메뉴 건너뛰기




Volumn 85, Issue 2, 2012, Pages 361-377

Role of DNA base excision repair in the mutability and virulence of Streptococcus mutans

Author keywords

[No Author keywords available]

Indexed keywords

2 AMINOPURINE; 7,8 DIHYDRO 8 OXO 2' DEOXYGUANINE; DNA FORMAMIDOPYRIMIDINE GLYCOSYLASE; DNA GLYCOSYLASE MUTY; ENDONUCLEASE; ENDONUCLEASE SMN; ENDONUCLEASE SMX; UNCLASSIFIED DRUG;

EID: 84863590936     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2012.08116.x     Document Type: Article
Times cited : (20)

References (81)
  • 1
    • 19944405112 scopus 로고    scopus 로고
    • Diversify or die: generation of diversity in response to stress
    • Aertsen, A., and Michiels, C.W. (2005) Diversify or die: generation of diversity in response to stress. Crit Rev Microbiol 31: 69-78.
    • (2005) Crit Rev Microbiol , vol.31 , pp. 69-78
    • Aertsen, A.1    Michiels, C.W.2
  • 3
    • 0022467287 scopus 로고
    • Cloning of a Streptococcus mutans glucosyltransferase gene coding for insoluble glucan synthesis
    • Aoki, H., Shiroza, T., Hayakawa, M., Sato, S., and Kuramitsu, H.K. (1986) Cloning of a Streptococcus mutans glucosyltransferase gene coding for insoluble glucan synthesis. Infect Immun 53: 587-594.
    • (1986) Infect Immun , vol.53 , pp. 587-594
    • Aoki, H.1    Shiroza, T.2    Hayakawa, M.3    Sato, S.4    Kuramitsu, H.K.5
  • 4
    • 34247547098 scopus 로고    scopus 로고
    • Galleria mellonella as a model host to study infection by the Francisella tularensis live vaccine strain
    • Aperis, G., Fuchs, B.B., Anderson, C.A., Warner, J.E., Calderwood, S.B., and Mylonakis, E. (2007) Galleria mellonella as a model host to study infection by the Francisella tularensis live vaccine strain. Microbes Infect 9: 729-734.
    • (2007) Microbes Infect , vol.9 , pp. 729-734
    • Aperis, G.1    Fuchs, B.B.2    Anderson, C.A.3    Warner, J.E.4    Calderwood, S.B.5    Mylonakis, E.6
  • 6
    • 2442715491 scopus 로고    scopus 로고
    • Virulence properties of Streptococcus mutans
    • Banas, J.A. (2004) Virulence properties of Streptococcus mutans. Front Biosci 9: 1267-1277.
    • (2004) Front Biosci , vol.9 , pp. 1267-1277
    • Banas, J.A.1
  • 7
    • 0029347105 scopus 로고
    • Structure and function of apurinic/apyrimidinic endonucleases
    • Barzilay, G., and Hickson, I.D. (1995) Structure and function of apurinic/apyrimidinic endonucleases. Bioessays 17: 713-719.
    • (1995) Bioessays , vol.17 , pp. 713-719
    • Barzilay, G.1    Hickson, I.D.2
  • 9
    • 21544481993 scopus 로고    scopus 로고
    • Superoxide production in Galleria mellonella hemocytes: identification of proteins homologous to the NADPH oxidase complex of human neutrophils
    • Bergin, D., Reeves, E., Renwick, J., Wientjes, F.B., and Kavanagh, K. (2005) Superoxide production in Galleria mellonella hemocytes: identification of proteins homologous to the NADPH oxidase complex of human neutrophils. Infect Immun 73: 4161-4170.
    • (2005) Infect Immun , vol.73 , pp. 4161-4170
    • Bergin, D.1    Reeves, E.2    Renwick, J.3    Wientjes, F.B.4    Kavanagh, K.5
  • 10
    • 0344586043 scopus 로고    scopus 로고
    • Mutagenicity, toxicity and repair of DNA base damage induced by oxidation
    • Bjelland, S., and Seeberg, E. (2003) Mutagenicity, toxicity and repair of DNA base damage induced by oxidation. Mutat Res 531: 37-80.
    • (2003) Mutat Res , vol.531 , pp. 37-80
    • Bjelland, S.1    Seeberg, E.2
  • 12
    • 0032716383 scopus 로고    scopus 로고
    • Base excision repair of 8-hydroxyguanine protects DNA from endogenous oxidative stress
    • Boiteux, S., and Radicella, J. (1999) Base excision repair of 8-hydroxyguanine protects DNA from endogenous oxidative stress. Biochimie 81: 59-67.
    • (1999) Biochimie , vol.81 , pp. 59-67
    • Boiteux, S.1    Radicella, J.2
  • 14
    • 0038799736 scopus 로고    scopus 로고
    • Oxidative DNA damage: mechanisms, mutation, and disease
    • Cooke, M.S., Evans, M.D., Dizdaroglu, M., and Lunec, J. (2003) Oxidative DNA damage: mechanisms, mutation, and disease. FASEB J 17: 1195-1214.
    • (2003) FASEB J , vol.17 , pp. 1195-1214
    • Cooke, M.S.1    Evans, M.D.2    Dizdaroglu, M.3    Lunec, J.4
  • 16
    • 34250900982 scopus 로고    scopus 로고
    • Base-excision repair of oxidative DNA damage
    • David, S.S., O'Shea, V.L., and Kundu, S. (2007) Base-excision repair of oxidative DNA damage. Nature 447: 941-950.
    • (2007) Nature , vol.447 , pp. 941-950
    • David, S.S.1    O'Shea, V.L.2    Kundu, S.3
  • 17
    • 16844383753 scopus 로고    scopus 로고
    • Antimutator role of DNA glycosylase MutY in pathogenic Neisseria species
    • Davidsen, T., Bjoras, M., Seeberg, E.C., and Tonjum, T. (2005) Antimutator role of DNA glycosylase MutY in pathogenic Neisseria species. J Bacteriol 187: 2801-2809.
    • (2005) J Bacteriol , vol.187 , pp. 2801-2809
    • Davidsen, T.1    Bjoras, M.2    Seeberg, E.C.3    Tonjum, T.4
  • 18
    • 34547622127 scopus 로고    scopus 로고
    • Genetic interactions of DNA repair pathways in the pathogen Neisseria meningitidis
    • Davidsen, T., Tuven, H.K., Bjoras, M., Rodland, E.A., and Tonjum, T. (2007) Genetic interactions of DNA repair pathways in the pathogen Neisseria meningitidis. J Bacteriol 189: 5728-5737.
    • (2007) J Bacteriol , vol.189 , pp. 5728-5737
    • Davidsen, T.1    Tuven, H.K.2    Bjoras, M.3    Rodland, E.A.4    Tonjum, T.5
  • 19
    • 0020693158 scopus 로고
    • Escherichia coli xth mutants are hypersensitive to hydrogen peroxide
    • Demple, B., Halbrook, J., and Linn, S. (1983) Escherichia coli xth mutants are hypersensitive to hydrogen peroxide. J Bacteriol 153: 1079-1082.
    • (1983) J Bacteriol , vol.153 , pp. 1079-1082
    • Demple, B.1    Halbrook, J.2    Linn, S.3
  • 20
    • 0343319790 scopus 로고
    • Exonuclease III and endonuclease IV remove 3′ blocks from DNA synthesis primers in H2O2-damaged Escherichia coli
    • Demple, B., Johnson, A., and Fung, D. (1986) Exonuclease III and endonuclease IV remove 3′ blocks from DNA synthesis primers in H2O2-damaged Escherichia coli. Proc Natl Acad Sci USA 83: 7731-7735.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 7731-7735
    • Demple, B.1    Johnson, A.2    Fung, D.3
  • 21
    • 33646397599 scopus 로고    scopus 로고
    • Evolution of mutation rates in bacteria
    • Denamur, E., and Matic, I. (2006) Evolution of mutation rates in bacteria. Mol Microbiol 60: 820-827.
    • (2006) Mol Microbiol , vol.60 , pp. 820-827
    • Denamur, E.1    Matic, I.2
  • 22
    • 84857089809 scopus 로고    scopus 로고
    • Mutation of NADH oxidase (nox) reveals an overlap of the oxygen- and acid-mediated stress responses in Streptococcus mutans
    • Derr, A.D., Faustoferri, R.C., Betzenhauser, M.J., Gonzalez, K., Marquis, R.E., and Quivey, R.G., Jr (2012) Mutation of NADH oxidase (nox) reveals an overlap of the oxygen- and acid-mediated stress responses in Streptococcus mutans. Appl Environ Microbiol 78: 1215-1227.
    • (2012) Appl Environ Microbiol , vol.78 , pp. 1215-1227
    • Derr, A.D.1    Faustoferri, R.C.2    Betzenhauser, M.J.3    Gonzalez, K.4    Marquis, R.E.5    Quivey Jr., R.G.6
  • 23
    • 0345448169 scopus 로고    scopus 로고
    • Substrate specificities and excision kinetics of DNA glycosylases involved in base-excision repair of oxidative DNA damage
    • Dizdaroglu, M. (2003) Substrate specificities and excision kinetics of DNA glycosylases involved in base-excision repair of oxidative DNA damage. Mutat Res 531: 109-126.
    • (2003) Mutat Res , vol.531 , pp. 109-126
    • Dizdaroglu, M.1
  • 24
    • 16844368560 scopus 로고    scopus 로고
    • Smx nuclease is the major, low-pH-inducible apurinic/apyrimidinic endonuclease in Streptococcus mutans
    • Faustoferri, R.C., Hahn, K., Weiss, K., and Quivey, R.G. (2005) Smx nuclease is the major, low-pH-inducible apurinic/apyrimidinic endonuclease in Streptococcus mutans. J Bacteriol 187: 2705-2714.
    • (2005) J Bacteriol , vol.187 , pp. 2705-2714
    • Faustoferri, R.C.1    Hahn, K.2    Weiss, K.3    Quivey, R.G.4
  • 25
    • 0037415388 scopus 로고    scopus 로고
    • Interactions among the Escherichia coli mutT, mutM, and mutY damage prevention pathways
    • Fowler, R.G., White, S.J., Koyama, C., Moore, S.C., Dunn, R.L., and Schaaper, R.M. (2003) Interactions among the Escherichia coli mutT, mutM, and mutY damage prevention pathways. DNA Repair (Amst) 2: 159-173.
    • (2003) DNA Repair (Amst) , vol.2 , pp. 159-173
    • Fowler, R.G.1    White, S.J.2    Koyama, C.3    Moore, S.C.4    Dunn, R.L.5    Schaaper, R.M.6
  • 26
    • 0036294464 scopus 로고    scopus 로고
    • Structural insights into lesion recognition and repair by the bacterial 8-oxoguanine DNA glycosylase MutM
    • Fromme, J.C., and Verdine, G.L. (2002) Structural insights into lesion recognition and repair by the bacterial 8-oxoguanine DNA glycosylase MutM. Nat Struct Biol 9: 544-552.
    • (2002) Nat Struct Biol , vol.9 , pp. 544-552
    • Fromme, J.C.1    Verdine, G.L.2
  • 27
    • 0034075816 scopus 로고    scopus 로고
    • Repair of DNA lesions induced by hydrogen peroxide in the presence of iron chelators in Escherichia coli: participation of endonuclease IV and Fpg
    • Galhardo, R.S., Almeida, C.E., Leitao, A.C., and Cabral-Neto, J.B. (2000) Repair of DNA lesions induced by hydrogen peroxide in the presence of iron chelators in Escherichia coli: participation of endonuclease IV and Fpg. J Bacteriol 182: 1964-1968.
    • (2000) J Bacteriol , vol.182 , pp. 1964-1968
    • Galhardo, R.S.1    Almeida, C.E.2    Leitao, A.C.3    Cabral-Neto, J.B.4
  • 28
    • 0014945242 scopus 로고
    • Fitness of an Escherichia coli mutator gene
    • Gibson, T.C., Scheppe, M.L., and Cox, E.C. (1970) Fitness of an Escherichia coli mutator gene. Science 169: 686-688.
    • (1970) Science , vol.169 , pp. 686-688
    • Gibson, T.C.1    Scheppe, M.L.2    Cox, E.C.3
  • 30
    • 0029095707 scopus 로고
    • Platelet receptors for the Streptococcus sanguis adhesin and aggregation-associated antigens are distinguished by anti-idiotypical monoclonal antibodies
    • Gong, K., Wen, D.Y., Ouyang, T., Rao, A.T., and Herzberg, M.C. (1995) Platelet receptors for the Streptococcus sanguis adhesin and aggregation-associated antigens are distinguished by anti-idiotypical monoclonal antibodies. Infect Immun 63: 3628-3633.
    • (1995) Infect Immun , vol.63 , pp. 3628-3633
    • Gong, K.1    Wen, D.Y.2    Ouyang, T.3    Rao, A.T.4    Herzberg, M.C.5
  • 31
    • 0027324378 scopus 로고
    • Mutagenesis by 8-oxoguanine: an enemy within
    • Grollman, A.P., and Moriya, M. (1993) Mutagenesis by 8-oxoguanine: an enemy within. Trends Genet 9: 246-249.
    • (1993) Trends Genet , vol.9 , pp. 246-249
    • Grollman, A.P.1    Moriya, M.2
  • 32
    • 0037115912 scopus 로고    scopus 로고
    • Enzymology of the repair of free radicals-induced DNA damage
    • Gros, L., Saparbaev, M.K., and Laval, J. (2002) Enzymology of the repair of free radicals-induced DNA damage. Oncogene 21: 8905-8925.
    • (2002) Oncogene , vol.21 , pp. 8905-8925
    • Gros, L.1    Saparbaev, M.K.2    Laval, J.3
  • 33
    • 0033014540 scopus 로고    scopus 로고
    • Induction of an AP endonuclease activity in Streptococcus mutans during growth at low pH
    • Hahn, K., Faustoferri, R.C., and Quivey, R.G., Jr (1999) Induction of an AP endonuclease activity in Streptococcus mutans during growth at low pH. Mol Microbiol 31: 1489-1498.
    • (1999) Mol Microbiol , vol.31 , pp. 1489-1498
    • Hahn, K.1    Faustoferri, R.C.2    Quivey Jr., R.G.3
  • 34
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension
    • Horton, R.M., Hunt, H.D., Ho, S.N., Pullen, J.K., and Pease, L.R. (1989) Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene 77: 61-68.
    • (1989) Gene , vol.77 , pp. 61-68
    • Horton, R.M.1    Hunt, H.D.2    Ho, S.N.3    Pullen, J.K.4    Pease, L.R.5
  • 35
    • 0027729359 scopus 로고
    • DNA polymerase-catalyzed addition of nontemplated extra nucleotides to the 3′ end of a DNA fragment
    • Hu, G. (1993) DNA polymerase-catalyzed addition of nontemplated extra nucleotides to the 3′ end of a DNA fragment. DNA Cell Biol 12: 763-770.
    • (1993) DNA Cell Biol , vol.12 , pp. 763-770
    • Hu, G.1
  • 36
    • 33749030720 scopus 로고    scopus 로고
    • Antimutator role of the DNA glycosylase mutY gene in Helicobacter pylori
    • Huang, S., Kang, J., and Blaser, M.J. (2006) Antimutator role of the DNA glycosylase mutY gene in Helicobacter pylori. J Bacteriol 188: 6224-6234.
    • (2006) J Bacteriol , vol.188 , pp. 6224-6234
    • Huang, S.1    Kang, J.2    Blaser, M.J.3
  • 37
    • 0015719182 scopus 로고
    • Transformability of group H Streptococcus challis. II. Transformation of hemolytic activity and competence-provoking factor nonproducibility
    • Ito, T., Hirano, T., Tomura, T., and Yoshioka, M. (1973) Transformability of group H Streptococcus challis. II. Transformation of hemolytic activity and competence-provoking factor nonproducibility. Jpn J Microbiol 17: 439-444.
    • (1973) Jpn J Microbiol , vol.17 , pp. 439-444
    • Ito, T.1    Hirano, T.2    Tomura, T.3    Yoshioka, M.4
  • 38
    • 35748939666 scopus 로고    scopus 로고
    • A distinct role of formamidopyrimidine DNA glycosylase (MutM) in down-regulation of accumulation of G, C mutations and protection against oxidative stress in mycobacteria
    • Jain, R., Kumar, P., and Varshney, U. (2007) A distinct role of formamidopyrimidine DNA glycosylase (MutM) in down-regulation of accumulation of G, C mutations and protection against oxidative stress in mycobacteria. DNA Repair (Amst) 6: 1774-1785.
    • (2007) DNA Repair (Amst) , vol.6 , pp. 1774-1785
    • Jain, R.1    Kumar, P.2    Varshney, U.3
  • 39
    • 73949101830 scopus 로고    scopus 로고
    • Mutators and hypermutability in bacteria: the Escherichia coli paradigm
    • Jayaraman, R. (2009) Mutators and hypermutability in bacteria: the Escherichia coli paradigm. J Genet 88: 379-391.
    • (2009) J Genet , vol.88 , pp. 379-391
    • Jayaraman, R.1
  • 40
    • 0020842025 scopus 로고
    • Plaque pH measurements by different methods on the buccal and approximal surfaces of human teeth after a sucrose rinse
    • Jensen, M.E., and Schachtele, C.F. (1983) Plaque pH measurements by different methods on the buccal and approximal surfaces of human teeth after a sucrose rinse. J Dent Res 62: 1058-1061.
    • (1983) J Dent Res , vol.62 , pp. 1058-1061
    • Jensen, M.E.1    Schachtele, C.F.2
  • 41
    • 0023749808 scopus 로고
    • Mapping and sequencing of mutations in the Escherichia coli rpoB gene that lead to rifampicin resistance
    • Jin, D.J., and Gross, C.A. (1988) Mapping and sequencing of mutations in the Escherichia coli rpoB gene that lead to rifampicin resistance. J Mol Biol 202: 45-58.
    • (1988) J Mol Biol , vol.202 , pp. 45-58
    • Jin, D.J.1    Gross, C.A.2
  • 42
    • 77952066060 scopus 로고    scopus 로고
    • Two Spx proteins modulate stress tolerance, survival, and virulence in Streptococcus mutans
    • Kajfasz, J.K., Rivera-Ramos, I., Abranches, J., Martinez, A.R., Rosalen, P.L., Derr, A.M., etal. (2010) Two Spx proteins modulate stress tolerance, survival, and virulence in Streptococcus mutans. J Bacteriol 192: 2546-2556.
    • (2010) J Bacteriol , vol.192 , pp. 2546-2556
    • Kajfasz, J.K.1    Rivera-Ramos, I.2    Abranches, J.3    Martinez, A.R.4    Rosalen, P.L.5    Derr, A.M.6
  • 43
    • 27144509129 scopus 로고    scopus 로고
    • Competition and coexistence between Streptococcus mutans and Streptococcus sanguinis in the dental biofilm
    • Kreth, J., Merritt, J., Shi, W., and Qi, F. (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
  • 44
    • 46049097957 scopus 로고    scopus 로고
    • Streptococcal antagonism in oral biofilms: Streptococcus sanguinis and Streptococcus gordonii interference with Streptococcus mutans
    • Kreth, J., Zhang, Y., and Herzberg, M.C. (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
  • 45
    • 0030861915 scopus 로고    scopus 로고
    • DNA glycosylases in the base excision repair of DNA
    • Krokan, H.E., Standal, R., and Slupphaug, G. (1997) DNA glycosylases in the base excision repair of DNA. Biochem J 325: 1-16.
    • (1997) Biochem J , vol.325 , pp. 1-16
    • Krokan, H.E.1    Standal, R.2    Slupphaug, G.3
  • 46
    • 10044236553 scopus 로고    scopus 로고
    • The F-ATPase operon promoter of Streptococcus mutans is transcriptionally regulated in response to external pH
    • Kuhnert, W.L., Zheng, G., Faustoferri, R.C., and Quivey, R.G. (2004) The F-ATPase operon promoter of Streptococcus mutans is transcriptionally regulated in response to external pH. J Bacteriol 186: 8524-8528.
    • (2004) J Bacteriol , vol.186 , pp. 8524-8528
    • Kuhnert, W.L.1    Zheng, G.2    Faustoferri, R.C.3    Quivey, R.G.4
  • 47
    • 0027530878 scopus 로고
    • Virulence factors of mutans streptococci: role of molecular genetics
    • Kuramitsu, H.K. (1993) Virulence factors of mutans streptococci: role of molecular genetics. Crit Rev Oral Biol Med 4: 159-176.
    • (1993) Crit Rev Oral Biol Med , vol.4 , pp. 159-176
    • Kuramitsu, H.K.1
  • 48
    • 19344368320 scopus 로고    scopus 로고
    • Mutator phenotype confers advantage in Escherichia coli chronic urinary tract infection pathogenesis
    • Labat, F., Pradillon, O., Garry, L., Peuchmaur, M., Fantin, B., and Denamur, E. (2005) Mutator phenotype confers advantage in Escherichia coli chronic urinary tract infection pathogenesis. FEMS Immunol Med Microbiol 44: 317-321.
    • (2005) FEMS Immunol Med Microbiol , vol.44 , pp. 317-321
    • Labat, F.1    Pradillon, O.2    Garry, L.3    Peuchmaur, M.4    Fantin, B.5    Denamur, E.6
  • 49
    • 0029860724 scopus 로고    scopus 로고
    • High mutation frequencies among Escherichia coli and Salmonella pathogens
    • LeClerc, J.E., Li, B., Payne, W.L., and Cebula, T.A. (1996) High mutation frequencies among Escherichia coli and Salmonella pathogens. Science 274: 1208-1211.
    • (1996) Science , vol.274 , pp. 1208-1211
    • LeClerc, J.E.1    Li, B.2    Payne, W.L.3    Cebula, T.A.4
  • 50
    • 0034610403 scopus 로고    scopus 로고
    • Removal of hydantoin products of 8-oxoguanine oxidation by the Escherichia coli DNA repair enzyme, FPG
    • Leipold, M.D., Muller, J.G., Burrows, C.J., and David, S.S. (2000) Removal of hydantoin products of 8-oxoguanine oxidation by the Escherichia coli DNA repair enzyme, FPG. Biochemistry 39: 14984-14992.
    • (2000) Biochemistry , vol.39 , pp. 14984-14992
    • Leipold, M.D.1    Muller, J.G.2    Burrows, C.J.3    David, S.S.4
  • 51
    • 57349140742 scopus 로고    scopus 로고
    • A model of efficiency: stress tolerance by Streptococcus mutans
    • Lemos, J.A., and Burne, R.A. (2008) A model of efficiency: stress tolerance by Streptococcus mutans. Microbiology 154: 3247-3255.
    • (2008) Microbiology , vol.154 , pp. 3247-3255
    • Lemos, J.A.1    Burne, R.A.2
  • 52
    • 0027278557 scopus 로고
    • Instability and decay of the primary structure of DNA
    • Lindahl, T. (1993) Instability and decay of the primary structure of DNA. Nature 362: 709-715.
    • (1993) Nature , vol.362 , pp. 709-715
    • Lindahl, T.1
  • 53
    • 0017161630 scopus 로고
    • Methyl methane sulfonate-sensitive mutant of Escherichia coli deficient in an endonuclease specific for apurinic sites in deoxyribonucleic acid
    • Ljungquist, S., Lindahl, T., and Howard-Flanders, P. (1976) Methyl methane sulfonate-sensitive mutant of Escherichia coli deficient in an endonuclease specific for apurinic sites in deoxyribonucleic acid. J Bacteriol 126: 646-653.
    • (1976) J Bacteriol , vol.126 , pp. 646-653
    • Ljungquist, S.1    Lindahl, T.2    Howard-Flanders, P.3
  • 54
    • 0031927314 scopus 로고    scopus 로고
    • Generation of bioluminescent Streptococcus mutans and its usage in rapid analysis of the efficacy of antimicrobial compounds
    • Loimaranta, V., Tenovuo, J., Koivisto, L., and Karp, M. (1998) Generation of bioluminescent 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
  • 55
    • 0026701365 scopus 로고
    • The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8-oxoguanine)
    • Michaels, M.L., and Miller, J.H. (1992) The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7, 8-dihydro-8-oxoguanine). J Bacteriol 174: 6321-6325.
    • (1992) J Bacteriol , vol.174 , pp. 6321-6325
    • Michaels, M.L.1    Miller, J.H.2
  • 56
    • 49649145410 scopus 로고
    • Mutants of Escherichia coli with altered deoxyribonucleases. I. Isolation and characterization of mutants for exonuclease 3
    • Milcarek, C., and Weiss, B. (1972) Mutants of Escherichia coli with altered deoxyribonucleases. I. Isolation and characterization of mutants for exonuclease 3. J Mol Biol 68: 303-318.
    • (1972) J Mol Biol , vol.68 , pp. 303-318
    • Milcarek, C.1    Weiss, B.2
  • 57
    • 0031029702 scopus 로고    scopus 로고
    • Role of oxidants in microbial pathophysiology
    • Miller, R.A., and Britigan, B.E. (1997) Role of oxidants in microbial pathophysiology. Clin Microbiol Rev 10: 1-18.
    • (1997) Clin Microbiol Rev , vol.10 , pp. 1-18
    • Miller, R.A.1    Britigan, B.E.2
  • 58
    • 1842456932 scopus 로고    scopus 로고
    • The pathogenesis of streptococcal infections: from tooth decay to meningitis
    • Mitchell, T.J. (2003) The pathogenesis of streptococcal infections: from tooth decay to meningitis. Nat Rev Microbiol 1: 219-230.
    • (2003) Nat Rev Microbiol , vol.1 , pp. 219-230
    • Mitchell, T.J.1
  • 60
    • 0023037541 scopus 로고
    • Transformation of Streptococcus mutans with chromosomal and shuttle plasmid (pYA629) DNAs
    • Murchison, H.H., Barrett, J.F., Cardineau, G.A., and Curtiss, R., 3rd (1986) Transformation of Streptococcus mutans with chromosomal and shuttle plasmid (pYA629) DNAs. Infect Immun 54: 273-282.
    • (1986) Infect Immun , vol.54 , pp. 273-282
    • Murchison, H.H.1    Barrett, J.F.2    Cardineau, G.A.3    Curtiss 3rd, R.4
  • 61
    • 23944480962 scopus 로고    scopus 로고
    • Transmission, diversity and virulence factors of Streptococcus mutans genotypes
    • Napimoga, M.H., Hofling, J.F., Klein, M.I., Kamiya, R.U., and Goncalves, R.B. (2005) Transmission, diversity and virulence factors of Streptococcus mutans genotypes. J Oral Sci 47: 59-64.
    • (2005) J Oral Sci , vol.47 , pp. 59-64
    • Napimoga, M.H.1    Hofling, J.F.2    Klein, M.I.3    Kamiya, R.U.4    Goncalves, R.B.5
  • 62
    • 0034930217 scopus 로고    scopus 로고
    • Base excision repair in a network of defence and tolerance
    • Nilsen, H., and Krokan, H.E. (2001) Base excision repair in a network of defence and tolerance. Carcinogenesis 22: 987-998.
    • (2001) Carcinogenesis , vol.22 , pp. 987-998
    • Nilsen, H.1    Krokan, H.E.2
  • 63
    • 0034685940 scopus 로고    scopus 로고
    • High frequency of hypermutable Pseudomonas aeruginosa in cystic fibrosis lung infection
    • Oliver, A., Canton, R., Campo, P., Baquero, F., and Blazquez, J. (2000) High frequency of hypermutable Pseudomonas aeruginosa in cystic fibrosis lung infection. Science 288: 1251-1254.
    • (2000) Science , vol.288 , pp. 1251-1254
    • Oliver, A.1    Canton, R.2    Campo, P.3    Baquero, F.4    Blazquez, J.5
  • 64
    • 0019482395 scopus 로고
    • Genetic transformation of Streptococcus mutans
    • Perry, D., and Kuramitsu, H.K. (1981) Genetic transformation of Streptococcus mutans. Infect Immun 32: 1295-1297.
    • (1981) Infect Immun , vol.32 , pp. 1295-1297
    • Perry, D.1    Kuramitsu, H.K.2
  • 65
    • 0037151055 scopus 로고    scopus 로고
    • Escherichia coli apurinic-apyrimidinic endonucleases enhance the turnover of the adenine glycosylase MutY with G:A substrates
    • Pope, M.A., Porello, S.L., and David, S.S. (2002) Escherichia coli apurinic-apyrimidinic endonucleases enhance the turnover of the adenine glycosylase MutY with G:A substrates. J Biol Chem 277: 22605-22615.
    • (2002) J Biol Chem , vol.277 , pp. 22605-22615
    • Pope, M.A.1    Porello, S.L.2    David, S.S.3
  • 66
    • 0026652539 scopus 로고
    • In vivo inactivation of the Streptococcus mutans recA gene mediated by PCR amplification and cloning of a recA DNA fragment
    • Quivey, R.G., Jr, and Faustoferri, R.C. (1992) In vivo inactivation of the Streptococcus mutans recA gene mediated by PCR amplification and cloning of a recA DNA fragment. Gene 116: 35-42.
    • (1992) Gene , vol.116 , pp. 35-42
    • Quivey Jr., R.G.1    Faustoferri, R.C.2
  • 68
    • 0037197858 scopus 로고    scopus 로고
    • Mutator clones of Neisseria meningitidis in epidemic serogroup A disease
    • Richardson, A.R., Yu, Z., Popovic, T., and Stojiljkovic, I. (2002) Mutator clones of Neisseria meningitidis in epidemic serogroup A disease. Proc Natl Acad Sci USA 99: 6103-6107.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 6103-6107
    • Richardson, A.R.1    Yu, Z.2    Popovic, T.3    Stojiljkovic, I.4
  • 69
    • 67249084716 scopus 로고    scopus 로고
    • The Base Excision Repair system of Salmonella enterica serovar typhimurium counteracts DNA damage by host nitric oxide
    • Richardson, A.R., Soliven, K.C., Castor, M.E., Barnes, P.D., Libby, S.J., and Fang, F.C. (2009) The Base Excision Repair system of Salmonella enterica serovar typhimurium counteracts DNA damage by host nitric oxide. PLoS Pathog 5: e1000451.
    • (2009) PLoS Pathog , vol.5
    • Richardson, A.R.1    Soliven, K.C.2    Castor, M.E.3    Barnes, P.D.4    Libby, S.J.5    Fang, F.C.6
  • 70
    • 0029353108 scopus 로고
    • Bacteria in human mouths involved in the production and utilization of hydrogen peroxide
    • Ryan, C.S., and Kleinberg, I. (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
  • 71
    • 0026032484 scopus 로고
    • Nitroxides block DNA scission and protect cells from oxidative damage
    • Samuni, A., Godinger, D., Aronovitch, J., Russo, A., and Mitchell, J.B. (1991) Nitroxides block DNA scission and protect cells from oxidative damage. Biochemistry 30: 555-561.
    • (1991) Biochemistry , vol.30 , pp. 555-561
    • Samuni, A.1    Godinger, D.2    Aronovitch, J.3    Russo, A.4    Mitchell, J.B.5
  • 72
    • 0015420798 scopus 로고
    • Bacteriocin production by transformable group H streptococci
    • Schlegel, R., and Slade, H.D. (1972) Bacteriocin production by transformable group H streptococci. J Bacteriol 112: 824-829.
    • (1972) J Bacteriol , vol.112 , pp. 824-829
    • Schlegel, R.1    Slade, H.D.2
  • 73
    • 0037363719 scopus 로고    scopus 로고
    • Identification of immunorelevant genes from greater wax moth (Galleria mellonella) by a subtractive hybridization approach
    • Seitz, V., Clermont, A., Wedde, M., Hummel, M., Vilcinskas, A., Schlatterer, K., and Podsiadlowski, L. (2003) Identification of immunorelevant genes from greater wax moth (Galleria mellonella) by a subtractive hybridization approach. Dev Comp Immunol 27: 207-215.
    • (2003) Dev Comp Immunol , vol.27 , pp. 207-215
    • Seitz, V.1    Clermont, A.2    Wedde, M.3    Hummel, M.4    Vilcinskas, A.5    Schlatterer, K.6    Podsiadlowski, L.7
  • 74
    • 0016415604 scopus 로고
    • Chloramphenicol acetyltransferase from chloramphenicol-resistant bacteria
    • Shaw, W.V. (1975) Chloramphenicol acetyltransferase from chloramphenicol-resistant bacteria. Methods Enzymol 43: 737-755.
    • (1975) Methods Enzymol , vol.43 , pp. 737-755
    • Shaw, W.V.1
  • 75
    • 0030004207 scopus 로고    scopus 로고
    • Cloning and sequencing a human homolog (hMYH) of the Escherichia coli mutY gene whose function is required for the repair of oxidative DNA damage
    • Slupska, M.M., Baikalov, C., Luther, W.M., Chiang, J.H., Wei, Y.F., and Miller, J.H. (1996) Cloning and sequencing a human homolog (hMYH) of the Escherichia coli mutY gene whose function is required for the repair of oxidative DNA damage. J Bacteriol 178: 3885-3892.
    • (1996) J Bacteriol , vol.178 , pp. 3885-3892
    • Slupska, M.M.1    Baikalov, C.2    Luther, W.M.3    Chiang, J.H.4    Wei, Y.F.5    Miller, J.H.6
  • 76
    • 0038686708 scopus 로고    scopus 로고
    • The role of DNA base excision repair in the pathogenesis of Salmonella enterica serovar Typhimurium
    • Suvarnapunya, A.E., Lagasse, H.A., and Stein, M.A. (2003) The role of DNA base excision repair in the pathogenesis of Salmonella enterica serovar Typhimurium. Mol Microbiol 48: 549-559.
    • (2003) Mol Microbiol , vol.48 , pp. 549-559
    • Suvarnapunya, A.E.1    Lagasse, H.A.2    Stein, M.A.3
  • 78
    • 0031126775 scopus 로고    scopus 로고
    • Bacteriocin production and sensitivity among coaggregating and noncoaggregating oral streptococci
    • Tompkins, G.R., Peavey, M.A., Birchmeier, K.R., and Tagg, J.R. (1997) Bacteriocin production and sensitivity among coaggregating and noncoaggregating oral streptococci. Oral Microbiol Immunol 12: 98-105.
    • (1997) Oral Microbiol Immunol , vol.12 , pp. 98-105
    • Tompkins, G.R.1    Peavey, M.A.2    Birchmeier, K.R.3    Tagg, J.R.4
  • 79
    • 0019051753 scopus 로고
    • Apurinic/apyrimidinic endonucleases in repair of pyrimidine dimers and other lesions in DNA
    • Warner, H.R., Demple, B.F., Deutsch, W.A., Kane, C.M., and Linn, S. (1980) Apurinic/apyrimidinic endonucleases in repair of pyrimidine dimers and other lesions in DNA. Proc Natl Acad Sci USA 77: 4602-4606.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 4602-4606
    • Warner, H.R.1    Demple, B.F.2    Deutsch, W.A.3    Kane, C.M.4    Linn, S.5
  • 80
    • 2442479591 scopus 로고    scopus 로고
    • Stress-directed adaptive mutations and evolution
    • Wright, B.E. (2004) Stress-directed adaptive mutations and evolution. Mol Microbiol 52: 643-650.
    • (2004) Mol Microbiol , vol.52 , pp. 643-650
    • Wright, B.E.1
  • 81
    • 0029814218 scopus 로고    scopus 로고
    • Development of a method based on alkaline gel electrophoresis for estimation of oxidative damage to DNA in Escherichia coli
    • Zirkle, R.E., and Krieg, N.R. (1996) Development of a method based on alkaline gel electrophoresis for estimation of oxidative damage to DNA in Escherichia coli. J Appl Bacteriol 81: 133-138.
    • (1996) J Appl Bacteriol , vol.81 , pp. 133-138
    • Zirkle, R.E.1    Krieg, N.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.