novel Helicobacter pylori therapeutic targets: The unusual suspects

Author keywords

Antibacterials; Essential genes; Essential proteins; Helicobacter pylori; Host colonization; Therapeutic targets

Indexed keywords

3 DEHYDROQUINATE DEHYDRATASE; ALPHA 1,3 FUCOSYLTRANSFERASE; AMOXICILLIN; ANTIBIOTIC AGENT; CARBONATE DEHYDRATASE; CLARITHROMYCIN; CYSTATHIONINE GAMMA LYASE; DIHYDROOROTATE DEHYDROGENASE; FLAGELLIN; FLAVODOXIN; FUMARATE REDUCTASE; METRONIDAZOLE; OROTATE PHOSPHORIBOSYLTRANSFERASE; PALMITOYL COENZYME A HYDROLASE; PROTON PUMP INHIBITOR; SHIKIMIC ACID; SPERMIDINE SYNTHASE; SUPEROXIDE DISMUTASE; THIOREDOXIN REDUCTASE; UREASE; URIDINE DIPHOSPHATE GLUCOSE 4 EPIMERASE;

EID: 70350641519     PISSN: 14787210     EISSN: 17448336     Source Type: Journal    
DOI: 10.1586/ERI.09.61     Document Type: Review
Times cited : (12)

References (249)
  • 2
    • 33144473431 scopus 로고    scopus 로고
    • Bad bugs need drugs: An update on the development pipeline from the Antimicrobial Availability Task Force of the Infectious Diseases Society of America
    • Talbot GH, Bradley J, Edwards JE Jr, Gilbert D, Scheld M, Bartlett JG. Bad bugs need drugs: an update on the development pipeline from the Antimicrobial Availability Task Force of the Infectious Diseases Society of America. Clin. Infect. Dis. 42, 657-668 (2006). (Pubitemid 43271379)
    • (2006) Clinical Infectious Diseases , vol.42 , Issue.5 , pp. 657-668
    • Talbot, G.H.1    Bradley, J.2    Edwards Jr., J.E.3    Gilbert, D.4    Scheid, M.5    Bartlett, J.G.6
  • 3
    • 12944302098 scopus 로고    scopus 로고
    • Lack of development of new antimicrobial drugs: A potential serious threat to public health
    • DOI 10.1016/S1473-3099(05)01283-1, PII S1473309905012831
    • Norrby SR, Nord CE, Finch R. Lack of development of new antimicrobial drugs: a potential serious threat to public health. Lancet Infect. Dis. 5, 115-119 (2005). (Pubitemid 40174782)
    • (2005) Lancet Infectious Diseases , vol.5 , Issue.2 , pp. 115-119
    • Norrby, S.R.1    Nord, C.E.2    Finch, R.3
  • 4
    • 0033762032 scopus 로고    scopus 로고
    • Peptide aptamers: Powerful new tools for molecular medicine
    • Hoppe-Seyler F, Butz K. Peptide aptamers: powerful new tools for molecular medicine. J. Mol. Med. 78, 426-430 (2000). (Pubitemid 30809272)
    • (2000) Journal of Molecular Medicine , vol.78 , Issue.8 , pp. 426-430
    • Hoppe-Seyler, F.1    Butz, K.2
  • 5
    • 26444558214 scopus 로고    scopus 로고
    • How essential are nonessential genes?
    • DOI 10.1093/molbev/msi211
    • Fang G, Rocha E, Danchin A. How essential are nonessential genes? Mol. Biol. Evol. 22, 2147-2156 (2005). (Pubitemid 41437796)
    • (2005) Molecular Biology and Evolution , vol.22 , Issue.11 , pp. 2147-2156
    • Fang, G.1    Rocha, E.2    Danchin, A.3
  • 6
    • 0032785020 scopus 로고    scopus 로고
    • The minimal genome concept
    • Mushegian A. The minimal genome concept. Curr. Opin. Genet. Dev. 9, 709-714 (1999).
    • (1999) Curr. Opin. Genet. Dev. , vol.9 , pp. 709-714
    • Mushegian, A.1
  • 7
    • 0036259348 scopus 로고    scopus 로고
    • Protein interaction domain mapping for the selection of validated targets and lead compounds in the anti-infectious area
    • DOI 10.2174/1381612023394872
    • Legrain P, Strosberg D. Protein interaction domain mapping for the selection of validated targets and lead compounds in the anti-infectious area. Curr. Pharm. Des. 8, 1189-1198 (2002). (Pubitemid 34594249)
    • (2002) Current Pharmaceutical Design , vol.8 , Issue.13 , pp. 1189-1198
    • Legrain, P.1    Strosberg, D.2
  • 10
    • 1342289469 scopus 로고    scopus 로고
    • Review article: Impact of Helicobacter pylori on society-role for a strategy of 'search and eradicate'
    • Forman D, Graham DY. Review article: impact of Helicobacter pylori on society-role for a strategy of 'search and eradicate'. Aliment. Pharmacol. Ther. 19(Suppl. 1), 17-21 (2004).
    • (2004) Aliment. Pharmacol. Ther. , vol.19 , Issue.SUPPL. 1 , pp. 17-21
    • Forman, D.1    Graham, D.Y.2
  • 12
    • 0033591290 scopus 로고    scopus 로고
    • Helicobacter pylori virulence and genetic geography
    • DOI 10.1126/science.284.5418.1328
    • Covacci A, Telford JL, Del Giudice G, Parsonnet J, Rappuoli R. Helicobacter pylori virulence and genetic geography. Science 284, 1328-1333 (1999). (Pubitemid 29289653)
    • (1999) Science , vol.284 , Issue.5418 , pp. 1328-1333
    • Covacci, A.1    Telford, J.L.2    Del Giudice, G.3    Parsonnet, J.4    Rappuoli, R.5
  • 15
    • 42349107551 scopus 로고    scopus 로고
    • Association of inflammatory cytokine gene polymorphisms with platelet recovery in idiopathic thrombocytopenic purpura patients after the eradication of Helicobacter pylori
    • DOI 10.1159/000121392
    • Suzuki T, Matsushima M, Shirakura K et al. Association of inflammatory cytokine gene polymorphisms with platelet recovery in idiopathic thrombocytopenic purpura patients after the eradication of Helicobacter pylori. Digestion 77, 73-78 (2008). (Pubitemid 351556383)
    • (2008) Digestion , vol.77 , Issue.2 , pp. 73-78
    • Suzuki, T.1    Matsushima, M.2    Shirakura, K.3    Koike, J.4    Masui, A.5    Takagi, A.6    Shirasugi, Y.7    Ogawa, Y.8    Shirai, T.9    Mine, T.10
  • 16
    • 50249116603 scopus 로고    scopus 로고
    • Adherence, internalization, and persistence of Helicobacter pylori in hepatocytes
    • Ito K, Yamaoka Y, Ota H, El-Zimaity H, Graham DY. Adherence, internalization, and persistence of Helicobacter pylori in hepatocytes. Dig. Dis. Sci. 53, 2541-2549 (2008).
    • (2008) Dig. Dis. Sci. , vol.53 , pp. 2541-2549
    • Ito, K.1    Yamaoka, Y.2    Ota, H.3    El-Zimaity, H.4    Graham, D.Y.5
  • 18
    • 33847609214 scopus 로고    scopus 로고
    • Helicobacter pylori infection is a potential protective factor against conventional multiple sclerosis in the Japanese population
    • DOI 10.1016/j.jneuroim.2006.12.010, PII S0165572806005236, Inflammation, Neurodegeneration and Neuroprotection in the Central Nervous System
    • Li W, Minohara M, Su JJ et al. Helicobacter pylori infection is a potential protective factor against conventional multiple sclerosis in the Japanese population. J. Neuroimmunol. 184, 227-231 (2007). (Pubitemid 46366004)
    • (2007) Journal of Neuroimmunology , vol.184 , Issue.1-2 , pp. 227-231
    • Li, W.1    Minohara, M.2    Su, J.J.3    Matsuoka, T.4    Osoegawa, M.5    Ishizu, T.6    Kira, J.-I.7
  • 19
    • 34548145839 scopus 로고    scopus 로고
    • Extragastric manifestations of Helicobacter pylori infection - Other Helicobacters
    • DOI 10.1111/j.1523-5378.2007.00564.x
    • Moyaert H, Franceschi F, Roccarina D, Ducatelle R, Haesebrouck F, Gasbarrini A. Extragastric manifestations of Helicobacter pylori infection: other Helicobacters. Helicobacter 13(Suppl. 1), 47-57 (2008). (Pubitemid 47312377)
    • (2007) Helicobacter , vol.12 , Issue.SUPPL. 1 , pp. 45-53
    • Bohr, U.R.M.1    Annibale, B.2    Franceschi, F.3    Roccarina, D.4    Gasbarrini, A.5
  • 22
    • 51949100158 scopus 로고    scopus 로고
    • Sequential therapy for Helicobacter pylori: Time to consider making the switch?
    • Vakil N, Vaira D. Sequential therapy for Helicobacter pylori: time to consider making the switch? JAMA 300, 1346-1347 (2008).
    • (2008) JAMA , vol.300 , pp. 1346-1347
    • Vakil, N.1    Vaira, D.2
  • 23
    • 38949179599 scopus 로고    scopus 로고
    • Systematic reviews of the clinical effectiveness and cost-effectiveness of proton pump inhibitors in acute upper gastrointestinal bleeding
    • Leontiadis GI, Sreedharan A, Dorward S et al. Systematic reviews of the clinical effectiveness and cost-effectiveness of proton pump inhibitors in acute upper gastrointestinal bleeding. Health Technol. Assess. 11, 1-164 (2007).
    • (2007) Health Technol. Assess. , vol.11 , pp. 1-164
    • Leontiadis, G.I.1    Sreedharan, A.2    Dorward, S.3
  • 24
    • 48149107365 scopus 로고    scopus 로고
    • Effect of eradication of Helicobacter pylori on incidence of metachronous gastric carcinoma after endoscopic resection of early gastric cancer: An open-label, randomised controlled trial
    • Fukase K, Kato M, Kikuchi S et al. Effect of eradication of Helicobacter pylori on incidence of metachronous gastric carcinoma after endoscopic resection of early gastric cancer: an open-label, randomised controlled trial. Lancet 372, 392-397 (2008).
    • (2008) Lancet , vol.372 , pp. 392-397
    • Fukase, K.1    Kato, M.2    Kikuchi, S.3
  • 25
    • 9244239747 scopus 로고    scopus 로고
    • Global transposon mutagenesis and essential gene analysis of H. pylori
    • Transposon insertion was employed to determine genes that are essential to the survival of Helicobacter pylori. Independent verification of the essentiality of several gene products was performed
    • Salama NR, Shepherd B, Falkow S. Global transposon mutagenesis and essential gene analysis of H. pylori. J. Bacteriol. 186, 7926-7935 (2004). • Transposon insertion was employed to determine genes that are essential to the survival of Helicobacter pylori. Independent verification of the essentiality of several gene products was performed.
    • (2004) J. Bacteriol. , vol.186 , pp. 7926-7935
    • Salama, N.R.1    Shepherd, B.2    Falkow, S.3
  • 26
    • 0035143428 scopus 로고    scopus 로고
    • Systematic identification of selective essential genes in H. pylori by genome prioritisation and allelic replacement mutagenesis
    • A comparative genomic approach was employed to identify H. pylori 26695 genes conserved in H. pylori J99 and that highly diverged in other eubacteria. A survey of selected pathways of central intermediary metabolism was also performed, and genes with a potentially essential role in H. pylori were identified
    • Chalker AF, Minehart HW, Hughes NJ et al. Systematic identification of selective essential genes in H. pylori by genome prioritisation and allelic replacement mutagenesis. J. Bacteriol. 183, 1259-1268 (2001). •• A comparative genomic approach was employed to identify H. pylori 26695 genes conserved in H. pylori J99 and that highly diverged in other eubacteria. A survey of selected pathways of central intermediary metabolism was also performed, and genes with a potentially essential role in H. pylori were identified.
    • (2001) J. Bacteriol. , vol.183 , pp. 1259-1268
    • Chalker, A.F.1    Minehart, H.W.2    Hughes, N.J.3
  • 27
    • 33846849047 scopus 로고    scopus 로고
    • Identification of H. pylori genes contributing to stomach colonisation
    • The C57BL/6 mouse model of infection was utilized to query 2400 transposon mutants in two different bacterial strain backgrounds for H. pylori genetic loci contributing to colonization of the stomach
    • Baldwin DN, Shepherd B, Kraemer P et al. Identification of H. pylori genes contributing to stomach colonisation. Infect. Immun. 75, 1005-1016 (2006). •• The C57BL/6 mouse model of infection was utilized to query 2400 transposon mutants in two different bacterial strain backgrounds for H. pylori genetic loci contributing to colonization of the stomach.
    • (2006) Infect. Immun. , vol.75 , pp. 1005-1016
    • Baldwin, D.N.1    Shepherd, B.2    Kraemer, P.3
  • 28
    • 0037388836 scopus 로고    scopus 로고
    • Identification and characterisation of H. pylori genes essential for gastric colonisation
    • A set of previously unknown H. pylori factors necessary for gastric colonization and pathogenesis were identified using the Mongolian gerbil as a model system to screen a set of 960 signature-tagged mutants
    • Kavermann H, Burns BP, Angermuller K et al. Identification and characterisation of H. pylori genes essential for gastric colonisation. J. Exp. Med. 197, 813-822 (2003). •• A set of previously unknown H. pylori factors necessary for gastric colonization and pathogenesis were identified using the Mongolian gerbil as a model system to screen a set of 960 signature-tagged mutants.
    • (2003) J. Exp. Med. , vol.197 , pp. 813-822
    • Kavermann, H.1    Burns, B.P.2    Angermuller, K.3
  • 29
    • 0346957064 scopus 로고    scopus 로고
    • Novel therapeutic targets in H. pylori
    • Reviews how genomic, proteomic and transcriptomic data to determine essential gene products as targets for novel therapeutic agents can be obtained, evaluated and eventually used as a basis for the development of both vaccine and novel anti-Helicobacter agents
    • Loughlin MF. Novel therapeutic targets in H. pylori. Expert Opin. Therap. Targets. 7, 725-735 (2003). •• Reviews how genomic, proteomic and transcriptomic data to determine essential gene products as targets for novel therapeutic agents can be obtained, evaluated and eventually used as a basis for the development of both vaccine and novel anti-Helicobacter agents.
    • (2003) Expert Opin. Therap. Targets. , vol.7 , pp. 725-735
    • Loughlin, M.F.1
  • 30
    • 0038825243 scopus 로고    scopus 로고
    • H. pylori tissue tropism: Mouse-colonising strains can target different gastric niches
    • Akada JK, Ogura K, Dailidiene D, Dailide G, Cheverud JM, Berg DE. H. pylori tissue tropism: mouse-colonising strains can target different gastric niches. Microbiology 149, 1901-1909 (2003).
    • (2003) Microbiology , vol.149 , pp. 1901-1909
    • Akada, J.K.1    Ogura, K.2    Dailidiene, D.3    Dailide, G.4    Cheverud, J.M.5    Berg, D.E.6
  • 32
    • 0030835739 scopus 로고    scopus 로고
    • The complete genome sequence of the gastric pathogen H. pylori
    • Tomb JF, White O, Kerlavage AR et al. The complete genome sequence of the gastric pathogen H. pylori. Nature 388, 539-547 (1997).
    • (1997) Nature , vol.388 , pp. 539-547
    • Tomb, J.F.1    White, O.2    Kerlavage, A.R.3
  • 33
    • 0033552961 scopus 로고    scopus 로고
    • Genomicsequence comparison of two unrelated isolates of the human gastric pathogen H. pylori
    • Alm RA, Ling LS, Moir DT et al. Genomicsequence comparison of two unrelated isolates of the human gastric pathogen H. pylori. Nature 397, 176-180 (1999).
    • (1999) Nature , vol.397 , pp. 176-180
    • Alm, R.A.1    Ling, L.S.2    Moir, D.T.3
  • 36
    • 0033982936 scopus 로고    scopus 로고
    • KEGG: Kyoto Encyclopedia of Genes and Genomes
    • Kanehisa M, Goto S. KEGG: Kyoto Encyclopedia of Genes and Genomes. Nucleic Acids Res. 28, 27-30 (2000). (Pubitemid 30047706)
    • (2000) Nucleic Acids Research , vol.28 , Issue.1 , pp. 27-30
    • Kanehisa, M.1    Goto, S.2
  • 37
    • 33947158325 scopus 로고    scopus 로고
    • Comparative genomics profiling of clinical isolates of H. pylori in Chinese populations using DNA microarray
    • Shows the use of whole genomic DNA microarray to characterize the genomic diversity of H. pylori strains isolated from clinical patients and concludes that clinical strains have extensive genomic diversity. The method may help select relatively significant genes for further development of a vaccine against H. pylori
    • Han YH, Liu WZ, Shi YZ et al. Comparative genomics profiling of clinical isolates of H. pylori in Chinese populations using DNA microarray. J. Microbiol. 45, 21-28 (2007). •• Shows the use of whole genomic DNA microarray to characterize the genomic diversity of H. pylori strains isolated from clinical patients and concludes that clinical strains have extensive genomic diversity. The method may help select relatively significant genes for further development of a vaccine against H. pylori.
    • (2007) J. Microbiol. , vol.45 , pp. 21-28
    • Han, Y.H.1    Liu, W.Z.2    Shi, Y.Z.3
  • 38
    • 34249276425 scopus 로고    scopus 로고
    • Gain and loss of multiple genes during evolution of H. pylori
    • Gressmann H, Linz B, Ghai R et al. Gain and loss of multiple genes during evolution of H. pylori. PLoS Genet. 1, 419-428 (2005).
    • (2005) PLoS Genet. , vol.1 , pp. 419-428
    • Gressmann, H.1    Linz, B.2    Ghai, R.3
  • 40
    • 0031657583 scopus 로고    scopus 로고
    • Nucleotide sequence and characterization of cdrA, a cell division- Related gene of Helicobacter pylori
    • Takeuchi H, Shirai M, Akada JK, Tsuda M, Nakazawa T. Nucleotide sequence and characterisation of cdrA, a cell division-related gene of H. pylori. J. Bacteriol. 180, 5263-5268 (1998). (Pubitemid 28470961)
    • (1998) Journal of Bacteriology , vol.180 , Issue.19 , pp. 5263-5268
    • Takeuchi, H.1    Shirai, M.2    Akada, J.K.3    Tsuda, M.4    Nakazawa, T.5
  • 42
    • 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, Beier D. Identification of immunodominant antigens from H. pylori and evaluation of their reactivities with sera from patients with different gastroduodenal pathologies. Infect. Immun. 68, 915-920 (2000). (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
  • 43
    • 0036828277 scopus 로고    scopus 로고
    • Global analysis of Helicobacter pylori gene expression in human gastric mucosa
    • Graham JE, Peek RM Jr, Krishna U, Cover TL. Global analysis of H. pylori gene expression in human gastric mucosa. Gastroenterology 123, 1637-1648 (2002). (Pubitemid 35231663)
    • (2002) Gastroenterology , vol.123 , Issue.5 , pp. 1637-1648
    • Graham, J.E.1    Peek Jr., R.M.2    Krishna, U.3    Cover, T.L.4
  • 44
    • 0032502899 scopus 로고    scopus 로고
    • Differential genome analysis applied to the species-specific features of Helicobacter pylori
    • DOI 10.1016/S0014-5793(98)00276-2, PII S0014579398002762
    • Huynen M, Dandekar T, Bork P. Differential genome analysis applied to the species-specific features of H. pylori. FEBS Lett. 426, 1-5 (1998). (Pubitemid 28198144)
    • (1998) FEBS Letters , vol.426 , Issue.1 , pp. 1-5
    • Huynen, M.1    Dandekar, T.2    Bork, P.3
  • 46
    • 0031042034 scopus 로고    scopus 로고
    • Synthesis and activity of Helicobacter pylori urease and catalase at low pH
    • Bauerfeind P, Garner R, Dunn BE, Mobley HL. Synthesis and activity of H. pylori urease and catalase at low pH. Gut 40, 25-30 (1997). (Pubitemid 27079746)
    • (1997) Gut , vol.40 , Issue.1 , pp. 25-30
    • Bauerfeind, P.1    Garner, R.2    Dunn, B.E.3    Mobley, H.L.T.4
  • 48
    • 38849143765 scopus 로고    scopus 로고
    • Carbonic anhydrases: Novel therapeutic applications for inhibitors and activators
    • Supuran CT. Carbonic anhydrases: novel therapeutic applications for inhibitors and activators. Nat. Rev. Drug Discov. 7, 168-181 (2008).
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 168-181
    • Supuran, C.T.1
  • 50
    • 0001626023 scopus 로고    scopus 로고
    • New inhibitors of Helicobacter pylori urease holoenzyme selected from phage-displayed peptide libraries
    • DOI 10.1046/j.1432-1327.1999.00430.x
    • Houimel M, Mach JP, Corthesy-Theulaz I, Corthesy B, Fisch I. New inhibitors of H. pylori urease holoenzyme selected from phage-displayed peptide libraries. Eur. J. Biochem. 262, 774-780 (1999). (Pubitemid 29291035)
    • (1999) European Journal of Biochemistry , vol.262 , Issue.3 , pp. 774-780
    • Houimel, M.1    Mach, J.-P.2    Corthesy-Theulaz, I.3    Corthesy, B.4    Fisch, I.5
  • 51
    • 24644457733 scopus 로고    scopus 로고
    • Specific degradation of H. pylori urease by a catalytic antibody light chain
    • Hifumi E, Hatiuchi K, Okuda T, Nishizono A, Okamura Y, Uda T. Specific degradation of H. pylori urease by a catalytic antibody light chain. FEBS J. 272, 4497-12505 (2005).
    • (2005) FEBS J. , vol.272 , pp. 4497-12505
    • Hifumi, E.1    Hatiuchi, K.2    Okuda, T.3    Nishizono, A.4    Okamura, Y.5    Uda, T.6
  • 52
    • 0031709045 scopus 로고    scopus 로고
    • Immunological features and inhibitory effects on enzymatic activity of monoclonal antibodies against H. pylori urease
    • Ikeda Y, Fujii R, Ogino K, Fukushima K, Hifumi E, Uda T. Immunological features and inhibitory effects on enzymatic activity of monoclonal antibodies against H. pylori urease. J. Ferm. Bio. 86, 271-276 (1998).
    • (1998) J. Ferm. Bio. , vol.86 , pp. 271-276
    • Ikeda, Y.1    Fujii, R.2    Ogino, K.3    Fukushima, K.4    Hifumi, E.5    Uda, T.6
  • 53
    • 37649025645 scopus 로고    scopus 로고
    • Preparation and in vitro characterisation of gellan based floating beads of acetohydroxamic acid for eradication of H. pylori
    • Rajinikanth PS, Mishra B. Preparation and in vitro characterisation of gellan based floating beads of acetohydroxamic acid for eradication of H. pylori. Acta Pharm. 57, 413-427 (2007).
    • (2007) Acta Pharm. , vol.57 , pp. 413-427
    • Rajinikanth, P.S.1    Mishra, B.2
  • 54
    • 0346690153 scopus 로고    scopus 로고
    • α-hydroxyketones as inhibitors of urease
    • Tanaka T, Kawase M, Tani S. α-hydroxyketones as inhibitors of urease. Bioorg. Med. Chem. 12, 501-505 (2004).
    • (2004) Bioorg. Med. Chem. , vol.12 , pp. 501-505
    • Tanaka, T.1    Kawase, M.2    Tani, S.3
  • 55
    • 0035991974 scopus 로고    scopus 로고
    • Three-dimensional quantitative structure-activity relationship and comparative molecular field analysis of dipeptide hydroxamic acid Helicobacter pylori urease inhibitors
    • DOI 10.1128/AAC.46.8.2613-2618.2002
    • Mishra H, Parrill AL, Williamson JS. Three-dimensional quantitative structure-activity relationship and comparative molecular field analysis of dipeptide hydroxamic acid H. pylori urease inhibitors. Antimicrob. Agents Chemother. 46, 2613-2618 (2002). (Pubitemid 34793472)
    • (2002) Antimicrobial Agents and Chemotherapy , vol.46 , Issue.8 , pp. 2613-2618
    • Mishra, H.1    Parrill, A.L.2    Williamson, J.S.3
  • 56
    • 0038053032 scopus 로고    scopus 로고
    • Design and synthesis of heterocyclic hydroxamic acid derivatives as inhibitors of H. pylori urease
    • Muri EMF, Mishra H, Avery MA, Williamson JS. Design and synthesis of heterocyclic hydroxamic acid derivatives as inhibitors of H. pylori urease. Synth. Comm. 33, 1977-1995 (2003).
    • (2003) Synth. Comm. , vol.33 , pp. 1977-1995
    • Muri, E.M.F.1    Mishra, H.2    Avery, M.A.3    Williamson, J.S.4
  • 57
    • 29244457006 scopus 로고    scopus 로고
    • Molecular modeling, synthesis and biological evalutation of heterocyclic hydroxamic acids designed as H. pylori urease inhibitors
    • Muri EMF, Mishra H, Stein SM, Williamson JS. Molecular modeling, synthesis and biological evalutation of heterocyclic hydroxamic acids designed as H. pylori urease inhibitors. Lett. Drug Des. Dis. 1, 30-34 (2004).
    • (2004) Lett. Drug Des. Dis. , vol.1 , pp. 30-34
    • Muri, E.M.F.1    Mishra, H.2    Stein, S.M.3    Williamson, J.S.4
  • 58
    • 33748458097 scopus 로고    scopus 로고
    • Urea, fluorofamide, and omeprazole treatments alter Helicobacter colonization in the mouse gastric mucosa
    • DOI 10.1111/j.1523-5378.2006.00439.x
    • Panayiota Aristoteli L, O'Rourke JL, Danon S et al. Urea, flurofamide, and omeprazole treatments alter Helicobacter colonisation in the mouse gastric mucosa. Helicobacter 11, 460-468 (2006). (Pubitemid 44352618)
    • (2006) Helicobacter , vol.11 , Issue.5 , pp. 460-468
    • Aristoteli, L.P.1    O'Rourke, J.L.2    Danon, S.3    Larsson, H.4    Mellgard, B.5    Mitchell, H.6    Lee, A.7
  • 59
    • 38149124883 scopus 로고    scopus 로고
    • Catalytic features and eradication ability of antibody light-chain UA15-L against H. pylori
    • Explains the development of a catalytic antibody capable of degrading the active site of the urease of H. pylori and eradicating the bacterial infection in a mouse stomach. This is the first example of a monoclonal catalytic antibody capable of functioning in vivo
    • Hifumi E, Morihara F, Hatiuchi K, Okuda T, Nishizono A, Uda T. Catalytic features and eradication ability of antibody light-chain UA15-L against H. pylori. J. Biol Chem. 283, 899-907 (2008). •• Explains the development of a catalytic antibody capable of degrading the active site of the urease of H. pylori and eradicating the bacterial infection in a mouse stomach. This is the first example of a monoclonal catalytic antibody capable of functioning in vivo.
    • (2008) J. Biol Chem. , vol.283 , pp. 899-907
    • Hifumi, E.1    Morihara, F.2    Hatiuchi, K.3    Okuda, T.4    Nishizono, A.5    Uda, T.6
  • 60
    • 33747885475 scopus 로고    scopus 로고
    • Inhibition of urease by bismuth(III): Implications for the mechanism of action of bismuth drugs
    • DOI 10.1007/s10534-005-5449-0
    • Zhang L, Mulrooney SB, Leung AFK et al. Inhibition of urease by bismuth(III): implications for the mechanism of action of bismuth drugs. BioMetals 19, 503-511 (2006). (Pubitemid 44291043)
    • (2006) BioMetals , vol.19 , Issue.5 , pp. 503-511
    • Zhang, L.1    Mulrooney, S.B.2    Leung, A.F.K.3    Zeng, Y.4    Ko, B.B.C.5    Hausinger, R.P.6    Sun, H.7
  • 62
    • 33749396618 scopus 로고    scopus 로고
    • Biochemical characterization and inhibitor discovery of shikimate dehydrogenase from Helicobacter pylori
    • DOI 10.1111/j.1742-4658.2006.05469.x
    • Han C, Wang L, Yu K et al. Biochemical characterisation and inhibitor discovery of shikimate dehydrogenase from H. pylori. FEBS J. 273, 4682-4692 (2006). (Pubitemid 44506909)
    • (2006) FEBS Journal , vol.273 , Issue.20 , pp. 4682-4692
    • Han, C.1    Wang, L.2    Yu, K.3    Chen, L.4    Hu, L.5    Chen, K.6    Jiang, H.7    Shen, X.8
  • 63
    • 28044450588 scopus 로고    scopus 로고
    • Structural basis for shikimate-binding specificity of H. pylori shikimate kinase
    • Cheng WC, Chang YN, Wang WC. Structural basis for shikimate-binding specificity of H. pylori shikimate kinase. J. Bacteriol. 187, 8156-8163 (2005).
    • (2005) J. Bacteriol. , vol.187 , pp. 8156-8163
    • Cheng, W.C.1    Chang, Y.N.2    Wang, W.C.3
  • 64
    • 33845398326 scopus 로고    scopus 로고
    • Discovery of Helicobacter pylori shikimate kinase inhibitors: Bioassay and molecular modeling
    • DOI 10.1016/j.bmc.2006.10.058, PII S0968089606009011
    • Han C, Zhang J, Chen L, Chen K, Shen X, Jiang H. Discovery of H. pylori shikimate kinase inhibitors: bioassay and molecular modelling. Bioorg. Med. Chem. 15, 656-662 (2007). (Pubitemid 44895506)
    • (2007) Bioorganic and Medicinal Chemistry , vol.15 , Issue.2 , pp. 656-662
    • Han, C.1    Zhang, J.2    Chen, L.3    Chen, K.4    Shen, X.5    Jiang, H.6
  • 65
    • 51349137033 scopus 로고    scopus 로고
    • Structural and enzymatic characterisation of Hp0496, a YbgC thioesterase from H. pylori
    • Angelini A, Cendron L, Goncalves S, Zanotti G, Terradot L. Structural and enzymatic characterisation of Hp0496, a YbgC thioesterase from H. pylori. Proteins 72, 1212-1221 (2008).
    • (2008) Proteins , vol.72 , pp. 1212-1221
    • Angelini, A.1    Cendron, L.2    Goncalves, S.3    Zanotti, G.4    Terradot, L.5
  • 67
    • 36048943978 scopus 로고    scopus 로고
    • Asn and novel aminoacyl-tRNA analogues are competitive inhibitors
    • Asn and novel aminoacyl-tRNA analogues are competitive inhibitors. Biochemistry 46, 13190-13198 (2007).
    • (2007) Biochemistry , vol.46 , pp. 13190-13198
    • Huot, J.L.1    Balg, C.2    Jahn, D.3
  • 68
    • 41449112157 scopus 로고    scopus 로고
    • Inhibition of H. pylori animoacyl-tRNA amidotransferase by puromycin analogues
    • Balg C, Huot JL, Lapointe J, Chenervert R. Inhibition of H. pylori animoacyl-tRNA amidotransferase by puromycin analogues. J. Am. Chem. Soc. 130, 3264-3265 (2008).
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 3264-3265
    • Balg, C.1    Huot, J.L.2    Lapointe, J.3    Chenervert, R.4
  • 70
    • 0033936704 scopus 로고    scopus 로고
    • Peptide deformylase as a target for new generation, broad spectrum antimicrobial agents
    • DOI 10.1046/j.1365-2958.2000.01908.x
    • Gigilone C, Pierre M, Melnnel T. Peptide deformylase as a target for new generation, broad spectrum antimicrobial agents. Mol. Microbiol. 36, 1197-1205 (2000). (Pubitemid 30449958)
    • (2000) Molecular Microbiology , vol.36 , Issue.6 , pp. 1197-1205
    • Giglione, C.1    Pierre, M.2    Meinnel, T.3
  • 72
    • 16244411296 scopus 로고    scopus 로고
    • Comparative antimicrobial characterization of LBM415 (NVP PDF-713), a new peptide deformylase inhibitor of clinical importance
    • DOI 10.1128/AAC.49.4.1468-1476.2005
    • Fritsche TR, Sader HS, Cleeland R, Jones RN. Comparative antimicrobial characterisation of LBM415 (NVP PDF-713), a new peptide deformylase inhibitor of clinical importance. Antimicrob. Agents Chemother. 49, 1468-1476 (2005). (Pubitemid 40463378)
    • (2005) Antimicrobial Agents and Chemotherapy , vol.49 , Issue.4 , pp. 1468-1476
    • Fritsche, T.R.1    Sader, H.S.2    Cleeland, R.3    Jones, R.N.4
  • 73
    • 33748189789 scopus 로고    scopus 로고
    • Peptide deformylase is a potential target for anti-Helicobacter pylori drugs: Reverse docking, enzymatic assay, and X-ray crystallography validation
    • DOI 10.1110/ps.062238406
    • Cai J, Han C, Hu T et al. Peptide deformylase is a potential target for anti-H. pylori drugs: reverse docking, enzymatic assay, and X-ray crystallography validation. Protein Sci. 15, 2071-2081 (2006). (Pubitemid 44316010)
    • (2006) Protein Science , vol.15 , Issue.9 , pp. 2071-2081
    • Cai, J.1    Han, C.2    Hu, T.3    Zhang, J.4    Wu, D.5    Wang, F.6    Liu, Y.7    Ding, J.8    Chen, K.9    Yue, J.10    Shen, X.11    Jiang, H.12
  • 74
    • 0034959986 scopus 로고    scopus 로고
    • New approaches for validation of lethal phenotypes and genetic reversion in Helicobacter pylori
    • DOI 10.1046/j.1523-5378.2001.00001.x
    • McDaniel TK, Dewalt KC, Salama NR, Falkow S. New approaches for validation of lethal phenotypes and genetic reversion in H. pylori. Helicobacter. 6, 15-23 (2001). (Pubitemid 32601680)
    • (2001) Helicobacter , vol.6 , Issue.1 , pp. 15-23
    • McDaniel, T.K.1    Dewalt, K.C.2    Salama, N.R.3    Falkow, S.4
  • 75
    • 17644397003 scopus 로고    scopus 로고
    • Phosphorylation-independent activity of atypical response regulators of Helicobacter pylori
    • DOI 10.1128/JB.187.9.3100-3109.2005
    • Schar J, Sickmann A, Beier D. Phosphorylation-independent activity of atypical response regulators of H. pylori. J. Bacteriol. 187, 3100-3109 (2005). (Pubitemid 40571603)
    • (2005) Journal of Bacteriology , vol.187 , Issue.9 , pp. 3100-3109
    • Schar, J.1    Sickmann, A.2    Beier, D.3
  • 76
    • 0042324147 scopus 로고    scopus 로고
    • Two-component systems of Helicobacter pylori contribute to virulence in a mouse infection model
    • DOI 10.1128/IAI.71.9.5381-5385.2003
    • Panthel K, Dietz P, Haas R, Beier D. Two-component systems of H. pylori contribute to virulence in a mouse infection model. Infect. Immun. 71, 5381-5385 (2003). (Pubitemid 37070788)
    • (2003) Infection and Immunity , vol.71 , Issue.9 , pp. 5381-5385
    • Panthel, K.1    Dietz, P.2    Haas, R.3    Beier, D.4
  • 77
    • 0034082804 scopus 로고    scopus 로고
    • Molecular characterization of two-component systems of Helicobacter pylori
    • DOI 10.1128/JB.182.8.2068-2076.2000
    • Beier D, Frank R. Molecular characterisation of two-component systems of H. pylori. J. Bacteriol. 182, 2068-2076 (2000). (Pubitemid 30183523)
    • (2000) Journal of Bacteriology , vol.182 , Issue.8 , pp. 2068-2076
    • Beier, D.1    Frank, R.2
  • 78
    • 0036718563 scopus 로고    scopus 로고
    • Growth phase-dependent regulation of target gene promoters for binding of the essential orphan response regulator HP1043 of Helicobacter pylori
    • DOI 10.1128/JB.184.17.4800-4810.2002
    • Delany I, Spohn G, Rappuoli R, Scarlato V. Growth phase-dependent regulation of target gene promoters for binding of the essential orphan response regulator Hp1043 of H. pylori. J. Bacteriol. 184, 4800-4810 (2002). (Pubitemid 34898268)
    • (2002) Journal of Bacteriology , vol.184 , Issue.17 , pp. 4800-4810
    • Delany, I.1    Spohn, G.2    Rappuoli, R.3    Scarlato, V.4
  • 80
    • 0036145495 scopus 로고    scopus 로고
    • Crystal structure of oxidized flavodoxin, an essential protein in Helicobacter pylori
    • DOI 10.1110/ps.28602
    • Freigang J, Diederichs K, Schafer KP, Welte W, Paul R. Crystal structure of oxidised flavodoxin, an essential protein in H. pylori. Protein Sci. 11, 253-261 (2002). (Pubitemid 34075788)
    • (2002) Protein Science , vol.11 , Issue.2 , pp. 253-261
    • Freigang, J.1    Diederichs, K.2    Schafer, K.P.3    Welte, W.4    Paul, R.5
  • 81
    • 0033913344 scopus 로고    scopus 로고
    • Analysis of rdxA and involvement of additional genes encoding NAD(P)H flavin oxidoreductase (FrxA) and ferredoxin-like protein (FdxB) in Metronidazole resistance of H. pylori
    • Kwon DH, El-Zaatari FAK, Kato M et al. Analysis of rdxA and involvement of additional genes encoding NAD(P)H flavin oxidoreductase (FrxA) and ferredoxin-like protein (FdxB) in Metronidazole resistance of H. pylori. Antimicrob. Agents Chemother. 44, 2133-2142 (2000).
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 2133-2142
    • Kwon, D.H.1    El-Zaatari, F.A.K.2    Kato, M.3
  • 82
    • 18044369328 scopus 로고    scopus 로고
    • Gene expression and protein profiling of AGS gastric epithelial cells upon infection with Helicobacterpylori
    • DOI 10.1002/pmic.200401240
    • Backert S, Gressmann H, Kwok T et al. Gene expression and protein profiling of AGS gastric epithelial cells upon infection with H. pylori. Proteomics 5, 3902-3918 (2005). (Pubitemid 41502487)
    • (2005) Proteomics , vol.5 , Issue.15 , pp. 3902-3918
    • Backert, S.1    Gressmann, H.2    Kwok, T.3    Zimny-Arndt, U.4    Konig, W.5    Jungblut, P.R.6    Meyer, T.F.7
  • 84
    • 14744268574 scopus 로고    scopus 로고
    • Towards a new therapeutic target: H. pylori flavodoxin
    • Provides an example of a potential target not present in the human host. Because H. pylori fladoxin has peculiar characteristics not found in other known flavodoxins, inhibition of its activity could allow the design of very specific anti-Helicobacter drugs
    • Cremades N, Bueno M, Toja M, Sancho J. Towards a new therapeutic target: H. pylori flavodoxin. Biophys. Chem. 115, 267-276 (2005). • Provides an example of a potential target not present in the human host. Because H. pylori fladoxin has peculiar characteristics not found in other known flavodoxins, inhibition of its activity could allow the design of very specific anti-Helicobacter drugs.
    • (2005) Biophys. Chem. , vol.115 , pp. 267-276
    • Cremades, N.1    Bueno, M.2    Toja, M.3    Sancho, J.4
  • 85
    • 0035108401 scopus 로고    scopus 로고
    • Essential thioredoxin-dependent peroxiredoxin system for H. pylori: Genetic and kinetic characterisation
    • Baker LMS, Raudonikiene A, Hoffman PS, Poole LB. Essential thioredoxin-dependent peroxiredoxin system for H. pylori: genetic and kinetic characterisation. J. Bacteriol. 183, 1961-1973 (2001).
    • (2001) J. Bacteriol. , vol.183 , pp. 1961-1973
    • Baker, L.M.S.1    Raudonikiene, A.2    Hoffman, P.S.3    Poole, L.B.4
  • 88
    • 34547676738 scopus 로고    scopus 로고
    • Structural similarity between the DnaA-binding proteins HobA (HP1230) from Helicobacter pylori and DiaA from Escherichia coli
    • DOI 10.1111/j.1365-2958.2007.05843.x
    • Natrajan G, Hall DR, Thompson AC, Gutsche I, Terradot L. Structural similarity between the DnaA-binding proteins HobA (Hp1230) from H. pylori and DiaA from E. coli. Mol. Microbiol. 65, 995-1005 (2007). (Pubitemid 47221078)
    • (2007) Molecular Microbiology , vol.65 , Issue.4 , pp. 995-1005
    • Natrajan, G.1    Hall, D.R.2    Thompson, A.C.3    Gutsche, I.4    Terradot, L.5
  • 90
    • 33644843231 scopus 로고    scopus 로고
    • Crystal structure of Hp0242, a hypothetical protein from H. pylori with a novel fold
    • Tsai JY, Chen BT, Cheng HC et al. Crystal structure of Hp0242, a hypothetical protein from H. pylori with a novel fold. Proteins. 62, 1138-1143 (2006).
    • (2006) Proteins. , vol.62 , pp. 1138-1143
    • Tsai, J.Y.1    Chen, B.T.2    Cheng, H.C.3
  • 91
    • 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. Identification of potential diagnostic and vaccine candidates of H. pylori by two-dimensional gel electrophoresis, sequence analysis, and serum profiling. Clin. Diagn. Lab. Immunol. 5, 537-542 (1998). (Pubitemid 28342884)
    • (1998) Clinical and Diagnostic Laboratory Immunology , vol.5 , Issue.4 , 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
  • 94
  • 95
    • 0036784678 scopus 로고    scopus 로고
    • Two predicted chemoreceptors of H. pylori promote stomach infection
    • Andermann TM, Chen YT, Ottemann KM. Two predicted chemoreceptors of H. pylori promote stomach infection. Infect. Immun. 70, 5877-5881 (2002).
    • (2002) Infect. Immun. , vol.70 , pp. 5877-5881
    • Andermann, T.M.1    Chen, Y.T.2    Ottemann, K.M.3
  • 96
    • 0042208145 scopus 로고    scopus 로고
    • Helicobacter pylori strain ATCC700392 encodes a methyl-accepting chemotaxis receptor protein (MCP) for arginine and sodium bicarbonate
    • DOI 10.1016/S0378-1097(03)00423-3
    • Cerda O, Rivas A, Toledo H. H. pylori strain ATCC700392 encodes a methyl-accepting chemotaxis receptor protein (MCP) for arginine and sodium bicarbonate. FEMS Microbiol. Lett. 224, 175-181 (2003). (Pubitemid 36929822)
    • (2003) FEMS Microbiology Letters , vol.224 , Issue.2 , pp. 175-181
    • Cerda, O.1    Rivas, A.2    Toledo, H.3
  • 97
    • 33746256645 scopus 로고    scopus 로고
    • Characterisation of flgK gene and FlgK protein required for H. pylori colonisation - From cloning to clinical relevance
    • Wu JJ, Sheu BS, Huang AH, Lin ST, Yang HB. Characterisation of flgK gene and FlgK protein required for H. pylori colonisation - from cloning to clinical relevance. World J. Gastroenterol. 12, 3989-3993 (2006).
    • (2006) World J. Gastroenterol. , vol.12 , pp. 3989-3993
    • Wu, J.J.1    Sheu, B.S.2    Huang, A.H.3    Lin, S.T.4    Yang, H.B.5
  • 98
    • 38849186664 scopus 로고    scopus 로고
    • Enzymatic characterization and inhibitor discovery of a new cystathionine g-synthase from Helicobacter pylori
    • DOI 10.1093/jb/mvm194
    • Kong Y, Wu D, Bai H et al. Enzymatic characterisation and inhibitor discovery of a new cystathionine g-synthase (CGS) from H. pylori. J. Biochem. 143, 59-68 (2008). (Pubitemid 351197714)
    • (2008) Journal of Biochemistry , vol.143 , Issue.1 , pp. 59-68
    • Kong, Y.1    Wu, D.2    Bai, H.3    Han, C.4    Chen, J.5    Chen, L.6    Hu, L.7    Jiang, H.8    Shen, X.9
  • 99
    • 34248186582 scopus 로고    scopus 로고
    • Structure and mechanism of H. pylori fucosyltransferase: A basis for lipopolysaccharide variation and inhibitor design
    • Sun HY, Lin SW, Ko TP et al. Structure and mechanism of H. pylori fucosyltransferase: a basis for lipopolysaccharide variation and inhibitor design. J. Biol. Chem. 282, 9973-9982 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 9973-9982
    • Sun, H.Y.1    Lin, S.W.2    Ko, T.P.3
  • 100
    • 0033031955 scopus 로고    scopus 로고
    • Molecular genetic basis for the variable expression of Lewis Y antigen in Helicobacter pylori: Analysis of the α(1,2) fucosyltransferase gene
    • DOI 10.1046/j.1365-2958.1999.01268.x
    • Wang G, Rasko DA, Sherburne R, Taylor DE. Molecular genetic basis for the variable expression of Lewis Y antigen in H. pylori: analysis of the α(1,2) fucosyltransferase gene. Mol. Microbiol. 31, 1265-1274 (1999). (Pubitemid 29082254)
    • (1999) Molecular Microbiology , vol.31 , Issue.4 , pp. 1265-1274
    • Wang, G.1    Rasko, D.A.2    Sherburne, R.3    Taylor, D.E.4
  • 101
    • 34250356440 scopus 로고    scopus 로고
    • Exploitation of structural and regulatory diversity in glutamate racemases
    • Characterizes the glutamate racemases of several pathogenic bacteria using structural and biochemical approaches, and identifies a series of uncompetitive inhibitors specifically targeting Helicobacter pylori glutamate racemase that provide a basis for designing narrow-spectrum antimicrobial agents
    • Lundqvist T, Fisher SL, Kern G et al. Exploitation of structural and regulatory diversity in glutamate racemases. Nature 447, 817-822 (2007). • Characterizes the glutamate racemases of several pathogenic bacteria using structural and biochemical approaches, and identifies a series of uncompetitive inhibitors specifically targeting Helicobacter pylori glutamate racemase that provide a basis for designing narrow-spectrum antimicrobial agents.
    • (2007) Nature , vol.447 , pp. 817-822
    • Lundqvist, T.1    Fisher, S.L.2    Kern, G.3
  • 103
    • 0036450733 scopus 로고    scopus 로고
    • Novel intervention strategies for Helicobacter pylori treatment
    • DOI 10.2174/1568005023342209
    • Noonan B, Alm RA. Novel intervention strategies for H. pylori treatment. Curr. Drug Targets Infect. Disord. 2, 331-338 (2002). (Pubitemid 35446266)
    • (2002) Current Drug Targets - Infectious Disorders , vol.2 , Issue.4 , pp. 331-338
    • Noonan, B.1    Alm, R.A.2
  • 105
    • 0033679155 scopus 로고    scopus 로고
    • A 26 kDa protein of Helicobacter pylori shows alkyl hydroperoxide reductase (AhpC) activity and the mono-cistronic transcription of the gene is affected by pH
    • DOI 10.1006/mpat.2000.0388
    • Lundstrom AM, Bolin I. A 26 kDa protein of H. pylori shows alkyl hydroperoxide reductase (AhpC) activity and the mono-cistronic transcription of the gene is affected by pH. Microb. Pathog. 29, 257-266 (2000). (Pubitemid 30945001)
    • (2000) Microbial Pathogenesis , vol.29 , Issue.5 , pp. 257-266
    • Lundstrom, A.M.1    Bolin, I.2
  • 106
    • 0036271268 scopus 로고    scopus 로고
    • Oxidative-stress resistance mutants of H. pylori
    • Olczak AA, Olson JW, Maier RJ. Oxidative-stress resistance mutants of H. pylori. J. Bacteriol. 184, 3186-3193 (2002).
    • (2002) J. Bacteriol. , vol.184 , pp. 3186-3193
    • Olczak, A.A.1    Olson, J.W.2    Maier, R.J.3
  • 107
    • 34247593067 scopus 로고    scopus 로고
    • Antisense RNA modulation of alkyl hydroperoxide reductase (AhpC) levels in H. pylori correlates with organic peroxide toxiciy but not infectivity
    • Croxen MA, Ernst PB, Hoffman PS. Antisense RNA modulation of alkyl hydroperoxide reductase (AhpC) levels in H. pylori correlates with organic peroxide toxiciy but not infectivity J. Bacteriol. 189, 3359-3368 (2007).
    • (2007) J. Bacteriol. , vol.189 , pp. 3359-3368
    • Croxen, M.A.1    Ernst, P.B.2    Hoffman, P.S.3
  • 109
    • 0037057584 scopus 로고    scopus 로고
    • Parallel synthesis of potent, pyrazole-based inhibitors of H. pylori dihydroorotate dehydrogenase
    • Haque TS, Tadesse S, Marcinkeviciene J et al. Parallel synthesis of potent, pyrazole-based inhibitors of H. pylori dihydroorotate dehydrogenase. J. Med. Chem. 45, 4669-4678 (2002).
    • (2002) J. Med. Chem. , vol.45 , pp. 4669-4678
    • Haque, T.S.1    Tadesse, S.2    Marcinkeviciene, J.3
  • 112
    • 57049095824 scopus 로고    scopus 로고
    • Casting a broader net for approaches to antibacterial research and development. Editorial overview
    • Payne D, Bush K. Casting a broader net for approaches to antibacterial research and development. Editorial overview. Curr. Opin. Biotechnol. 19(6), 606-607 (2008).
    • (2008) Curr. Opin. Biotechnol. , vol.19 , Issue.6 , pp. 606-607
    • Payne, D.1    Bush, K.2
  • 113
    • 44949137137 scopus 로고    scopus 로고
    • Helicobacter pylori infection and the pathogenesis of gastric cancer: A paradigm for host-bacterial interactions
    • McNamara D, El-Omar E. Helicobacter pylori infection and the pathogenesis of gastric cancer: a paradigm for host-bacterial interactions. Dig. Liver Dis. 40(7), 504-509 (2008).
    • (2008) Dig. Liver Dis. , vol.40 , Issue.7 , pp. 504-509
    • McNamara, D.1    El-Omar, E.2
  • 114
    • 14844298604 scopus 로고    scopus 로고
    • Drug delivery strategies for the treatment of Helicobacter pylori infections
    • Conway BR. Drug delivery strategies for the treatment of Helicobacter pylori infections. Curr. Pharm. Des. 11(6), 775-790 (2005).
    • (2005) Curr. Pharm. Des. , vol.11 , Issue.6 , pp. 775-790
    • Conway, B.R.1
  • 115
    • 48249152198 scopus 로고    scopus 로고
    • Phytoceuticals: Mighty but ignored weapons against Helicobacter pylori infection
    • Lee SY, Shin YW, Hahm KB. Phytoceuticals: mighty but ignored weapons against Helicobacter pylori infection. J. Dig. Dis. 9(3), 129-139 (2008).
    • (2008) J. Dig. Dis. , vol.9 , Issue.3 , pp. 129-139
    • Lee, S.Y.1    Shin, Y.W.2    Hahm, K.B.3
  • 116
    • 0030990844 scopus 로고    scopus 로고
    • The Helicobacter pylori ureC gene codes for a phosphoglucosamine mutase
    • De Reuse H, Labigne A, Mengin-Lecreulx D. The H. pylori ureC gene codes for a phosphoglucosamine mutase. J. Bacteriol. 179, 3488-3493 (1997). (Pubitemid 27232984)
    • (1997) Journal of Bacteriology , vol.179 , Issue.11 , pp. 3488-3493
    • De Reuse, H.1    Labigne, A.2    Mengin-Lecreulx, D.3
  • 117
    • 33745202607 scopus 로고    scopus 로고
    • In silico identification of potential therapeutic targets in the human pathogen H. pylori
    • Uses a subtractive genomics approach to identify a small subset of the Helicobacter proteome that could be investigated further for identifying potential drug and vaccine targets
    • Dutta A, Singh SK, Ghosh P, Mukherjee R, Mitter S, Bandyopadhyay D. In silico identification of potential therapeutic targets in the human pathogen H. pylori. In Silico Biol. 6, 43-47 (2006). • Uses a subtractive genomics approach to identify a small subset of the Helicobacter proteome that could be investigated further for identifying potential drug and vaccine targets.
    • (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
  • 119
    • 0028064605 scopus 로고
    • A urease-negative mutant of Helicobacter pylori constructed by allelic exchange mutagenesis lacks the ability to colonize the nude mouse stomach
    • Tsuda M, Karita M, Golam Morshed M, Okita K, Nakazawa T. A urease negative mutant of H. pylori constructed by allelic exchange mutagenesis lacks the ability to colonise the nude mouse stomach. Infect. Immun. 62, 3586-3589 (1994). (Pubitemid 24232155)
    • (1994) Infection and Immunity , vol.62 , Issue.8 , pp. 3586-3589
    • Tsuda, M.1    Karita, M.2    Morshed, M.G.3    Okita, K.4    Nakazawa, T.5
  • 120
    • 34247844630 scopus 로고    scopus 로고
    • HorB (Hp0127) is a gastric epithelial cell adhesin
    • Snelling WJ, Moran AP, Ryan KA et al. HorB (Hp0127) is a gastric epithelial cell adhesin. Helicobacter 12, 200-209 (2007).
    • (2007) Helicobacter , vol.12 , pp. 200-209
    • Snelling, W.J.1    Moran, A.P.2    Ryan, K.A.3
  • 121
    • 0033679563 scopus 로고    scopus 로고
    • Fumarate reductase is essential for Helicobacter pylori colonization of the mouse stomach
    • DOI 10.1006/mpat.2000.0391
    • Ge Z, Feng Y, Dangler CA, Xu S, Taylor NS, Fox JG. Fumarate reductase is essential for H. pylori colonisation of the mouse stomach. Microb. Pathog. 29, 279-287 (2000). (Pubitemid 30945003)
    • (2000) Microbial Pathogenesis , vol.29 , Issue.5 , pp. 279-287
    • Ge, Z.1    Feng, Y.2    Dangler, C.A.3    Xu, S.4    Taylor, N.S.5    Fox, J.G.6
  • 122
    • 0037062509 scopus 로고    scopus 로고
    • Rapid genetic analysis of H. pylori gastric mucosal colonisation in suckling mice
    • Guo BP, Mekalanos JJ. Rapid genetic analysis of H. pylori gastric mucosal colonisation in suckling mice. Proc. Natl Acad. Sci. USA 99 8354-8359 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 8354-8359
    • Guo, B.P.1    Mekalanos, J.J.2
  • 123
    • 0035001195 scopus 로고    scopus 로고
    • Superoxide dismutase-deficient mutants of H. pylori are hypersensitive to oxidative stress and defective in host colonisation
    • Seyler Jr RW, Olson JW, Maier RJ. Superoxide dismutase-deficient mutants of H. pylori are hypersensitive to oxidative stress and defective in host colonisation. Infect. Immun. 69, 4034-4040 (2001).
    • (2001) Infect. Immun. , vol.69 , pp. 4034-4040
    • Seyler Jr., R.W.1    Olson, J.W.2    Maier, R.J.3
  • 124
    • 0030002653 scopus 로고    scopus 로고
    • Colonization of gnotobiotic piglets by Helicobacter pylori deficient in two flagellin genes
    • Eaton KA, Suerbaum S, Josenhans C, Krakowka S. Colonisation of gnotobiotic piglets by H. pylori deficient in two flagellin genes. Infect. Immun. 64, 2445-2448 (1996). (Pubitemid 26226803)
    • (1996) Infection and Immunity , vol.64 , Issue.7 , pp. 2445-2448
    • Eaton, K.A.1    Suerbaum, S.2    Josenhans, C.3    Krakowka, S.4
  • 125
    • 0005805224 scopus 로고    scopus 로고
    • Molecular cloning and characterisation of the H. pylori fliD gene, an essential factor in flagellar structure and motility
    • Kim JS, Chang JH, Chung SI, Yum JS. Molecular cloning and characterisation of the H. pylori fliD gene, an essential factor in flagellar structure and motility. J. Bacteriol. 181, 6969-6976 (1999).
    • (1999) J. Bacteriol. , vol.181 , pp. 6969-6976
    • Kim, J.S.1    Chang, J.H.2    Chung, S.I.3    Yum, J.S.4
  • 126
    • 33745597636 scopus 로고    scopus 로고
    • The novel Helicobacter pylori CznABC metal efflux pump is required for cadmium, zinc, and nickel resistance, urease modulation, and gastric colonization
    • DOI 10.1128/IAI.02025-05
    • Stahler FN, Odenbreit S, Haas R et al. The novel H. pylori CznABC metal efflux pump is required for cadmium, zinc, and nickel resistance, urease modulation and gastric colonisation. Infect. Immun. 74, 3845-3852 (2006). (Pubitemid 43993315)
    • (2006) Infection and Immunity , vol.74 , Issue.7 , pp. 3845-3852
    • Stahler, F.N.1    Odenbreit, S.2    Haas, R.3    Wilrich, J.4    Van Vliet, A.H.M.5    Kusters, J.G.6    Kist, M.7    Bereswill, S.8
  • 128
    • 0033916226 scopus 로고    scopus 로고
    • Adherence of isogenic flagellum-negative mutants of Helicobacter pylori and Helicobacter mustelae to human and ferret gastric epithelial cells
    • DOI 10.1128/IAI.68.7.4335-4339.2000
    • Clyne M, Ocroinin T, Suerbaum S, Josenhans C, Drumm B. Adherence of isogenic flagellum-negative mutants of H. pylori and H. mustelae to human and ferret gastric epithelial cells. Infect. Immun. 68, 4335-4339 (2000). (Pubitemid 30434593)
    • (2000) Infection and Immunity , vol.68 , Issue.7 , pp. 4335-4339
    • Clyne, M.1    Ocroinin, T.2    Suerbaum, S.3    Josenhans, C.4    Drumm, B.5
  • 129
    • 24344454388 scopus 로고    scopus 로고
    • Mutational analysis of the Helicobacter pylori carbonic anhydrases
    • DOI 10.1016/j.femsim.2004.10.021, PII S0928824404002330, Pathogenesis and Host Response in Helicobacter Infections
    • Stahler FN, Ganter L, Lederer K, Kist M, Bereswill S. Mutational analysis of the H. pylori carbonic anhydrases. FEMS Immunol. Med. Microbiol. 44, 183-189 (2005). (Pubitemid 41373375)
    • (2005) FEMS Immunology and Medical Microbiology , vol.44 , Issue.2 , pp. 183-189
    • Nils Stahler, F.1    Ganter, L.2    Lederer, K.3    Kist, M.4    Bereswill, S.5
  • 130
    • 11844269324 scopus 로고    scopus 로고
    • The periplasmic α-carbonic anhydrase activity of Helicobacter pylori is essential for acid acclimation
    • DOI 10.1128/JB.187.2.729-738.2005
    • Marcus EA, Moshfegh AP, Sachs G, Scott DR. The periplasmic α-carbonic anhydrase activity of H. pylori is essential for acid acclimation. J. Bacteriol. 187, 729-738 (2005). (Pubitemid 40096259)
    • (2005) Journal of Bacteriology , vol.187 , Issue.2 , pp. 729-738
    • Marcus, E.A.1    Moshfegh, A.P.2    Sachs, G.3    Scott, D.R.4
  • 131
    • 33644811878 scopus 로고    scopus 로고
    • Carbonic anhydrase inhibitors: Cloning and sulfonamide inhibition studies of a carboxyterminal truncated α-carbonic anhydrase from Helicobacter pylori
    • DOI 10.1016/j.bmcl.2006.01.044, PII S0960894X06000801
    • Nishimori I, Vullow D, Minakuchi T et al. Carbonic anhydrase inhibitors: cloning and sulfonamide inhibition studies of a carboxyterminal truncated α-carbonic anhydrase from H. pylori. Bioorg. Med. Chem. 16, 2182-2188 (2006). (Pubitemid 43351075)
    • (2006) Bioorganic and Medicinal Chemistry Letters , vol.16 , Issue.8 , pp. 2182-2188
    • Nishimori, I.1    Vullo, D.2    Minakuchi, T.3    Morimoto, K.4    Onishi, S.5    Scozzafava, A.6    Supuran, C.T.7
  • 133
    • 0035663935 scopus 로고    scopus 로고
    • Cloning and expression of Helicobacter pylori GDP-L-fucose synthesizing enzymes (GMD and GMER) in Saccharomyces cerevisiae
    • DOI 10.1046/j.0014-2956.2001.02601.x
    • Jarvinen N, Maki M, Rabina J, Roos C, Mattila P, Renkonen R. Cloning and expression of H. pylori GDP-L-fucose synthesizing enzymes (GMD and GMER) in S. cerevisiae. Eur. J. Biochem. 268, 6458-6464 (2001). (Pubitemid 34014753)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.24 , pp. 6458-6464
    • Jarvinen, N.1    Maki, M.2    Rabina, J.3    Roos, C.4    Mattila, P.5    Renkonen, R.6
  • 134
    • 0034806401 scopus 로고    scopus 로고
    • Identification and characterization of GDP-D-mannose 4,6-dehydratase and GDP-L-fucose synthetase in a GDP-L-fucose biosynthetic gene cluster from Helicobacter pylori
    • DOI 10.1006/bbrc.2001.5137
    • Wu B, Zhang Y, Wang PG. Identification and characterisation of GDP-D-mannose 4,6-dehydratase and GDP-L-fucose synthetase in a GDP-L-fucose biosynthesis gene cluster from H. pylori. Biochem. Biophys. Res. Commun. 285, 364-371 (2001). (Pubitemid 32918079)
    • (2001) Biochemical and Biophysical Research Communications , vol.285 , Issue.2 , pp. 364-371
    • Wu, B.1    Zhang, Y.2    Wang, P.G.3
  • 135
    • 0028122564 scopus 로고
    • Effect of gastric pH on urease-dependent colonization of gnotobiotic piglets by Helicobacter pylori
    • Eaton KA, Krakowka S. Effect of gastric pH on urease-dependent colonisation of gnotobiotic piglets by H. pylori. Infect. Immun. 62, 3604-3607 (1994). (Pubitemid 24264297)
    • (1994) Infection and Immunity , vol.62 , Issue.9 , pp. 3604-3607
    • Eaton, K.A.1    Krakowka, S.2
  • 136
    • 0141681866 scopus 로고    scopus 로고
    • Roles of conserved nucleotide-binding domains in accessory proteins, HypB and UreG, in the maturation of nickel-enzymes required for efficient Helicobacter pylori colonization
    • DOI 10.1016/S0882-4010(03)00151-7
    • Mehta N, Benoit S, Maier RJ. Roles of conserved nucleotide-binding domains in accessory proteins, HypB and UreG, in the maturation of nickel-enzymes required for efficient H. pylori colonisation. Microb. Pathog. 35, 229-234 (2003). (Pubitemid 37163723)
    • (2003) Microbial Pathogenesis , vol.35 , Issue.5 , pp. 229-234
    • Mehta, N.1    Benoit, S.2    Maier, R.J.3
  • 137
    • 34249007915 scopus 로고    scopus 로고
    • Interaction between the Helicobacter pylori accessory proteins HypA and UreE is needed for urease maturation
    • DOI 10.1099/mic.0.2006/003228-0
    • Benoit SL, Mehta N, Weinberg MV, Maier C, Maier RJ. Interaction between the H. pylori accessory proteins HypA and UreE is needed for urease maturation. Microbiology 153, 1474-1482 (2007). (Pubitemid 46780003)
    • (2007) Microbiology , vol.153 , Issue.5 , pp. 1474-1482
    • Benoit, S.L.1    Mehta, N.2    Weinberg, M.V.3    Maier, C.4    Maier, R.J.5
  • 138
    • 0041559754 scopus 로고    scopus 로고
    • Dependence of Helicobacter pylori urease activity on the nickel-sequestering ability of the UreE accessory protein
    • DOI 10.1128/JB.185.16.4787-4795.2003
    • Benoit S, Maier RJ. Dependence of H. pylori urease activity on the nickel-sequestering ability of the UreE accessory protein. J. Bacteriol. 185, 4787-4795 (2003). (Pubitemid 36962286)
    • (2003) Journal of Bacteriology , vol.185 , Issue.16 , pp. 4787-4795
    • Benoit, S.1    Maier, R.J.2
  • 139
    • 0031661885 scopus 로고    scopus 로고
    • The Helicobacter pylori UreI protein is not involved in urease activity but is essential for bacterial survival in vivo
    • Skouloubris S, Thiberge JM, Labigne A, De Reuse H. The H. pylori UreI protein is not involved in urease activity but is essential for bacterial survival in vivo. Infect. Immun. 66, 4517-4521 (1998). (Pubitemid 28402735)
    • (1998) Infection and Immunity , vol.66 , Issue.9 , pp. 4517-4521
    • Skouloubris, S.1    Thiberge, J.-M.2    Labigne, A.3    De Reuse, H.4
  • 140
    • 0036898882 scopus 로고    scopus 로고
    • Expression of UreI is required for intragastric transit and colonization of gerbil gastric mucosa by Helicobacter pylori
    • DOI 10.1016/S0923-2508(02)01380-3, PII S0923250802013803
    • Mollenhauer-Rektorschek M, Hanauer G, Sachs G, Melchers K. Expression of UreI is required for intragastric transit and colonisation of gerbil gastric mucosa by H. pylori. Res. Microbiol. 153, 659-666 (2002). (Pubitemid 35449269)
    • (2002) Research in Microbiology , vol.153 , Issue.10 , pp. 659-666
    • Mollenhauer-Rektorschek, M.1    Hanauer, G.2    Sachs, G.3    Melchers, K.4
  • 142
    • 0034932504 scopus 로고    scopus 로고
    • Sites of PH regulation of the urea channel of Helicobacter pylori
    • DOI 10.1046/j.1365-2958.2001.02466.x
    • Weeks DL, Sachs G. Sites of pH regulation of the urea channel of H. pylori. Mol. Microbiol. 40, 1249-1259 (2001). (Pubitemid 32635296)
    • (2001) Molecular Microbiology , vol.40 , Issue.6 , pp. 1249-1259
    • Weeks, D.L.1    Sachs, G.2
  • 143
    • 0033958917 scopus 로고    scopus 로고
    • Expression of the Helicobacter pylori ureI gene is required for acidic pH activation of cytoplasmic urease
    • DOI 10.1128/IAI.68.2.470-477.2000
    • Scott DR, Marcus EA, Weeks GL, Lee A, Melchers K, Sachs G. Expression of the H. pylori ureI gene is required for acidic pH activation of cytoplasmic urease. Infect. Immun. 68, 470-477 (2000). (Pubitemid 30056496)
    • (2000) Infection and Immunity , vol.68 , Issue.2 , pp. 470-477
    • Scott, D.R.1    Marcus, E.A.2    Weeks, D.L.3    Lee, A.4    Melchers, K.5    Sachs, G.6
  • 144
    • 0034695684 scopus 로고    scopus 로고
    • +-gated urea channel: The link between Helicobacter pylori urease and gastric colonization
    • DOI 10.1126/science.287.5452.482
    • Weeks DL, Eskandari S, Scott DR, Sachs G. A H+-gated urea channel: the link between H. pylori urease and gastric colonisation. Science. 287, 482-485 (2000). (Pubitemid 33595255)
    • (2000) Science , vol.287 , Issue.5452 , pp. 482-485
    • Weeks, D.L.1    Eskandari, S.2    Scott, D.R.3    Sachs, G.4
  • 145
    • 27444440094 scopus 로고    scopus 로고
    • Cloning of Helicobacter pylori urease subunit B gene and its expression in tobacco (Nicotiana tabacum L.)
    • DOI 10.1007/s00299-005-0962-8
    • Gu Q, Han N, Liu J, Zhu M. Cloning of H. pylori urease subunit B gene and its expression in tobacco (Nicotiana tabacum L.). Plant Cell Rep. 24, 532-539 (2005). (Pubitemid 41531541)
    • (2005) Plant Cell Reports , vol.24 , Issue.9 , pp. 532-539
    • Gu, Q.1    Han, N.2    Liu, J.3    Zhu, M.4
  • 146
    • 0025979283 scopus 로고
    • Shuttle cloning and nucleotide sequences of H. pylori genes responsible for urease activity
    • Labigne A, Cussac V, Courcoux P. Shuttle cloning and nucleotide sequences of H. pylori genes responsible for urease activity. J. Bacteriol. 173, 1920-1931 (1991).
    • (1991) J. Bacteriol. , vol.173 , pp. 1920-1931
    • Labigne, A.1    Cussac, V.2    Courcoux, P.3
  • 147
    • 0034109116 scopus 로고    scopus 로고
    • Another unusual type of citric acid cycle enzyme in Helicobacter pylori: The malate:quinone oxidoreductase
    • DOI 10.1128/JB.182.11.3204-3209.2000
    • Kather B, Stingl K, van der Rest ME, Altendorf K, Molenaar D. Another unusual type of citric acid cycle enzyme in H. pylori: the malate:quinone oxidoreductase. J. Bacteriol. 182, 3204-3209 (2000). (Pubitemid 30326937)
    • (2000) Journal of Bacteriology , vol.182 , Issue.11 , pp. 3204-3209
    • Kather, B.1    Stingl, K.2    Van Der Rest, M.E.3    Altendorf, K.4    Molenaar, D.5
  • 148
    • 0033909787 scopus 로고    scopus 로고
    • Transcriptional analysis of major heat shock genes of Helicobacter pylori
    • DOI 10.1128/JB.182.15.4257-4263.2000
    • Homuth G, Domm S, Kleiner D, Schumann W. Transcription analysis of major heat shock genes of H. pylori. J. Bacteriol. 182, 4257-4263 (2000). (Pubitemid 30465652)
    • (2000) Journal of Bacteriology , vol.182 , Issue.15 , pp. 4257-4263
    • Homuth, G.1    Domm, S.2    Kleiner, D.3    Schumann, W.4
  • 149
    • 33644556825 scopus 로고    scopus 로고
    • Comparative proteomic analysis of H. pylori strains associated with iron deficiency anemia
    • Park SA, Lee HW, Hong MH et al. Comparative proteomic analysis of H. pylori strains associated with iron deficiency anemia. Proteomics 6, 1319-1328 (2006).
    • (2006) Proteomics , vol.6 , pp. 1319-1328
    • Park, S.A.1    Lee, H.W.2    Hong, M.H.3
  • 150
    • 33746541640 scopus 로고    scopus 로고
    • The adverse antioxidant systems of H. pylori
    • Elucidates the roles of all of these antioxidant systems by a targeted mutant analysis approach and shows their importance in host colonization. Some of the described antioxidant systems in H. pylori are potential therapeutic targets
    • Wang G, Alamuri P, Maier RJ. The adverse antioxidant systems of H. pylori. Mol. Microbiol. 61, 847-860 (2006). • Elucidates the roles of all of these antioxidant systems by a targeted mutant analysis approach and shows their importance in host colonization. Some of the described antioxidant systems in H. pylori are potential therapeutic targets.
    • (2006) Mol. Microbiol. , vol.61 , pp. 847-860
    • Wang, G.1    Alamuri, P.2    Maier, R.J.3
  • 151
    • 11144328882 scopus 로고    scopus 로고
    • Contribution of the Helicobacter pylori thiol peroxidase bacterioferritin comigratory protein to oxidative stress resistance and host colonization
    • DOI 10.1128/IAI.73.1.378-384.2005
    • Wang G, Olczak AA, Walton JP, Maier RJ. Contribution of the H. pylori thiol peroxidase bacterioferritin comigratory protein to oxidative stress resistance and host colonisation. Infect. Immun. 73, 378-384 (2005). (Pubitemid 40041130)
    • (2005) Infection and Immunity , vol.73 , Issue.1 , pp. 378-384
    • Wang, G.1    Olczak, A.A.2    Walton, J.P.3    Maier, R.J.4
  • 152
    • 33646581347 scopus 로고    scopus 로고
    • Characterization of the ArsRS regulon of Helicobacter pylon, involved in acid adaptation
    • DOI 10.1128/JB.188.10.3449-3462.2006
    • Pflock M, Finsterer N, Joseph B, Mollenkopf H, Meyer TF, Beier D. Characterisation of the ArsRS regulon of H. pylori involved in acid adaptation. J. Bacteriol. 188, 3449-3462 (2006). (Pubitemid 43726208)
    • (2006) Journal of Bacteriology , vol.188 , Issue.10 , pp. 3449-3462
    • Pflock, M.1    Finsterer, N.2    Joseph, B.3    Mollenkopf, H.4    Meyer, T.F.5    Beier, D.6
  • 153
    • 0036134955 scopus 로고    scopus 로고
    • Identification of target genes regulated by the two-component system HP166-HP165 of helicobacter pylori
    • DOI 10.1128/JB.184.2.350-362.2002
    • Dietz P, Gerlach G, Beier D. Identification of target genes regulated by the two-component system Hp0166-Hp0165 of H. pylori. J. Bacteriol. 184, 350-362 (2002). (Pubitemid 34027374)
    • (2002) Journal of Bacteriology , vol.184 , Issue.2 , pp. 350-362
    • Dietz, P.1    Gerlach, G.2    Beier, D.3
  • 154
    • 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
    • DOI 10.1016/S0378-1119(97)00550-7, PII S0378111997005507
    • Ge Z, Jiang Q, Kalisiak MS, Taylor DE. Cloning and functional characterisation of H. pylori fumarate reductase operon comprising three structural genes coding for subunits C, A and B. Gene. 204, 227-234 (1997). (Pubitemid 28022193)
    • (1997) Gene , vol.204 , Issue.1-2 , pp. 227-234
    • Ge, Z.1    Jiang, Q.2    Kalisiak, M.S.3    Taylor, D.E.4
  • 155
    • 0029113366 scopus 로고
    • Fumarate reductase: A target for therapeutic intervention against H. pylori
    • Mendz GL, Hazell SH, Srinivasan S. Fumarate reductase: a target for therapeutic intervention against H. pylori. Arch. Biochem. Biophys. 321, 153-159 (1995).
    • (1995) Arch. Biochem. Biophys. , vol.321 , pp. 153-159
    • Mendz, G.L.1    Hazell, S.H.2    Srinivasan, S.3
  • 157
    • 4444275438 scopus 로고    scopus 로고
    • Methionine sulphoxide reductase is an important antioxidant enzyme in the gastric pathogen Helicobacter pylori
    • DOI 10.1111/j.1365-2958.2004.04190.x
    • Alamuri P, Maier RJ. Methionine sulphoxide reductase is an important antioxidant enzyme in the gastric pathogen H. pylori. Mol. Microbiol. 53, 1397-1406 (2004). (Pubitemid 39209113)
    • (2004) Molecular Microbiology , vol.53 , Issue.5 , pp. 1397-1406
    • Alamuri, P.1    Maier, R.J.2
  • 159
    • 0033821176 scopus 로고    scopus 로고
    • Mutational analysis of genes encoding the early flagellar components of Helicobacter pylori: Evidence for transcriptional regulation of flagellin a biosynthesis
    • DOI 10.1128/JB.182.18.5274-5277.2000
    • Allan E, Dorrell N, Foynes S, Anyim M, Wren BW. Mutational analysis of genes encoding the early flagellar components of H. pylori: evidence for transcriptional regulation of flagellin A biosynthesis. J. Bacteriol. 182, 5274-5277 (2000). (Pubitemid 30700779)
    • (2000) Journal of Bacteriology , vol.182 , Issue.18 , pp. 5274-5277
    • Allan, E.1    Dorrell, N.2    Foynes, S.3    Anyim, M.4    Wren, B.W.5
  • 160
    • 33646827681 scopus 로고    scopus 로고
    • Structural and functional characterisation of PseC, an aminotransferase involved in the biosynthesis of pseudaminic acid, an essential flagellar modification in H. pylori
    • Presents an example of an enzyme co-crystallized with its natural ligand and its functional characterization
    • Schoenhofen IC, Lunin VV, Julien JP et al. Structural and functional characterisation of PseC, an aminotransferase involved in the biosynthesis of pseudaminic acid, an essential flagellar modification in H. pylori. J. Biol. Chem. 281, 8907-8916 (2006). • Presents an example of an enzyme co-crystallized with its natural ligand and its functional characterization.
    • (2006) J. Biol. Chem. , vol.281 , pp. 8907-8916
    • Schoenhofen, I.C.1    Lunin, V.V.2    Julien, J.P.3
  • 161
    • 0034802293 scopus 로고    scopus 로고
    • Chemotaxis in the human gastric pathogen Helicobacter pylori: Different roles for CheW and the three CheV paralogues, and evidence for CheV2 phosphorylation
    • Pittman MS, Goodwin M, Kelly DJ. Chemotaxis in the human gastric pathogen H. pylori: different roles for CheW and the three CheV paralogues, and evidence for CheV2 phosphorylation. Microbiology 147, 2493-2504 (2001). (Pubitemid 32899245)
    • (2001) Microbiology , vol.147 , Issue.9 , pp. 2493-2504
    • Pittman, M.S.1    Goodwin, M.2    Kelly, D.J.3
  • 162
    • 0034061330 scopus 로고    scopus 로고
    • Helicobacter pylori possesses two CheY response regulators and a histidine kinase sensor, CheA, which are essential for chemotaxis and colonization of the gastric mucosa
    • DOI 10.1128/IAI.68.4.2016-2023.2000
    • Foynes S, Dorrell N, Ward SJ et al. H. pylori possesses two CheY repsonse regulators and a histidine kinase sensor, CheA, which are essential for chemotaxis and colonisation of the gastric mucosa. Infect. Immun. 68, 2016-2023 (2000). (Pubitemid 30164832)
    • (2000) Infection and Immunity , vol.68 , Issue.4 , pp. 2016-2023
    • Foynes, S.1    Dorrell, N.2    Ward, S.J.3    Stabler, R.A.4    McColm, A.A.5    Rycroft, A.N.6    Wren, B.W.7
  • 163
    • 12844264798 scopus 로고    scopus 로고
    • Chemotaxis plays multiple roles during H. pylori animal infection
    • The data elucidate the roles for chemotaxis in H. pylori mouse infections showing that genes involved in this function are candidate targets
    • Terry K, Williams SM, Connolly L, Ottemann KM. Chemotaxis plays multiple roles during H. pylori animal infection. Infect. Immun. 73, 803-811 (2005). • The data elucidate the roles for chemotaxis in H. pylori mouse infections showing that genes involved in this function are candidate targets.
    • (2005) Infect. Immun. , vol.73 , pp. 803-811
    • Terry, K.1    Williams, S.M.2    Connolly, L.3    Ottemann, K.M.4
  • 164
    • 27144511247 scopus 로고    scopus 로고
    • Phosphate flow in the chemotactic response system of Helicobacter pylori
    • DOI 10.1099/mic.0.28217-0
    • Jimenez-Pearson MA, Delany I, Scarlato V, Beier D. Phosphate flow in the chemotactic response system of H. pylori. Microbiology 151, 3299-3311 (2005). (Pubitemid 41488913)
    • (2005) Microbiology , vol.151 , Issue.10 , pp. 3299-3311
    • Jimenez-Pearson, M.-A.1    Delany, I.2    Scarlato, V.3    Beier, D.4
  • 168
    • 0031885642 scopus 로고    scopus 로고
    • H. pylori porCDAB and oorDABC genes encode distinct pyruvate:flavodoxin and 2-oxoglutarate:acceptor oxidoreductases which mediate electron transport to NADP
    • Hughes NJ, Clayton CL, Chalk PA, Kelly DJ. H. 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).
    • (1998) J. Bacteriol. , vol.180 , pp. 1119-1128
    • Hughes, N.J.1    Clayton, C.L.2    Chalk, P.A.3    Kelly, D.J.4
  • 169
    • 0033811410 scopus 로고    scopus 로고
    • Sequential inactivation of rdxA (Hp0954) and frxA (Hp0642) nitroreductase genes causes moderate and high-level metronidazole resistance in H. pylori
    • Jeong JY, Mukhopadhyay AK, Dailidiene D et al. Sequential inactivation of rdxA (Hp0954) and frxA (Hp0642) nitroreductase genes causes moderate and high-level metronidazole resistance in H. pylori. J. Bacteriol. 182, 5082-5090 (2000).
    • (2000) J. Bacteriol. , vol.182 , pp. 5082-5090
    • Jeong, J.Y.1    Mukhopadhyay, A.K.2    Dailidiene, D.3
  • 170
    • 39149119270 scopus 로고    scopus 로고
    • Tip-a (hp0596 gene product) is a highly immunogenic H. pylori protein involved in colonisation of mouse gastric mucosa
    • Godlewska R, Pawlowski M, Dzwonek A et al. Tip-a (hp0596 gene product) is a highly immunogenic H. pylori protein involved in colonisation of mouse gastric mucosa. Curr. Microbiol. 56, 279-286 (2008).
    • (2008) Curr. Microbiol. , vol.56 , pp. 279-286
    • Godlewska, R.1    Pawlowski, M.2    Dzwonek, A.3
  • 173
    • 0142244385 scopus 로고    scopus 로고
    • Construction of expression systems for flaA and flaB genes of Helicobacter pylori and determination of immunoreactivity and antigenicity of recombinant proteins
    • Yan J, Liang SH, Mao YF, Li LW, Li SP. Construction of expression systems for flaA and flaB genes of H. pylori and determination of immunoreactivity and antigenicity of recombinant proteins. World J. Gastroenterol. 9, 2240-2250 (2003). (Pubitemid 37321453)
    • (2003) World Journal of Gastroenterology , vol.9 , Issue.10 , pp. 2240-2250
    • Yan, J.1    Liang, S.-H.2    Mao, Y.-F.3    Li, L.-W.4    Li, S.-P.5
  • 174
    • 0027252455 scopus 로고
    • Cloning and genetic characterization of the Helicobacter pylori and Helicobacter mustelae flaB flagellin genes and construction of H. pylori flaA- And flaB-negative mutants by electroporation-mediated allelic exchange
    • Suerbaum S, Josenhans C, Labigne A. Cloning and genetic characterisation of the H. pylori and H. mustelae flaB flagellin genes and construction of H. pylori flaA- and flaB-negative mutants by electroporation-mediated allelic exchange. J. Bacteriol. 175, 3278-3288 (1993). (Pubitemid 23163369)
    • (1993) Journal of Bacteriology , vol.175 , Issue.11 , pp. 3278-3288
    • Suerbaum, S.1    Josenhans, C.2    Labigne, A.3
  • 175
    • 26244452150 scopus 로고    scopus 로고
    • The Helicobacter pylori MutS protein confers protection from oxidative DNA damage
    • DOI 10.1111/j.1365-2958.2005.04833.x
    • Wang G, Alamuri P, Humayun MZ, Taylor DE, Maier RJ. The H. pylori MutS protein confers protection from oxidative DNA damage. Mol. Microbiol. 58(1), 166-176 (2005). (Pubitemid 41415038)
    • (2005) Molecular Microbiology , vol.58 , Issue.1 , pp. 166-176
    • Wang, G.1    Alamuri, P.2    Zafri Humayun, M.3    Taylor, D.E.4    Maier, R.J.5
  • 176
    • 1342344978 scopus 로고    scopus 로고
    • An NADPH Quinone Reductase of Helicobacter pylori Plays An Important Role in Oxidative Stress Resistance and Host Colonization
    • DOI 10.1128/IAI.72.3.1391-1396.2004
    • Wang G, Maier RJ. An NADPH quinone reductase of H. pylori plays an important role in oxidative stress resistance and host colonisation. Infect. Immun. 72, 1391-1396 (2004). (Pubitemid 38263760)
    • (2004) Infection and Immunity , vol.72 , Issue.3 , pp. 1391-1396
    • Wang, G.1    Maier, R.J.2
  • 178
    • 0034076830 scopus 로고    scopus 로고
    • Identification of the urease operon in Helicobacter pylori and its control by mRNA decay in response to pH
    • DOI 10.1046/j.1365-2958.2000.01918.x
    • Akada JK, Shirai M, Takeuchi H, Tsuda M, Nakazawa T. Identification of the urease operon in H. pylori and its control by mRNA decay in response to pH. Mol. Microbiol. 36, 1071-1084 (2000). (Pubitemid 30330679)
    • (2000) Molecular Microbiology , vol.36 , Issue.5 , pp. 1071-1084
    • Akada, J.K.1    Shirai, M.2    Takeuchi, H.3    Tsuda, M.4    Nakazawa, T.5
  • 180
    • 1042275584 scopus 로고    scopus 로고
    • Crystal structure of chorismate synthase: A novel FMN-binding protein fold and functional insights
    • Ahn HJ, Yoon HJ, Lee BI, Suh SW. Crystal structure of chorismate synthase: a novel FMN-binding protein fold and functional insights. J. Mol. Biol. 336, 903-915 (2004).
    • (2004) J. Mol. Biol. , vol.336 , pp. 903-915
    • Ahn, H.J.1    Yoon, H.J.2    Lee, B.I.3    Suh, S.W.4
  • 181
    • 0033915316 scopus 로고    scopus 로고
    • Switching of flagellar motility in Helicobacter pylori by reversible length variation of a short homopolymeric sequence repeat in fliP, a gene encoding a basal body protein
    • DOI 10.1128/IAI.68.8.4598-4603.2000
    • Josenhans C, Eaton KA, Thevenot T, Suerbaum S. Switching of flagellar motility in H. pylori by reversible length variation of a short homopolymeric sequence repeat in fliP, a gene encoding a basal body protein. Infect. Immun. 68, 4598-4603 (2000). (Pubitemid 30497729)
    • (2000) Infection and Immunity , vol.68 , Issue.8 , pp. 4598-4603
    • Josenhans, C.1    Eaton, K.A.2    Thevenot, T.3    Suerbaum, S.4
  • 183
    • 3042733355 scopus 로고    scopus 로고
    • H. pylori FlgR is an enhancerin-dependent activator of s54-RNA polymerase holoenzyme
    • Brahmachary P, Dashti MG, Olson JW, Hoover TR. H. pylori FlgR is an enhancerin-dependent activator of s54-RNA polymerase holoenzyme. J. Bacteriol. 186, 4535-4542 (2004).
    • (2004) J. Bacteriol. , vol.186 , pp. 4535-4542
    • Brahmachary, P.1    Dashti, M.G.2    Olson, J.W.3    Hoover, T.R.4
  • 184
    • 0032589796 scopus 로고    scopus 로고
    • Motility of Helicobacter priori is coordinately regulated by the transcriptional activator FlgR, an NtrC homolog
    • Spohn G, Scarlato V. Motility of H. pylori is coordinately regulated by the transcriptional activator FlgR, an NtrC homolog. J. Bacteriol. 181, 593-599 (1999). (Pubitemid 29045152)
    • (1999) Journal of Bacteriology , vol.181 , Issue.2 , pp. 593-599
    • Spohn, G.1    Scarlato, V.2
  • 185
    • 0034765681 scopus 로고    scopus 로고
    • Allelic exchange mutagenesis of rpoN encoding RNA-polymerase s54 subunit in H. pylori
    • Fujinaga R, Nakazawa T, Shirai M. Allelic exchange mutagenesis of rpoN encoding RNA-polymerase s54 subunit in H. pylori. J. Infect. Chemother. 7, 148-155 (2001).
    • (2001) J. Infect. Chemother. , vol.7 , pp. 148-155
    • Fujinaga, R.1    Nakazawa, T.2    Shirai, M.3
  • 187
    • 33745899620 scopus 로고    scopus 로고
    • Bioinformatic analysis of Helicobacter pylori XGPRTase: A potential therapeutic target
    • DOI 10.1111/j.1523-5378.2006.00409.x
    • Duckworth M, Menard A, Megraud F, Mendz GL. Bioinformatic analysis of H. pylori XGPRTase: a potential therapeutic target. Helicobacter 11, 287-295 (2006). (Pubitemid 44051355)
    • (2006) Helicobacter , vol.11 , Issue.4 , pp. 287-295
    • Duckworth, M.1    Menard, A.2    Megraud, F.3    Mendz, G.L.4
  • 188
    • 7444238081 scopus 로고    scopus 로고
    • Substrate specificity of Helicobacter pylori histone-like HU protein is determined by insufficient stabilization of DNA flexure points
    • DOI 10.1042/BJ20040938
    • Chen C, Ghosh S, Grove A. Substrate specificity of H. pylori histone-like HU protein is determined by insufficient stabilisation of DNA flexure points. Biochem. J. 383, 343-351 (2004). (Pubitemid 39446696)
    • (2004) Biochemical Journal , vol.383 , Issue.2 , pp. 343-351
    • Chen, C.1    Ghosh, S.2    Grove, A.3
  • 190
    • 33846043578 scopus 로고    scopus 로고
    • A dynamic Zn site in H. pylori HypA: A potential mechanism for metal-specific protein activity
    • Kennedy DC, Herbst RW, Iwig JS, Chivers PT, Maroney MJ. A dynamic Zn site in H. pylori HypA: a potential mechanism for metal-specific protein activity. J. Am. Chem. Soc. 129, 1-17 (2007).
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 1-17
    • Kennedy, D.C.1    Herbst, R.W.2    Iwig, J.S.3    Chivers, P.T.4    Maroney, M.J.5
  • 191
    • 0035191007 scopus 로고    scopus 로고
    • Requirement of nickel metabolism proteins HypA and HypB for full activity of both hydrogenase and urease in H. pylori
    • Olson JW, Mehta NS, Maier RJ. Requirement of nickel metabolism proteins HypA and HypB for full activity of both hydrogenase and urease in H. pylori. Mol. Microbiol. 39, 176-182 (2001).
    • (2001) Mol. Microbiol. , vol.39 , pp. 176-182
    • Olson, J.W.1    Mehta, N.S.2    Maier, R.J.3
  • 192
    • 0037307747 scopus 로고    scopus 로고
    • Characterization of Helicobacter pylori nickel metabolism accessory proteins needed for maturation of both urease and hydrogenase
    • DOI 10.1128/JB.185.3.726-734.2003
    • Mehta N, Olson JW, Maier RJ. Characterisation of H. pylori nickel metabolism accessory proteins needed for maturation of both urease and hydrogenase. J. Bacteriol. 185, 726-734 (2003). (Pubitemid 36139432)
    • (2003) Journal of Bacteriology , vol.185 , Issue.3 , pp. 726-734
    • Mehta, N.1    Olson, J.W.2    Maier, R.J.3
  • 193
    • 0037350476 scopus 로고    scopus 로고
    • Catalase (KatA) and KatA-associated protein (KapA) are essential to persistent colonization in the Helicobacter pylori SS1 mouse model
    • DOI 10.1099/mic.0.26012-0
    • Harris AG, Wilson JE, Danon SJ, Dixon MF, Donegan K, Hazell SH. Catalase (KatA) and KatA-associated protein (KapA) are essential to persistent colonisation in the H. pylori SS1 mouse model. Microbiology 149, 665-672 (2003). (Pubitemid 36395101)
    • (2003) Microbiology , vol.149 , Issue.3 , pp. 665-672
    • Harris, A.G.1    Wilson, J.E.2    Danon, S.J.3    Dixon, M.F.4    Donegan, K.5    Hazell, S.L.6
  • 194
    • 0037378144 scopus 로고    scopus 로고
    • Helicobacter pylori mutants defective in RuvC Holliday junction resolvase display reduced macrophage survival and spontaneous clearance from the murine gastric mucosa
    • DOI 10.1128/IAI.71.4.2022-2031.2003
    • Loughlin MF, Barnard FM, Jenkins D, Sharples GJ, Jenks PJ. H. pylori mutants defective in RuvC Holliday junction resolvase display reduced macrophage survival and spontaneous clearance from the murine gastric mucosa. Infect. Immun. 71, 2022-2031 (2003). (Pubitemid 36368736)
    • (2003) Infection and Immunity , vol.71 , Issue.4 , pp. 2022-2031
    • Loughlin, M.F.1    Barnard, F.M.2    Jenkins, D.3    Sharples, G.J.4    Jenks, P.J.5
  • 195
    • 21144433281 scopus 로고    scopus 로고
    • 54 in H. pylori requires the novel protein Hp0958
    • 54 in H. pylori requires the novel protein Hp0958. J. Bacteriol. 187, 4463-4469 (2005).
    • (2005) J. Bacteriol. , vol.187 , pp. 4463-4469
    • Pereira, L.1    Hoover, T.R.2
  • 197
    • 29644439241 scopus 로고    scopus 로고
    • Iron and pH homeostasis intersect at the level of fur regulation in the gastric pathogen Helicobacter pylori
    • DOI 10.1128/IAI.74.1.602-614.2006
    • Gancz H, Censini S, Merrell DS. Iron and pH homeostasis intersect at the level of Fur regulation in the gastric pathogen H. pylori. Infect. Immun. 74, 602-614 (2006). (Pubitemid 43023116)
    • (2006) Infection and Immunity , vol.74 , Issue.1 , pp. 602-614
    • Gancz, H.1    Censini, S.2    Merrell, D.S.3
  • 199
    • 3242881125 scopus 로고    scopus 로고
    • Responsiveness to activity via metal ion regulators mediates virulense in the gastric pathogen Helicobacter pylori
    • DOI 10.1111/j.1365-2958.2004.04137.x
    • Bury-Mone S, Thiberge JM, Contreras M, Maitournam A, Labigne A, De Reuse H. Responsiveness of acidity via metal ion regulators mediates virulence in the gastric pathogen H. pylori. Mol. Microbiol. 53, 623-638 (2004). (Pubitemid 38998180)
    • (2004) Molecular Microbiology , vol.53 , Issue.2 , pp. 623-638
    • Bury-Mone, S.1    Thiberge, J.-M.2    Contreras, M.3    Maitournam, A.4    Labigne, A.5    De Reuse, H.6
  • 200
    • 27744481253 scopus 로고    scopus 로고
    • In vitro analysis of protein-operator interactions of the NikR and fur metal-responsive regulators of coregulated genes in Helicobacter pylori
    • DOI 10.1128/JB.187.22.7703-7715.2005
    • Delany I, Ieva R, Soragni A, Hilleringmann M, Rappuoli R, Scarlato V. In vitro analysis of protein-operator interactions of the NikR and Fur metal-responsive regulators of coregulated genes in H. pylori. J. Bacteriol. 187, 7703-7715 (2005). (Pubitemid 41587709)
    • (2005) Journal of Bacteriology , vol.187 , Issue.22 , pp. 7703-7715
    • Delany, I.1    Ieva, R.2    Soragni, A.3    Hilleringmann, M.4    Rappuoli, R.5    Scarlato, V.6
  • 201
    • 4644320428 scopus 로고    scopus 로고
    • H. pylori Hp1034 (ylxH) is required for motility
    • van Amsterdam K, van der Ende A. H. pylori Hp1034 (ylxH) is required for motility. Helicobacter. 9, 387-395 (2004).
    • (2004) Helicobacter. , vol.9 , pp. 387-395
    • Van Amsterdam, K.1    Van Der Ende, A.2
  • 203
    • 0029833135 scopus 로고    scopus 로고
    • Cloning, sequencing, expression, purification and preliminary characterization of a type II dehydroquinase from Helicobacter pylori
    • Bottomley JR, Clayton CL, Chalk PA, Kleanthous C. Cloning, sequencing, expression, purification and preliminary characterisation of a type II dehydroquinase from H. pylori. Biochem. J. 319, 559-565 (1996). (Pubitemid 26372217)
    • (1996) Biochemical Journal , vol.319 , Issue.2 , pp. 559-565
    • Bottomley, J.R.1    Clayton, C.L.2    Chalk, P.A.3    Kleanthous, C.4
  • 204
    • 0037603068 scopus 로고    scopus 로고
    • Crystal structure of the type II 3-dehydroquinase from H. pylori
    • Lee BI, Kwak JE, Suh SW. Crystal structure of the type II 3-dehydroquinase from H. pylori. Protein. 51, 616-617 (2003).
    • (2003) Protein. , vol.51 , pp. 616-617
    • Lee, B.I.1    Kwak, J.E.2    Suh, S.W.3
  • 205
    • 47649120747 scopus 로고    scopus 로고
    • Competitive inhibitors of H. pylori type II dehydroquinase: Synthesis, biological evaluation, and NMR studies
    • Sanchez-Sixto C, Prazeres VFV, Castedo L et al. Competitive inhibitors of H. pylori type II dehydroquinase: synthesis, biological evaluation, and NMR studies. Chem. Med. Chem. 3, 756-770 (2008).
    • (2008) Chem. Med. Chem. , vol.3 , pp. 756-770
    • Sanchez-Sixto, C.1    Prazeres, V.F.V.2    Castedo, L.3
  • 206
    • 15544364461 scopus 로고    scopus 로고
    • Colonisation and inflammation deficiencies in Mongolian gerbils infected by H. pylori chemotaxis mutants
    • Clarifies the role of a chemoreceptor in the inflammatory response to H. pylori and of a chemotaxis regulator in initial colonization
    • McGee DJ, Langford ML, Watson EL, Carter JE, Chen YT, Ottemann KM. Colonisation and inflammation deficiencies in Mongolian gerbils infected by H. pylori chemotaxis mutants. Infect. Immun. 73, 1820-1827 (2005). • Clarifies the role of a chemoreceptor in the inflammatory response to H. pylori and of a chemotaxis regulator in initial colonization.
    • (2005) Infect. Immun. , vol.73 , pp. 1820-1827
    • McGee, D.J.1    Langford, M.L.2    Watson, E.L.3    Carter, J.E.4    Chen, Y.T.5    Ottemann, K.M.6
  • 207
    • 0030741916 scopus 로고    scopus 로고
    • Identification and characterization of an operon of Helicobacter pylori that is involved in motility and stress adaptation
    • Beier D, Spohn G, Rappuoli R, Scarlato V. Identification and characterisation of an operon of H. pylori that is involved in motility and stress adaptation. J. Bacteriol. 179, 4676-4683 (1997). (Pubitemid 27339710)
    • (1997) Journal of Bacteriology , vol.179 , Issue.15 , pp. 4676-4683
    • Beier, D.1    Spohn, G.2    Rappuoli, R.3    Scarlato, V.4
  • 208
    • 0036175155 scopus 로고    scopus 로고
    • Conserved low-affinity nickel-binding amino acids are essential for the function of the nickel permease NixA of Helicobacter pylori
    • Wolfram L, Bauerfeind P. Conserved low-affinity nickel-binding amino acids are essential for the function of the nickel permease NixA of H. pylori. J. Bacteriol. 184, 1438-1443 (2002). (Pubitemid 34157568)
    • (2002) Journal of Bacteriology , vol.184 , Issue.5 , pp. 1438-1443
    • Wolfram, L.1    Bauerfeind, P.2
  • 209
    • 0031982679 scopus 로고    scopus 로고
    • Conserved residues and motifs in the NixA protein of H. pylori are critical for the high affinity transport of nickel ions
    • Fulkerson JF Jr, Garner RM, Mobley HLT. Conserved residues and motifs in the NixA protein of H. pylori are critical for the high affinity transport of nickel ions. J. Biol. Chem. 273, 235-241 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 235-241
    • Fulkerson Jr., J.F.1    Garner, R.M.2    Mobley, H.L.T.3
  • 210
    • 0030955227 scopus 로고    scopus 로고
    • H. pylori ABC transporter: Effect of allelic exchange mutagenesis on urease activity
    • Hendricks JK, Mobley HLT. H. pylori ABC transporter: effect of allelic exchange mutagenesis on urease activity. J. Bacteriol. 179, 5892-5902 (1997).
    • (1997) J. Bacteriol. , vol.179 , pp. 5892-5902
    • Hendricks, J.K.1    Mobley, H.L.T.2
  • 211
    • 0034104188 scopus 로고    scopus 로고
    • Membrane topology of the NixA nickel transporter of H. pylori: Two nickel tranport-specific motifs within transmembrane helices II and III
    • Fulkerson JF Jr, Mobley HLT. Membrane topology of the NixA nickel transporter of H. pylori: two nickel tranport-specific motifs within transmembrane helices II and III. J. Bacteriol. 182, 1722-1730 (2000).
    • (2000) J. Bacteriol. , vol.182 , pp. 1722-1730
    • Fulkerson Jr., J.F.1    Mobley, H.L.T.2
  • 212
    • 0036155961 scopus 로고    scopus 로고
    • In vivo behaviour of a H. pylori SS1 nixA mutant with reduced urease activity
    • Nolan KJ, McGee DJ, Mitchell HM et al. In vivo behaviour of a H. pylori SS1 nixA mutant with reduced urease activity. Infect. Immun. 70, 685-691 (2002).
    • (2002) Infect. Immun. , vol.70 , pp. 685-691
    • Nolan, K.J.1    McGee, D.J.2    Mitchell, H.M.3
  • 213
    • 0031282431 scopus 로고    scopus 로고
    • In situ properties of H. pylori aspartate carbamoyltransferase
    • Burns BP, Mendz GL, Hazell SL. In situ properties of H. pylori aspartate carbamoyltransferase. Arch. Biochem. Biophys. 347, 119-125 (1997).
    • (1997) Arch. Biochem. Biophys. , vol.347 , pp. 119-125
    • Burns, B.P.1    Mendz, G.L.2    Hazell, S.L.3
  • 215
    • 0242584874 scopus 로고    scopus 로고
    • The Entner-Doudoroff pathway has little effect on Helicobacter pylori colonization of mice
    • DOI 10.1128/IAI.71.5.2920-2923.2003
    • Wanken AE, Conway T, Eaton KA. The entner-doudoroff pathway has little effect on H. pylori colonisation of mice. Infect. Immun. 71, 2920-2923 (2003). (Pubitemid 36519910)
    • (2003) Infection and Immunity , vol.71 , Issue.5 , pp. 2920-2923
    • Wanken, A.E.1    Conway, T.2    Eaton, K.A.3
  • 216
    • 0029046363 scopus 로고
    • Identification of carboxylation enzymes and characterisation of a novel four-subunit pyruvate:flavodoxin oxidoreductase from H. pylori
    • Hughes NJ, Chalk PA, Clayton CL, Kelly DJ. Identification of carboxylation enzymes and characterisation of a novel four-subunit pyruvate:flavodoxin oxidoreductase from H. pylori. J. Bacteriol. 177, 3953-3959 (1995).
    • (1995) J. Bacteriol. , vol.177 , pp. 3953-3959
    • Hughes, N.J.1    Chalk, P.A.2    Clayton, C.L.3    Kelly, D.J.4
  • 217
    • 33847660062 scopus 로고    scopus 로고
    • Antiparasitic drug nitazoxanide inhibits the pyruvate oxidoreductase of H. pylori and selected anaerobic bacteria and parasites, and C. jejuni
    • Hoffman PS, Sisson G, Croxen MA et al. Antiparasitic drug nitazoxanide inhibits the pyruvate oxidoreductase of H. pylori and selected anaerobic bacteria and parasites, and C. jejuni. Antimicrob. Agents Chemother. 51, 868-876 (2006).
    • (2006) Antimicrob. Agents Chemother. , vol.51 , pp. 868-876
    • Hoffman, P.S.1    Sisson, G.2    Croxen, Ma.3
  • 219
    • 0344734063 scopus 로고    scopus 로고
    • Nitazoxanide, a potential drug for eradication of Helicobacter pylori with no cross-resistance to metronidazole
    • Megraud F, Occhialini A, Rossignol JF. Nitazoxanide, a potential drug to eradicate H. pylori with no cross resistance to metronidazole. Antimicrob. Agents Chemother. 42, 2836-2840 (1998). (Pubitemid 28501212)
    • (1998) Antimicrobial Agents and Chemotherapy , vol.42 , Issue.11 , pp. 2836-2840
    • Megraud, F.1    Occhialini, A.2    Rossignol, J.F.3
  • 220
    • 0035017794 scopus 로고    scopus 로고
    • γ-glutamyltransferase is a Helicobacter pylori virulence factor but is not essential for colonization
    • DOI 10.1128/IAI.69.6.4168-4173.2001
    • McGovern KJ, Blanchard TG, Gutierrez JA, Czinn SJ, Krakowka S, Youngman P. γ-glutamyltransferase is a H. pylori virulence factor but is not essential for colonisation. Infect. Immun. 69, 4168-4173 (2001). (Pubitemid 32493346)
    • (2001) Infection and Immunity , vol.69 , Issue.6 , pp. 4168-4173
    • McGovern, K.J.1    Blanchard, T.G.2    Gutierrez, J.A.3    Czinn, S.J.4    Krakowka, S.5    Youngman, P.6
  • 221
    • 0032982703 scopus 로고    scopus 로고
    • Essential role of Helicobacter pylori γ-glutamyltranspeptidase for the colonization of the gastric mucosa of mice
    • Chevalier C, Thiberge JM, Ferrero RL, Labigne A. Essential role of H. pylori γ-glutamyltranspeptidase for the colonisation of the gastric mucosa of mice. Mol. Microbiol. 31, 1359-1372 (1999). (Pubitemid 29110095)
    • (1999) Molecular Microbiology , vol.31 , Issue.5 , pp. 1359-1372
    • Chevalier, C.1    Thiberge, J.-M.2    Ferrero, R.L.3    Labigne, A.4
  • 223
    • 36248940234 scopus 로고    scopus 로고
    • Characterization of Helicobacter pylori γ-glutamyltranspeptidase reveals the molecular basis for substrate specificity and a critical role for the tyrosine 433-containing loop in catalysis
    • DOI 10.1021/bi701599e
    • Morrow AL, Williams K, Sand A, Boanca G, Barycki JJ. Characterisation of H. pylori γ-glutamyltranspeptidase reveals the molecular basis for substrate specificity and a critical role for the tyrosine 433-containing loop in catalysis. Biochemistry 46, 13407-13414 (2007). (Pubitemid 350136379)
    • (2007) Biochemistry , vol.46 , Issue.46 , pp. 13407-13414
    • Morrow, A.L.1    Williams, K.2    Sand, A.3    Boanca, G.4    Barycki, J.J.5
  • 224
    • 38849142536 scopus 로고    scopus 로고
    • The flavodoxin from Helicobacter pylori: Structural determinants of thermostability and FMN cofactor binding
    • DOI 10.1021/bi701365e
    • Cremades N, Velazquez-Campoy A, Freire E, Sancho J. The flavodoxin from H. pylori: structural determinants of thermostability and FMN cofactor binding. Biochemistry 47, 627-639 (2007). (Pubitemid 351195434)
    • (2008) Biochemistry , vol.47 , Issue.2 , pp. 627-639
    • Cremades, N.1    Velazquez-Campoy, A.2    Freire, E.3    Sancho, J.4
  • 225
    • 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
    • DOI 10.1128/JB.00287-07
    • St Maurice M, Cremades N, Croxen MA, Sisson G, Sancho J, Hoffman PS. Flavodoxin:quinone reductase (FqrB): a redox partner of pyruvate:ferredoxin oxidoreductase that reversibly couples pyruvate oxidation ot NADPH production in H. pylori and C. jejuni. J. Bacteriol. 189, 4764-4773 (2007). (Pubitemid 47025588)
    • (2007) Journal of Bacteriology , vol.189 , Issue.13 , pp. 4764-4773
    • St Maurice, M.1    Cremades, N.2    Croxen, M.A.3    Sisson, G.4    Sancho, J.5    Hoffman, P.S.6
  • 226
    • 60649117715 scopus 로고    scopus 로고
    • Obstinate contaminants in a picrogram scale. One more bottleneck in the membrane protein structure pipeline
    • Psakis G, Polaczek J, Essen LO et al. Obstinate contaminants in a picrogram scale. One more bottleneck in the membrane protein structure pipeline. J. Struct. Biol. 166. 107-111 (2009).
    • (2009) J. Struct. Biol. , vol.166 , pp. 107-111
    • Psakis, G.1    Polaczek, J.2    Essen, L.O.3
  • 227
    • 33846184987 scopus 로고    scopus 로고
    • Identification and characterisation of an organic solvent tolerance gene in H. pylori
    • Chiu HC, Lin TL, Wang JT. Identification and characterisation of an organic solvent tolerance gene in H. pylori. Helicobacter 12, 74-81 (2007).
    • (2007) Helicobacter , vol.12 , pp. 74-81
    • Chiu, H.C.1    Lin, T.L.2    Wang, J.T.3
  • 228
    • 0038154081 scopus 로고    scopus 로고
    • The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode
    • DOI 10.1128/JB.185.14.4144-4151.2003
    • Ye S, Von Delft F, Brooun A, Knuth MW, Swanson RV, McRee DE. The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode. J. Bacteriol. 185, 4144-4151 (2003). (Pubitemid 36835254)
    • (2003) Journal of Bacteriology , vol.185 , Issue.14 , pp. 4144-4151
    • Ye, S.1    Von Delft, F.2    Brooun, A.3    Knuth, M.W.4    Swanson, R.V.5    McRee, D.E.6
  • 229
    • 28844499031 scopus 로고    scopus 로고
    • Prospects for aminoacyl-tRNA synthetase inhibitors as new antimicrobial agents
    • DOI 10.1128/AAC.49.12.4821-4833.2005
    • Hurdle JG, O'Neill AJ, Chopra I. Prospects for aminoacyl-tRNA synthetase inhibitors as new antimicrobial agents. Antimicrob Agents Chemother. 49, 4821-4833 (2005). (Pubitemid 41778891)
    • (2005) Antimicrobial Agents and Chemotherapy , vol.49 , Issue.12 , pp. 4821-4833
    • Hurdle, J.G.1    O'Neill, A.J.2    Chopra, I.3
  • 232
    • 0037844668 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetases and their inhibitors as a novel family of antibiotics
    • Kim S, Lee SW, Choi EC, Choi SY. Aminoacyl-tRNA synthetases and their inhibitors as a novel family of antibiotics. Appl. Microbiol. Biotechnol. 61, 278-288 (2003). (Pubitemid 36683523)
    • (2003) Applied Microbiology and Biotechnology , vol.61 , Issue.4 , pp. 278-288
    • Kim, S.1    Lee, S.W.2    Choi, E.-C.3    Choi, S.Y.4
  • 233
    • 2142692746 scopus 로고    scopus 로고
    • Crystallisation and preliminary X-ray crystallographic analysis of orotate phosphoribosyltransferase from H. pylori
    • Kim MK, Song HE, Kim YS et al. Crystallisation and preliminary X-ray crystallographic analysis of orotate phosphoribosyltransferase from H. pylori. Mol. Cell. 15, 361-363 (2003).
    • (2003) Mol. Cell. , vol.15 , pp. 361-363
    • Kim, M.K.1    Song, H.E.2    Kim, Y.S.3
  • 234
    • 33646359655 scopus 로고    scopus 로고
    • Requirement of hisitine kinases Hp0165 and Hp1364 for acid resistance in H. pylori
    • Loh JT, Clover TL. Requirement of hisitine kinases Hp0165 and Hp1364 for acid resistance in H. pylori. Infect. Immun. 74, 3052-3059 (2006).
    • (2006) Infect. Immun. , vol.74 , pp. 3052-3059
    • Loh, J.T.1    Clover, T.L.2
  • 235
    • 33947409952 scopus 로고    scopus 로고
    • The CrdRS (HP1365-HP1364) two-component system is not involved in pH-responsive gene regulation in the Helicobacter pylori strains 26695 and G27
    • DOI 10.1007/s00284-006-0520-9
    • Pflock M, Muller S, Beier D. The CrdRS (Hp1365-Hp1364) two-component system is not involved in pH-responsive gene regulation in the H. pylori strains 26695 and G27. Curr. Microbiol. 54, 320-324 (2007). (Pubitemid 46452247)
    • (2007) Current Microbiology , vol.54 , Issue.4 , pp. 320-324
    • Pflock, M.1    Muller, S.2    Beier, D.3
  • 236
    • 0036263170 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic analysis of UDP-N-acetylglucosamine acyltransferase from Helicobacter pylori
    • DOI 10.1107/S0907444902004845
    • Lee B, Lee JY, Moon J, Han BW, Suh SW. Crystallisation and preliminary X-ray crystallographic analysis of UDP-N-aceylglucosamine acyltransferase from H. pylori. Acta Crystallogr. D. Biol. Crystallogr. 58, 864-866 (2002). (Pubitemid 34557304)
    • (2002) Acta Crystallographica Section D: Biological Crystallography , vol.58 , Issue.5 , pp. 864-866
    • Byung, I.L.1    Jae, Y.L.2    Moon, J.3    Byung, W.H.4    Se, W.S.5
  • 237
    • 0242362183 scopus 로고    scopus 로고
    • Crystal structure of UDP-N-acetylglucosamine acyltransferase from H. pylori
    • Lee B, Suh SW. Crystal structure of UDP-N-acetylglucosamine acyltransferase from H. pylori. Proteins 53, 772-774 (2003).
    • (2003) Proteins , vol.53 , pp. 772-774
    • Lee, B.1    Suh, S.W.2
  • 238
    • 37749034749 scopus 로고    scopus 로고
    • Critical role of RecN in recombinational DNA repair and survival of H. pylori
    • Identifies H. pylori RecN as a component of DNA recombinational repair that plays a significant role in survival of the bacterium in vivo
    • Wang G, Maier RJ. Critical role of RecN in recombinational DNA repair and survival of H. pylori. Infect. Immun. 76, 153-160 (2008). • Identifies H. pylori RecN as a component of DNA recombinational repair that plays a significant role in survival of the bacterium in vivo.
    • (2008) Infect. Immun. , vol.76 , pp. 153-160
    • Wang, G.1    Maier, R.J.2
  • 239
    • 0032925510 scopus 로고    scopus 로고
    • Molecular characterization of a flagellar export locus of Helicobacter pylori
    • Porwollik S, Noonan B, O'Toole PW. Molecular characterisation of a flagellar export locus of H. pylori. Infect. Immun. 67, 2060-2070 (1999). (Pubitemid 29200453)
    • (1999) Infection and Immunity , vol.67 , Issue.5 , pp. 2060-2070
    • Porwollik, S.1    Noonan, B.2    O'Toole, P.W.3
  • 240
    • 0036251307 scopus 로고    scopus 로고
    • Helicobacter pylori adherence to gastric epithelial cells: A role for non-adhesin virulence genes
    • Zhang ZW, Dorrell N, Wren BW, Farthing MJG. H. pylori adherence to gastric epithelial cells: a role for non-adhesin virulence genes. J. Med. Microbiol. 52, 495-502 (2002). (Pubitemid 34492978)
    • (2002) Journal of Medical Microbiology , vol.51 , Issue.6 , pp. 495-502
    • Zhang, Z.-W.1    Dorrell, N.2    Wren, B.W.3    Farthing, M.J.G.4
  • 241
    • 0030852276 scopus 로고    scopus 로고
    • A flagellar-specific ATPase (FliI) is necessary for flagellar export in Helicobacter pylori
    • DOI 10.1016/S0378-1097(97)00170-5, PII S00378109797001705
    • Jenks PJ, Foynes S, Ward SJ, Constantinidou C, Penn CW, Wren BW. A flagellar-specific ATPase (FliI) is necessary for flagellar export in H. pylori. FEMS Microbiol. Lett. 152, 205-211 (1997). (Pubitemid 27316685)
    • (1997) FEMS Microbiology Letters , vol.152 , Issue.2 , pp. 205-211
    • Jenks, P.J.1    Foynes, S.2    Ward, S.J.3    Constantinidou, C.4    Penn, C.W.5    Wren, B.W.6
  • 242
    • 33644853360 scopus 로고    scopus 로고
    • Molecular basis of the interaction between the flagellar export proteins FliI and FliH from H. pylori
    • Lane MC, O'Toole PW, Moore SA. Molecular basis of the interaction between the flagellar export proteins FliI and FliH from H. pylori. J. Biol Chem. 281, 508-517 (2006).
    • (2006) J. Biol Chem. , vol.281 , pp. 508-517
    • Lane, M.C.1    O'Toole, P.W.2    Moore, S.A.3
  • 243
    • 31344443610 scopus 로고    scopus 로고
    • Functional and topological characterization of novel components of the comB DNA transformation competence system in Helicobacter pylori
    • DOI 10.1128/JB.188.3.882-893.2006
    • Karnholz A, Hoefler C, Odenbreit S, Fischer W, Hofreuter D, Haas R. Functional and topologicl characterisation of novel components of the comB DNA transformation competence system in H. pylori. J. Bacteriol. 188, 882-893 (2006). (Pubitemid 43146403)
    • (2006) Journal of Bacteriology , vol.188 , Issue.3 , pp. 882-893
    • Karnholz, A.1    Hoefler, C.2    Odenbreit, S.3    Fischer, W.4    Hofreuter, D.5    Haas, R.6
  • 244
    • 0348225097 scopus 로고    scopus 로고
    • Global regulation of virulence and the stress response by CsrA in the highly adapted human gastric pathogen H. pylori
    • Barnard FM, Loughlin MF, Fainberg HP et al. Global regulation of virulence and the stress response by CsrA in the highly adapted human gastric pathogen H. pylori. Mol. Microbiol. 51, 15-32 (2004).
    • (2004) Mol. Microbiol. , vol.51 , pp. 15-32
    • Barnard, F.M.1    Loughlin, M.F.2    Fainberg, H.P.3
  • 245
    • 0038159606 scopus 로고    scopus 로고
    • + antiporter (NhaA) protein from H. pylori required for ion transport and pH sensing
    • + antiporter (NhaA) protein from H. pylori required for ion transport and pH sensing. J. Biol. Chem. 278, 21467-21473 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 21467-21473
    • Tsuboi, Y.1    Inoue, H.2    Nakamura, N.3    Kanazawa, H.4
  • 249
    • 0034817055 scopus 로고    scopus 로고
    • Identification of nonessential Helicobacter pylori genes using random mutagenesis and loop amplification
    • DOI 10.1016/S0923-2508(01)01253-0
    • Jenks PJ, Chevalier C, Ecobichon C, Labigne A. Identification of nonessential H. pylori genes using random mutagenesis and loop amplification. Res. Microbiol. 152, 725-734 (2001). (Pubitemid 32905505)
    • (2001) Research in Microbiology , vol.152 , Issue.8 , pp. 725-734
    • Jenks, P.J.1    Chevalier, C.2    Ecobichon, C.3    Labigne, A.4


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