메뉴 건너뛰기




Volumn 68, Issue 8, 2000, Pages 4441-4451

Genetic characterization of a Streptococcus mutans LraI family operon and role in virulence

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN; LIPOPROTEIN RECEPTOR;

EID: 0033943809     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.68.8.4441-4451.2000     Document Type: Article
Times cited : (77)

References (64)
  • 1
    • 0025327409 scopus 로고
    • The ami locus of the gram-positive bacterium Streptococcus pneumoniae is similar to binding protein-dependent transport operons of Gram-negative bacteria
    • Alloing, G., M. C. Trombe, and J. P. Claverys. 1990. The ami locus of the Gram-positive bacterium Streptococcus pneumoniae is similar to binding protein-dependent transport operons of Gram-negative bacteria. Mol. Microbiol. 4:633-644.
    • (1990) Mol. Microbiol. , vol.4 , pp. 633-644
    • Alloing, G.1    Trombe, M.C.2    Claverys, J.P.3
  • 3
    • 0030867539 scopus 로고    scopus 로고
    • Determination of the transcript size and start site of the putative sca operon of Streptococcus gordonii ATCC 51656 (formerly strain PK488)
    • Andersen, R. N., R. D. Lunsford, and P. E. Kolenbrander. 1997. Determination of the transcript size and start site of the putative sca operon of Streptococcus gordonii ATCC 51656 (formerly strain PK488). Adv. Exp. Med. Biol. 418:657-660.
    • (1997) Adv. Exp. Med. Biol. , vol.418 , pp. 657-660
    • Andersen, R.N.1    Lunsford, R.D.2    Kolenbrander, P.E.3
  • 4
    • 0029027150 scopus 로고
    • Molecular identification of an ABC transporter complex for manganese: Analysis of a cyanobacterial mutant strain impaired in the photosynthetic oxygen evolution process
    • Bartsevich, V. V., and H. B. Pakrasi. 1995. Molecular identification of an ABC transporter complex for manganese: analysis of a cyanobacterial mutant strain impaired in the photosynthetic oxygen evolution process. EMBO J. 14:1845-1853.
    • (1995) EMBO J. , vol.14 , pp. 1845-1853
    • Bartsevich, V.V.1    Pakrasi, H.B.2
  • 5
    • 0033037294 scopus 로고    scopus 로고
    • Membrane topology of MntB, the transmembrane protein component of an ABC transporter system for manganese in the cyanobacterium Synechocystis sp strain PCC 6803
    • Bartsevich, V. V., and H. B. Pakrasi. 1999. Membrane topology of MntB, the transmembrane protein component of an ABC transporter system for manganese in the cyanobacterium Synechocystis sp strain PCC 6803. J. Bacteriol. 181:3591-3593.
    • (1999) J. Bacteriol. , vol.181 , pp. 3591-3593
    • Bartsevich, V.V.1    Pakrasi, H.B.2
  • 6
    • 0001769249 scopus 로고    scopus 로고
    • Periplasmic binding protein-dependent ABC transporters
    • F. C. Neidhardt et al. (ed.), American Society for Microbiology, Washington, D.C.
    • Boos, W., and J. M. Lucht. 1996. Periplasmic binding protein-dependent ABC transporters, p. 1175-1209. In F. C. Neidhardt et al. (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. American Society for Microbiology, Washington, D.C.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology, 2nd Ed. , pp. 1175-1209
    • Boos, W.1    Lucht, J.M.2
  • 7
    • 0025300518 scopus 로고
    • Molecular cloning and DNA sequence analysis of a diphtheria tox iron-dependent regulatory element (dtxR) from Corynebacterium diphtheriae
    • Boyd, J., M. N. Oza, and J. R. Murphy. 1990. Molecular cloning and DNA sequence analysis of a diphtheria tox iron-dependent regulatory element (dtxR) from Corynebacterium diphtheriae. Proc. Natl. Acad. Sci. USA 87: 5968-5972.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5968-5972
    • Boyd, J.1    Oza, M.N.2    Murphy, J.R.3
  • 10
    • 0028568176 scopus 로고
    • TopPred II: An improved software for membrane protein structure predictions
    • Claros, M. G., and G. von Heijne. 1994. TopPred II: an improved software for membrane protein structure predictions. Comput. Appl. Biosci. 10:685-686.
    • (1994) Comput. Appl. Biosci. , vol.10 , pp. 685-686
    • Claros, M.G.1    Von Heijne, G.2
  • 11
    • 0031871386 scopus 로고    scopus 로고
    • Molecular cloning of a 32-kilodalton lipoprotein component of a novel iron-regulated Staphylococcus epidermidis ABC transporter
    • Cockayne, A., P. J. Hill, N. B. Powell, K. Bishop, C. Sims, and P. Williams. 1998. Molecular cloning of a 32-kilodalton lipoprotein component of a novel iron-regulated Staphylococcus epidermidis ABC transporter. Infect. Immun. 66:3767-3774.
    • (1998) Infect. Immun. , vol.66 , pp. 3767-3774
    • Cockayne, A.1    Hill, P.J.2    Powell, N.B.3    Bishop, K.4    Sims, C.5    Williams, P.6
  • 12
    • 0029929219 scopus 로고    scopus 로고
    • scbA from Streptococcus crista CC5A: An atypical member of the lraI gene family
    • Correla, F. F., J. M. DiRienzo, T. L. McKay, and B. Rosan. 1996. scbA from Streptococcus crista CC5A: an atypical member of the lraI gene family. Infect. Immun. 64:2114-2121.
    • (1996) Infect. Immun. , vol.64 , pp. 2114-2121
    • Correla, F.F.1    DiRienzo, J.M.2    McKay, T.L.3    Rosan, B.4
  • 13
    • 0031718255 scopus 로고    scopus 로고
    • Prevention of bacterial endocarditis: Highlights of the latest recommendations by the American Heart Association
    • Dajani, A. S. 1998. Prevention of bacterial endocarditis: highlights of the latest recommendations by the American Heart Association. Pediatr. Infect. Dis. J. 17:824-825.
    • (1998) Pediatr. Infect. Dis. J. , vol.17 , pp. 824-825
    • Dajani, A.S.1
  • 14
    • 0022125681 scopus 로고
    • Sequence of gene malG in E. coli K12: Homologies between integral membrane components from binding protein-dependent transport systems
    • Dassa, E., and M. Hofnung. 1985. Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems. EMBO J. 4:2287-2293.
    • (1985) EMBO J. , vol.4 , pp. 2287-2293
    • Dassa, E.1    Hofnung, M.2
  • 15
    • 0025663103 scopus 로고
    • Prediction of rho-independent Escherichia coli transcription terminators. A statistical analysis of their RNA stem-loop structures
    • d'Aubenton, C. Y., E. Brody, and C. Thermes. 1990. Prediction of rho-independent Escherichia coli transcription terminators. A statistical analysis of their RNA stem-loop structures. J. Mol. Biol. 216:835-858.
    • (1990) J. Mol. Biol. , vol.216 , pp. 835-858
    • D'Aubenton, C.Y.1    Brody, E.2    Thermes, C.3
  • 16
    • 0029964556 scopus 로고    scopus 로고
    • Identification of the primary metal ion-activation sites of the diphtheria tox represser by X-ray crystallography and site-directed mutational analysis
    • Ding, X., H. Zeng, N. Schiering, D. Ringe, and J. R. Murphy. 1996. Identification of the primary metal ion-activation sites of the diphtheria tox represser by X-ray crystallography and site-directed mutational analysis. Nat. Struct. Biol. 3:382-387.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 382-387
    • Ding, X.1    Zeng, H.2    Schiering, N.3    Ringe, D.4    Murphy, J.R.5
  • 17
    • 0030868591 scopus 로고    scopus 로고
    • Competence and virulence of Streptococcus pneumoniae: Adc and PsaA mutants exhibit a requirement for Zn and Mn resulting from inactivation of putative ABC metal permeases
    • Dintilhac, A., G. Alloing, C. Granadel, and J. P. Claverys. 1997. Competence and virulence of Streptococcus pneumoniae: Adc and PsaA mutants exhibit a requirement for Zn and Mn resulting from inactivation of putative ABC metal permeases. Mol. Microbiol. 25:727-739.
    • (1997) Mol. Microbiol. , vol.25 , pp. 727-739
    • Dintilhac, A.1    Alloing, G.2    Granadel, C.3    Claverys, J.P.4
  • 18
    • 0031081208 scopus 로고    scopus 로고
    • The adc locus, which affects competence for genetic transformation in Streptococcus pneumoniae, encodes an ABC transporter with a putative lipoprotein homologous to a family of streptococcal adhesins
    • Dintilhac, A., and J. P. Claverys. 1997. The adc locus, which affects competence for genetic transformation in Streptococcus pneumoniae, encodes an ABC transporter with a putative lipoprotein homologous to a family of streptococcal adhesins. Res. Microbiol. 148:119-131.
    • (1997) Res. Microbiol. , vol.148 , pp. 119-131
    • Dintilhac, A.1    Claverys, J.P.2
  • 19
    • 0028960851 scopus 로고
    • The fimA locus of Streptococcus parasanguis encodes an ATP-binding membrane transport system
    • Fenno, J. C., A. Shaikh, G. Spatafora, and P. Fives-Taylor. 1995. The fimA locus of Streptococcus parasanguis encodes an ATP-binding membrane transport system. Mol. Microbiol. 15:849-863.
    • (1995) Mol. Microbiol. , vol.15 , pp. 849-863
    • Fenno, J.C.1    Shaikh, A.2    Spatafora, G.3    Fives-Taylor, P.4
  • 20
    • 0027497734 scopus 로고
    • Saliva-binding protein (SsaB) from Streptococcus sanguis 12 is a lipoprotein
    • Ganeshkumar, N., N. Arora, and P. E. Kolenbrander. 1993. Saliva-binding protein (SsaB) from Streptococcus sanguis 12 is a lipoprotein. J. Bacteriol. 175:572-574.
    • (1993) J. Bacteriol. , vol.175 , pp. 572-574
    • Ganeshkumar, N.1    Arora, N.2    Kolenbrander, P.E.3
  • 21
    • 0025976447 scopus 로고
    • Nucleotide sequence of a gene coding for a saliva-binding protein (SsaB) from Streptococcus sanguis 12 and possible role of the protein in coaggregation with actinomyces
    • Ganeshkumar, N., P. M. Hannara, P. E. Kolenbrander, and B. C. McBride, 1991. Nucleotide sequence of a gene coding for a saliva-binding protein (SsaB) from Streptococcus sanguis 12 and possible role of the protein in coaggregation with actinomyces. Infect. Immun. 59:1093-1099.
    • (1991) Infect. Immun. , vol.59 , pp. 1093-1099
    • Ganeshkumar, N.1    Hannara, P.M.2    Kolenbrander, P.E.3    McBride, B.C.4
  • 22
    • 0023948277 scopus 로고
    • Cloning of a Streptococcus sanguis adhesin which mediates binding to saliva-coated hydroxyapatite
    • Ganeshkumar, N., M. Song, and B. C. McBride. 1988. Cloning of a Streptococcus sanguis adhesin which mediates binding to saliva-coated hydroxyapatite. Infect. Immun. 56:1150-1157.
    • (1988) Infect. Immun. , vol.56 , pp. 1150-1157
    • Ganeshkumar, N.1    Song, M.2    McBride, B.C.3
  • 23
    • 0024198129 scopus 로고
    • Evidence for high affinity binding-protein dependent transport systems in Gram-positive bacteria and in Mycoplasma
    • Gilson, E., G. Alloing, T. Schmidt, J. P. Claverys, R. Dudler, and M. Hofnung. 1988. Evidence for high affinity binding-protein dependent transport systems in Gram-positive bacteria and in Mycoplasma. EMBO J. 7:3971-3974.
    • (1988) EMBO J. , vol.7 , pp. 3971-3974
    • Gilson, E.1    Alloing, G.2    Schmidt, T.3    Claverys, J.P.4    Dudler, R.5    Hofnung, M.6
  • 24
    • 0033051018 scopus 로고    scopus 로고
    • Anion-coordinating residues at binding site 1 are essential for the biological activity of the diphtheria toxin repressor
    • Goranson-Siekierke, J., E. Pohl, W. G. Hol, and R. K. Holmes. 1999. Anion-coordinating residues at binding site 1 are essential for the biological activity of the diphtheria toxin repressor. Infect. Immun. 67:1806-1811.
    • (1999) Infect. Immun. , vol.67 , pp. 1806-1811
    • Goranson-Siekierke, J.1    Pohl, E.2    Hol, W.G.3    Holmes, R.K.4
  • 25
    • 0019255349 scopus 로고
    • Biology, immunology and cariogenicity of Streptococcus mutans
    • Hamada, S., and H. D. Slade. 1980. Biology, immunology and cariogenicity of Streptococcus mutans. Microbiol. Rev. 44:331-384.
    • (1980) Microbiol. Rev. , vol.44 , pp. 331-384
    • Hamada, S.1    Slade, H.D.2
  • 26
    • 0030766168 scopus 로고    scopus 로고
    • Identification and transcriptional analysis of a Treponema pallidum operon encoding a putative ABC transport system, an iron-activated repressor protein homolog, and a glycolytic pathway enzyme homolog
    • Hardham, J. M., L. V. Stamm, S. F. Porcella, J. G. Frye, N. Y. Barnes, J. K. Howell, S. L. Mueller, J. D. Radolf, G. M. Weinstock, and S. J. Norris. 1997. Identification and transcriptional analysis of a Treponema pallidum operon encoding a putative ABC transport system, an iron-activated repressor protein homolog, and a glycolytic pathway enzyme homolog. Gene 197:47-64.
    • (1997) Gene , vol.197 , pp. 47-64
    • Hardham, J.M.1    Stamm, L.V.2    Porcella, S.F.3    Frye, J.G.4    Barnes, N.Y.5    Howell, J.K.6    Mueller, S.L.7    Radolf, J.D.8    Weinstock, G.M.9    Norris, S.J.10
  • 29
    • 0029285787 scopus 로고
    • PCR-mediated recombination and mutagenesis. SOE-ing together tailor-made genes
    • Horton, R. M. 1995. PCR-mediated recombination and mutagenesis. SOE-ing together tailor-made genes. Mol. Biotechnol. 3:93-99.
    • (1995) Mol. Biotechnol. , vol.3 , pp. 93-99
    • Horton, R.M.1
  • 30
    • 0032746814 scopus 로고    scopus 로고
    • Identification and characterization of a Streptococcus pyogenes ABC transporter with multiple specificity for metal cations
    • Janulczyk, R., J. Pallon, and L. Bjorck. 1999. Identification and characterization of a Streptococcus pyogenes ABC transporter with multiple specificity for metal cations. Mol. Microbiol. 34:596-606.
    • (1999) Mol. Microbiol. , vol.34 , pp. 596-606
    • Janulczyk, R.1    Pallon, J.2    Bjorck, L.3
  • 31
    • 0027992299 scopus 로고
    • Cell surface protein receptors in oral streptococci
    • Jenkinson. H. F. 1994. Cell surface protein receptors in oral streptococci. FEMS Microbiol. Lett. 121:133-140.
    • (1994) FEMS Microbiol. Lett. , vol.121 , pp. 133-140
    • Jenkinson, H.F.1
  • 32
    • 0028337422 scopus 로고
    • Genetic analysis of fructan-hyperproducing strains of Streptococcus mutans
    • Kiska, D. L., and F. L. Macrina. 1994. Genetic analysis of fructan-hyperproducing strains of Streptococcus mutans. Infect. Immun. 62:2679-2686.
    • (1994) Infect. Immun. , vol.62 , pp. 2679-2686
    • Kiska, D.L.1    Macrina, F.L.2
  • 33
    • 0025030403 scopus 로고
    • Characterization of Streptococcus gordonii (S. sanguis) PK488 adhesin-mediated coaggregation with Actinomyces naeslundii PK606
    • Kolenbrander, P. E., and R. N. Andersen. 1990. Characterization of Streptococcus gordonii (S. sanguis) PK488 adhesin-mediated coaggregation with Actinomyces naeslundii PK606. Infect. Immun. 58:3064-3072.
    • (1990) Infect. Immun. , vol.58 , pp. 3064-3072
    • Kolenbrander, P.E.1    Andersen, R.N.2
  • 35
    • 0028100391 scopus 로고
    • Nucleotide sequence of the Streptococcus gordonii PK488 coaggregation adhesin gene. ScaA, and ATP-binding cassette
    • Kolenbrander, P. E., R. N. Andersen, and N. Ganeshkumar. 1994. Nucleotide sequence of the Streptococcus gordonii PK488 coaggregation adhesin gene. scaA, and ATP-binding cassette. Infect. Immun. 62:4469-4480.
    • (1994) Infect. Immun. , vol.62 , pp. 4469-4480
    • Kolenbrander, P.E.1    Andersen, R.N.2    Ganeshkumar, N.3
  • 36
    • 0032902142 scopus 로고    scopus 로고
    • Concentrations of trace elements in sera of newborns, young infants, and adults
    • Krachler, M., E. Rossipal, and D. Micetic-Turk. 1999. Concentrations of trace elements in sera of newborns, young infants, and adults. Biol. Trace Elem. Res. 68:121-135.
    • (1999) Biol. Trace Elem. Res. , vol.68 , pp. 121-135
    • Krachler, M.1    Rossipal, E.2    Micetic-Turk, D.3
  • 37
    • 0016780422 scopus 로고
    • Indirect selection of bacterial plasmids lacking identifiable phenotypic properties
    • Kretschmer, F. J., A. C. Chang, and S. N. Cohen. 1975. Indirect selection of bacterial plasmids lacking identifiable phenotypic properties. J. Bacleriol. 124:225-231.
    • (1975) J. Bacleriol. , vol.124 , pp. 225-231
    • Kretschmer, F.J.1    Chang, A.C.2    Cohen, S.N.3
  • 38
    • 0022570865 scopus 로고
    • Characterization of genetic transformation in Streptococcus mutans by using a novel high-efficiency plasmid marker rescue system
    • Lindler, L. E., and F. L. Macrina. 1986. Characterization of genetic transformation in Streptococcus mutans by using a novel high-efficiency plasmid marker rescue system. J. Bacteriol. 166:658-665.
    • (1986) J. Bacteriol. , vol.166 , pp. 658-665
    • Lindler, L.E.1    Macrina, F.L.2
  • 39
    • 0030796260 scopus 로고    scopus 로고
    • Methods for generating precise deletions and insertions in the genome of wild-type Escherichia coli: Application to open reading frame characterization
    • Link, A. J., D. Phillips, and G. M. Church. 1997. Methods for generating precise deletions and insertions in the genome of wild-type Escherichia coli: application to open reading frame characterization. J. Bacteriol. 179:6228-6237.
    • (1997) J. Bacteriol. , vol.179 , pp. 6228-6237
    • Link, A.J.1    Phillips, D.2    Church, G.M.3
  • 40
    • 0031943304 scopus 로고    scopus 로고
    • The Escherichia coli ATP-binding cassette (ABC) proteins
    • Linton, K. J., and C. F. Higgins. 1998. The Escherichia coli ATP-binding cassette (ABC) proteins. Mol. Microbiol. 28:5-13.
    • (1998) Mol. Microbiol. , vol.28 , pp. 5-13
    • Linton, K.J.1    Higgins, C.F.2
  • 41
    • 0028861721 scopus 로고
    • Recovery of RNA from oral streptococci
    • Lunsford, R. D. 1995. Recovery of RNA from oral streptococci. BioTechniques 18:412-414.
    • (1995) BioTechniques , vol.18 , pp. 412-414
    • Lunsford, R.D.1
  • 42
    • 0021059592 scopus 로고
    • Novel shuttle plasmid vehicles for Escherichia-streptococcus transgeneric cloning
    • Macrina, F. L., R. P. Evans, J. A. Tobian, D. L. Hartley, D. B. Clewell, and K. R. Jones. 1983. Novel shuttle plasmid vehicles for Escherichia-Streptococcus transgeneric cloning. Gene 25:145-150.
    • (1983) Gene , vol.25 , pp. 145-150
    • Macrina, F.L.1    Evans, R.P.2    Tobian, J.A.3    Hartley, D.L.4    Clewell, D.B.5    Jones, K.R.6
  • 43
    • 0020464403 scopus 로고
    • A cloning vector able to replicate in Escherichia coli and Streptococcus sanguis
    • Macrina, F. L., J. A. Tobian, K. R. Jones, R. P. Evans, and D. B. Clewell. 1982. A cloning vector able to replicate in Escherichia coli and Streptococcus sanguis. Gene 19:345-353.
    • (1982) Gene , vol.19 , pp. 345-353
    • Macrina, F.L.1    Tobian, J.A.2    Jones, K.R.3    Evans, R.P.4    Clewell, D.B.5
  • 44
    • 0033607166 scopus 로고    scopus 로고
    • Attenuation of virulence in Mycobacterium tuberculosis expressing a constitutively active iron repressor
    • Manabe, Y. C., B. J. Saviola, L. Sun, J. R. Murphy, and W. R. Bishai. 1999. Attenuation of virulence in Mycobacterium tuberculosis expressing a constitutively active iron repressor. Proc. Natl. Acad. Sci. USA 96:12844-12848.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12844-12848
    • Manabe, Y.C.1    Saviola, B.J.2    Sun, L.3    Murphy, J.R.4    Bishai, W.R.5
  • 46
    • 0016682802 scopus 로고
    • Virulence of streptococcus mutans: A sensitive method for evaluating cariogenicity in young gnotobiotic rats
    • Michalek, S. M., J. R. McGhee, and J. M. Navia. 1975. Virulence of Streptococcus mutans: a sensitive method for evaluating cariogenicity in young gnotobiotic rats. Infect. Immun. 12:69-75.
    • (1975) Infect. Immun. , vol.12 , pp. 69-75
    • Michalek, S.M.1    McGhee, J.R.2    Navia, J.M.3
  • 47
    • 0025741198 scopus 로고
    • Cariogenicity of Streptococcus mutans V403 glucosyltransferase and fructosyltransferase mutants constructed by allelic exchange
    • Munro, C, S. M. Michalek, and F. L. Macrina. 1991. Cariogenicity of Streptococcus mutans V403 glucosyltransferase and fructosyltransferase mutants constructed by allelic exchange. Infect. Immun. 59:2316-2323.
    • (1991) Infect. Immun. , vol.59 , pp. 2316-2323
    • Munro, C.1    Michalek, S.M.2    Macrina, F.L.3
  • 48
    • 0027453283 scopus 로고
    • Sucrose-derived exopolysaccharides of Streptococcus mutans V403 contribute to infectivity in endocarditis
    • Munro, C. L., and F. L. Macrina. 1993. Sucrose-derived exopolysaccharides of Streptococcus mutans V403 contribute to infectivity in endocarditis. Mol. Microbiol. 8:133-142.
    • (1993) Mol. Microbiol. , vol.8 , pp. 133-142
    • Munro, C.L.1    Macrina, F.L.2
  • 49
    • 0023037541 scopus 로고
    • Transformation of Streptococcus mutans with chromosomal and plasmid (pYA629) DNAs
    • Murchison, H. H., J. F. Barrett, G. A. Cardineau, and R. Curtiss III. 1986. Transformation of Streptococcus mutans with chromosomal and 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 R. III4
  • 50
    • 0031689661 scopus 로고    scopus 로고
    • Penicillin tolerance genes of Streptococcus pneumoniae: The ABC-type manganese permease complex Psa
    • Novak, R., J. S. Braun, E. Charpentier, and E. Tuomanen. 1998. Penicillin tolerance genes of Streptococcus pneumoniae: the ABC-type manganese permease complex Psa. Mol. Microbiol. 29:1285-1296.
    • (1998) Mol. Microbiol. , vol.29 , pp. 1285-1296
    • Novak, R.1    Braun, J.S.2    Charpentier, E.3    Tuomanen, E.4
  • 51
    • 0027450367 scopus 로고
    • Overexpression and purification of a fimbria-associated adhesin of Streptococcus parasanguis
    • Oligino, L., and P. Fives-Taylor. 1993. Overexpression and purification of a fimbria-associated adhesin of Streptococcus parasanguis. Infect. Immun. 61: 1016-1022.
    • (1993) Infect. Immun. , vol.61 , pp. 1016-1022
    • Oligino, L.1    Fives-Taylor, P.2
  • 52
    • 0032851843 scopus 로고    scopus 로고
    • Characterization of a manganese-dependent regulatory protein, TroR, from Treponema pallidum
    • Posey, J. E., J. M. Hardham, S. J. Morris, and F. C. Gherardini. 1999. Characterization of a manganese-dependent regulatory protein, TroR, from Treponema pallidum. Proc. Natl. Acad. Sci. USA 96:10887-10892.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10887-10892
    • Posey, J.E.1    Hardham, J.M.2    Morris, S.J.3    Gherardini, F.C.4
  • 53
    • 0021822477 scopus 로고
    • Binding of manganese in human and rat plasma
    • Scheuhammer, A. M., and M. G. Cherian. 1985. Binding of manganese in human and rat plasma. Biochim. Biophys. Acta 840:163-169.
    • (1985) Biochim. Biophys. Acta , vol.840 , pp. 163-169
    • Scheuhammer, A.M.1    Cherian, M.G.2
  • 54
    • 0027210121 scopus 로고
    • Analysis of diphtheria toxin repressor-operator interactions and characterization of a mutant repressor with decreased binding activity for divalent metals
    • Schmitt, M. P., and R. K. Holmes. 1993. Analysis of diphtheria toxin repressor-operator interactions and characterization of a mutant repressor with decreased binding activity for divalent metals. Mol. Microbiol. 9:173-181.
    • (1993) Mol. Microbiol. , vol.9 , pp. 173-181
    • Schmitt, M.P.1    Holmes, R.K.2
  • 55
    • 0024457840 scopus 로고
    • Biochemical characterization and evaluation of virulence of a fructosyltransferase-deficient mutant of Streptococcus mutans V403
    • Schroeder, V. A., S. M. Michalek, and F. L. Macrina. 1989. Biochemical characterization and evaluation of virulence of a fructosyltransferase-deficient mutant of Streptococcus mutans V403. Infect. Immun. 57:3560-3569.
    • (1989) Infect. Immun. , vol.57 , pp. 3560-3569
    • Schroeder, V.A.1    Michalek, S.M.2    Macrina, F.L.3
  • 57
    • 0027447001 scopus 로고
    • MsmE, a lipoprotein involved in sugar transport in Streptococcus mutans
    • Sutcliffe, I. C., L. Tao, J. J. Ferretti, and R. R. B. Russell. 1993. MsmE, a lipoprotein involved in sugar transport in Streptococcus mutans. J. Bacteriol. 175:1853-1855.
    • (1993) J. Bacteriol. , vol.175 , pp. 1853-1855
    • Sutcliffe, I.C.1    Tao, L.2    Ferretti, J.J.3    Russell, R.R.B.4
  • 58
    • 0026667137 scopus 로고
    • Specific binding of the diphtheria tox regulatory element DtxR to the tox operator requires divalent heavy metal ions and a 9-base-pair interrupted palindromic sequence
    • Tao, X., J. Boyd, and J. R. Murphy. 1992. Specific binding of the diphtheria tox regulatory element DtxR to the tox operator requires divalent heavy metal ions and a 9-base-pair interrupted palindromic sequence. Proc. Natl. Acad. Sci. USA 89:5897-5901.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5897-5901
    • Tao, X.1    Boyd, J.2    Murphy, J.R.3
  • 59
    • 0026800843 scopus 로고
    • Binding of the metalloregulatory protein DtxR to the diphtheria tox operator requires a divalent heavy metal ion and protects the palindromic sequence from DNase 1 digestion
    • Tao, X., and J. R. Murphy. 1992. Binding of the metalloregulatory protein DtxR to the diphtheria tox operator requires a divalent heavy metal ion and protects the palindromic sequence from DNase 1 digestion. J. Biol. Chem. 267:21761-21764.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21761-21764
    • Tao, X.1    Murphy, J.R.2
  • 60
    • 0027294003 scopus 로고
    • Cysteine-102 is positioned in the metal binding activation site of the Corynebacterium diphtheriae regulatory element DtxR
    • Tao, X., and J. R. Murphy. 1993. Cysteine-102 is positioned in the metal binding activation site of the Corynebacterium diphtheriae regulatory element DtxR. Proc. Natl. Acad. Sci. USA 90:8524-8528.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8524-8528
    • Tao, X.1    Murphy, J.R.2
  • 61
    • 0028149973 scopus 로고
    • Iron, DtxR, and the regulation of diphtheria toxin expression
    • Tao, X., N. Schiering, H. Y. Zeng, D. Ringe, and J. R. Murphy. 1994. Iron, DtxR, and the regulation of diphtheria toxin expression. Mol. Microbiol. 14:191-197.
    • (1994) Mol. Microbiol. , vol.14 , pp. 191-197
    • Tao, X.1    Schiering, N.2    Zeng, H.Y.3    Ringe, D.4    Murphy, J.R.5
  • 62
  • 63
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J. E., M. Saraste, M. J. Runswick, and N. J. Gay. 1982. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1:945-951.
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.