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Volumn 91, Issue SUPPL. 1, 2011, Pages

OsmC proteins of Mycobacterium tuberculosis and Mycobacterium smegmatis protect against organic hydroperoxide stress

Author keywords

Antioxidants; Evasion; INH; Macrophage; Mycobacteria; Ohr; Organic hydroperoxides; OsmC; Oxidative stress

Indexed keywords

BACTERIAL PROTEIN; CUMENE HYDROPEROXIDE; HYDROGEN PEROXIDE; HYDROPEROXIDE; OSMC PROTEIN; PROTEIN C; TERT BUTYL HYDROPEROXIDE; UNCLASSIFIED DRUG;

EID: 84655169708     PISSN: 14729792     EISSN: 1873281X     Source Type: Journal    
DOI: 10.1016/j.tube.2011.10.021     Document Type: Article
Times cited : (41)

References (56)
  • 1
    • 67650164516 scopus 로고    scopus 로고
    • Mycobacterial survival strategies in the phagosome: Defence against host stresses
    • S. Ehrt, and D. Schnappinger Mycobacterial survival strategies in the phagosome: defence against host stresses Cell Microbiol 11 2009 1170 1178
    • (2009) Cell Microbiol , vol.11 , pp. 1170-1178
    • Ehrt, S.1    Schnappinger, D.2
  • 2
    • 0037022417 scopus 로고    scopus 로고
    • Current status of immune mechanisms of killing of intracellular microorganims
    • DOI 10.1016/S0378-1097(01)00553-5, PII S0378109701005535
    • N. Ismail, J.P. Olano, H.M. Feng, and D.H. Walker Current status of immune mechanisms of killing of intracellular microorganisms FEMS Microbiol Lett 207 2002 111 120 (Pubitemid 34215003)
    • (2002) FEMS Microbiology Letters , vol.207 , Issue.2 , pp. 111-120
    • Ismail, N.1    Olano, J.P.2    Feng, H.-M.3    Walker, D.H.4
  • 4
    • 0036710445 scopus 로고    scopus 로고
    • The superoxide-generating NADPH oxidase: Structural aspects and activation mechanism
    • DOI 10.1007/s00018-002-8520-9
    • P.V. Vignais The superoxide-generating NADPH oxidase: structural aspects and activation mechanism Cell Mol Life Sci 59 2002 1428 1459 (Pubitemid 35239301)
    • (2002) Cellular and Molecular Life Sciences , vol.59 , Issue.9 , pp. 1428-1459
    • Vignais, P.V.1
  • 6
    • 0032213375 scopus 로고    scopus 로고
    • Inside the neutrophil phagosome: Oxidants, myeloperoxidase, and bacterial killing
    • M.B. Hampton, A.J. Kettle, and C.C. Winterbourn Inside the neutrophil phagosome: oxidants, myeloperoxidase, and bacterial killing Blood 92 1998 3007 3017 (Pubitemid 28492304)
    • (1998) Blood , vol.92 , Issue.9 , pp. 3007-3017
    • Hampton, M.B.1    Kettle, A.J.2    Winterbourn, C.C.3
  • 7
    • 0025189864 scopus 로고
    • Apparent hydroxyl radical production by peroxynitrite: Implications for endothelial injury from nitric oxide and superoxide
    • J.S. Beckman, T.W. Beckman, J. Chen, P.A. Marshall, and B.A. Freeman Apparent hydroxyl radical production by peroxynitrite: implications for endothelial injury from nitric oxide and superoxide Proc Natl Acad Sci U S A 87 1990 1620 1624
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 1620-1624
    • Beckman, J.S.1    Beckman, T.W.2    Chen, J.3    Marshall, P.A.4    Freeman, B.A.5
  • 8
    • 0042095633 scopus 로고    scopus 로고
    • Nitric oxide in tuberculosis
    • W. Rom, S. Garay, Lippincott, Williams and Wilkins Philadelphia
    • C.F. Nathan, and S. Ehrt Nitric oxide in tuberculosis W. Rom, S. Garay, Tuberculosis 2004 Lippincott, Williams and Wilkins Philadelphia 215 235
    • (2004) Tuberculosis , pp. 215-235
    • Nathan, C.F.1    Ehrt, S.2
  • 9
    • 0035064072 scopus 로고    scopus 로고
    • Immunology of tuberculosis
    • DOI 10.1146/annurev.immunol.19.1.93
    • J.L. Flynn, and J. Chan Immunology of tuberculosis Annu Rev Immunol 19 2001 93 129 (Pubitemid 32368031)
    • (2001) Annual Review of Immunology , vol.19 , pp. 93-129
    • Flynn, J.L.1    Chan, J.2
  • 10
    • 0034917354 scopus 로고    scopus 로고
    • Cu,Zn superoxide dismutase of Mycobacterium tuberculosis contributes to survival in activated macrophages that are generating an oxidative burst
    • DOI 10.1128/IAI.69.8.4980-4987.2001
    • D.L. Piddington, F.C. Fang, T. Laessig, A.M. Cooper, I.M. Orme, and N.A. Buchmeier Cu, Zn superoxide dismutase of Mycobacterium tuberculosis contributes to survival in activated macrophages that are generating an oxidative burst Infect Immun 69 2001 4980 4987 (Pubitemid 32674481)
    • (2001) Infection and Immunity , vol.69 , Issue.8 , 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
  • 11
    • 0032515092 scopus 로고    scopus 로고
    • Identification and subcellular localization of a novel Cu,Zn superoxide dismutase of Mycobacterium tuberculosis
    • DOI 10.1016/S0014-5793(98)01373-8, PII S0014579398013738
    • C.H. Wu, J.J. Tsai-Wu, Y.T. Huang, C.Y. Lin, G.G. Lioua, and F.J. Lee Identification and subcellular localization of a novel Cu, Zn superoxide dismutase of Mycobacterium tuberculosis FEBS Lett 439 1998 192 196 (Pubitemid 28537890)
    • (1998) FEBS Letters , vol.439 , Issue.1-2 , pp. 192-196
    • Wu, C.H.H.1    Tsai-Wu, J.-J.2    Huang, Y.-T.3    Lin, C.-Y.4    Lioua, G.-G.5    Lee, F.-J.S.6
  • 13
    • 2942538880 scopus 로고    scopus 로고
    • Role of KatG catalase-peroxidase in mycobacterial pathogenisis: Countering the phagocyte oxidative burst
    • DOI 10.1111/j.1365-2958.2004.04078.x
    • V.H. Ng, J.S. Cox, A.O. Sousa, J.D. MacMicking, and J.D. McKinney Role of KatG catalase-peroxidase in mycobacterial pathogenesis: countering the phagocyte oxidative burst Mol Microbiol 52 2004 1291 1302 (Pubitemid 38746304)
    • (2004) Molecular Microbiology , vol.52 , Issue.5 , pp. 1291-1302
    • Ng, V.H.1    Cox, J.S.2    Sousa, A.O.3    MacMicking, J.D.4    McKinney, J.D.5
  • 14
    • 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
    • DOI 10.1128/IAI.69.10.5967-5973.2001
    • B. Springer, S. Master, P. Sander, T. Zahrt, M. McFalone, J. Song, K.G. Papavinasasundaram, M.J. Colston, E. Boettger, and V. Deretic Silencing of oxidative stress response in Mycobacterium tuberculosis: expression patterns of ahpC in virulent and avirulent strains and effect of ahpC inactivation Infect Immun 69 2001 5967 5973 (Pubitemid 32885154)
    • (2001) Infection and Immunity , vol.69 , Issue.10 , 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
  • 15
    • 0036772990 scopus 로고    scopus 로고
    • Oxidative stress response genes in Mycobacterium tuberculosis: Role of ahpC in resistance to peroxynitrite and stage-specific survival in macrophages
    • S.S. Master, B. Springer, P. Sander, E.C. Boettger, V. Deretic, and G.S. Timmins Oxidative stress response genes in Mycobacterium tuberculosis: role of ahpC in resistance to peroxynitrite and stage-specific survival in macrophages Microbiology 148 2002 3139 3144 (Pubitemid 35243713)
    • (2002) Microbiology , vol.148 , Issue.10 , pp. 3139-3144
    • Master, S.S.1    Springer, B.2    Sander, P.3    Boettger, E.C.4    Deretic, V.5    Timmins, G.S.6
  • 16
    • 0037039818 scopus 로고    scopus 로고
    • Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein
    • DOI 10.1126/science.1067798
    • R. Bryk, C.D. Lima, H. Erdjument-Bromage, P. Tempst, and C. Nathan Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein Science 295 2002 1073 1077 (Pubitemid 34132237)
    • (2002) Science , vol.295 , Issue.5557 , pp. 1073-1077
    • Bryk, R.1    Lima, C.D.2    Erdjument-Bromage, H.3    Tempst, P.4    Nathan, C.5
  • 17
    • 51949098757 scopus 로고    scopus 로고
    • Biosynthesis and functions of mycothiol, the unique protective thiol of Actinobacteria
    • G.L. Newton, N. Buchmeier, and R.C. Fahey Biosynthesis and functions of mycothiol, the unique protective thiol of Actinobacteria Microbiol Mol Biol Rev 72 2008 471 494
    • (2008) Microbiol Mol Biol Rev , vol.72 , pp. 471-494
    • Newton, G.L.1    Buchmeier, N.2    Fahey, R.C.3
  • 19
    • 33749428834 scopus 로고    scopus 로고
    • The mshA gene encoding the glycosyltransferase of mycothiol biosynthesis is essential in Mycobacterium tuberculosis Erdman
    • DOI 10.1111/j.1574-6968.2006.00441.x
    • N. Buchmeier, and R.C. Fahey The mshA gene encoding the glycosyltransferase of mycothiol biosynthesis is essential in Mycobacterium tuberculosis Erdman FEMS Microbiol Lett 264 2006 74 79 (Pubitemid 44511057)
    • (2006) FEMS Microbiology Letters , vol.264 , Issue.1 , pp. 74-79
    • Buchmeier, N.1    Fahey, R.C.2
  • 20
    • 33748987070 scopus 로고    scopus 로고
    • A mycothiol synthase mutant of Mycobacterium tuberculosis has an altered thiol-disulfide content and limited tolerance to stress
    • DOI 10.1128/JB.00393-06
    • N.A. Buchmeier, G.L. Newton, and R.C. Fahey A mycothiol synthase mutant of Mycobacterium tuberculosis has an altered thiol-disulfide content and limited tolerance to stress J Bacteriol 188 2006 6245 6252 (Pubitemid 44448566)
    • (2006) Journal of Bacteriology , vol.188 , Issue.17 , pp. 6245-6252
    • Buchmeier, N.A.1    Newton, G.L.2    Fahey, R.C.3
  • 22
    • 2442701595 scopus 로고    scopus 로고
    • Methionine sulfoxide reductase A (MsrA) deficiency affects the survival of Mycobacterium smegmatis within macrophages
    • DOI 10.1128/JB.186.11.3590-3598.2004
    • T. Douglas, D.S. Daniel, B.K. Parida, C. Jagannath, and S. Dhandayuthapani Methionine sulfoxide reductase A (MsrA) deficiency affects the survival of Mycobacterium smegmatis within macrophages J Bacteriol 186 2004 3590 3598 (Pubitemid 38661557)
    • (2004) Journal of Bacteriology , vol.186 , Issue.11 , pp. 3590-3598
    • Douglas, T.1    Daniel, D.S.2    Parida, B.K.3    Jagannath, C.4    Dhandayuthapani, S.5
  • 24
    • 65549125853 scopus 로고    scopus 로고
    • Conversion of NO2 to NO by reduced coenzyme F420 protects mycobacteria from nitrosative damage
    • E. Purwantini, and B. Mukhopadhyay Conversion of NO2 to NO by reduced coenzyme F420 protects mycobacteria from nitrosative damage Proc Natl Acad Sci U S A 106 2009 6333 6338
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 6333-6338
    • Purwantini, E.1    Mukhopadhyay, B.2
  • 25
    • 0025812628 scopus 로고
    • Osmotic induction of gene osmC expression in Escherichia coli K12
    • C. Gutierrez, and J.C. Devedjian Osmotic induction of gene osmC expression in Escherichia coli K12 J Mol Biol 220 1991 959 973
    • (1991) J Mol Biol , vol.220 , pp. 959-973
    • Gutierrez, C.1    Devedjian, J.C.2
  • 26
    • 0034915594 scopus 로고    scopus 로고
    • Bacterial Ohr and OsmC paralogues define two protein families with distinct functions and patterns of expression
    • S. Atichartpongkul, S. Loprasert, P. Vattanaviboon, W. Whangsuk, J.D. Helmann, and S. Mongkolsuk Bacterial Ohr and OsmC paralogues define two protein families with distinct functions and patterns of expression Microbiology 147 2001 1775 1782 (Pubitemid 32684920)
    • (2001) Microbiology , vol.147 , Issue.7 , pp. 1775-1782
    • Atichartpongkul, S.1    Loprasert, S.2    Vattanaviboon, P.3    Whangsuk, W.4    Helmann, J.D.5    Mongkolsuk, S.6
  • 27
    • 0345708209 scopus 로고    scopus 로고
    • Structural and functional features of the Escherichia coli hydroperoxide resistance protein OsmC
    • DOI 10.1110/ps.03375603
    • J. Lesniak, W.A. Barton, and D.B. Nikolov Structural and functional features of the Escherichia coli hydroperoxide resistance protein OsmC Protein Sci 12 2003 2838 2843 (Pubitemid 37445108)
    • (2003) Protein Science , vol.12 , Issue.12 , pp. 2838-2843
    • Lesniak, J.1    Barton, W.A.2    Nikolov, D.B.3
  • 31
    • 79951951663 scopus 로고    scopus 로고
    • Biochemical and physiological characterization of the GTP-binding protein Obg of Mycobacterium tuberculosis
    • S.J. Sasindran, S. Saikolappan, V.L. Scofield, and S. Dhandayuthapani Biochemical and physiological characterization of the GTP-binding protein Obg of Mycobacterium tuberculosis BMC Microbiol 11 2011 43
    • (2011) BMC Microbiol , vol.11 , pp. 43
    • Sasindran, S.J.1    Saikolappan, S.2    Scofield, V.L.3    Dhandayuthapani, S.4
  • 32
    • 0028167732 scopus 로고
    • Measurement of plasma hydroperoxide concentrations by the ferrous oxidation-xylenol orange assay in conjunction with triphenylphosphine
    • J. Nourooz-Zadeh, J. Tajaddini-Sarmadi, and S.P. Wolff Measurement of plasma hydroperoxide concentrations by the ferrous oxidation-xylenol orange assay in conjunction with triphenylphosphine Anal Biochem 220 1994 403 409
    • (1994) Anal Biochem , vol.220 , pp. 403-409
    • Nourooz-Zadeh, J.1    Tajaddini-Sarmadi, J.2    Wolff, S.P.3
  • 33
    • 34347235804 scopus 로고    scopus 로고
    • Stress response of genes encoding putative stress signaling molecules of Mycobacterium tuberculosis
    • S. Dhandayuthapani Stress response of genes encoding putative stress signaling molecules of Mycobacterium tuberculosis Front Biosci 12 2007 4676 4681
    • (2007) Front Biosci , vol.12 , pp. 4676-4681
    • Dhandayuthapani, S.1
  • 34
    • 0029888258 scopus 로고    scopus 로고
    • Oxidative stress response and its role in sensitivity to isoniazid in mycobacteria: Characterization and inducibility of ahpC by peroxides in Mycobacterium smegmatis and lack of expression in M. aurum and M. tuberculosis
    • S. Dhandayuthapani, Y. Zhang, M.H. Mudd, and V. Deretic Oxidative stress response and its role in sensitivity to isoniazid in mycobacteria: characterization and inducibility of ahpC by peroxides in Mycobacterium smegmatis and lack of expression in M. aurum and M. tuberculosis J Bacteriol 178 1996 3641 3649
    • (1996) J Bacteriol , vol.178 , pp. 3641-3649
    • Dhandayuthapani, S.1    Zhang, Y.2    Mudd, M.H.3    Deretic, V.4
  • 35
    • 12244252764 scopus 로고    scopus 로고
    • Structural and functional characterization of the Pseudomonas hydroperoxide resistance protein Ohr
    • DOI 10.1093/emboj/cdf670
    • J. Lesniak, W.A. Barton, and D.B. Nikolov Structural and functional characterization of the Pseudomonas hydroperoxide resistance protein Ohr Embo J 21 2002 6649 6659 (Pubitemid 36014537)
    • (2002) EMBO Journal , vol.21 , Issue.24 , pp. 6649-6659
    • Lesniak, J.1    Barton, W.A.2    Nikolov, D.B.3
  • 37
    • 17644426975 scopus 로고    scopus 로고
    • Novel roles of ohrR-ohr in Xanthomonas sensing, metabolism, and physiological adaptive response to lipid hydroperoxide
    • DOI 10.1128/JB.187.9.3277-3281.2005
    • C. Klomsiri, W. Panmanee, S. Dharmsthiti, P. Vattanaviboon, and S. Mongkolsuk Novel roles of ohrR-ohr in Xanthomonas sensing, metabolism, and physiological adaptive response to lipid hydroperoxide J Bacteriol 187 2005 3277 3281 (Pubitemid 40571623)
    • (2005) Journal of Bacteriology , vol.187 , Issue.9 , pp. 3277-3281
    • Klomsiri, C.1    Panmanee, W.2    Dharmsthiti, S.3    Vattanaviboon, P.4    Mongkolsuk, S.5
  • 38
    • 0036032183 scopus 로고    scopus 로고
    • OhrR, a transcription repressor that senses and responds to changes in organic peroxide levels in Xanthomonas campestris pv. phaseoli
    • DOI 10.1046/j.1365-2958.2002.03116.x
    • W. Panmanee, P. Vattanaviboon, W. Eiamphungporn, W. Whangsuk, R. Sallabhan, and S. Mongkolsuk OhrR, a transcription repressor that senses and responds to changes in organic peroxide levels in Xanthomonas campestris pv. phaseoli Mol Microbiol 45 2002 1647 1654 (Pubitemid 35231980)
    • (2002) Molecular Microbiology , vol.45 , Issue.6 , pp. 1647-1654
    • Panmanee, W.1    Vattanaviboon, P.2    Eiamphungporn, W.3    Whangsuk, W.4    Sallabhan, R.5    Mongkolsuk, S.6
  • 39
    • 31344471227 scopus 로고    scopus 로고
    • OHRR and OHR are the primary sensor/regulator and protective genes against organic hydroperoxide stress in Agrobacterium tumefaciens
    • DOI 10.1128/JB.188.3.842-851.2006
    • T. Chuchue, W. Tanboon, B. Prapagdee, J.M. Dubbs, P. Vattanaviboon, and S. Mongkolsuk ohrR and ohr are the primary sensor/regulator and protective genes against organic hydroperoxide stress in Agrobacterium tumefaciens J Bacteriol 188 2006 842 851 (Pubitemid 43146399)
    • (2006) Journal of Bacteriology , vol.188 , Issue.3 , pp. 842-851
    • Chuchue, T.1    Tanboon, W.2    Prapagdee, B.3    Dubbs, J.M.4    Vattanaviboon, P.5    Monkolsuk, S.6
  • 40
    • 0030050577 scopus 로고    scopus 로고
    • Growth-phase-dependent expression of the osmotically inducible gene osmC of Escherichia coli K-12
    • S. Gordia, and C. Gutierrez Growth-phase-dependent expression of the osmotically inducible gene osmC of Escherichia coli K-12 Mol Microbiol 19 1996 729 736 (Pubitemid 26068588)
    • (1996) Molecular Microbiology , vol.19 , Issue.4 , pp. 729-736
    • Gordia, S.1    Gutierrez, C.2
  • 42
    • 0037500300 scopus 로고    scopus 로고
    • Organic hydroperoxide resistance gene encodes a thiol-dependent peroxidase
    • DOI 10.1074/jbc.M300252200
    • J.R. Cussiol, S.V. Alves, M.A. de Oliveira, and L.E. Netto Organic hydroperoxide resistance gene encodes a thiol-dependent peroxidase J Biol Chem 278 2003 11570 11578 (Pubitemid 36792719)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.13 , pp. 11570-11578
    • Cussiol, J.R.R.1    Alves, S.V.2    De Oliveira, M.A.3    Netto, L.E.S.4
  • 43
    • 40549139820 scopus 로고    scopus 로고
    • Structural and functional characterization of an organic hydroperoxide resistance protein from Mycoplasma gallisepticum
    • DOI 10.1128/JB.01685-07
    • C. Jenkins, R. Samudrala, S.J. Geary, and S.P. Djordjevic Structural and functional characterization of an organic hydroperoxide resistance protein from Mycoplasma gallisepticum J Bacteriol 190 2008 2206 2216 (Pubitemid 351356105)
    • (2008) Journal of Bacteriology , vol.190 , Issue.6 , pp. 2206-2216
    • Jenkins, C.1    Samudrala, R.2    Geary, S.J.3    Djordjevic, S.P.4
  • 44
    • 0030066091 scopus 로고    scopus 로고
    • Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 2. Cystine disulfides involved in catalysis of peroxide reduction
    • DOI 10.1021/bi951888k
    • L.B. Poole Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 2. Cystine disulfides involved in catalysis of peroxide reduction Biochemistry 35 1996 65 75 (Pubitemid 26036407)
    • (1996) Biochemistry , vol.35 , Issue.1 , pp. 65-75
    • Poole, L.B.1
  • 45
    • 0036436682 scopus 로고    scopus 로고
    • Evaluation of the roles that alkyl hydroperoxide reductase and Ohr play in organic peroxide-induced gene expression and protection against organic peroxides in Xanthomonas campestris
    • DOI 10.1016/S0006-291X(02)02602-5, PII S0006291X02026025
    • P. Vattanaviboon, W. Whangsuk, W. Panmanee, C. Klomsiri, S. Dharmsthiti, and S. Mongkolsuk Evaluation of the roles that alkyl hydroperoxide reductase and Ohr play in organic peroxide-induced gene expression and protection against organic peroxides in Xanthomonas campestris Biochem Biophys Res Commun 299 2002 177 182 (Pubitemid 35373694)
    • (2002) Biochemical and Biophysical Research Communications , vol.299 , Issue.2 , pp. 177-182
    • Vattanaviboon, P.1    Whangsuk, W.2    Panmanee, W.3    Klomsiri, C.4    Dharmsthiti, S.5    Mongkolsuk, S.6
  • 46
    • 0031899593 scopus 로고    scopus 로고
    • Identification and characterization of a new organic hydroperoxide resistance (ohr) gene with a novel pattern of oxidative stress regulation from Xanthomonas campestris pv. phaseoli
    • S. Mongkolsuk, W. Praituan, S. Loprasert, M. Fuangthong, and S. Chamnongpol Identification and characterization of a new organic hydroperoxide resistance (ohr) gene with a novel pattern of oxidative stress regulation from Xanthomonas campestris pv. phaseoli J Bacteriol 180 1998 2636 2643 (Pubitemid 28213261)
    • (1998) Journal of Bacteriology , vol.180 , Issue.10 , pp. 2636-2643
    • Mongkolsuk, S.1    Praituan, W.2    Loprasert, S.3    Fuangthong, M.4    Chamnongpol, S.5
  • 47
    • 0035157997 scopus 로고    scopus 로고
    • Genetic and physiological characterization of ohr, encoding a protein involved in organic hydroperoxide resistance in Pseudomonas aeruginosa
    • DOI 10.1128/JB.183.2.773-778.2001
    • U.A. Ochsner, D.J. Hassett, and M.L. Vasil Genetic and physiological characterization of ohr, encoding a protein involved in organic hydroperoxide resistance in Pseudomonas aeruginosa J Bacteriol 183 2001 773 778 (Pubitemid 32048139)
    • (2001) Journal of Bacteriology , vol.183 , Issue.2 , pp. 773-778
    • Ochsner, U.A.1    Hassett, D.J.2    Vasil, M.L.3
  • 48
    • 0034971954 scopus 로고    scopus 로고
    • OhrR is a repressor of ohrA, a key organic hydroperoxide resistance determinant in Bacillus subtilis
    • DOI 10.1128/JB.183.14.4134-4141.2001
    • M. Fuangthong, S. Atichartpongkul, S. Mongkolsuk, and J.D. Helmann OhrR is a repressor of ohrA, a key organic hydroperoxide resistance determinant in Bacillus subtilis J Bacteriol 183 2001 4134 4141 (Pubitemid 32568063)
    • (2001) Journal of Bacteriology , vol.183 , Issue.14 , pp. 4134-4141
    • Fuangthong, M.1    Atichartpongkul, S.2    Mongkolsuk, S.3    Helmann, J.D.4
  • 49
    • 70350457960 scopus 로고    scopus 로고
    • The Mycoplasma genitalium MG-454 gene product resists killing by organic hydroperoxides
    • S. Saikolappan, S.J. Sasindran, H.D. Yu, J.B. Baseman, and S. Dhandayuthapani The Mycoplasma genitalium MG-454 gene product resists killing by organic hydroperoxides J Bacteriol 191 2009 6675 6682
    • (2009) J Bacteriol , vol.191 , pp. 6675-6682
    • Saikolappan, S.1    Sasindran, S.J.2    Yu, H.D.3    Baseman, J.B.4    Dhandayuthapani, S.5
  • 50
    • 0033968059 scopus 로고    scopus 로고
    • Reactive nitrogen intermediates and the pathogenesis of Salmonella and Mycobacteria
    • DOI 10.1016/S1369-5274(99)00048-X
    • M.U. Shiloh, and C.F. Nathan Reactive nitrogen intermediates and the pathogenesis of Salmonella and mycobacteria Curr Opin Microbiol 3 2000 35 42 (Pubitemid 30094261)
    • (2000) Current Opinion in Microbiology , vol.3 , Issue.1 , pp. 35-42
    • Shiloh, M.U.1    Nathan, C.F.2
  • 52
    • 0031829737 scopus 로고    scopus 로고
    • One of two OsmC homologs in Bacillus subtilis is part of the σ(B)- dependent general stress regulon
    • U. Volker, K.K. Andersen, H. Antelmann, K.M. Devine, and M. Hecker One of two osmC homologs in Bacillus subtilis is part of the sigmaB-dependent general stress regulon J Bacteriol 180 1998 4212 4218 (Pubitemid 28373527)
    • (1998) Journal of Bacteriology , vol.180 , Issue.16 , pp. 4212-4218
    • Volker, U.1    Andersen, K.K.2    Antelmann, H.3    Devine, K.M.4    Hecker, M.5
  • 53
    • 0032466234 scopus 로고    scopus 로고
    • Molecular genetic basis of antimicrobial agent resistance in Mycobacterium tuberculosis: 1998 update
    • DOI 10.1054/tuld.1998.0002
    • S. Ramaswamy, and J.M. Musser Molecular genetic basis of antimicrobial agent resistance in Mycobacterium tuberculosis: 1998 update Tuber Lung Dis 79 1998 3 29 (Pubitemid 29050434)
    • (1998) Tubercle and Lung Disease , vol.79 , Issue.1 , pp. 3-29
    • Ramaswamy, S.1    Musser, J.M.2
  • 54
    • 33750699963 scopus 로고    scopus 로고
    • Mechanisms of action of isoniazid
    • DOI 10.1111/j.1365-2958.2006.05467.x
    • G.S. Timmins, and V. Deretic Mechanisms of action of isoniazid Mol Microbiol 62 2006 1220 1227 (Pubitemid 44707189)
    • (2006) Molecular Microbiology , vol.62 , Issue.5 , pp. 1220-1227
    • Timmins, G.S.1    Deretic, V.2
  • 55
    • 0029959745 scopus 로고    scopus 로고
    • The extreme sensitivity of Mycobacterium tuberculosis to the front-line antituberculosis drug isoniazid
    • V. Deretic, E. Pagan-Ramos, Y. Zhang, S. Dhandayuthapani, and L.E. Via The extreme sensitivity of Mycobacterium tuberculosis to the front-line antituberculosis drug isoniazid Nat Biotechnol 14 1996 1557 1561 (Pubitemid 26365548)
    • (1996) Nature Biotechnology , vol.14 , Issue.11 , pp. 1557-1561
    • Deretic, V.1    Pagan-Ramos, E.2    Zhang, Y.3    Dhandayuthapani, S.4    Via, L.E.5
  • 56
    • 0029996734 scopus 로고    scopus 로고
    • Compensatory ahpC gene expression in isoniazid-resistant Mycobacterium tuberculosis
    • D.R. Sherman, K. Mdluli, M.J. Hickey, T.M. Arain, S.L. Morris, C.E. Barry 3rd, and C.K. Stover Compensatory ahpC gene expression in isoniazid-resistant Mycobacterium tuberculosis Science 272 1996 1641 1643 (Pubitemid 26200020)
    • (1996) Science , vol.272 , Issue.5268 , pp. 1641-1643
    • Sherman, D.R.1    Mdluli, K.2    Hickey, M.J.3    Arain, T.M.4    Morris, S.L.5    Barry III, C.E.6    Stover, C.K.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.