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Volumn 75, Issue 9, 2007, Pages 4490-4497

Interaction between leukotoxin and Cu,Zn superoxide dismutase in Aggregatibacter actinomycetemcomitans

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; BACTERIAL TOXIN; COPPER ZINC SUPEROXIDE DISMUTASE; LEUKOTOXIN; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; VIRULENCE FACTOR;

EID: 34548510165     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.00288-07     Document Type: Article
Times cited : (18)

References (78)
  • 1
    • 33645523450 scopus 로고    scopus 로고
    • Leukotoxin confers beta-hemolytic activity to Actinobacillus actinomycetemcomitans
    • Balashova, N. V., J. A. Crosby, L. Al Ghofaily, and S. C. Kachlany. 2006. Leukotoxin confers beta-hemolytic activity to Actinobacillus actinomycetemcomitans. Infect. Immun. 74:2015-2021.
    • (2006) Infect. Immun , vol.74 , pp. 2015-2021
    • Balashova, N.V.1    Crosby, J.A.2    Al Ghofaily, L.3    Kachlany, S.C.4
  • 2
    • 33845400561 scopus 로고    scopus 로고
    • Regulation of Aggregatibacter (Actinobacillus) actinomycetemcomitans leukotoxin secretion by iron
    • Balashova, N. V., R. Diaz, S. V. Balashov, J. A. Crosby, and S. C. Kachlany. 2006. Regulation of Aggregatibacter (Actinobacillus) actinomycetemcomitans leukotoxin secretion by iron. J. Bacteriol. 188:8658-8661.
    • (2006) J. Bacteriol , vol.188 , pp. 8658-8661
    • Balashova, N.V.1    Diaz, R.2    Balashov, S.V.3    Crosby, J.A.4    Kachlany, S.C.5
  • 3
    • 0348049821 scopus 로고    scopus 로고
    • Role of prokaryotic Cu,Zn superoxide dismutase in pathogenesis
    • Battistoni, A. 2003. Role of prokaryotic Cu,Zn superoxide dismutase in pathogenesis. Biochem. Soc. Trans. 31:1326-1329.
    • (2003) Biochem. Soc. Trans , vol.31 , pp. 1326-1329
    • Battistoni, A.1
  • 4
    • 0035839491 scopus 로고    scopus 로고
    • A histidine-rich metal binding domain at the N terminus of Cu,Zn-superoxide dismutases from pathogenic bacteria: A novel strategy for metal chaperoning
    • Battistoni, A., F. Pacello, A. P. Mazzetti, C. Capo, J. S. Kroll, P. R. Langford, A. Sansone, G. Donnarumma, P. Valenti, and G. Rotilio. 2001. A histidine-rich metal binding domain at the N terminus of Cu,Zn-superoxide dismutases from pathogenic bacteria: a novel strategy for metal chaperoning. J. Biol. Chem. 276:30315-30325.
    • (2001) J. Biol. Chem , vol.276 , pp. 30315-30325
    • Battistoni, A.1    Pacello, F.2    Mazzetti, A.P.3    Capo, C.4    Kroll, J.S.5    Langford, P.R.6    Sansone, A.7    Donnarumma, G.8    Valenti, P.9    Rotilio, G.10
  • 5
    • 0015153416 scopus 로고
    • Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels
    • Beauchamp, C., and I. Fridovich. 1971. Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal. Biochem. 44:276-287.
    • (1971) Anal. Biochem , vol.44 , pp. 276-287
    • Beauchamp, C.1    Fridovich, I.2
  • 6
    • 0031154923 scopus 로고    scopus 로고
    • Infective endocarditis due to unusual or fastidious microorganisms
    • Berbari, E. F., F. R. Cockerill III, and J. M. Steckelberg. 1997. Infective endocarditis due to unusual or fastidious microorganisms. Mayo Clin. Proc. 72:532-542.
    • (1997) Mayo Clin. Proc , vol.72 , pp. 532-542
    • Berbari, E.F.1    Cockerill III, F.R.2    Steckelberg, J.M.3
  • 8
    • 0034816350 scopus 로고    scopus 로고
    • Nonspecific adherence and fibril biogenesis by Actinobacillus actinomycetemcomitans: TadA protein is an ATPase
    • Bhattacharjee, M. K., S. C. Kachlany, D. H. Fine, and D. H. Figurski. 2001. Nonspecific adherence and fibril biogenesis by Actinobacillus actinomycetemcomitans: TadA protein is an ATPase. J. Bacteriol. 183:5927-5936.
    • (2001) J. Bacteriol , vol.183 , pp. 5927-5936
    • Bhattacharjee, M.K.1    Kachlany, S.C.2    Fine, D.H.3    Figurski, D.H.4
  • 10
    • 0028847858 scopus 로고
    • The comparative toxicity of nitric oxide and peroxynitrite to Escherichia coli
    • Brunelli, L., J. P. Crow, and J. S. Beckman. 1995. The comparative toxicity of nitric oxide and peroxynitrite to Escherichia coli. Arch. Biochem. Biophys. 316:327-334.
    • (1995) Arch. Biochem. Biophys , vol.316 , pp. 327-334
    • Brunelli, L.1    Crow, J.P.2    Beckman, J.S.3
  • 11
    • 0033980783 scopus 로고    scopus 로고
    • Taxonomy and virulence of oral spirochetes
    • Chan, E. C., and R. McLaughlin. 2000. Taxonomy and virulence of oral spirochetes. Oral Microbiol. Immunol. 15:1-9.
    • (2000) Oral Microbiol. Immunol , vol.15 , pp. 1-9
    • Chan, E.C.1    McLaughlin, R.2
  • 12
    • 0026816008 scopus 로고
    • Structural and functional relationships among the RTX toxin determinants of gram-negative bacteria
    • Coote, J. G. 1992. Structural and functional relationships among the RTX toxin determinants of gram-negative bacteria. FEMS Microbiol. Rev. 8:137-161.
    • (1992) FEMS Microbiol. Rev , vol.8 , pp. 137-161
    • Coote, J.G.1
  • 13
    • 33845881184 scopus 로고    scopus 로고
    • TdeA, a TolC-like protein required for toxin and drug export in Aggregatibacter (Actinobacillus) actinomycetemcomitans
    • Crosby, J. A., and S. C. Kachlany. 2007. TdeA, a TolC-like protein required for toxin and drug export in Aggregatibacter (Actinobacillus) actinomycetemcomitans. Gene 388:83-92.
    • (2007) Gene , vol.388 , pp. 83-92
    • Crosby, J.A.1    Kachlany, S.C.2
  • 15
    • 0037303720 scopus 로고    scopus 로고
    • Interaction of Actinobacillus actinomycetemcomitans outer membrane vesicles with HL60 cells does not require leukotoxin
    • Demuth, D. R., D. James, Y. Kowashi, and S. Kato. 2003. Interaction of Actinobacillus actinomycetemcomitans outer membrane vesicles with HL60 cells does not require leukotoxin. Cell. Microbiol. 5:111-121.
    • (2003) Cell. Microbiol , vol.5 , pp. 111-121
    • Demuth, D.R.1    James, D.2    Kowashi, Y.3    Kato, S.4
  • 17
    • 0029809008 scopus 로고    scopus 로고
    • The effects of calcium and other polyvalent cations on channel formation by Escherichia coli alpha-hemolysin in red blood cells and lipid bilayer membranes
    • Dobereiner, A., A. Schmid, A. Ludwig, W. Goebel, and R. Benz. 1996. The effects of calcium and other polyvalent cations on channel formation by Escherichia coli alpha-hemolysin in red blood cells and lipid bilayer membranes. Eur. J. Biochem. 240:454-460.
    • (1996) Eur. J. Biochem , vol.240 , pp. 454-460
    • Dobereiner, A.1    Schmid, A.2    Ludwig, A.3    Goebel, W.4    Benz, R.5
  • 18
  • 19
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
    • Esterbauer, H., R. J. Schaur, and H. Zollner. 1991. Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Radic. Biol. Med. 11:81-128.
    • (1991) Free Radic. Biol. Med , vol.11 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 20
  • 21
    • 0033386211 scopus 로고    scopus 로고
    • Tenacious adhesion of Actinobacillus actinomycetemcomitans strain CU1000 to salivary-coated hydroxyapatite
    • Fine, D. H., D. Furgang, J. Kaplan, J. Charlesworth, and D. H. Figurski. 1999. Tenacious adhesion of Actinobacillus actinomycetemcomitans strain CU1000 to salivary-coated hydroxyapatite. Arch. Oral Biol. 44:1063-1076.
    • (1999) Arch. Oral Biol , vol.44 , pp. 1063-1076
    • Fine, D.H.1    Furgang, D.2    Kaplan, J.3    Charlesworth, J.4    Figurski, D.H.5
  • 23
    • 33747830391 scopus 로고    scopus 로고
    • How we got attached to Actinobacillus actinomycetemcomitans: A model for infectious diseases
    • Fine, D. H., J. B. Kaplan, S. C. Kachlany, and H. C. Schreiner. 2006. How we got attached to Actinobacillus actinomycetemcomitans: a model for infectious diseases. Periodontol. 2000 42:114-157.
    • (2006) Periodontol. 2000 , vol.42 , pp. 114-157
    • Fine, D.H.1    Kaplan, J.B.2    Kachlany, S.C.3    Schreiner, H.C.4
  • 24
    • 0034953017 scopus 로고    scopus 로고
    • Analysis of the effect of changing environmental conditions on the expression patterns of exported surface-associated proteins of the oral pathogen Actinobacillus actinomycetemcomitans
    • Fletcher, J. M., S. P. Nair, J. M. Ward, B. Henderson, and M. Wilson. 2001. Analysis of the effect of changing environmental conditions on the expression patterns of exported surface-associated proteins of the oral pathogen Actinobacillus actinomycetemcomitans. Microb. Pathog. 30:359-368.
    • (2001) Microb. Pathog , vol.30 , pp. 359-368
    • Fletcher, J.M.1    Nair, S.P.2    Ward, J.M.3    Henderson, B.4    Wilson, M.5
  • 25
    • 0027165156 scopus 로고
    • The role and properties of the iron-sulfur cluster in Escherichia coli dihydroxy-acid dehydratase
    • Flint, D. H., M. H. Emptage, M. G. Finnegan, W. Fu, and M. K. Johnson. 1993. The role and properties of the iron-sulfur cluster in Escherichia coli dihydroxy-acid dehydratase. J. Biol. Chem. 268:14732- 14742.
    • (1993) J. Biol. Chem , vol.268 , pp. 14732-14742
    • Flint, D.H.1    Emptage, M.H.2    Finnegan, M.G.3    Fu, W.4    Johnson, M.K.5
  • 26
    • 0026011632 scopus 로고
    • Superoxide sensitivity of the Escherichia coli 6-phosphogluconate dehydratase
    • Gardner, P. R., and I. Fridovich. 1991. Superoxide sensitivity of the Escherichia coli 6-phosphogluconate dehydratase. J. Biol. Chem. 266:1478-1483.
    • (1991) J. Biol. Chem , vol.266 , pp. 1478-1483
    • Gardner, P.R.1    Fridovich, I.2
  • 27
    • 0026045587 scopus 로고
    • Superoxide sensitivity of the Escherichia coli aconitase
    • Gardner, P. R., and I. Fridovich. 1991. Superoxide sensitivity of the Escherichia coli aconitase. J. Biol. Chem. 266:19328-19333.
    • (1991) J. Biol. Chem , vol.266 , pp. 19328-19333
    • Gardner, P.R.1    Fridovich, I.2
  • 28
    • 0035181250 scopus 로고    scopus 로고
    • Emerging strategies in microbial haem capture
    • Genco, C. A., and D. W. Dixon. 2001. Emerging strategies in microbial haem capture. Mol. Microbiol. 39:1-11.
    • (2001) Mol. Microbiol , vol.39 , pp. 1-11
    • Genco, C.A.1    Dixon, D.W.2
  • 29
    • 0024195829 scopus 로고
    • Secretion of cyclolysin, the calmodulin-sensitive adenylate cyclase-haemolysin bifunctional protein of Bordetella pertussis
    • Glaser, P., H. Sakamoto, J. Bellalou, A. Ullmann, and A. Danchin. 1988. Secretion of cyclolysin, the calmodulin-sensitive adenylate cyclase-haemolysin bifunctional protein of Bordetella pertussis. EMBO J. 7:3997-4004.
    • (1988) EMBO J , vol.7 , pp. 3997-4004
    • Glaser, P.1    Sakamoto, H.2    Bellalou, J.3    Ullmann, A.4    Danchin, A.5
  • 30
    • 0027565977 scopus 로고
    • The role of induced virulence factors produced by Pasteurella haemolytica in the pathogenesis of bovine pneumonic pasteurellosis: Review and hypotheses
    • Gonzalez, C. T., and S. K. Maheswaran. 1993. The role of induced virulence factors produced by Pasteurella haemolytica in the pathogenesis of bovine pneumonic pasteurellosis: review and hypotheses. Br. Vet. J. 149:183-193.
    • (1993) Br. Vet. J , vol.149 , pp. 183-193
    • Gonzalez, C.T.1    Maheswaran, S.K.2
  • 31
    • 0030832571 scopus 로고    scopus 로고
    • Interaction between Actinobacillus actinomycetemcomitans lipopolysaccharides and human hemoglobin
    • Grenier, D., A. Leduc, and D. Mayrand. 1997. Interaction between Actinobacillus actinomycetemcomitans lipopolysaccharides and human hemoglobin. FEMS Microbiol. Lett. 151:77-81.
    • (1997) FEMS Microbiol. Lett , vol.151 , pp. 77-81
    • Grenier, D.1    Leduc, A.2    Mayrand, D.3
  • 32
    • 0029152281 scopus 로고
    • Mutational analysis of the putative leukotoxin transport genes in Actinobacillus actinomycetemcomitans
    • Guthmiller, J. M., D. Kolodrubetz, and E. Kraig. 1995. Mutational analysis of the putative leukotoxin transport genes in Actinobacillus actinomycetemcomitans. Microb. Pathog. 18:307-321.
    • (1995) Microb. Pathog , vol.18 , pp. 307-321
    • Guthmiller, J.M.1    Kolodrubetz, D.2    Kraig, E.3
  • 33
    • 0032984036 scopus 로고    scopus 로고
    • Identification and molecular analysis of rough-colony-specific outer membrane proteins of Actinobacillus actinomycetemcomitans
    • Haase, E. M., J. L. Zmuda, and F. A. Scannapieco. 1999. Identification and molecular analysis of rough-colony-specific outer membrane proteins of Actinobacillus actinomycetemcomitans. Infect. Immun. 67:2901-2908.
    • (1999) Infect. Immun , vol.67 , pp. 2901-2908
    • Haase, E.M.1    Zmuda, J.L.2    Scannapieco, F.A.3
  • 34
    • 0029048241 scopus 로고
    • Hemolytic, but not cell-invasive activity, of adenylate cyclase toxin is selectively affected by differential fatty-acylation in Escherichia coli
    • Hackett, M., C. B. Walker, L. Guo, M. C. Gray, S. Van Cuyk, A. Ullmann, J. Shabanowitz, D. F. Hunt, E. L. Hewlett, and P. Sebo. 1995. Hemolytic, but not cell-invasive activity, of adenylate cyclase toxin is selectively affected by differential fatty-acylation in Escherichia coli. J. Biol. Chem. 270:20250-20253.
    • (1995) J. Biol. Chem , vol.270 , pp. 20250-20253
    • Hackett, M.1    Walker, C.B.2    Guo, L.3    Gray, M.C.4    Van Cuyk, S.5    Ullmann, A.6    Shabanowitz, J.7    Hunt, D.F.8    Hewlett, E.L.9    Sebo, P.10
  • 35
    • 0021759809 scopus 로고
    • Free radicals, lipid peroxidation, and cell damage
    • Halliwell, B., and J. M. Gutteridge. 1984. Free radicals, lipid peroxidation, and cell damage. Lancet 2:1095.
    • (1984) Lancet , vol.2 , pp. 1095
    • Halliwell, B.1    Gutteridge, J.M.2
  • 36
    • 0036947622 scopus 로고    scopus 로고
    • Differences in iron acquisition from human haemoglobin among strains of Actinobacillus actinomycetemcomitans
    • Hayashida, H., K. Poulsen, and M. Kilian. 2002. Differences in iron acquisition from human haemoglobin among strains of Actinobacillus actinomycetemcomitans. Microbiology 148:3993-4001.
    • (2002) Microbiology , vol.148 , pp. 3993-4001
    • Hayashida, H.1    Poulsen, K.2    Kilian, M.3
  • 37
    • 0242693180 scopus 로고    scopus 로고
    • Molecular pathogenicity of the oral opportunistic pathogen Actinobacillus actinomycetemcomitans
    • Henderson, B., S. P. Nair, J. M. Ward, and M. Wilson. 2003. Molecular pathogenicity of the oral opportunistic pathogen Actinobacillus actinomycetemcomitans. Annu. Rev. Microbiol. 57:29-55.
    • (2003) Annu. Rev. Microbiol , vol.57 , pp. 29-55
    • Henderson, B.1    Nair, S.P.2    Ward, J.M.3    Wilson, M.4
  • 38
    • 0029111530 scopus 로고
    • Oxidative DNA damage induced by simultaneous generation of nitric oxide and superoxide
    • Inoue, S., and S. Kawanishi. 1995. Oxidative DNA damage induced by simultaneous generation of nitric oxide and superoxide. FEBS Lett. 371:86-88.
    • (1995) FEBS Lett , vol.371 , pp. 86-88
    • Inoue, S.1    Kawanishi, S.2
  • 39
    • 0029039754 scopus 로고
    • Peroxynitrite- mediated oxidative protein modifications
    • Ischiropoulos, H., and A. B. al-Mehdi. 1995. Peroxynitrite- mediated oxidative protein modifications. FEBS Lett. 364:279-282.
    • (1995) FEBS Lett , vol.364 , pp. 279-282
    • Ischiropoulos, H.1    al-Mehdi, A.B.2
  • 40
    • 0026453418 scopus 로고
    • Peroxynitrite formation from macrophage-derived nitric oxide
    • Ischiropoulos, H., L. Zhu, and J. S. Beckman. 1992. Peroxynitrite formation from macrophage-derived nitric oxide. Arch. Biochem. Biophys. 298:446-451.
    • (1992) Arch. Biochem. Biophys , vol.298 , pp. 446-451
    • Ischiropoulos, H.1    Zhu, L.2    Beckman, J.S.3
  • 41
    • 0027317892 scopus 로고
    • Expression of an iron-regulated hemolysin by Edwardsiella tarda
    • Janda, J. M., and S. L. Abbott. 1993. Expression of an iron-regulated hemolysin by Edwardsiella tarda. FEMS Microbiol. Lett. 111:275-280.
    • (1993) FEMS Microbiol. Lett , vol.111 , pp. 275-280
    • Janda, J.M.1    Abbott, S.L.2
  • 43
    • 0042012705 scopus 로고    scopus 로고
    • Serum-mediated release of leukotoxin from the cell surface of the periodontal pathogen Actinobacillus actinomycetemcomitans
    • Johansson, A., R. Claesson, L. Hanstrom, and S. Kalfas. 2003. Serum-mediated release of leukotoxin from the cell surface of the periodontal pathogen Actinobacillus actinomycetemcomitans. Eur. J. Oral Sci. 111:209-215.
    • (2003) Eur. J. Oral Sci , vol.111 , pp. 209-215
    • Johansson, A.1    Claesson, R.2    Hanstrom, L.3    Kalfas, S.4
  • 44
    • 0036411760 scopus 로고    scopus 로고
    • Purification of secreted leukotoxin (LtxA) from Actinobacillus actinomycetemcomitans
    • Kachlany, S. C., D. H. Fine, and D. H. Figurski. 2002. Purification of secreted leukotoxin (LtxA) from Actinobacillus actinomycetemcomitans. Protein Expr. Purif. 25:465-471.
    • (2002) Protein Expr. Purif , vol.25 , pp. 465-471
    • Kachlany, S.C.1    Fine, D.H.2    Figurski, D.H.3
  • 45
    • 0033784510 scopus 로고    scopus 로고
    • Secretion of RTX leukotoxin by Actinobacillus actinomycetemcomitans
    • Kachlany, S. C., D. H. Fine, and D. H. Figurski. 2000. Secretion of RTX leukotoxin by Actinobacillus actinomycetemcomitans. Infect. Immun. 68:6094-6100.
    • (2000) Infect. Immun , vol.68 , pp. 6094-6100
    • Kachlany, S.C.1    Fine, D.H.2    Figurski, D.H.3
  • 46
    • 0033758854 scopus 로고    scopus 로고
    • Nonspecific adherence by Actinobacillus actinomycetemcomitans requires genes widespread in bacteria and archaea
    • Kachlany, S. C., P. J. Planet, M. K. Bhattacharjee, E. Kollia, R. DeSalle, D. H. Fine, and D. H. Figurski. 2000. Nonspecific adherence by Actinobacillus actinomycetemcomitans requires genes widespread in bacteria and archaea. J. Bacteriol. 182:6169-6176.
    • (2000) J. Bacteriol , vol.182 , pp. 6169-6176
    • Kachlany, S.C.1    Planet, P.J.2    Bhattacharjee, M.K.3    Kollia, E.4    DeSalle, R.5    Fine, D.H.6    Figurski, D.H.7
  • 47
    • 0036208842 scopus 로고    scopus 로고
    • Population structure and genetic diversity of Actinobacillus actinomycetemcomitans strains isolated from localized juvenile periodontitis patients
    • Kaplan, J. B., H. C. Schreiner, D. Furgang, and D. H. Fine. 2002. Population structure and genetic diversity of Actinobacillus actinomycetemcomitans strains isolated from localized juvenile periodontitis patients. J. Clin. Microbiol. 40:1181-1187.
    • (2002) J. Clin. Microbiol , vol.40 , pp. 1181-1187
    • Kaplan, J.B.1    Schreiner, H.C.2    Furgang, D.3    Fine, D.H.4
  • 48
    • 33749017348 scopus 로고    scopus 로고
    • Detection and quantification of superoxide formed within the periplasm of Escherichia coli
    • Korshunov, S., and J. A. Imlay. 2006. Detection and quantification of superoxide formed within the periplasm of Escherichia coli. J. Bacteriol. 188:6326-6334.
    • (2006) J. Bacteriol , vol.188 , pp. 6326-6334
    • Korshunov, S.1    Imlay, J.A.2
  • 49
    • 0025885796 scopus 로고
    • Copper-zinc superoxide dismutase of Haemophilus influenzae and H. parainfluenzae
    • Kroll, J. S., P. R. Langford, and B. M. Loynds. 1991. Copper-zinc superoxide dismutase of Haemophilus influenzae and H. parainfluenzae. J. Bacteriol. 173:7449-7457.
    • (1991) J. Bacteriol , vol.173 , pp. 7449-7457
    • Kroll, J.S.1    Langford, P.R.2    Loynds, B.M.3
  • 52
    • 0029806690 scopus 로고    scopus 로고
    • Cloning and molecular characterization of Cu,Zn superoxide dismutase from Actinobacillus pleuropneumoniae
    • Langford, P. R., B. M. Loynds, and J. S. Kroll. 1996. Cloning and molecular characterization of Cu,Zn superoxide dismutase from Actinobacillus pleuropneumoniae. Infect. Immun. 64:5035-5041.
    • (1996) Infect. Immun , vol.64 , pp. 5035-5041
    • Langford, P.R.1    Loynds, B.M.2    Kroll, J.S.3
  • 53
    • 0032855431 scopus 로고    scopus 로고
    • Hemoglobinase activity of the lysine gingipain protease (Kgp) of Porphyromonas gingivalis W83
    • Lewis, J. P., J. A. Dawson, J. C. Hannis, D. Muddiman, and F. L. Macrina. 1999. Hemoglobinase activity of the lysine gingipain protease (Kgp) of Porphyromonas gingivalis W83. J. Bacteriol. 181:4905-4913.
    • (1999) J. Bacteriol , vol.181 , pp. 4905-4913
    • Lewis, J.P.1    Dawson, J.A.2    Hannis, J.C.3    Muddiman, D.4    Macrina, F.L.5
  • 54
    • 0029812094 scopus 로고    scopus 로고
    • Analysis of the in vivo activation of hemolysin (HlyA) from Escherichia coli
    • Ludwig, A., F. Garcia, S. Bauer, T. Jarchau, R. Benz, J. Hoppe, and W. Goebel. 1996. Analysis of the in vivo activation of hemolysin (HlyA) from Escherichia coli. J. Bacteriol. 178:5422-5430.
    • (1996) J. Bacteriol , vol.178 , pp. 5422-5430
    • Ludwig, A.1    Garcia, F.2    Bauer, S.3    Jarchau, T.4    Benz, R.5    Hoppe, J.6    Goebel, W.7
  • 55
    • 0033914179 scopus 로고    scopus 로고
    • Dangerous signals from E. coli toxin
    • Ludwig, A., and W. Goebel. 2000. Dangerous signals from E. coli toxin. Nat. Med. 6:741-742.
    • (2000) Nat. Med , vol.6 , pp. 741-742
    • Ludwig, A.1    Goebel, W.2
  • 56
    • 0024116495 scopus 로고
    • The repeat domain of Escherichia coli haemolysin (HlyA) is responsible for its Ca2+-dependent binding to erythrocytes
    • Ludwig, A., T. Jarchau, R. Benz, and W. Goebel. 1988. The repeat domain of Escherichia coli haemolysin (HlyA) is responsible for its Ca2+-dependent binding to erythrocytes. Mol. Gen. Genet. 214:553-561.
    • (1988) Mol. Gen. Genet , vol.214 , pp. 553-561
    • Ludwig, A.1    Jarchau, T.2    Benz, R.3    Goebel, W.4
  • 57
    • 0033535371 scopus 로고    scopus 로고
    • Lipid peroxidation-DNA damage by malondialdehyde
    • Marnett, L. J. 1999. Lipid peroxidation-DNA damage by malondialdehyde. Mutat. Res. 424:83-95.
    • (1999) Mutat. Res , vol.424 , pp. 83-95
    • Marnett, L.J.1
  • 58
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • McCord, J. M., and I. Fridovich. 1969. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244:6049-6055.
    • (1969) J. Biol. Chem , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 59
    • 0028819525 scopus 로고
    • The binding of divalent cations to Escherichia coli alpha-haemolysin
    • Ostolaza, H., A. Soloaga, and F. M. Goni. 1995. The binding of divalent cations to Escherichia coli alpha-haemolysin. Eur. J. Biochem. 228:39-44.
    • (1995) Eur. J. Biochem , vol.228 , pp. 39-44
    • Ostolaza, H.1    Soloaga, A.2    Goni, F.M.3
  • 61
    • 0034917354 scopus 로고    scopus 로고
    • Cu,Zn superoxide dismutase of Mycobacterium tuberculosis contributes to survival in activated macrophages that are generating an oxidative burst
    • Piddington, D. L., F. C. Fang, T. Laessig, A. M. Cooper, I. M. Orme, and N. A. Buchmeier. 2001. Cu,Zn superoxide dismutase of Mycobacterium tuberculosis contributes to survival in activated macrophages that are generating an oxidative burst. Infect. Immun. 69:4980-4987.
    • (2001) Infect. Immun , vol.69 , pp. 4980-4987
    • Piddington, D.L.1    Fang, F.C.2    Laessig, T.3    Cooper, A.M.4    Orme, I.M.5    Buchmeier, N.A.6
  • 62
    • 19744370552 scopus 로고    scopus 로고
    • Genetic and functional analyses of the Actinobacillus actinomycetemcomitans AfeABCD siderophore-independent iron acquisition system
    • Rhodes, E. R., A. P. Tomaras, G. McGillivary, P. L. Connerly, and L. A. Actis. 2005. Genetic and functional analyses of the Actinobacillus actinomycetemcomitans AfeABCD siderophore-independent iron acquisition system. Infect. Immun. 73:3758-3763.
    • (2005) Infect. Immun , vol.73 , pp. 3758-3763
    • Rhodes, E.R.1    Tomaras, A.P.2    McGillivary, G.3    Connerly, P.L.4    Actis, L.A.5
  • 64
    • 0033929390 scopus 로고    scopus 로고
    • Cu,Zn]-superoxide dismutase mutants of the swine pathogen Actinobacillus pleuropneumoniae are unattenuated in infections of the natural host
    • Sheehan, B. J., P. R. Langford, A. N. Rycroft, and J. S. Kroll. 2000. [Cu,Zn]-superoxide dismutase mutants of the swine pathogen Actinobacillus pleuropneumoniae are unattenuated in infections of the natural host. Infect. Immun. 68:4778-4781.
    • (2000) Infect. Immun , vol.68 , pp. 4778-4781
    • Sheehan, B.J.1    Langford, P.R.2    Rycroft, A.N.3    Kroll, J.S.4
  • 65
    • 2342518271 scopus 로고    scopus 로고
    • Role of oxidant species in aging
    • Stadtman, E. R. 2004. Role of oxidant species in aging. Curr. Med. Chem. 11:1105-1112.
    • (2004) Curr. Med. Chem , vol.11 , pp. 1105-1112
    • Stadtman, E.R.1
  • 66
    • 0031596205 scopus 로고    scopus 로고
    • Acylation of Escherichia coli hemolysin: A unique protein lipidation mechanism underlying toxin function
    • Stanley, P., V. Koronakis, and C. Hughes. 1998. Acylation of Escherichia coli hemolysin: a unique protein lipidation mechanism underlying toxin function. Microbiol. Mol. Biol. Rev. 62:309-333.
    • (1998) Microbiol. Mol. Biol. Rev , vol.62 , pp. 309-333
    • Stanley, P.1    Koronakis, V.2    Hughes, C.3
  • 67
    • 0018827360 scopus 로고
    • Biochemical and morphological characterization of the killing of human monocytes by a leukotoxin derived from Actinobacillus actinomycetemcomitans
    • Taichman, N. S., R. T. Dean, and C. J. Sanderson. 1980. Biochemical and morphological characterization of the killing of human monocytes by a leukotoxin derived from Actinobacillus actinomycetemcomitans. Infect. Immun. 28:258-268.
    • (1980) Infect. Immun , vol.28 , pp. 258-268
    • Taichman, N.S.1    Dean, R.T.2    Sanderson, C.J.3
  • 69
    • 0019433957 scopus 로고
    • Leukotoxicity of an extract from Actinobacillus actinomycetemcomitans for human gingival polymorphonuclear leukocytes
    • Taichman, N. S., and J. M. Wilton. 1981. Leukotoxicity of an extract from Actinobacillus actinomycetemcomitans for human gingival polymorphonuclear leukocytes. Inflammation 5:1-12.
    • (1981) Inflammation , vol.5 , pp. 1-12
    • Taichman, N.S.1    Wilton, J.M.2
  • 70
    • 0032720316 scopus 로고    scopus 로고
    • Direct selection of IS903 transposon insertions by use of a broad-host-range vector: Isolation of catalase-deficient mutants of Actinobacillus actinomycetemcomitans
    • Thomson, V. J., M. K. Bhattacharjee, D. H. Fine, K. M. Derbyshire, and D. H. Figurski. 1999. Direct selection of IS903 transposon insertions by use of a broad-host-range vector: isolation of catalase-deficient mutants of Actinobacillus actinomycetemcomitans. J. Bacteriol. 181:7298-7307.
    • (1999) J. Bacteriol , vol.181 , pp. 7298-7307
    • Thomson, V.J.1    Bhattacharjee, M.K.2    Fine, D.H.3    Derbyshire, K.M.4    Figurski, D.H.5
  • 71
    • 0021349420 scopus 로고
    • Extraction and isolation of a leukotoxin from Actinobacillus actinomycetemcomitans with polymyxin B
    • Tsai, C. C., B. J. Shenker, J. M. DiRienzo, D. Malamud, and N. S. Taichman. 1984. Extraction and isolation of a leukotoxin from Actinobacillus actinomycetemcomitans with polymyxin B. Infect. Immun. 43:700-705.
    • (1984) Infect. Immun , vol.43 , pp. 700-705
    • Tsai, C.C.1    Shenker, B.J.2    DiRienzo, J.M.3    Malamud, D.4    Taichman, N.S.5
  • 72
    • 32444433202 scopus 로고    scopus 로고
    • Free radicals, metals and antioxidants in oxidative stress-induced cancer
    • Valko, M., C. J. Rhodes, J. Moncol, M. Izakovic, and M. Mazur. 2006. Free radicals, metals and antioxidants in oxidative stress-induced cancer. Chem. Biol. Interact. 160:1-40.
    • (2006) Chem. Biol. Interact , vol.160 , pp. 1-40
    • Valko, M.1    Rhodes, C.J.2    Moncol, J.3    Izakovic, M.4    Mazur, M.5
  • 73
    • 0036282335 scopus 로고    scopus 로고
    • Natural transformation and DNA uptake signal sequences in Actinobacillus actinomycetemcomitans
    • Wang, Y., S. D. Goodman, R. J. Redfield, and C. Chen. 2002. Natural transformation and DNA uptake signal sequences in Actinobacillus actinomycetemcomitans. J. Bacteriol. 184:3442-3449.
    • (2002) J. Bacteriol , vol.184 , pp. 3442-3449
    • Wang, Y.1    Goodman, S.D.2    Redfield, R.J.3    Chen, C.4
  • 74
    • 0034467679 scopus 로고    scopus 로고
    • RTX toxin structure and function: A story of numerous anomalies and few analogies in toxin biology
    • Welch, R. A. 2001. RTX toxin structure and function: a story of numerous anomalies and few analogies in toxin biology. Curr. Top. Microbiol. Immunol. 257:85-111.
    • (2001) Curr. Top. Microbiol. Immunol , vol.257 , pp. 85-111
    • Welch, R.A.1
  • 76
    • 0035210384 scopus 로고    scopus 로고
    • Maintenance of oxidative phosphorylation protects cells from Actinobacillus actinomycetemcomitans leukotoxin-induced apoptosis
    • Yamaguchi, N., I. R. Kieba, J. Korostoff, P. S. Howard, B. J. Shenker, and E. T. Lally. 2001. Maintenance of oxidative phosphorylation protects cells from Actinobacillus actinomycetemcomitans leukotoxin-induced apoptosis. Cell. Microbiol. 3:811-823.
    • (2001) Cell. Microbiol , vol.3 , pp. 811-823
    • Yamaguchi, N.1    Kieba, I.R.2    Korostoff, J.3    Howard, P.S.4    Shenker, B.J.5    Lally, E.T.6
  • 77
    • 0021911144 scopus 로고
    • Actinobacillus actinomycetemcomitans in human periodontal disease
    • Zambon, J. J. 1985. Actinobacillus actinomycetemcomitans in human periodontal disease. J. Clin. Periodontol. 12:1-20.
    • (1985) J. Clin. Periodontol , vol.12 , pp. 1-20
    • Zambon, J.J.1
  • 78


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