메뉴 건너뛰기




Volumn 77, Issue 13, 2011, Pages 4318-4328

Environmental influences on competitive hydrogen peroxide production in Streptococcus gordonii

Author keywords

[No Author keywords available]

Indexed keywords

CARBON CATABOLITE REPRESSION; CATABOLITE CONTROL PROTEIN A; COMPETITIVE FITNESS; ELECTROPHORETIC MOBILITY SHIFT ASSAY; ENVIRONMENTAL INFLUENCES; HYDROGEN PEROXIDE PRODUCTION; MOLECULAR MECHANISM; ORAL CAVITY; OXYGEN TENSION; PHENOTYPIC TRAITS; PRODUCTION OF HYDROGEN; PYRUVATE OXIDASE; STREPTOCOCCUS GORDONII; STREPTOCOCCUS MUTANS;

EID: 79960084945     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.00309-11     Document Type: Article
Times cited : (47)

References (55)
  • 2
    • 70450260422 scopus 로고    scopus 로고
    • Influence of a model human defensive peroxidase system on oral streptococcal antagonism
    • Ashby, M. T., J. Kreth, M. Soundarajan, and L. S. Sivuilu. 2009. Influence of a model human defensive peroxidase system on oral streptococcal antagonism. Microbiology 155:3691-3700.
    • (2009) Microbiology , vol.155 , pp. 3691-3700
    • Ashby, M.T.1    Kreth, J.2    Soundarajan, M.3    Sivuilu, L.S.4
  • 3
    • 0032727137 scopus 로고    scopus 로고
    • Influence of environmental conditions on hydrogen peroxide formation by Streptococcus gordonii
    • Barnard, J. P., and M. W. Stinson. 1999. Influence of environmental conditions on hydrogen peroxide formation by Streptococcus gordonii. Infect. Immun. 67:6558-6564.
    • (1999) Infect. Immun. , vol.67 , pp. 6558-6564
    • Barnard, J.P.1    Stinson, M.W.2
  • 4
    • 0036197764 scopus 로고    scopus 로고
    • Molecular analysis of bacterial species associated with childhood caries
    • Becker, M. R., et al. 2002. Molecular analysis of bacterial species associated with childhood caries. J. Clin. Microbiol. 40:1001-1009.
    • (2002) J. Clin. Microbiol. , vol.40 , pp. 1001-1009
    • Becker, M.R.1
  • 5
    • 34249980190 scopus 로고    scopus 로고
    • Loss of penicillin tolerancetolerance by inactivating the carbon catabolite repression determinant CcpA in Streptococcus gordonii
    • Bizzini, A., J. M. Entenza, and P. Moreillon. 2007. Loss of penicillin tolerancetolerance by inactivating the carbon catabolite repression determinant CcpA in Streptococcus gordonii. J. Antimicrob. Chemother. 59:607-615.
    • (2007) J. Antimicrob. Chemother. , vol.59 , pp. 607-615
    • Bizzini, A.1    Entenza, J.M.2    Moreillon, P.3
  • 6
    • 0023302621 scopus 로고
    • Pyruvate oxidase in Streptococcus sanguis under various growth conditions
    • Carlsson, J., and M. B. Edlund. 1987. Pyruvate oxidase in Streptococcus sanguis under various growth conditions. Oral Microbiol. Immunol. 2:10-14.
    • (1987) Oral Microbiol. Immunol. , vol.2 , pp. 10-14
    • Carlsson, J.1    Edlund, M.B.2
  • 7
    • 0023300495 scopus 로고
    • Characteristics of a hydrogen peroxide-forming pyruvate oxidase from Streptococcus sanguis
    • Carlsson, J., M. B. Edlund, and S. K. Lundmark. 1987. Characteristics of a hydrogen peroxide-forming pyruvate oxidase from Streptococcus sanguis. Oral Microbiol. Immunol. 2:15-20.
    • (1987) Oral Microbiol. Immunol. , vol.2 , pp. 15-20
    • Carlsson, J.1    Edlund, M.B.2    Lundmark, S.K.3
  • 8
    • 0033946225 scopus 로고    scopus 로고
    • Natural history of Streptococcus sanguinis in the oral cavity of infants: evidence for a discrete window of infectivity
    • Caufield, P. W., et al. 2000. Natural history of Streptococcus sanguinis in the oral cavity of infants: evidence for a discrete window of infectivity. Infect. Immun. 68:4018-4023.
    • (2000) Infect. Immun. , vol.68 , pp. 4018-4023
    • Caufield, P.W.1
  • 10
    • 0028917215 scopus 로고
    • Protein kinase-dependent HPr/CcpA interaction links glycolytic activity to carbon catabolite repression in gram-positive bacteria
    • Deutscher, J., E. Kuster, U. Bergstedt, V. Charrier, and W. Hillen. 1995. Protein kinase-dependent HPr/CcpA interaction links glycolytic activity to carbon catabolite repression in gram-positive bacteria. Mol. Microbiol. 15: 1049-1053.
    • (1995) Mol. Microbiol. , vol.15 , pp. 1049-1053
    • Deutscher, J.1    Kuster, E.2    Bergstedt, U.3    Charrier, V.4    Hillen, W.5
  • 11
    • 79952085066 scopus 로고    scopus 로고
    • Extracellular DNA is abundant and important for microcolony strength in mixed microbial biofilms
    • Dominiak, D. M., J. L. Nielsen, and P. H. Nielsen. 2011. Extracellular DNA is abundant and important for microcolony strength in mixed microbial biofilms. Environ. Microbiol. 13:710-721.
    • (2011) Environ. Microbiol. , vol.13 , pp. 710-721
    • Dominiak, D.M.1    Nielsen, J.L.2    Nielsen, P.H.3
  • 12
    • 1842454273 scopus 로고    scopus 로고
    • Control of expression of the arginine deiminase operon of Streptococcus gordonii by CcpA and Flp
    • Dong, Y., Y. Y. Chen, and R. A. Burne. 2004. Control of expression of the arginine deiminase operon of Streptococcus gordonii by CcpA and Flp. J. Bacteriol. 186:2511-2514.
    • (2004) J. Bacteriol. , vol.186 , pp. 2511-2514
    • Dong, Y.1    Chen, Y.Y.2    Burne, R.A.3
  • 13
    • 0025893868 scopus 로고
    • Improved electroporation and cloning vector system for gram-positive bacteria
    • Dunny, G. M., L. N. Lee, and D. J. LeBlanc. 1991. Improved electroporation and cloning vector system for gram-positive bacteria. Appl. Environ. Microbiol. 57:1194-1201.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 1194-1201
    • Dunny, G.M.1    Lee, L.N.2    LeBlanc, D.J.3
  • 15
    • 0034708676 scopus 로고    scopus 로고
    • Salivary film expresses a complex, macromolecular binding site for Streptococcus sanguis
    • Gong, K., L. Mailloux, and M. C. Herzberg. 2000. Salivary film expresses a complex, macromolecular binding site for Streptococcus sanguis. J. Biol. Chem. 275:8970-8974.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8970-8974
    • Gong, K.1    Mailloux, L.2    Herzberg, M.C.3
  • 16
    • 47549110972 scopus 로고    scopus 로고
    • Carbon catabolite repression in bacteria: many ways to make the most out of nutrients
    • Görke, B., and J. Stulke. 2008. Carbon catabolite repression in bacteria: many ways to make the most out of nutrients. Nat. Rev. Microbiol. 6:613-624.
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 613-624
    • Görke, B.1    Stulke, J.2
  • 17
    • 0031557402 scopus 로고    scopus 로고
    • Cooperative and non-cooperative DNA binding modes of catabolite control protein CcpA from Bacillus megaterium result from sensing two different signals
    • Gösseringer, R., E. Kuster, A. Galinier, J. Deutscher, and W. Hillen. 1997. Cooperative and non-cooperative DNA binding modes of catabolite control protein CcpA from Bacillus megaterium result from sensing two different signals. J. Mol. Biol. 266:665-676.
    • (1997) J. Mol. Biol. , vol.266 , pp. 665-676
    • Gösseringer, R.1    Kuster, E.2    Galinier, A.3    Deutscher, J.4    Hillen, W.5
  • 18
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan, D. 1983. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166:557-580.
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 19
    • 28844482813 scopus 로고    scopus 로고
    • Catabolite control protein A (CcpA) contributes to virulence and regulation of sugar metabolism in Streptococcus pneumoniae
    • Iyer, R., N. S. Baliga, and A. Camilli. 2005. Catabolite control protein A (CcpA) contributes to virulence and regulation of sugar metabolism in Streptococcus pneumoniae. J. Bacteriol. 187:8340-8349.
    • (2005) J. Bacteriol. , vol.187 , pp. 8340-8349
    • Iyer, R.1    Baliga, N.S.2    Camilli, A.3
  • 20
    • 76149138468 scopus 로고    scopus 로고
    • Talk of the town: interspecies communication in oral biofilms
    • Jakubovics, N. S. 2010. Talk of the town: interspecies communication in oral biofilms. Mol. Oral Microbiol. 25:4-14.
    • (2010) Mol. Oral Microbiol. , vol.25 , pp. 4-14
    • Jakubovics, N.S.1
  • 21
    • 47049083063 scopus 로고    scopus 로고
    • Regulation of gene expression in a mixed-genus community: stabilized arginine biosynthesis in Streptococcus gordonii by coaggregation with Actinomyces naeslundii
    • Jakubovics, N. S., S. R. Gill, S. E. Iobst, M. M. Vickerman, and P. E. Kolenbrander. 2008. Regulation of gene expression in a mixed-genus community: stabilized arginine biosynthesis in Streptococcus gordonii by coaggregation with Actinomyces naeslundii. J. Bacteriol. 190:3646-3657.
    • (2008) J. Bacteriol. , vol.190 , pp. 3646-3657
    • Jakubovics, N.S.1    Gill, S.R.2    Iobst, S.E.3    Vickerman, M.M.4    Kolenbrander, P.E.5
  • 22
    • 55949111668 scopus 로고    scopus 로고
    • Role of hydrogen peroxide in competition and cooperation between Streptococcus gordonii and Actinomyces naeslundii
    • Jakubovics, N. S., S. R. Gill, M. M. Vickerman, and P. E. Kolenbrander. 2008. Role of hydrogen peroxide in competition and cooperation between Streptococcus gordonii and Actinomyces naeslundii. FEMS Microbiol. Ecol. 66:637-644.
    • (2008) FEMS Microbiol. Ecol. , vol.66 , pp. 637-644
    • Jakubovics, N.S.1    Gill, S.R.2    Vickerman, M.M.3    Kolenbrander, P.E.4
  • 23
    • 68949151884 scopus 로고    scopus 로고
    • Interspecies signaling between Veillonella atypica and Streptococcus gordonii requires the transcription factor CcpA
    • Johnson, B. P., et al. 2009. Interspecies signaling between Veillonella atypica and Streptococcus gordonii requires the transcription factor CcpA. J. Bacteriol. 191:5563-5565.
    • (2009) J. Bacteriol. , vol.191 , pp. 5563-5565
    • Johnson, B.P.1
  • 24
    • 0030725260 scopus 로고    scopus 로고
    • Binding of the catabolite repressor protein CcpA to its DNA target is regulated by phosphorylation of its corepressor HPr
    • Jones, B. E., et al. 1997. Binding of the catabolite repressor protein CcpA to its DNA target is regulated by phosphorylation of its corepressor HPr. J. Biol. Chem. 272:26530-26535.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26530-26535
    • Jones, B.E.1
  • 25
    • 0029092003 scopus 로고
    • Specificity of DNA binding activity of the Bacillus subtilis catabolite control protein CcpA
    • Kim, J. H., Z. T. Guvener, J. Y. Cho, K. C. Chung, and G. H. Chambliss. 1995. Specificity of DNA binding activity of the Bacillus subtilis catabolite control protein CcpA. J. Bacteriol. 177:5129-5134.
    • (1995) J. Bacteriol. , vol.177 , pp. 5129-5134
    • Kim, J.H.1    Guvener, Z.T.2    Cho, J.Y.3    Chung, K.C.4    Chambliss, G.H.5
  • 26
    • 16244392719 scopus 로고    scopus 로고
    • Evidence that Bacillus catabolite control protein CcpA interacts with RNA polymerase to inhibit transcription
    • Kim, J. H., Y. K. Yang, and G. H. Chambliss. 2005. Evidence that Bacillus catabolite control protein CcpA interacts with RNA polymerase to inhibit transcription. Mol. Microbiol. 56:155-162.
    • (2005) Mol. Microbiol. , vol.56 , pp. 155-162
    • Kim, J.H.1    Yang, Y.K.2    Chambliss, G.H.3
  • 27
    • 78149425398 scopus 로고    scopus 로고
    • Dynamics of Streptococcus mutans transcriptome in response to starch and sucrose during biofilm development
    • Klein, M. I., et al. 2010. Dynamics of Streptococcus mutans transcriptome in response to starch and sucrose during biofilm development. PLoS One 5:e13478.
    • (2010) PLoS One , vol.5
    • Klein, M.I.1
  • 28
    • 33747870432 scopus 로고    scopus 로고
    • Bacterial interactions and successions during plaque development
    • Kolenbrander, P. E., et al. 2006. Bacterial interactions and successions during plaque development. Periodontol. 2000 42:47-79.
    • (2006) Periodontol , vol.2000 , pp. 47-79
    • Kolenbrander, P.E.1
  • 29
    • 70249149327 scopus 로고    scopus 로고
    • Bacterial and host interactions of oral streptococci
    • Kreth, J., J. Merritt, and F. Qi. 2009. Bacterial and host interactions of oral streptococci. DNA Cell Biol. 28:397-403.
    • (2009) DNA Cell Biol , vol.28 , pp. 397-403
    • Kreth, J.1    Merritt, J.2    Qi, F.3
  • 30
    • 27144509129 scopus 로고    scopus 로고
    • Competition and coexistence between Streptococcus mutans and Streptococcus sanguinis in the dental biofilm
    • Kreth, J., J. Merritt, W. Shi, and F. Qi. 2005. Competition and coexistence between Streptococcus mutans and Streptococcus sanguinis in the dental biofilm. J. Bacteriol. 187:7193-7203.
    • (2005) J. Bacteriol. , vol.187 , pp. 7193-7203
    • Kreth, J.1    Merritt, J.2    Shi, W.3    Qi, F.4
  • 31
    • 70350462733 scopus 로고    scopus 로고
    • Characterization of hydrogen peroxide-induced DNA release by Streptococcus sanguinis and Streptococcus gordonii
    • Kreth, J., H. Vu, Y. Zhang, and M. C. Herzberg. 2009. Characterization of hydrogen peroxide-induced DNA release by Streptococcus sanguinis and Streptococcus gordonii. J. Bacteriol. 191:6281-6291.
    • (2009) J. Bacteriol. , vol.191 , pp. 6281-6291
    • Kreth, J.1    Vu, H.2    Zhang, Y.3    Herzberg, M.C.4
  • 32
    • 46049097957 scopus 로고    scopus 로고
    • Streptococcal antagonism in oral biofilms: Streptococcus sanguinis and Streptococcus gordonii interference with Streptococcus mutans
    • Kreth, J., Y. Zhang, and M. C. Herzberg. 2008. Streptococcal antagonism in oral biofilms: Streptococcus sanguinis and Streptococcus gordonii interference with Streptococcus mutans. J. Bacteriol. 190:4632-4640.
    • (2008) J. Bacteriol. , vol.190 , pp. 4632-4640
    • Kreth, J.1    Zhang, Y.2    Herzberg, M.C.3
  • 33
    • 0031927314 scopus 로고    scopus 로고
    • Generation ofbioluminescent Streptococcus mutans and its usage in rapid analysis of the efficacy of antimicrobial compounds
    • Loimaranta, V., J. Tenovuo, L. Koivisto, and M. Karp. 1998. Generation ofbioluminescent Streptococcus mutans and its usage in rapid analysis of the efficacy of antimicrobial compounds. Antimicrob. Agents Chemother. 42: 1906-1910.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 1906-1910
    • Loimaranta, V.1    Tenovuo, J.2    Koivisto, L.3    Karp, M.4
  • 34
    • 0023445601 scopus 로고
    • Constitutive expression of erythromycin resistance mediated by the ermAM determinant of plasmid pAMβ1 results from deletion of 5' leader peptide sequences
    • Martin, B., G. Alloing, V. Mejean, and J. P. Claverys. 1987. Constitutive expression of erythromycin resistance mediated by the ermAM determinant of plasmid pAMβ1 results from deletion of 5' leader peptide sequences. Plasmid 18:250-253.
    • (1987) Plasmid , vol.18 , pp. 250-253
    • Martin, B.1    Alloing, G.2    Mejean, V.3    Claverys, J.P.4
  • 35
    • 0023663369 scopus 로고
    • T7 lysozyme inhibits transcription by T7 RNA polymerase
    • Moffatt, B. A., and F. W. Studier. 1987. T7 lysozyme inhibits transcription by T7 RNA polymerase. Cell 49:221-227.
    • (1987) Cell , vol.49 , pp. 221-227
    • Moffatt, B.A.1    Studier, F.W.2
  • 37
    • 75549086541 scopus 로고    scopus 로고
    • RegPrecise: a database of curated genomic inferences of transcriptional regulatory interactions in prokaryotes
    • Novichkov, P. S., et al. 2010. RegPrecise: a database of curated genomic inferences of transcriptional regulatory interactions in prokaryotes. Nucleic Acids Res. 38:D111-D118.
    • (2010) Nucleic Acids Res , vol.38
    • Novichkov, P.S.1
  • 38
    • 77951962327 scopus 로고    scopus 로고
    • Examination of the hdrRM regulon yields insight into the competence system of Streptococcus mutans
    • Okinaga, T., Z. Xie, G. Niu, F. Qi, and J. Merritt. 2010. Examination of the hdrRM regulon yields insight into the competence system of Streptococcus mutans. Mol. Oral Microbiol. 25:165-177.
    • (2010) Mol. Oral Microbiol. , vol.25 , pp. 165-177
    • Okinaga, T.1    Xie, Z.2    Niu, G.3    Qi, F.4    Merritt, J.5
  • 39
    • 0001255656 scopus 로고
    • On the nature of competence of transformable streptococci
    • Pakula, R., and W. Walczak. 1963. On the nature of competence of transformable streptococci. J. Gen. Microbiol. 31:125-133.
    • (1963) J. Gen. Microbiol. , vol.31 , pp. 125-133
    • Pakula, R.1    Walczak, W.2
  • 40
    • 0030600488 scopus 로고    scopus 로고
    • Novel series of plasmid vectors for gene inactivation and expression analysis in group A streptococci (GAS)
    • Podbielski, A., B. Spellerberg, M. Woischnik, B. Pohl, and R. Lutticken. 1996. Novel series of plasmid vectors for gene inactivation and expression analysis in group A streptococci (GAS). Gene 177:137-147.
    • (1996) Gene , vol.177 , pp. 137-147
    • Podbielski, A.1    Spellerberg, B.2    Woischnik, M.3    Pohl, B.4    Lutticken, R.5
  • 41
    • 3843072089 scopus 로고    scopus 로고
    • Association between carriage of Streptococcus pneumoniae and Staphylococcus aureus in children
    • Regev-Yochay, G., et al. 2004. Association between carriage of Streptococcus pneumoniae and Staphylococcus aureus in children. JAMA 292:716-720.
    • (2004) JAMA , vol.292 , pp. 716-720
    • Regev-Yochay, G.1
  • 42
    • 33745460121 scopus 로고    scopus 로고
    • Interference between Streptococcus pneumoniae and Staphylococcus aureus: in vitro hydrogen peroxide-mediated killing by Streptococcus pneumoniae
    • Regev-Yochay, G., K. Trzcinski, C. M. Thompson, R. Malley, and M. Lipsitch. 2006. Interference between Streptococcus pneumoniae and Staphylococcus aureus: in vitro hydrogen peroxide-mediated killing by Streptococcus pneumoniae. J. Bacteriol. 188:4996-5001.
    • (2006) J. Bacteriol. , vol.188 , pp. 4996-5001
    • Regev-Yochay, G.1    Trzcinski, K.2    Thompson, C.M.3    Malley, R.4    Lipsitch, M.5
  • 43
    • 0035026476 scopus 로고    scopus 로고
    • RegG, a CcpA homolog, participates in regulation of amylase-binding protein A gene (abpA) expression in Streptococcus gordonii
    • Rogers, J. D., and F. A. Scannapieco. 2001. RegG, a CcpA homolog, participates in regulation of amylase-binding protein A gene (abpA) expression in Streptococcus gordonii. J. Bacteriol. 183:3521-3525.
    • (2001) J. Bacteriol. , vol.183 , pp. 3521-3525
    • Rogers, J.D.1    Scannapieco, F.A.2
  • 44
    • 0033694722 scopus 로고    scopus 로고
    • Dental plaque formation
    • Rosan, B., and R. J. Lamont. 2000. Dental plaque formation. Microbes Infect. 2:1599-1607.
    • (2000) Microbes Infect , vol.2 , pp. 1599-1607
    • Rosan, B.1    Lamont, R.J.2
  • 45
    • 0029353108 scopus 로고
    • Bacteria in human mouths involved in the production and utilization of hydrogen peroxide
    • Ryan, C. S., and I. Kleinberg. 1995. Bacteria in human mouths involved in the production and utilization of hydrogen peroxide. Arch. Oral Biol. 40: 753-763.
    • (1995) Arch. Oral Biol. , vol.40 , pp. 753-763
    • Ryan, C.S.1    Kleinberg, I.2
  • 46
    • 34548864382 scopus 로고    scopus 로고
    • A novel agar medium to detect hydrogen peroxide-producing bacteria based on the Prussian blue-forming reaction
    • Saito, M., M. Seki, K. Iida, H. Nakayama, and S. Yoshida. 2007. A novel agar medium to detect hydrogen peroxide-producing bacteria based on the Prussian blue-forming reaction. Microbiol. Immunol. 51:889-892.
    • (2007) Microbiol. Immunol. , vol.51 , pp. 889-892
    • Saito, M.1    Seki, M.2    Iida, K.3    Nakayama, H.4    Yoshida, S.5
  • 47
    • 59049089396 scopus 로고    scopus 로고
    • Killing niche competitors by remote-control bacteriophage induction
    • Selva, L., et al. 2009. Killing niche competitors by remote-control bacteriophage induction. Proc. Natl. Acad. Sci. U. S. A. 106:1234-1238.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 1234-1238
    • Selva, L.1
  • 48
    • 0030029521 scopus 로고    scopus 로고
    • Pyruvate oxidase, as a determinant of virulence in Streptococcus pneumoniae
    • Spellerberg, B., et al. 1996. Pyruvate oxidase, as a determinant of virulence in Streptococcus pneumoniae. Mol. Microbiol. 19:803-813.
    • (1996) Mol. Microbiol. , vol.19 , pp. 803-813
    • Spellerberg, B.1
  • 49
    • 79953251969 scopus 로고    scopus 로고
    • The EIIABMan phosphotransferase system permease regulates carbohydrate catabolite repression in Streptococcus gordonii
    • Tong, H., L. Zeng, and R. A. Burne. 2011. The EIIABMan phosphotransferase system permease regulates carbohydrate catabolite repression in Streptococcus gordonii. Appl. Environ. Microbiol. 77:1957-1965.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 1957-1965
    • Tong, H.1    Zeng, L.2    Burne, R.A.3
  • 50
    • 0020604683 scopus 로고
    • Nucleotide sequence of the Streptococcus faecalis plasmid gene encoding the 3'5''-aminoglycoside phosphotransferase type III
    • Trieu-Cuot, P., and P. Courvalin. 1983. Nucleotide sequence of the Streptococcus faecalis plasmid gene encoding the 3'5''-aminoglycoside phosphotransferase type III. Gene 23:331-341.
    • (1983) Gene , vol.23 , pp. 331-341
    • Trieu-Cuot, P.1    Courvalin, P.2
  • 51
    • 0348109341 scopus 로고    scopus 로고
    • CcpA-dependent carbon catabolite repression in bacteria
    • Warner, J. B., and J. S. Lolkema. 2003. CcpA-dependent carbon catabolite repression in bacteria. Microbiol. Mol. Biol. Rev. 67:475-490.
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 475-490
    • Warner, J.B.1    Lolkema, J.S.2
  • 52
    • 77949914858 scopus 로고    scopus 로고
    • Physiologically relevant small phosphodonors link metabolism to signal transduction
    • Wolfe, A. J. 2010. Physiologically relevant small phosphodonors link metabolism to signal transduction. Curr. Opin. Microbiol. 13:204-209.
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 204-209
    • Wolfe, A.J.1
  • 53
    • 77349124258 scopus 로고    scopus 로고
    • Seryl-phosphorylated HPr regulates CcpAindependent carbon catabolite repression in conjunction with PTS permeases in Streptococcus mutans
    • Zeng, L., and R. A. Burne. 2010. Seryl-phosphorylated HPr regulates CcpAindependent carbon catabolite repression in conjunction with PTS permeases in Streptococcus mutans. Mol. Microbiol. 75:1145-1158.
    • (2010) Mol. Microbiol. , vol.75 , pp. 1145-1158
    • Zeng, L.1    Burne, R.A.2
  • 54
    • 77951061673 scopus 로고    scopus 로고
    • Utilization of lactose and galactose by Streptococcus mutans: transport, toxicity, and carbon catabolite repression
    • Zeng, L., S. Das, and R. A. Burne. 2010. Utilization of lactose and galactose by Streptococcus mutans: transport, toxicity, and carbon catabolite repression. J. Bacteriol. 192:2434-2444.
    • (2010) J. Bacteriol. , vol.192 , pp. 2434-2444
    • Zeng, L.1    Das, S.2    Burne, R.A.3
  • 55
    • 78650856199 scopus 로고    scopus 로고
    • Catabolite control protein A controls hydrogen peroxide production and cell death in Streptococcus sanguinis
    • Zheng, L., Z. Chen, A. Itzek, M. Ashby, and J. Kreth. 2011. Catabolite control protein A controls hydrogen peroxide production and cell death in Streptococcus sanguinis. J. Bacteriol. 193:516-526
    • (2011) J. Bacteriol. , vol.193 , pp. 516-526
    • Zheng, L.1    Chen, Z.2    Itzek, A.3    Ashby, M.4    Kreth, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.