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Volumn 295, Issue 5, 2005, Pages 307-315

Staying alive overdosed: How does Helicobacter pylori control urease activity

Author keywords

Acid resistance; Epigenetic inheritance; Nickel incorporation; Urea channel; Urease accessory proteins; Urel

Indexed keywords

NICKEL; UREASE; BACTERIAL PROTEIN; CARRIER PROTEIN; UREI PROTEIN, HELICOBACTER PYLORI;

EID: 26944483560     PISSN: 14384221     EISSN: 16180607     Source Type: Journal    
DOI: 10.1016/j.ijmm.2005.06.006     Document Type: Review
Times cited : (95)

References (62)
  • 1
    • 0034076830 scopus 로고    scopus 로고
    • Identification of the urease operon in Helicobacter pylori and its control by mRNA decay in response to pH
    • Akada, J.K., Shirai, M., Takeuchi, H., Tsuda, M., Nakazawa, T., 2000. Identification of the urease operon in Helicobacter pylori and its control by mRNA decay in response to pH. Mol. Microbiol. 36, 1071-1084.
    • (2000) Mol. Microbiol. , vol.36 , pp. 1071-1084
    • Akada, J.K.1    Shirai, M.2    Takeuchi, H.3    Tsuda, M.4    Nakazawa, T.5
  • 3
    • 0029994917 scopus 로고    scopus 로고
    • Allelic exchange mutagenesis of nixA in Helicobacter pylori results in reduced nickel transport and urease activity
    • Bauerfeind, P., Garner, R.M., Mobley, H.L.T., 1996. Allelic exchange mutagenesis of nixA in Helicobacter pylori results in reduced nickel transport and urease activity. Infect. Immun. 64, 2877-2880.
    • (1996) Infect. Immun. , vol.64 , pp. 2877-2880
    • Bauerfeind, P.1    Garner, R.M.2    Mobley, H.L.T.3
  • 4
    • 0031042034 scopus 로고    scopus 로고
    • Synthesis and activity of Helicobacter pylori urease and catalase at low pH
    • Bauerfeind, P., Garner, R., Dunn, B.E., Mobley, H.L.T., 1997. Synthesis and activity of Helicobacter pylori urease and catalase at low pH. Gut 40, 25-30.
    • (1997) Gut , vol.40 , pp. 25-30
    • Bauerfeind, P.1    Garner, R.2    Dunn, B.E.3    Mobley, H.L.T.4
  • 5
    • 0041559754 scopus 로고    scopus 로고
    • Dependence of Helicobacter pylori urease activity on the nickel-sequestering ability of the UreE accessory protein
    • Benoit, S., Maier, R.J., 2003. Dependence of Helicobacter pylori urease activity on the nickel-sequestering ability of the UreE accessory protein. J. Bacteriol. 185, 4787-4795.
    • (2003) J. Bacteriol. , vol.185 , pp. 4787-4795
    • Benoit, S.1    Maier, R.J.2
  • 6
    • 0029812727 scopus 로고    scopus 로고
    • Purification, characterization, and functional analysis of a truncated Klebsiella aerogenes UreE urease accessory protein lacking the histidine-rich carboxyl terminus
    • Brayman, T.G., Hausinger, R.T., 1996. Purification, characterization, and functional analysis of a truncated Klebsiella aerogenes UreE urease accessory protein lacking the histidine-rich carboxyl terminus. J. Bacteriol. 178, 5410-5416.
    • (1996) J. Bacteriol. , vol.178 , pp. 5410-5416
    • Brayman, T.G.1    Hausinger, R.T.2
  • 7
    • 0034747001 scopus 로고    scopus 로고
    • The Helicobacter pylori Urel protein: Role in adaptation to acidity and identification of residues essential for its activity and for acid activation
    • Bury-Moné, S., Skouloubris, S., Labigne, A., De Reuse, H., 2001a. The Helicobacter pylori Urel protein: role in adaptation to acidity and identification of residues essential for its activity and for acid activation. Mol. Microbiol. 42, 1021-1034.
    • (2001) Mol. Microbiol. , vol.42 , pp. 1021-1034
    • Bury-Moné, S.1    Skouloubris, S.2    Labigne, A.3    De Reuse, H.4
  • 8
    • 0034741226 scopus 로고    scopus 로고
    • Urel: Une protéine de Helicobacter pylori essentielle à la résistance àl'acidité et aux étapes précoses de l'infection de la muqueuse gastrique
    • Bury-Moné, S., Skouloubris, S., Labigne, A., De Reuse, H., 2001b. Urel: une protéine de Helicobacter pylori essentielle à la résistance àl'acidité et aux étapes précoses de l'infection de la muqueuse gastrique. Gastroenterol. Clin. Biol. 25, 659-663.
    • (2001) Gastroenterol. Clin. Biol. , vol.25 , pp. 659-663
    • Bury-Moné, S.1    Skouloubris, S.2    Labigne, A.3    De Reuse, H.4
  • 9
    • 3242881125 scopus 로고    scopus 로고
    • Responsiveness to acidity via metal ion regulators mediates virulence in the gastric pathogen Helicobacter pylori
    • Bury-Moné, S., Thiberge, J.-M., Contreras, M., Maitournam, A., Labigne, A., De Reuse, H., 2004. Responsiveness to acidity via metal ion regulators mediates virulence in the gastric pathogen Helicobacter pylori. Mol. Microbiol. 53, 623-638.
    • (2004) Mol. Microbiol. , vol.53 , pp. 623-638
    • Bury-Moné, S.1    Thiberge, J.-M.2    Contreras, M.3    Maitournam, A.4    Labigne, A.5    De Reuse, H.6
  • 10
    • 0028940849 scopus 로고
    • Helicobacter pylori requires an acidic environment to survive in the presence of urea
    • Clyne, M., Labigne, A., Drumm, B., 1995. Helicobacter pylori requires an acidic environment to survive in the presence of urea. Infect. Immun. 63, 1669-1673.
    • (1995) Infect. Immun. , vol.63 , pp. 1669-1673
    • Clyne, M.1    Labigne, A.2    Drumm, B.3
  • 11
    • 0033616728 scopus 로고    scopus 로고
    • Identification of metal-binding residues in the Klebsiella aerogenes urease nickel metallochaperone, UreE
    • Colpas, G.J., Brayman, T.G., Ming, L.J., Hausinger, R.P., 1999. Identification of metal-binding residues in the Klebsiella aerogenes urease nickel metallochaperone, UreE. Biochemistry 38, 4078-4088.
    • (1999) Biochemistry , vol.38 , pp. 4078-4088
    • Colpas, G.J.1    Brayman, T.G.2    Ming, L.J.3    Hausinger, R.P.4
  • 12
    • 0042065267 scopus 로고    scopus 로고
    • Characterization of the roles of NikR, a nickel-responsive pleitropic autoregulator of Helicobacter pylori
    • Contreras, M., Thiberge, J.-M., Mandrand-Berthelot, M.-A., Labigne, A., 2003. Characterization of the roles of NikR, a nickel-responsive pleitropic autoregulator of Helicobacter pylori. Mol. Microbiol. 49, 947-963.
    • (2003) Mol. Microbiol. , vol.49 , pp. 947-963
    • Contreras, M.1    Thiberge, J.-M.2    Mandrand-Berthelot, M.-A.3    Labigne, A.4
  • 13
    • 0026723973 scopus 로고
    • Expression of Helicobacter pylori urease genes in Escherichia coli grown under nitrogen-limiting conditions
    • Cussac, V., Ferrero, R.L., Labigne, A., 1992. Expression of Helicobacter pylori urease genes in Escherichia coli grown under nitrogen-limiting conditions. J. Bacteriol. 174, 2466-2473.
    • (1992) J. Bacteriol. , vol.174 , pp. 2466-2473
    • Cussac, V.1    Ferrero, R.L.2    Labigne, A.3
  • 15
    • 0025369322 scopus 로고
    • Purification and characterization of urease from Helicobacter pylori
    • Dunn, B.E., Campbell, G.P., Perez-Perez, G.I., Blaser, M.J., 1990. Purification and characterization of urease from Helicobacter pylori. J. Biol. Chem. 265, 9464-9469.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9464-9469
    • Dunn, B.E.1    Campbell, G.P.2    Perez-Perez, G.I.3    Blaser, M.J.4
  • 16
    • 0028122564 scopus 로고
    • Effect of gastric pH on urease-dependent colonization of gnotobiotic piglets by Helicobacter pylori
    • Eaton, K.A., Krakowka, S., 1994. Effect of gastric pH on urease-dependent colonization of gnotobiotic piglets by Helicobacter pylori. Infect. Immun. 62, 3604-3607.
    • (1994) Infect. Immun. , vol.62 , pp. 3604-3607
    • Eaton, K.A.1    Krakowka, S.2
  • 17
    • 0026753106 scopus 로고
    • Construction of isogenic urease-negative mutants of Helicobacter pylori by allelic exchange
    • Ferrero, R.L., Cussac, V., Courcoux, P., Labigne, A., 1992. Construction of isogenic urease-negative mutants of Helicobacter pylori by allelic exchange. J. Bacteriol. 174, 4212-4217.
    • (1992) J. Bacteriol. , vol.174 , pp. 4212-4217
    • Ferrero, R.L.1    Cussac, V.2    Courcoux, P.3    Labigne, A.4
  • 18
    • 0031982679 scopus 로고    scopus 로고
    • Conserved residues and motifs in the NixA protein of Helicobacter pylori are critical for the high affinity transport of nickel ions
    • Fulkerson Jr., J.F., Garner, R.M., Mobley, H.L., 1998. Conserved residues and motifs in the NixA protein of Helicobacter pylori are critical for the high affinity transport of nickel ions. J. Biol. Chem. 273, 235-241.
    • (1998) J. Biol. Chem. , vol.273 , pp. 235-241
    • Fulkerson Jr., J.F.1    Garner, R.M.2    Mobley, H.L.3
  • 19
    • 0031900966 scopus 로고    scopus 로고
    • Helicobacter pylori glutamine synthetase lacks features associated with transcriptional and posttranslational regulation
    • Garner, R.M., Fulkerson Jr., J., Mobley, H.L., 1998. Helicobacter pylori glutamine synthetase lacks features associated with transcriptional and posttranslational regulation. Infect. Immun. 66, 1839-1847.
    • (1998) Infect. Immun. , vol.66 , pp. 1839-1847
    • Garner, R.M.1    Fulkerson Jr., J.2    Mobley, H.L.3
  • 20
    • 0030561586 scopus 로고    scopus 로고
    • Helicobacter pylori genes hpcopA and hpcopP constitute a cop operon involved in copper export
    • Ge, Z., Taylor, D.E., 1996. Helicobacter pylori genes hpcopA and hpcopP constitute a cop operon involved in copper export. FEMS Microbiol. Lett. 145, 181-188.
    • (1996) FEMS Microbiol. Lett. , vol.145 , pp. 181-188
    • Ge, Z.1    Taylor, D.E.2
  • 21
    • 0029070195 scopus 로고
    • Protein Hpn: Cloning and characterization of a histidine-rich metal-binding polypeptide in Helicobacter pylori and Helicobacter mustelae
    • Gilbert, J.V., Ramakrishna, J., Sunderman Jr., F.W., Wright, A., Plaut, A.G., 1995. Protein Hpn: cloning and characterization of a histidine-rich metal-binding polypeptide in Helicobacter pylori and Helicobacter mustelae. Infect. Immun. 63, 2682-2688.
    • (1995) Infect. Immun. , vol.63 , pp. 2682-2688
    • Gilbert, J.V.1    Ramakrishna, J.2    Sunderman Jr., F.W.3    Wright, A.4    Plaut, A.G.5
  • 22
    • 0037097533 scopus 로고    scopus 로고
    • Cutting edge: Urease release by Helicobacter pylori stimulates macrophage inducibel nitric oxide synthase
    • Gobert, A., Mersey, B.D., Cheng, Y., Blumberg, D.R., Newton, J.C., Wilson, K.T., 2002. Cutting edge: urease release by Helicobacter pylori stimulates macrophage inducibel nitric oxide synthase. J. Immunol. 168, 6002-6006.
    • (2002) J. Immunol. , vol.168 , pp. 6002-6006
    • Gobert, A.1    Mersey, B.D.2    Cheng, Y.3    Blumberg, D.R.4    Newton, J.C.5    Wilson, K.T.6
  • 23
    • 0034995248 scopus 로고    scopus 로고
    • Supramolecular assembly and acid resistance of Helicobacter pylori urease
    • Ha, N.C., Oh, S.T., Sung, J.Y., Cha, K.A., Lee, M.H., Oh, B.H., 2001. Supramolecular assembly and acid resistance of Helicobacter pylori urease. Nat. Struct. Biol. 8, 505-509.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 505-509
    • Ha, N.C.1    Oh, S.T.2    Sung, J.Y.3    Cha, K.A.4    Lee, M.H.5    Oh, B.H.6
  • 24
    • 0032791578 scopus 로고    scopus 로고
    • Helicobacter pylori cadA encodes an essential Cd(II)-Zn(II)-Co(II) resistance factor influencing urease activity
    • Herrmann, L., Schwan, D., Garner, R., Mobley, H., Haas, R., Schaefer, K.P., Melchers, K., 1999. Helicobacter pylori cadA encodes an essential Cd(II)-Zn(II)-Co(II) resistance factor influencing urease activity. Mol. Microbiol. 33, 524-536.
    • (1999) Mol. Microbiol. , vol.33 , pp. 524-536
    • Herrmann, L.1    Schwan, D.2    Garner, R.3    Mobley, H.4    Haas, R.5    Schaefer, K.P.6    Melchers, K.7
  • 25
    • 0025247997 scopus 로고
    • Purification and N-terminal analysis of urease from Helicobacter pylori
    • Hu, L.T., Mobley, H.L.T., 1990. Purification and N-terminal analysis of urease from Helicobacter pylori. Infect. Immun. 58, 992-998.
    • (1990) Infect. Immun. , vol.58 , pp. 992-998
    • Hu, L.T.1    Mobley, H.L.T.2
  • 26
    • 0029994559 scopus 로고    scopus 로고
    • Heat shock proteins of Helicobacter pylori
    • Kansau, I., Labigne, A., 1996. Heat shock proteins of Helicobacter pylori. Aliment. Pharmacol. Ther. 10 (Suppl. 1), 51-56.
    • (1996) Aliment. Pharmacol. Ther. , vol.10 , Issue.SUPPL. 1 , pp. 51-56
    • Kansau, I.1    Labigne, A.2
  • 28
    • 0034468995 scopus 로고    scopus 로고
    • Construction and characterization of an E. coli strain genetically engineered for Ni(II) bioaccumulation
    • Krishnaswamy, R., Wilson, D.B., 2000. Construction and characterization of an E. coli strain genetically engineered for Ni(II) bioaccumulation. Appl. Environ. Microbiol. 66, 5383-5386.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 5383-5386
    • Krishnaswamy, R.1    Wilson, D.B.2
  • 29
    • 0034951587 scopus 로고    scopus 로고
    • Cell lysis is responsible for the appearance of extracellular urease in Helicobacter pylori
    • Marcus, E.A., Scott, D.R., 2001. Cell lysis is responsible for the appearance of extracellular urease in Helicobacter pylori. Helicobacter 6, 93-99.
    • (2001) Helicobacter , vol.6 , pp. 93-99
    • Marcus, E.A.1    Scott, D.R.2
  • 30
    • 0032696916 scopus 로고    scopus 로고
    • H. pylori rocF is required for arginase activity and acid protection in vitro but is not essential for colonization of mice or for urease activity
    • McGee, D.J., Radcliff, F., Mendz, G.L., Ferrero, R.L., Mobley, H.L.T., 1999. H. pylori rocF is required for arginase activity and acid protection in vitro but is not essential for colonization of mice or for urease activity. J. Bacteriol. 181, 7314-7322.
    • (1999) J. Bacteriol. , vol.181 , pp. 7314-7322
    • McGee, D.J.1    Radcliff, F.2    Mendz, G.L.3    Ferrero, R.L.4    Mobley, H.L.T.5
  • 31
    • 0033192731 scopus 로고    scopus 로고
    • Role of Hpn and NixA of Helicobacter pylori in susceptibility and resistance to bismuth and other metal ions
    • Mobley, H.L., Garner, R.M., Chippendale, G.R., Gilbert, J.V., Kane, A.V., Plaut, A.G., 1999. Role of Hpn and NixA of Helicobacter pylori in susceptibility and resistance to bismuth and other metal ions. Helicobacter 4, 162-169.
    • (1999) Helicobacter , vol.4 , pp. 162-169
    • Mobley, H.L.1    Garner, R.M.2    Chippendale, G.R.3    Gilbert, J.V.4    Kane, A.V.5    Plaut, A.G.6
  • 33
    • 0036898882 scopus 로고    scopus 로고
    • Expression of Urel is required for intragastric transit and colonization of gerbil gastric mucosa by Helicobacter pylori
    • Mollenhauer-Rektorschek, M., Hanauer, G., Sachs, G., Melchers, K., 2002. Expression of Urel is required for intragastric transit and colonization of gerbil gastric mucosa by Helicobacter pylori. Res. Microbiol. 153, 659-666.
    • (2002) Res. Microbiol. , vol.153 , pp. 659-666
    • Mollenhauer-Rektorschek, M.1    Hanauer, G.2    Sachs, G.3    Melchers, K.4
  • 34
    • 0029809744 scopus 로고    scopus 로고
    • Purification and activation properties of UreD-UreF-urease apoprotein complexes
    • Moncrief, M.B., Hausinger, R.P., 1996. Purification and activation properties of UreD-UreF-urease apoprotein complexes. J. Bacteriol. 178, 5417-5421.
    • (1996) J. Bacteriol. , vol.178 , pp. 5417-5421
    • Moncrief, M.B.1    Hausinger, R.P.2
  • 35
    • 0030873130 scopus 로고    scopus 로고
    • Characterization of UreG, identification of a UreD-UreF-UreG complex, and evidence suggesting that a nucleotide-binding site in UreG is required for in vivo metallocenter assembly of Klebsiella aerogenes urease
    • Moncrief, M.B., Hausinger, R.P., 1997. Characterization of UreG, identification of a UreD-UreF-UreG complex, and evidence suggesting that a nucleotide-binding site in UreG is required for in vivo metallocenter assembly of Klebsiella aerogenes urease. J. Bacteriol. 179, 4081-4086.
    • (1997) J. Bacteriol. , vol.179 , pp. 4081-4086
    • Moncrief, M.B.1    Hausinger, R.P.2
  • 36
    • 0035191007 scopus 로고    scopus 로고
    • Requirement of nickel metabolism proteins HypA and HypB for full activity of both hydrogenase and urease in Helicobacter pylori
    • Olson, J.W., Mehta, N.S., Maier, R.J., 2001. Requirement of nickel metabolism proteins HypA and HypB for full activity of both hydrogenase and urease in Helicobacter pylori. Mol. Microbiol. 39, 176-182.
    • (2001) Mol. Microbiol. , vol.39 , pp. 176-182
    • Olson, J.W.1    Mehta, N.S.2    Maier, R.J.3
  • 37
    • 23444435977 scopus 로고
    • In vitro activation of urease apoprotein and role of UreD as a chaperone required for nickel metallocenter assembly
    • Park, I.S., Carr, M.B., Hausinger, R.P., 1994. In vitro activation of urease apoprotein and role of UreD as a chaperone required for nickel metallocenter assembly. Proc. Natl. Acad. Sci. USA 91, 3233-3237.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3233-3237
    • Park, I.S.1    Carr, M.B.2    Hausinger, R.P.3
  • 38
    • 1942502327 scopus 로고    scopus 로고
    • Genetic evidence for histidine kinase HP165 being an acid sensor of Helicobacter pylori
    • Pflock, M., Dietz, P., Shaer, J., Beier, D., 2004. Genetic evidence for histidine kinase HP165 being an acid sensor of Helicobacter pylori. FEMS Microbiol. Lett. 234, 51-61.
    • (2004) FEMS Microbiol. Lett. , vol.234 , pp. 51-61
    • Pflock, M.1    Dietz, P.2    Shaer, J.3    Beier, D.4
  • 40
    • 0031658740 scopus 로고    scopus 로고
    • Influence of pH on metabolism and urease activity of Helicobacter pylori
    • Rektorschek, M., Weeks, D., Sachs, G., Melchers, K., 1998. Influence of pH on metabolism and urease activity of Helicobacter pylori. Gastroenterology 115, 628-641.
    • (1998) Gastroenterology , vol.115 , pp. 628-641
    • Rektorschek, M.1    Weeks, D.2    Sachs, G.3    Melchers, K.4
  • 44
    • 0033958917 scopus 로고    scopus 로고
    • Expression of the Helicobacter pylori urel gene is required for acidic pH activation of cytoplasmic urease
    • Scott, D.R., Marcus, E.A., Weeks, D.L., Lee, A., Melchers, K., Sachs, G., 2000. Expression of the Helicobacter pylori urel gene is required for acidic pH activation of cytoplasmic urease. Infect. Immun. 68, 470-477.
    • (2000) Infect. Immun. , vol.68 , pp. 470-477
    • Scott, D.R.1    Marcus, E.A.2    Weeks, D.L.3    Lee, A.4    Melchers, K.5    Sachs, G.6
  • 45
    • 0036303568 scopus 로고    scopus 로고
    • Mechanisms of acid resistance due to the urease system of Helicobacter pylori
    • Scott, D.R., Marcus, E.A., Weeks, D.L., Sachs, G., 2002. Mechanisms of acid resistance due to the urease system of Helicobacter pylori. Gastroenterology 123, 187-195.
    • (2002) Gastroenterology , vol.123 , pp. 187-195
    • Scott, D.R.1    Marcus, E.A.2    Weeks, D.L.3    Sachs, G.4
  • 46
    • 0036037358 scopus 로고    scopus 로고
    • The Yersinia pseudotuberculosis Yut protein, a new type of urea transporter homologous to eukaryotic channels and functionally interchangeable with the Helicobacter pylori Urel protein
    • Sebbane, F., Bury-Moné, S., Cailliau, K., Browaeys-Poly, E., De Reuse, H., Simonet, M., 2002. The Yersinia pseudotuberculosis Yut protein, a new type of urea transporter homologous to eukaryotic channels and functionally interchangeable with the Helicobacter pylori Urel protein. Mol. Microbiol. 45, 1165-1174.
    • (2002) Mol. Microbiol. , vol.45 , pp. 1165-1174
    • Sebbane, F.1    Bury-Moné, S.2    Cailliau, K.3    Browaeys-Poly, E.4    De Reuse, H.5    Simonet, M.6
  • 48
    • 0032757429 scopus 로고    scopus 로고
    • Activation of Helicobacter pylori ureA promoter by a hybrid E. coli-H. pylori rpoD gene in E. coli
    • Shirai, M., Fujinaga, R., Akada, J.K., Nakazawa, T., 1999. Activation of Helicobacter pylori ureA promoter by a hybrid E. coli-H. pylori rpoD gene in E. coli. Gene 239, 351-359.
    • (1999) Gene , vol.239 , pp. 351-359
    • Shirai, M.1    Fujinaga, R.2    Akada, J.K.3    Nakazawa, T.4
  • 49
    • 0031661885 scopus 로고    scopus 로고
    • The Helicobacter pylori Urel protein is not involved in urease activity but is essential for bacterial survival in vivo
    • Skouloubris, S., Thiberge, J.-M., Labigne, A., De Reuse, H., 1998. The Helicobacter pylori Urel protein is not involved in urease activity but is essential for bacterial survival in vivo. Infect. Immun. 66, 4517-4521.
    • (1998) Infect. Immun. , vol.66 , pp. 4517-4521
    • Skouloubris, S.1    Thiberge, J.-M.2    Labigne, A.3    De Reuse, H.4
  • 50
    • 0029740061 scopus 로고    scopus 로고
    • Significance of ammonia in the genesis of gastric epithelial lesions induced by Helicobacter pylori: An in vitro study with different bacterial strains and urea concentrations
    • Sommi, P., Ricci, V., Fiocca, R., Romano, M., Ivey, K.J., Cova, E., Solcia, E., Ventura, U., 1996. Significance of ammonia in the genesis of gastric epithelial lesions induced by Helicobacter pylori: an in vitro study with different bacterial strains and urea concentrations. Digestion 57, 299-304.
    • (1996) Digestion , vol.57 , pp. 299-304
    • Sommi, P.1    Ricci, V.2    Fiocca, R.3    Romano, M.4    Ivey, K.J.5    Cova, E.6    Solcia, E.7    Ventura, U.8
  • 52
    • 0036468233 scopus 로고    scopus 로고
    • Acid survival of Helicobacter pylori: How does urease activity trigger cytoplasmic pH homeostasis?
    • Stingl, K., Altendorf, K., Bakker, E.P., 2002. Acid survival of Helicobacter pylori: how does urease activity trigger cytoplasmic pH homeostasis? Trends Microbiol. 10, 70-74.
    • (2002) Trends Microbiol. , vol.10 , pp. 70-74
    • Stingl, K.1    Altendorf, K.2    Bakker, E.P.3
  • 53
    • 0028052002 scopus 로고
    • Helicobacter pylori hspA-hspB heat-shock gene cluster: Nucleotide sequence, expression, putative function and immunogenicity
    • Suerbaum, S., Thiberge, J.-M., Kansau, I., Ferrero, R.L., Labigne, A., 1994. Helicobacter pylori hspA-hspB heat-shock gene cluster: nucleotide sequence, expression, putative function and immunogenicity. Mol. Microbiol. 14, 959-974.
    • (1994) Mol. Microbiol. , vol.14 , pp. 959-974
    • Suerbaum, S.1    Thiberge, J.-M.2    Kansau, I.3    Ferrero, R.L.4    Labigne, A.5
  • 54
    • 0024459370 scopus 로고
    • Competitive inhibitors of Klebsiella aerogenes urease. Mechanisms of interaction with the nickel active site
    • Todd, M.J., Hausinger, R.P., 1989. Competitive inhibitors of Klebsiella aerogenes urease. Mechanisms of interaction with the nickel active site. J. Biol. Chem. 264, 15835-15842.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15835-15842
    • Todd, M.J.1    Hausinger, R.P.2
  • 55
    • 0034836586 scopus 로고    scopus 로고
    • The Helicobacter pylori VacA toxin is a urea permease that promotes urea diffusion across epithelia
    • Tombola, F., Morbiato, L., Del Giudice, G., Rappuoli, R., Zoratti, M., Papini, E., 2001. The Helicobacter pylori VacA toxin is a urea permease that promotes urea diffusion across epithelia. J. Clin. Invest. 108, 929-937.
    • (2001) J. Clin. Invest. , vol.108 , pp. 929-937
    • Tombola, F.1    Morbiato, L.2    Del Giudice, G.3    Rappuoli, R.4    Zoratti, M.5    Papini, E.6
  • 58
    • 5644252852 scopus 로고    scopus 로고
    • NikR-mediated regulation of Helicobacter pylori acid adaptation
    • van Vliet, A.H., Ernst, F.D., Kusters, J.G., 2004a. NikR-mediated regulation of Helicobacter pylori acid adaptation. Trends Microbiol. 12, 489-494.
    • (2004) Trends Microbiol. , vol.12 , pp. 489-494
    • Van Vliet, A.H.1    Ernst, F.D.2    Kusters, J.G.3
  • 59
    • 0842305636 scopus 로고    scopus 로고
    • Acid-responsive gene induction of ammonia-producing enzymes in Helicobacter pylori is mediated via a metal-responsive represser cascade
    • van Vliet, A.H., Kuipers, E.J., Stoof, J., Poppelaars, S.W., Kusters, J.G., 2004b. Acid-responsive gene induction of ammonia-producing enzymes in Helicobacter pylori is mediated via a metal-responsive represser cascade. Infect. Immun. 72, 766-773.
    • (2004) Infect. Immun. , vol.72 , pp. 766-773
    • Van Vliet, A.H.1    Kuipers, E.J.2    Stoof, J.3    Poppelaars, S.W.4    Kusters, J.G.5
  • 61
    • 0034932504 scopus 로고    scopus 로고
    • Sites of pH regulation of the urea channel of Helicobacter pylori
    • Weeks, D.L., Sachs, G., 2001. Sites of pH regulation of the urea channel of Helicobacter pylori. Mol. Microbiol. 40, 1249-1259.
    • (2001) Mol. Microbiol. , vol.40 , pp. 1249-1259
    • Weeks, D.L.1    Sachs, G.2
  • 62
    • 0034695684 scopus 로고    scopus 로고
    • +-gated urea channel: The link between Helicobacter pylori urease and gastric colonization
    • +-gated urea channel: the link between Helicobacter pylori urease and gastric colonization. Science 287, 482-485.
    • (2000) Science , vol.287 , pp. 482-485
    • Weeks, D.L.1    Eskandari, S.2    Scott, D.R.3    Sachs, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.