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Volumn 43, Issue 24, 2009, Pages 9465-9472

Microarray analysis of Mycobacterium bovis BCG revealed induction of iron acquisition related genes in response to hydrogen peroxide

Author keywords

[No Author keywords available]

Indexed keywords

CELL CYCLE CONTROL; CELL METABOLISM; DEFENSE MECHANISM; DNA REPLICATIONS; DOWN-REGULATION; IRON ACQUISITION; IRON METABOLISM; LIPID TRANSPORT; MICROARRAY ANALYSIS; MYCOBACTERIUM BOVIS; OXIDATIVE STRESS RESPONSE; UP-REGULATION;

EID: 72849139871     PISSN: 0013936X     EISSN: 15205851     Source Type: Journal    
DOI: 10.1021/es902255q     Document Type: Article
Times cited : (14)

References (79)
  • 1
    • 0033586425 scopus 로고    scopus 로고
    • Post, DOTS. post genomics: The next century of tuberculosis control
    • Pym, A. S.; Cole, S. T.; Post, DOTS. post genomics: the next century of tuberculosis control. Lancet 1999, 353, 1004-1005.
    • (1999) Lancet , vol.353 , pp. 1004-1005
    • Pym, A.S.1    Cole, S.T.2
  • 2
    • 0037841362 scopus 로고    scopus 로고
    • The global situation of MDR-TB
    • Edinb
    • Espinal, M. A. The global situation of MDR-TB. Tuberculosis (Edinb) 2003, 83, 44-51.
    • (2003) Tuberculosis , vol.83 , pp. 44-51
    • Espinal, M.A.1
  • 5
    • 0027963346 scopus 로고
    • Stimulation or inhibition of the respiratory burst in cultured macrophages in a mycobacterium model: Initial stimulation is followed by inhibition after phagocytosis
    • Gordon, A. H.; Hart, P. D. Stimulation or inhibition of the respiratory burst in cultured macrophages in a mycobacterium model: Initial stimulation is followed by inhibition after phagocytosis. Infect. Immun. 1994, 62, 4650-4651.
    • (1994) Infect. Immun. , vol.62 , pp. 4650-4651
    • Gordon, A.H.1    Hart, P.D.2
  • 6
    • 0033039677 scopus 로고    scopus 로고
    • Growth of Mycobacterium bovis, Bacille Calmette-Guerin, within human monocytes-macrophages cultured in serum-free medium
    • Lamhamedi-Cherradi, S.; de Chastellier, C.; Casanova, J. L. Growth of Mycobacterium bovis, Bacille Calmette-Guerin, within human monocytes-macrophages cultured in serum-free medium. J. Immunol. Methods 1999, 225, 75-86.
    • (1999) J. Immunol. Methods , vol.225 , pp. 75-86
    • Lamhamedi-Cherradi, S.1    De Chastellier, C.2    Casanova, J.L.3
  • 8
    • 0037344575 scopus 로고    scopus 로고
    • Mechanisms of iron regulation in mycobacteria: Role in physiology and virulence
    • DOI 10.1046/j.1365-2958.2003.03384.x
    • Rodriguez, G. M.; Smith, I. Mechanisms of iron regulation in mycobacteria: Role in physiology and virulence. Mol. Microbiol. 2003, 47, 1485-1494. (Pubitemid 36363334)
    • (2003) Molecular Microbiology , vol.47 , Issue.6 , pp. 1485-1494
    • Rodriguez, G.M.1    Smith, I.2
  • 9
    • 0031783529 scopus 로고    scopus 로고
    • Analysis of the exochelin locus in Mycobacterium smegmatis: Biosynthesis genes have homology with genes of the peptide synthetase family
    • Yu, S.; Fiss, E.; Jacobs, W. R., Jr. Analysis of the exochelin locus in Mycobacterium smegmatis: Biosynthesis genes havehomology with genes of the peptide synthetase family. J. Bacteriol. 1998, 180, 4676-4685. (Pubitemid 28405597)
    • (1998) Journal of Bacteriology , vol.180 , Issue.17 , pp. 4676-4685
    • Yu, S.1    Fiss, E.2    Jacobs Jr., W.R.3
  • 10
    • 0033973479 scopus 로고    scopus 로고
    • The salicylate-derived mycobactin siderophores of Mycobacterium tuberculosis are essential for growth in macrophages
    • De Voss, J. J.; Rutter, K.; Schroeder, B. G.; Su, H.; Zhu, Y.; Barry, C. E., 3rd. The salicylate-derived mycobactin siderophores of Mycobacterium tuberculosis are essential for growth in macrophages. Proc. Natl. Acad. Sci. U. S. A. 2000, 97, 1252-1257.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 1252-1257
    • De Voss, J.J.1    Rutter, K.2    Schroeder, B.G.3    Su, H.4    Zhu, Y.5    Barry III, C.E.6
  • 12
    • 0036081140 scopus 로고    scopus 로고
    • IdeR, An essential gene in Mycobacterium tuberculosis: Role of IdeR in iron-dependent gene expression, iron metabolism, and oxidative stress response
    • Rodriguez, G. M.; Voskuil, M. I.; Gold, B.; Schoolnik, G. K.; Smith, I. ideR, An essential gene in Mycobacterium tuberculosis: role of IdeR in iron-dependent gene expression, iron metabolism, and oxidative stress response. Infect. Immun. 2002, 70, 3371-3381.
    • (2002) Infect. Immun. , vol.70 , pp. 3371-3381
    • Rodriguez, G.M.1    Voskuil, M.I.2    Gold, B.3    Schoolnik, G.K.4    Smith, I.5
  • 13
    • 33846190647 scopus 로고    scopus 로고
    • Crystal structures, metal activation, and DNA-binding properties of two-domain IdeR from Mycobacterium tuberculosis
    • Wisedchaisri, G.; Chou, C. J.; Wu, M.; Roach, C.; Rice, A. E.; Holmes, R. K.; Beeson, C.; Hol, W. G. Crystal structures, metal activation, and DNA-binding properties of two-domain IdeR from Mycobacterium tuberculosis. Biochemistry 2007, 46, 436-447.
    • (2007) Biochemistry , vol.46 , pp. 436-447
    • Wisedchaisri, G.1    Chou, C.J.2    Wu, M.3    Roach, C.4    Rice, A.E.5    Holmes, R.K.6    Beeson, C.7    Hol, W.G.8
  • 14
    • 0035164513 scopus 로고    scopus 로고
    • Transcriptional regulation of furA and katG upon oxidative stress in Mycobacterium smegmatis
    • DOI 10.1128/JB.183.23.6801-6806.2001
    • Milano, A.; Forti, F.; Sala, C.; Riccardi, G.; Ghisotti, D. Transcriptional regulation of furA and katG upon oxidative stress in Mycobacterium smegmatis. J. Bacteriol. 2001, 183, 6801-6806. (Pubitemid 33064193)
    • (2001) Journal of Bacteriology , vol.183 , Issue.23 , pp. 6801-6806
    • Milano, A.1    Forti, F.2    Sala, C.3    Riccardi, G.4    Ghisotti, D.5
  • 15
    • 0035100597 scopus 로고    scopus 로고
    • Mycobacterial FurA is a negative regulator of catalase-peroxidase gene katG
    • DOI 10.1046/j.1365-2958.2001.02321.x
    • Zahrt, T. C.; Song, J.; Siple, J.; Deretic, V. Mycobacterial FurA is a negative regulator of catalase-peroxidase gene katG. Mol. Microbiol. 2001, 39, 1174-1185. (Pubitemid 32225129)
    • (2001) Molecular Microbiology , vol.39 , Issue.5 , pp. 1174-1185
    • Zahrt, T.C.1    Song, J.2    Siple, J.3    Deretic, V.4
  • 16
    • 0017618295 scopus 로고
    • Virulence-associated acquisition of iron in mammalian serum by Escherichia coli
    • Kochan, I.; Kvach, J. T.; Wiles, T. I. Virulence-associated acquisition of iron in mammalian serum by Escherichia coli. J. Infect. Dis. 1977, 135, 623-632.
    • (1977) J. Infect. Dis. , vol.135 , pp. 623-632
    • Kochan, I.1    Kvach, J.T.2    Wiles, T.I.3
  • 18
    • 0033137082 scopus 로고    scopus 로고
    • The role of iron in protozoan and fungal infectious diseases
    • Weinberg, E. D. The role of iron in protozoan and fungal infectious diseases. J. Eukaryotic Microbiol 1999, 46, 231-238. (Pubitemid 29284923)
    • (1999) Journal of Eukaryotic Microbiology , vol.46 , Issue.3 , pp. 231-238
    • Weinberg, E.D.1
  • 19
    • 0022637734 scopus 로고
    • Iron, infection, and neoplasia
    • Weinberg, E. D. Iron, infection, and neoplasia. Clin. Physiol. Biochem. 1986, 4, 50-60.
    • (1986) Clin. Physiol. Biochem. , vol.4 , pp. 50-60
    • Weinberg, E.D.1
  • 20
    • 67650869356 scopus 로고    scopus 로고
    • Efficacy of detergents and fresh produce disinfectants against microorganisms associated with mixed raw vegetables
    • Samadi, N.; Abadian, N.; Bakhtiari, D.; Fazeli, M. R.; Jamalifar, H. Efficacy of detergents and fresh produce disinfectants against microorganisms associated with mixed raw vegetables. J. Food Prot. 2009, 72, 1486-1490.
    • (2009) J. Food Prot. , vol.72 , pp. 1486-1490
    • Samadi, N.1    Abadian, N.2    Bakhtiari, D.3    Fazeli, M.R.4    Jamalifar, H.5
  • 21
    • 67650090954 scopus 로고    scopus 로고
    • Inactivation of Listeria monocytogenes, Escherichia coli O157:H7, and Salmonella typhimurium with compounds available in households
    • Yang, H.; Kendall, P. A.; Medeiros, L.; Sofos, J. N. Inactivation of Listeria monocytogenes, Escherichia coli O157:H7, and Salmonella typhimurium with compounds available in households. J. Food Prot. 2009, 72, 1201-1208.
    • (2009) J. Food Prot. , vol.72 , pp. 1201-1208
    • Yang, H.1    Kendall, P.A.2    Medeiros, L.3    Sofos, J.N.4
  • 22
    • 0033120542 scopus 로고    scopus 로고
    • Effect of hydrogen peroxide disinfection during incubation of chicken eggs on microbial levels and productivity
    • Sander, J. E.; Wilson, J. L. Effect of hydrogen peroxide disinfection during incubation of chicken eggs on microbial levels and productivity. Avian Dis. 1999, 43, 227-233.
    • (1999) Avian Dis , vol.43 , pp. 227-233
    • Sander, J.E.1    Wilson, J.L.2
  • 23
    • 0031029702 scopus 로고    scopus 로고
    • Role of oxidants in microbial pathophysiology
    • Miller, R. A.; Britigan, B. E. Role of oxidants in microbial pathophysiology. Clin. Microbiol. Rev. 1997, 10, 1-18.
    • (1997) Clin. Microbiol. Rev. , vol.10 , pp. 1-18
    • Miller, R.A.1    Britigan, B.E.2
  • 24
    • 0031935122 scopus 로고    scopus 로고
    • B. G. R. B. B. E. Endogenous superoxide dismutase levels regulate iron-dependent hydroxyl radical formation in Escherichia coli exposed to hydrogen peroxide
    • McCormick Ml, B. G. R. B. B. E. Endogenous superoxide dismutase levels regulate iron-dependent hydroxyl radical formation in Escherichia coli exposed to hydrogen peroxide. J. Bacteriol. 1998, 180, 622-625.
    • (1998) J. Bacteriol. , vol.180 , pp. 622-625
    • Ml, M.1
  • 25
    • 0028871420 scopus 로고
    • Superoxide and the production of oxidative DNA damage
    • Keyer, K.; Gort, A. S.; Imlay, J. A. Superoxide and the production of oxidative DNA damage. J. Bacteriol. 1995, 177, 6782-6790.
    • (1995) J. Bacteriol. , vol.177 , pp. 6782-6790
    • Keyer, K.1    Gort, A.S.2    Imlay, J.A.3
  • 26
    • 0030465238 scopus 로고    scopus 로고
    • Superoxide accelerates DNA damage by elevating free-iron levels
    • Keyer, K.; Imlay, J. A. Superoxide accelerates DNA damage by elevating free-iron levels. Proc. Natl. Acad. Sci. U. S. A. 1996, 93, 13635-13640.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 13635-13640
    • Keyer, K.1    Imlay, J.A.2
  • 27
    • 0242608621 scopus 로고    scopus 로고
    • Pathways of oxidative damage
    • Imlay, J. A. Pathways of oxidative damage. Annu. Rev. Microbiol. 2003, 57, 395-418.
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 395-418
    • Imlay, J.A.1
  • 28
    • 50849145229 scopus 로고    scopus 로고
    • The metaldependent regulators FurA and FurB from Mycobacterium tuberculosis
    • Lucarelli, D.; Vasil, M. L.; Meyer-Klaucke, W.; Pohl, E. The metaldependent regulators FurA and FurB from Mycobacterium tuberculosis. Int. J. Mo.l Sci. 2008, 9, 1548-1560.
    • (2008) Int. J. Mo.l Sci. , vol.9 , pp. 1548-1560
    • Lucarelli, D.1    Vasil, M.L.2    Meyer-Klaucke, W.3    Pohl, E.4
  • 29
    • 32444433730 scopus 로고    scopus 로고
    • Global transcriptome analysis of Staphylococcus aureus response to hydrogen peroxide
    • DOI 10.1109/TPWRD.2006.875859
    • Chang, W.; Small, D. A.; Toghrol, F.; Bentley, W. E. Global transcriptome analysis of Staphylococcus aureus response to hydrogen peroxide. J. Bacteriol. 2006, 188, 1648-1659. (Pubitemid 43228700)
    • (2006) Journal of Bacteriology , vol.188 , Issue.4 , pp. 1648-1659
    • Chang, W.1    Small, D.A.2    Toghrol, F.3    Bentley, W.E.4
  • 30
    • 25444502996 scopus 로고    scopus 로고
    • Microarray analysis of Pseudomonas aeruginosa reveals induction of pyocin genes in response to hydrogen peroxide
    • Chang, W.; Small, D. A.; Toghrol, F.; Bentley, W. E. Microarray analysis of Pseudomonas aeruginosa reveals induction of pyocin genes in response to hydrogen peroxide. BMC Genomics 2005, 6, 115.
    • (2005) BMC Genomics , vol.6 , pp. 115
    • Chang, W.1    Small, D.A.2    Toghrol, F.3    Bentley, W.E.4
  • 31
    • 22144483734 scopus 로고    scopus 로고
    • Thiol specific oxidative stress response in Mycobacteria
    • DOI 10.1016/j.femsle.2005.06.004, PII S0378109705003800
    • Dosanjh, N. S.; Rawat, M.; Chung, J. H.; Av-Gay, Y. Thiol specific oxidative stress response in mycobacteria.FEMSMicrobiol. Lett. 2005, 249, 87-94. (Pubitemid 40981884)
    • (2005) FEMS Microbiology Letters , vol.249 , Issue.1 , pp. 87-94
    • Dosanjh, N.S.1    Rawat, M.2    Chung, J.-H.3    Av-Gay, Y.4
  • 32
    • 35948992186 scopus 로고    scopus 로고
    • Toxicogenomic response to chlorination includes induction of major virulence genes in Staphylococcus aureus
    • Chang, M. W.; Toghrol, F.; Bentley, W. E. Toxicogenomic response to chlorination includes induction of major virulence genes in Staphylococcus aureus. Environ. Sci. Technol. 2007, 41, 7570-7575.
    • (2007) Environ. Sci. Technol. , vol.41 , pp. 7570-7575
    • Chang, M.W.1    Toghrol, F.2    Bentley, W.E.3
  • 33
    • 53649090529 scopus 로고    scopus 로고
    • Microarray analysis of toxicogenomic effects of ortho-phenylphenol in Staphylococcus aureus
    • Jang, H. J.; Nde, C.; Toghrol, F.; Bentley,W.E. Microarray analysis of toxicogenomic effects of ortho-phenylphenol in Staphylococcus aureus. BMC Genomics 2008, 9, 411.
    • (2008) BMC Genomics , vol.9 , pp. 411
    • Jang, H.J.1    Nde, C.2    Toghrol, F.3    Bentley, W.E.4
  • 34
    • 33846569357 scopus 로고    scopus 로고
    • Toxicogenomic analysis of sodium hypochlorite antimicrobial mechanisms in Pseudomonas aeruginosa
    • Small, D. A.; Chang, W.; Toghrol, F.; Bentley,W.E. Toxicogenomic analysis of sodium hypochlorite antimicrobial mechanisms in Pseudomonas aeruginosa. Appl. Microbiol. Biotechnol. 2007, 74, 176-185.
    • (2007) Appl. Microbiol. Biotechnol. , vol.74 , pp. 176-185
    • Small, D.A.1    Chang, W.2    Toghrol, F.3    Bentley, W.E.4
  • 36
    • 33747499889 scopus 로고    scopus 로고
    • Toxicogenomic response of Staphylococcus aureus to peracetic acid
    • Chang, W.; Toghrol, F.; Bentley, W. E. Toxicogenomic response of Staphylococcus aureus to peracetic acid. Environ. Sci. Technol. 2006, 40, 5124-5131.
    • (2006) Environ. Sci. Technol. , vol.40 , pp. 5124-5131
    • Chang, W.1    Toghrol, F.2    Bentley, W.E.3
  • 38
    • 0023664923 scopus 로고
    • Ferric uptake regulation protein acts as a repressor, employing iron (II) as a cofactor to bind the operator of an iron transport operon in Escherichia coli
    • Bagg, A.; Neilands, J. B. Ferric uptake regulation protein acts as a repressor, employing iron (II) as a cofactor to bind the operator of an iron transport operon in Escherichia coli. Biochemistry 1987, 26, 5471-5477.
    • (1987) Biochemistry , vol.26 , pp. 5471-5477
    • Bagg, A.1    Neilands, J.B.2
  • 39
    • 0023258960 scopus 로고
    • Operator sequences of the aerobactin operon of plasmid ColV-K30 binding the ferric uptake regulation (fur) repressor
    • de Lorenzo, V.; Wee, S.; Herrero, M.; Neilands, J. B. Operator sequences of the aerobactin operon of plasmid ColV-K30 binding the ferric uptake regulation (fur) repressor. J. Bacteriol. 1987, 169, 2624-2630.
    • (1987) J. Bacteriol. , vol.169 , pp. 2624-2630
    • De Lorenzo, V.1    Wee, S.2    Herrero, M.3    Neilands, J.B.4
  • 40
    • 0023692463 scopus 로고
    • Metal ion regulation of gene expression. Fur repressor-operator interaction at the promoter region of the aerobactin system of pColV-K30
    • de Lorenzo, V.; Giovannini, F.; Herrero, M.; Neilands, J. B. Metal ion regulation of gene expression. Fur repressor-operator interaction at the promoter region of the aerobactin system of pColV-K30. J. Mol. Biol. 1988, 203, 875-884.
    • (1988) J. Mol. Biol. , vol.203 , pp. 875-884
    • De Lorenzo, V.1    Giovannini, F.2    Herrero, M.3    Neilands, J.B.4
  • 41
    • 0030663311 scopus 로고    scopus 로고
    • Metalloregulation in vitro of the aerobactin promoter of Escherichia coli by the Fur (ferric uptake regulation) protein
    • Escolar, L.; de Lorenzo, V.; Perez-Martin, J. Metalloregulation in vitro of the aerobactin promoter of Escherichia coli by the Fur (ferric uptake regulation) protein. Mol. Microbiol. 1997, 26, 799-808.
    • (1997) Mol. Microbiol. , vol.26 , pp. 799-808
    • Escolar, L.1    De Lorenzo, V.2    Perez-Martin, J.3
  • 42
    • 0034976601 scopus 로고    scopus 로고
    • Mapping of Mycobacterium tuberculosis katG promoters and their differential expression in infected macrophages
    • DOI 10.1128/JB.183.13.4033-4039.2001
    • Master, S.; Zahrt, T. C.; Song, J.; Deretic, V. Mapping of Mycobacterium tuberculosis katG promoters and their differential expression in infected macrophages. J. Bacteriol. 2001, 183, 4033-4039. (Pubitemid 32565484)
    • (2001) Journal of Bacteriology , vol.183 , Issue.13 , pp. 4033-4039
    • Master, S.1    Zahrt, T.C.2    Song, J.3    Deretic, V.4
  • 43
    • 0035013527 scopus 로고    scopus 로고
    • Regulation of catalase-peroxidase (KatG) expression, isoniazid sensitivity and virulence by furA of Mycobacterium tuberculosis
    • Pym, A. S.; Domenech, P.; Honore, N.; Song, J.; Deretic, V.; Cole, S. T. Regulation of catalase-peroxidase (KatG) expression, isoniazid sensitivity and virulence by furA of Mycobacterium tuberculosis. Mol. Microbiol. 2001, 40, 879-889.
    • (2001) Mol. Microbiol. , vol.40 , pp. 879-889
    • Pym, A.S.1    Domenech, P.2    Honore, N.3    Song, J.4    Deretic, V.5    Cole, S.T.6
  • 46
    • 0030795074 scopus 로고    scopus 로고
    • Enhanced hydrogen peroxide sensitivity and altered stress protein expression in iron-starved Mycobacterium smegmatis
    • Lundrigan,M.D.; Arceneaux, J. E.; Zhu, W.; Byers, B. R. Enhanced hydrogen peroxide sensitivity and altered stress protein expression in iron-starved Mycobacterium smegmatis. Biometals 1997, 10, 215-225.
    • (1997) Biometals , vol.10 , pp. 215-225
    • Arceneaux, J.E.1    Zhu, W.2    Byers, B.R.3
  • 47
    • 0032167951 scopus 로고    scopus 로고
    • Interdependence of mycobacterial iron regulation, oxidative-stress response and isoniazid resistance
    • DOI 10.1016/S0966-842X(98)01307-9, PII S0966842X98013079
    • Dussurget, O.; Smith, I. Interdependence of mycobacterial iron regulation, oxidative-stress response and isoniazid resistance. Trends Microbiol 1998, 6, 354-358. (Pubitemid 28473195)
    • (1998) Trends in Microbiology , vol.6 , Issue.9 , pp. 354-358
    • Dussurget, O.1    Smith, I.2
  • 48
    • 0032833150 scopus 로고    scopus 로고
    • Identification and characterization of two divergently transcribed iron regulated genes in Mycobacterium tuberculosis
    • Rodriguez, G. M.; Gold, B.; Gomez, M.; Dussurget, O.; Smith, I. Identification and characterization of two divergently transcribed iron regulated genes in Mycobacterium tuberculosis. Tuber. Lung Dis. 1999, 79, 287-298.
    • (1999) Tuber. Lung Dis. , vol.79 , pp. 287-298
    • Rodriguez, G.M.1    Gold, B.2    Gomez, M.3    Dussurget, O.4    Smith, I.5
  • 49
    • 0030297121 scopus 로고    scopus 로고
    • In search of tuberculosis virulence genes
    • Collins, D. M. In search of tuberculosis virulence genes. Trends Microbiol. 1996, 4, 426-430.
    • (1996) Trends Microbiol , vol.4 , pp. 426-430
    • Collins, D.M.1
  • 50
    • 0031957229 scopus 로고    scopus 로고
    • Expression of katG in Mycobacterium tuberculosis is associated with its growth and persistence in mice and guinea pigs
    • Li, Z.; Kelley, C.; Collins, F.; Rouse, D.; Morris, S. Expression of katG in Mycobacterium tuberculosis is associated with its growth and persistence in mice and guinea pigs. J. Infect. Dis. 1998, 177, 1030-1035. (Pubitemid 28155158)
    • (1998) Journal of Infectious Diseases , vol.177 , Issue.4 , pp. 1030-1035
    • Li, Z.1    Kelley, C.2    Collins, F.3    Rouse, D.4    Morris, S.5
  • 51
    • 0035162817 scopus 로고    scopus 로고
    • Role of Mycobacterium tuberculosis copper-zinc superoxide dismutase
    • DOI 10.1128/IAI.69.1.529-533.2001
    • Dussurget, O.; Stewart, G.; Neyrolles, O.; Pescher, P.; Young, D.; Marchal, G. Role of Mycobacterium tuberculosis copper-zinc superoxide dismutase. Infect. Immun. 2001, 69, 529-533. (Pubitemid 32038353)
    • (2001) Infection and Immunity , vol.69 , Issue.1 , pp. 529-533
    • Dussurget, O.1    Stewart, G.2    Neyrolles, O.3    Pescher, P.4    Young, D.5    Marchal, G.6
  • 53
    • 0036046297 scopus 로고    scopus 로고
    • Iron transport and regulation, cell signalling and genomics: Lessons from Escherichia coli and Pseudomonas
    • Visca, P.; Leoni, L.; Wilson, M. J.; Lamont, I. L. Iron transport and regulation, cell signalling and genomics: lessons from Escherichia coli and Pseudomonas. Mol. Microbiol 2002, 45, 1177-1190.
    • (2002) Mol. Microbiol , vol.45 , pp. 1177-1190
    • Visca, P.1    Leoni, L.2    Wilson, M.J.3    Lamont, I.L.4
  • 54
    • 0024393963 scopus 로고
    • Thioredoxin and glutaredoxin systems
    • Holmgren, A. Thioredoxin and glutaredoxin systems. J. Biol. Chem. 1989, 264, 13963-13966.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13963-13966
    • Holmgren, A.1
  • 55
    • 0035584857 scopus 로고    scopus 로고
    • Reactive oxygen species, antioxidants, and the mammalian thioredoxin system
    • DOI 10.1016/S0891-5849(01)00724-9, PII S0891584901007249
    • Nordberg, J.; Arner, E. S. Reactive oxygen species, antioxidants, and the mammalian thioredoxin system. Free Radic Biol Med 2001, 31, 1287-1312. (Pubitemid 33145299)
    • (2001) Free Radical Biology and Medicine , vol.31 , Issue.11 , pp. 1287-1312
    • Nordberg, J.1    Arner, E.S.J.2
  • 56
    • 0019781166 scopus 로고
    • Wild-type isopropylmalate isomerase in Salmonella typhimurium is composed of two different subunits
    • Fultz, P. N.; Kemper, J. Wild-type isopropylmalate isomerase in Salmonella typhimurium is composed of two different subunits. J. Bacteriol. 1981, 148, 210-219. (Pubitemid 12209417)
    • (1981) Journal of Bacteriology , vol.148 , Issue.1 , pp. 210-219
    • Fultz, P.N.1    Kemper, J.2
  • 57
    • 0032487743 scopus 로고    scopus 로고
    • The organization of the leuC, leuD and leuB genes of the extreme thermophile Thermus thermophilus
    • DOI 10.1016/S0378-1119(98)00482-X, PII S037811199800482X
    • Tamakoshi, M.; Yamagishi, A.; Oshima, T. The organization of the leuC, leuD and leuB genes of the extreme thermophile Thermus thermophilus. Gene 1998, 222, 125-132. (Pubitemid 28566160)
    • (1998) Gene , vol.222 , Issue.1 , pp. 125-132
    • Tamakoshi, M.1    Yamagishi, A.2    Oshima, T.3
  • 58
    • 0025865421 scopus 로고
    • Homology between IRE-BP, a regulatory RNA-binding protein, aconitase, and isopropylmalate isomerase
    • Hentze,M.W.; Argos, P. Homology between IRE-BP, a regulatory RNA-binding protein, aconitase,andisopropylmalate isomerase. Nucleic Acids Res. 1991, 19, 1739-1740. (Pubitemid 21913272)
    • (1991) Nucleic Acids Research , vol.19 , Issue.8 , pp. 1739-1740
    • Hentze, M.W.1    Argos, P.2
  • 59
    • 0026517563 scopus 로고
    • The aconitase of Escherichia coli. Nucleotide sequence of the aconitase gene and amino acid sequence similarity with mitochondrial aconitases, the iron-responsive-element-binding protein and isopropylmalate isomerases
    • Prodromou, C.; Artymiuk, P. J.; Guest, J. R. The aconitase of Escherichia coli. Nucleotide sequence of the aconitase gene and amino acid sequence similarity with mitochondrial aconitases, the iron-responsive-element-binding protein and isopropylmalate isomerases. Eur. J. Biochem. 1992, 204, 599-609.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 599-609
    • Prodromou, C.1    Artymiuk, P.J.2    Guest, J.R.3
  • 60
    • 33847218318 scopus 로고    scopus 로고
    • Two polyketide-synthase-associated acyltransferases are required for sulfolipid biosynthesis in Mycobacterium tuberculosis
    • DOI 10.1099/mic.0.2006/003103-0
    • Bhatt, K.; Gurcha, S. S.; Bhatt, A.; Besra, G. S.; Jacobs, W. R., Jr. Two polyketide-synthase-associated acyltransferases are required for sulfolipid biosynthesis in Mycobacterium tuberculosis. Microbiology 2007, 153, 513-520. (Pubitemid 46306499)
    • (2007) Microbiology , vol.153 , Issue.2 , pp. 513-520
    • Bhatt, K.1    Gurcha, S.S.2    Bhatt, A.3    Besra, G.S.4    Jacobs Jr., W.R.5
  • 61
    • 0027983767 scopus 로고
    • Identification, cloning, and sequencing of a gene required for ferric vibriobactin utilization by Vibrio cholerae
    • Butterton, J. R.; Calderwood, S. B. Identification, cloning, and sequencing of a gene required for ferric vibriobactin utilization by Vibrio cholerae. J. Bacteriol. 1994, 176, 5631-5638.
    • (1994) J. Bacteriol. , vol.176 , pp. 5631-5638
    • Butterton, J.R.1    Calderwood, S.B.2
  • 62
    • 33947369443 scopus 로고    scopus 로고
    • Macrophage-specific Mycobacterium tuberculosis genes: Identification by green fluorescent protein and kanamycin resistance selection
    • Srivastava, V.; Rouanet, C.; Srivastava, R.; Ramalingam, B.; Locht, C.; Srivastava, B. S. Macrophage-specific Mycobacterium tuberculosis genes: identification by green fluorescent protein and kanamycin resistance selection. Microbiology 2007, 153, 659-666.
    • (2007) Microbiology , vol.153 , pp. 659-666
    • Srivastava, V.1    Rouanet, C.2    Srivastava, R.3    Ramalingam, B.4    Locht, C.5    Srivastava, B.S.6
  • 64
    • 0026329379 scopus 로고
    • The sequence of squash NADH:nitrate reductase and its relationship to the sequences of other flavoprotein oxidoreductases. A family of flavoprotein pyridine nucleotide cytochrome reductases
    • Hyde, G. E.; Crawford, N. M.; Campbell, W. H. The sequence of squash NADH:nitrate reductase and its relationship to the sequences of other flavoprotein oxidoreductases. A family of flavoprotein pyridine nucleotide cytochrome reductases. J. Biol. Chem. 1991, 266, 23542-23547.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23542-23547
    • Hyde, G.E.1    Crawford, N.M.2    Campbell, W.H.3
  • 66
    • 0036775772 scopus 로고    scopus 로고
    • Comparative and functional genomics of the Mycobacterium tuberculosis complex
    • Cole, S. T. Comparative and functional genomics of the Mycobacterium tuberculosis complex. Microbiology 2002, 148, 2919-2928.
    • (2002) Microbiology , vol.148 , pp. 2919-2928
    • Cole, S.T.1
  • 68
    • 0035177858 scopus 로고    scopus 로고
    • Evidence that mycobacterialPE-PGRS proteins are cell surface constituents that influence interactions with other cells
    • Brennan, M. J.; Delogu, G.; Chen, Y.; Bardarov, S.; Kriakov, J.; Alavi, M.; Jacobs,W.R., Jr. Evidence that mycobacterialPE-PGRS proteins are cell surface constituents that influence interactions with other cells. Infect. Immun. 2001, 69, 7326-7333.
    • (2001) Infect. Immun. , vol.69 , pp. 7326-7333
    • Brennan, M.J.1    Delogu, G.2    Chen, Y.3    Bardarov, S.4    Kriakov, J.5    Alavi, M.6    Jacobs Jr., W.R.7
  • 69
    • 0034872325 scopus 로고    scopus 로고
    • Comparative immune response to PE and PE-PGRS antigens of Mycobacterium tuberculosis
    • Delogu, G.; Brennan, M. J. Comparative immune response to PE and PE-PGRS antigens of Mycobacterium tuberculosis. Infect. Immun. 2001, 69, 5606-5611.
    • (2001) Infect. Immun. , vol.69 , pp. 5606-5611
    • Delogu, G.1    Brennan, M.J.2
  • 70
    • 0035173341 scopus 로고    scopus 로고
    • Molecular characterization of a chromosomal locus in Staphylococcus aureus that contributes to oxidative defence and is highly induced by the cell-wall-active antibiotic oxacillin
    • Singh, V. K.; Moskovitz, J.; Wilkinson, B. J.; Jayaswal, R. K. Molecular characterization of a chromosomal locus in Staphylococcus aureus that contributes to oxidative defence and is highly induced by the cell-wall-active antibiotic oxacillin. Microbiology 2001, 147, 3037-3045. (Pubitemid 33076992)
    • (2001) Microbiology , vol.147 , Issue.11 , pp. 3037-3045
    • Singh, V.K.1    Moskovitz, J.2    Wilkinson, B.J.3    Jayaswal, R.K.4
  • 72
    • 46249102682 scopus 로고    scopus 로고
    • Identification of a novel multidrug efflux pump of Mycobacterium tuberculosis
    • Danilchanka, O.; Mailaender, C.; Niederweis, M. Identification of a novel multidrug efflux pump of Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 2008, 52, 2503-2511.
    • (2008) Antimicrob. Agents Chemother. , vol.52 , pp. 2503-2511
    • Danilchanka, O.1    Mailaender, C.2    Niederweis, M.3
  • 73
    • 0030811135 scopus 로고    scopus 로고
    • Protection of DNA during oxidative stress by the nonspecific DNA- Binding protein Dps
    • Martinez, A.; Kolter, R. Protection ofDNAduring oxidative stress by the nonspecific DNA- binding protein Dps. J. Bacteriol. 1997, 179, 5188-5194. (Pubitemid 27340555)
    • (1997) Journal of Bacteriology , vol.179 , Issue.16 , pp. 5188-5194
    • Martinez, A.1    Kolter, R.2
  • 74
    • 0346991729 scopus 로고    scopus 로고
    • Transcriptome analysis of the response of Pseudomonas aeruginosa to hydrogen peroxide
    • Palma, M.; DeLuca, D.; Worgall, S.; Quadri, L. E. Transcriptome analysis of the response of Pseudomonas aeruginosa to hydrogen peroxide. J. Bacteriol. 2004, 186, 248-252.
    • (2004) J. Bacteriol. , vol.186 , pp. 248-252
    • Palma, M.1    Deluca, D.2    Worgall, S.3    Quadri, L.E.4
  • 76
    • 0842283048 scopus 로고    scopus 로고
    • Molecular characterization of a glucose-inhibited division gene, gidA, that regulates cytotoxic enterotoxin of Aeromonas hydrophila
    • Sha, J.; Kozlova, E. V.; Fadl, A. A.; Olano, J. P.; Houston, C. W.; Peterson, J. W.; Chopra, A. K. Molecular characterization of a glucose-inhibited division gene, gidA, that regulates cytotoxic enterotoxin of Aeromonas hydrophila. Infect. Immun. 2004, 72, 1084-1095.
    • (2004) Infect. Immun. , vol.72 , pp. 1084-1095
    • Sha, J.1    Kozlova, E.V.2    Fadl, A.A.3    Olano, J.P.4    Houston, C.W.5    Peterson, J.W.6    Chopra, A.K.7
  • 77
    • 0034824668 scopus 로고    scopus 로고
    • Regulation of the cytotoxic enterotoxin gene in Aeromonas hydrophila: Characterization of an iron uptake regulator
    • Sha, J.; Lu, M.; Chopra, A. K. Regulation of the cytotoxic enterotoxin gene in Aeromonas hydrophila: Characterization of an iron uptake regulator. Infect. Immun. 2001, 69, 6370-6381.
    • (2001) Infect. Immun. , vol.69 , pp. 6370-6381
    • Sha, J.1    Lu, M.2    Chopra, A.K.3
  • 78
    • 0036568632 scopus 로고    scopus 로고
    • The PE multigene family: A 'molecular mantra' for mycobacteria
    • Brennan, M. J.; Delogu, G. The PE multigene family: a 'molecular mantra' for mycobacteria. Trends Microbiol 2002, 10, 246-249.
    • (2002) Trends Microbiol , vol.10 , pp. 246-249
    • Brennan, M.J.1    Delogu, G.2
  • 79
    • 0034826633 scopus 로고    scopus 로고
    • Silencing of oxidative stress response in Mycobacterium tuberculosis: Expression patterns of ahpC in virulent and avirulent strains and effect of ahpC inactivation
    • Springer, B.; Master, S.; Sander, P.; Zahrt, T.; McFalone, M.; Song, J.; Papavinasasundaram, K. G.; Colston, M. J.; Boettger, E.; Deretic, V. Silencing of oxidative stress response in Mycobacterium tuberculosis: expression patterns of ahpC in virulent and avirulent strains and effect of ahpC inactivation. Infect. Immun. 2001, 69, 5967-5973.
    • (2001) Infect. Immun. , vol.69 , pp. 5967-5973
    • Springer, B.1    Master, S.2    Sander, P.3    Zahrt, T.4    McFalone, M.5    Song, J.6    Papavinasasundaram, K.G.7    Colston, M.J.8    Boettger, E.9    Deretic, V.10


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