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Volumn 508, Issue 1-2, 2002, Pages 59-70

Identification and characterization of SnrA, an inducible oxygen-insensitive nitroreductase in Salmonella enterica serovar Typhimurium TA1535

Author keywords

FMN oxidoreductase; NfsA; Nitroreductase; Salmonella; SoxRS regulon

Indexed keywords

FLAVINE MONONUCLEOTIDE; GENE PRODUCT; NITROREDUCTASE; OXYGEN; PARAQUAT; PROTEIN SNRA; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG;

EID: 0037206601     PISSN: 00275107     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0027-5107(02)00174-4     Document Type: Article
Times cited : (30)

References (51)
  • 1
    • 0021027459 scopus 로고
    • Mutagenicity of nitrofuran derivatives: Review
    • McCalla D.R. Mutagenicity of nitrofuran derivatives: review. Environ. Mutagen. 5:1983;745-765.
    • (1983) Environ. Mutagen. , vol.5 , pp. 745-765
    • McCalla, D.R.1
  • 3
    • 0030027820 scopus 로고    scopus 로고
    • Mutation spectra of chemical fractions of a complex mixture: Role of nitroarenes in the mutagenic specificity of municipal waste incinerator emissions
    • DeMarini D.M., Shelton M.L., Bell D.A. Mutation spectra of chemical fractions of a complex mixture: role of nitroarenes in the mutagenic specificity of municipal waste incinerator emissions. Mutat. Res. 349:1996;1-20.
    • (1996) Mutat. Res. , vol.349 , pp. 1-20
    • DeMarini, D.M.1    Shelton, M.L.2    Bell, D.A.3
  • 5
    • 0020060654 scopus 로고
    • Mutagens in diesel exhaust particulate. Identification and direct activities of 6-nitrobenzo[a]pyrene, 9-nitroanthracene, 1-nitropyrene and 5h-phenanthro[4,5-bcd]pyran-5-one
    • Pitts J.N., Lokensgard D.M., Harger W., Fisher T.S., Mejia V., Schuler J.J., Scorziell G.M., Katzenstein Y.A. Mutagens in diesel exhaust particulate. Identification and direct activities of 6-nitrobenzo[a]pyrene, 9-nitroanthracene, 1-nitropyrene and 5h-phenanthro[4,5-bcd]pyran-5-one. Mutat. Res. 103:1982;241-249.
    • (1982) Mutat. Res. , vol.103 , pp. 241-249
    • Pitts, J.N.1    Lokensgard, D.M.2    Harger, W.3    Fisher, T.S.4    Mejia, V.5    Schuler, J.J.6    Scorziell, G.M.7    Katzenstein, Y.A.8
  • 6
    • 0019230518 scopus 로고
    • Nitropyrenes: Isolation identification, and reduction of mutagenic impurities in carbon black and toners
    • Rosenkranz H.S., McCoy E.C., Sanders D.R., Butler M., Kiriazides D.K., Mermelstein R. Nitropyrenes: isolation identification, and reduction of mutagenic impurities in carbon black and toners. Science. 209:1980;1039-1043.
    • (1980) Science , vol.209 , pp. 1039-1043
    • Rosenkranz, H.S.1    McCoy, E.C.2    Sanders, D.R.3    Butler, M.4    Kiriazides, D.K.5    Mermelstein, R.6
  • 7
    • 0020579803 scopus 로고
    • Mutagenicity and genotoxicity of nitroarenes. All nitro-containing chemicals were not created equal
    • Rosenkranz H.S., Mermelstein R. Mutagenicity and genotoxicity of nitroarenes. All nitro-containing chemicals were not created equal. Mutat. Res. 114:1983;217-267.
    • (1983) Mutat. Res. , vol.114 , pp. 217-267
    • Rosenkranz, H.S.1    Mermelstein, R.2
  • 8
    • 0019359134 scopus 로고
    • The identification of polynuclear aromatic hydrocarbon (PAH) derivatives in mutagenic fractions of diesel particulate extracts
    • Schuetzle D., Lee F.S., Prater T.J. The identification of polynuclear aromatic hydrocarbon (PAH) derivatives in mutagenic fractions of diesel particulate extracts. Int. J. Environ. Anal. Chem. 9:1981;93-144.
    • (1981) Int. J. Environ. Anal. Chem. , vol.9 , pp. 93-144
    • Schuetzle, D.1    Lee, F.S.2    Prater, T.J.3
  • 9
    • 0022464920 scopus 로고
    • Mutagenicity and carcinogenicity of nitroarenes and their sources in the environment
    • Tokiwa H., Ohnishi Y. Mutagenicity and carcinogenicity of nitroarenes and their sources in the environment. Crit. Rev. Toxicol. 17:1986;23-60.
    • (1986) Crit. Rev. Toxicol. , vol.17 , pp. 23-60
    • Tokiwa, H.1    Ohnishi, Y.2
  • 10
    • 0033841374 scopus 로고    scopus 로고
    • Mutagenicity of nitroaromatic compounds
    • Purohit V., Basu A.K. Mutagenicity of nitroaromatic compounds. Chem. Res. Toxicol. 13:2000;673-692.
    • (2000) Chem. Res. Toxicol. , vol.13 , pp. 673-692
    • Purohit, V.1    Basu, A.K.2
  • 12
    • 0029745672 scopus 로고    scopus 로고
    • Biochemical characterization of NfsA, the Escherichia coli major nitroreductase exhibiting a high amino acid sequence homology to Frp, a Vibrio harveyi flavin oxidoreductase
    • Zenno S., Koike H., Kumar A.N., Jayaraman R., Tanokura M., Saigo K. Biochemical characterization of NfsA, the Escherichia coli major nitroreductase exhibiting a high amino acid sequence homology to Frp, a Vibrio harveyi flavin oxidoreductase. J. Bacteriol. 178:1996;4508-4514.
    • (1996) J. Bacteriol. , vol.178 , pp. 4508-4514
    • Zenno, S.1    Koike, H.2    Kumar, A.N.3    Jayaraman, R.4    Tanokura, M.5    Saigo, K.6
  • 13
    • 0029808844 scopus 로고    scopus 로고
    • Gene cloning, purification, and characterization of NfsB, a minor oxygen-insensitive nitroreductase from Escherichia coli, similar in biochemical properties to FRase I, the major flavin reductase in Vibrio fischeri
    • Zenno S., Koike H., Tanokura M., Saigo K. Gene cloning, purification, and characterization of NfsB, a minor oxygen-insensitive nitroreductase from Escherichia coli, similar in biochemical properties to FRase I, the major flavin reductase in Vibrio fischeri. J. Biochem. (Tokyo). 120:1996;736-744.
    • (1996) J. Biochem. (Tokyo) , vol.120 , pp. 736-744
    • Zenno, S.1    Koike, H.2    Tanokura, M.3    Saigo, K.4
  • 14
    • 0031771290 scopus 로고    scopus 로고
    • Oxygen-insensitive nitroreductases: Analysis of the roles of nfsA and nfsB in development of resistance to 5-nitrofuran derivatives in Escherichia coli
    • Whiteway J., Koziarz P., Veall J., Sandhu N., Kumar P., Hoecher B., Lambert I.B. Oxygen-insensitive nitroreductases: analysis of the roles of nfsA and nfsB in development of resistance to 5-nitrofuran derivatives in Escherichia coli. J. Bacteriol. 180:1998;5529-5539.
    • (1998) J. Bacteriol. , vol.180 , pp. 5529-5539
    • Whiteway, J.1    Koziarz, P.2    Veall, J.3    Sandhu, N.4    Kumar, P.5    Hoecher, B.6    Lambert, I.B.7
  • 15
    • 0035951874 scopus 로고    scopus 로고
    • Structure and site-directed mutagenesis of a flavoprotein from Escherichia coli that reduces nitrocompounds: Alteration of pyridine nucleotide binding by a single amino acid substitution
    • Kobori T., Sasaki H., Lee W.C., Zenno S., Saigo K., Murphy M.E., Tanokura M. Structure and site-directed mutagenesis of a flavoprotein from Escherichia coli that reduces nitrocompounds: alteration of pyridine nucleotide binding by a single amino acid substitution. J. Biol. Chem. 276:2000;2816-2823.
    • (2000) J. Biol. Chem. , vol.276 , pp. 2816-2823
    • Kobori, T.1    Sasaki, H.2    Lee, W.C.3    Zenno, S.4    Saigo, K.5    Murphy, M.E.6    Tanokura, M.7
  • 16
    • 0028180756 scopus 로고
    • Vibrio harveyi NADPH-flavin oxidoreductase: Cloning, sequencing and overexpression of the gene and purification and characterization of the cloned enzyme
    • Lei B., Liu M., Huang S., Tu S.C. Vibrio harveyi NADPH-flavin oxidoreductase: cloning, sequencing and overexpression of the gene and purification and characterization of the cloned enzyme. J. Bacteriol. 176:1994;3552-3558.
    • (1994) J. Bacteriol. , vol.176 , pp. 3552-3558
    • Lei, B.1    Liu, M.2    Huang, S.3    Tu, S.C.4
  • 17
    • 0031952137 scopus 로고    scopus 로고
    • Conversion of NfsA, the major Escherichia coli nitroreductase, to a flavin reductase with an activity similar to that of Frp, a flavin reductase in Vibrio harveyi, by a single amino acid substitution
    • Zenno S., Kobori T., Tanokura M., Saigo K. Conversion of NfsA, the major Escherichia coli nitroreductase, to a flavin reductase with an activity similar to that of Frp, a flavin reductase in Vibrio harveyi, by a single amino acid substitution. J. Bacteriol. 180:1998;422-425.
    • (1998) J. Bacteriol. , vol.180 , pp. 422-425
    • Zenno, S.1    Kobori, T.2    Tanokura, M.3    Saigo, K.4
  • 18
    • 0029960505 scopus 로고    scopus 로고
    • Flavin reductase P: Structure of a dimeric enzyme that reduces flavin
    • Tanner J.J., Lei B., Tu S.C., Krause K.L. Flavin reductase P: structure of a dimeric enzyme that reduces flavin. Biochemistry. 35:1996;13531-13539.
    • (1996) Biochemistry , vol.35 , pp. 13531-13539
    • Tanner, J.J.1    Lei, B.2    Tu, S.C.3    Krause, K.L.4
  • 19
    • 0033616612 scopus 로고    scopus 로고
    • Nitroreductase A is regulated as a member of the soxRS regulon of Escherichia coli
    • Liochev S.I., Hausladen A., Fridovich I. Nitroreductase A is regulated as a member of the soxRS regulon of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 96:1999;3537-3539.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 3537-3539
    • Liochev, S.I.1    Hausladen, A.2    Fridovich, I.3
  • 20
    • 0033515449 scopus 로고    scopus 로고
    • Induction of the soxRS regulon of Escherichia coli by superoxide
    • Liochev S.I., Benov L., Touati D., Fridovich I. Induction of the soxRS regulon of Escherichia coli by superoxide. J. Biol. Chem. 274:1999;9479-9481.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9479-9481
    • Liochev, S.I.1    Benov, L.2    Touati, D.3    Fridovich, I.4
  • 21
    • 0034152767 scopus 로고    scopus 로고
    • Oxidative stress in bacteria protein damage by reactive oxygen species
    • Cabiscol E., Tamarit J., Ros J. Oxidative stress in bacteria protein damage by reactive oxygen species. Int. Microbiol. 3:2000;3-8.
    • (2000) Int. Microbiol. , vol.3 , pp. 3-8
    • Cabiscol, E.1    Tamarit, J.2    Ros, J.3
  • 22
    • 0032612908 scopus 로고    scopus 로고
    • Transcriptional regulation via redox-sensitive iron-sulphur centres in an oxidative stress response
    • Demple B., Hidalgo E., Ding H. Transcriptional regulation via redox-sensitive iron-sulphur centres in an oxidative stress response. Biochem. Soc. Symp. 64:1999;119-128.
    • (1999) Biochem. Soc. Symp. , vol.64 , pp. 119-128
    • Demple, B.1    Hidalgo, E.2    Ding, H.3
  • 23
    • 0025303874 scopus 로고
    • Nucleotide sequence of Salmonella typhimurium nitroreductase gene
    • Watanabe M., Ishidate M., Nohmi T. Nucleotide sequence of Salmonella typhimurium nitroreductase gene. Nucl. Acids Res. 18:1990;1059.
    • (1990) Nucl. Acids Res. , vol.18 , pp. 1059
    • Watanabe, M.1    Ishidate, M.2    Nohmi, T.3
  • 24
    • 0032508631 scopus 로고    scopus 로고
    • Purification and characterization of wild-type and mutant "classical" nitroreductases of Salmonella typhimurium L33R mutation greatly diminishes binding of FMN to the nitroreductase of S. typhimurium
    • Watanabe M., Nishino T., Takio K., Sofuni T., Nohmi T. Purification and characterization of wild-type and mutant "classical" nitroreductases of Salmonella typhimurium L33R mutation greatly diminishes binding of FMN to the nitroreductase of S. typhimurium. J. Biol. Chem. 273:1998;23922-23928.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23922-23928
    • Watanabe, M.1    Nishino, T.2    Takio, K.3    Sofuni, T.4    Nohmi, T.5
  • 25
    • 0032503694 scopus 로고    scopus 로고
    • 1.8 A crystal structure of the major NAD(P)H:FMN oxidoreductase of a bioluminescent bacterium, Vibrio fischeri: Overall structure, cofactor and substrate-analog binding, and comparison with related flavoproteins
    • Koike H., Sasaki H., Kobori T., Zenno S., Saigo K., Murphy M.E., Adman E.T., Tanokura M. 1.8 A crystal structure of the major NAD(P)H:FMN oxidoreductase of a bioluminescent bacterium, Vibrio fischeri: overall structure, cofactor and substrate-analog binding, and comparison with related flavoproteins. J. Mol. Biol. 280:1998;259-273.
    • (1998) J. Mol. Biol. , vol.280 , pp. 259-273
    • Koike, H.1    Sasaki, H.2    Kobori, T.3    Zenno, S.4    Saigo, K.5    Murphy, M.E.6    Adman, E.T.7    Tanokura, M.8
  • 26
    • 0030978166 scopus 로고    scopus 로고
    • Targeted disruption of the gene encoding the classical nitroreductase enzyme in Salmonella typhimurium Ames test strains TA1535 and TA1538
    • Yamada M., Espinosa-Aguirre J.J., Watanabe M., Matsui K., Sofuni T., Nohmi T. Targeted disruption of the gene encoding the classical nitroreductase enzyme in Salmonella typhimurium Ames test strains TA1535 and TA1538. Mutat. Res. 375:1997;9-17.
    • (1997) Mutat. Res. , vol.375 , pp. 9-17
    • Yamada, M.1    Espinosa-Aguirre, J.J.2    Watanabe, M.3    Matsui, K.4    Sofuni, T.5    Nohmi, T.6
  • 27
    • 0010735468 scopus 로고    scopus 로고
    • Metabolic differences in Ames strains: Molecular characterization of a nitroreductase protein that is present in Salmonella typhimurium TA1535 but absent in TA1538
    • Boroumandi S., Nokhbeh M.R., Pokorny N., Koziarz P., Lambert I.B. Metabolic differences in Ames strains: molecular characterization of a nitroreductase protein that is present in Salmonella typhimurium TA1535 but absent in TA1538. Environ. Mol. Mutagen. 35(Suppl. 31):2000;14.
    • (2000) Environ. Mol. Mutagen. , vol.35 , Issue.SUPPL. 31 , pp. 14
    • Boroumandi, S.1    Nokhbeh, M.R.2    Pokorny, N.3    Koziarz, P.4    Lambert, I.B.5
  • 29
    • 0035852075 scopus 로고    scopus 로고
    • Corrigendum to "The ΔuvrB mutations in the Ames strains of Salmonella span 15 to 119 genes" [Mutat. Res. 483 (2001) 1-11]
    • Porwollik S., Wong R.M., Sims S.H., Schaaper R.M., DeMarini D.M., McClelland M. Corrigendum to "The ΔuvrB mutations in the Ames strains of Salmonella span 15 to 119 genes" [Mutat. Res. 483 (2001) 1-11]. Mutat. Res. 484:2001;107-110.
    • (2001) Mutat. Res. , vol.484 , pp. 107-110
    • Porwollik, S.1    Wong, R.M.2    Sims, S.H.3    Schaaper, R.M.4    DeMarini, D.M.5    McClelland, M.6
  • 30
    • 0000179727 scopus 로고
    • Carcinogens are mutagens: A simple test system combining liver homogenates for activation and bacteria for detection
    • Ames B.N., Durston W.E., Yamasaki E., Lee F.D. Carcinogens are mutagens: a simple test system combining liver homogenates for activation and bacteria for detection. Proc. Natl. Acad. Sci. U.S.A. 70:1973;2281-2285.
    • (1973) Proc. Natl. Acad. Sci. U.S.A. , vol.70 , pp. 2281-2285
    • Ames, B.N.1    Durston, W.E.2    Yamasaki, E.3    Lee, F.D.4
  • 31
    • 0016685233 scopus 로고
    • Methods for detecting carcinogens and mutagens with the Salmonella/mammalian-microsome mutagenicity test
    • Ames B.N., McCann J., Yamasaki E. Methods for detecting carcinogens and mutagens with the Salmonella/mammalian-microsome mutagenicity test. Mutat. Res. 31:1975;347-364.
    • (1975) Mutat. Res. , vol.31 , pp. 347-364
    • Ames, B.N.1    McCann, J.2    Yamasaki, E.3
  • 32
    • 0001246049 scopus 로고
    • Derivations and genotypes of some mutant derivatives of Escherichia coli K-12
    • F.C. Neidhardt (Ed.), American Society for Microbiology, Washington, DC
    • B.J. Bachmann, Derivations and genotypes of some mutant derivatives of Escherichia coli K-12, in: F.C. Neidhardt (Ed.), Escherichia coli and Salmonella typhimurium, Cellular and Molecular Biology, vol. 2, American Society for Microbiology, Washington, DC, 1987, 1190-1219.
    • (1987) Escherichia coli and Salmonella typhimurium, Cellular and Molecular Biology , vol.2 , pp. 1190-1219
    • Bachmann, B.J.1
  • 34
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron C., Vieira J., Messing J. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene. 33:1985;103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 36
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 38
    • 0030941829 scopus 로고    scopus 로고
    • The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm
    • Prinz W.A., Aslund F., Holmgren A., Beckwith J. The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm. J. Biol. Chem. 272:1997;15661-15667.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15661-15667
    • Prinz, W.A.1    Aslund, F.2    Holmgren, A.3    Beckwith, J.4
  • 39
    • 0018736799 scopus 로고
    • Summary of kinetic reaction mechanisms
    • S. Colowick, N.O. Kaplan (Eds.), Academic Press, New York
    • H.J. Fromm, Summary of kinetic reaction mechanisms, in: S. Colowick, N.O. Kaplan (Eds.), Methods in Enzymology, vol. 63, Academic Press, New York, 1979, pp. 42-53.
    • (1979) Methods in Enzymology , vol.63 , pp. 42-53
    • Fromm, H.J.1
  • 40
    • 0018690805 scopus 로고
    • Plotting methods for analyzing enzyme rate data
    • S. Colowick, N.O. Kaplan (Eds.), Academic Press, New York
    • F.B. Rudolph, H.J. Fromm, Plotting methods for analyzing enzyme rate data, in: S. Colowick, N.O. Kaplan (Eds.), Methods in Enzymology, vol. 63, Academic Press, New York, 1979, pp. 138-159.
    • (1979) Methods in Enzymology , vol.63 , pp. 138-159
    • Rudolph, F.B.1    Fromm, H.J.2
  • 41
    • 0020044825 scopus 로고
    • Evidence for the existence of distinct nitroreductases in Salmonella typhimurium: Roles in mutagenesis
    • Rosenkranz E.J., McCoy E.C., Mermelstein R., Rosenkranz H.S. Evidence for the existence of distinct nitroreductases in Salmonella typhimurium: roles in mutagenesis. Carcinogenesis. 3:1982;121-123.
    • (1982) Carcinogenesis , vol.3 , pp. 121-123
    • Rosenkranz, E.J.1    McCoy, E.C.2    Mermelstein, R.3    Rosenkranz, H.S.4
  • 42
    • 0019364204 scopus 로고
    • A cautionary note the use of nitroreductase-deficient strains of Salmonella typhimurium for the detection of nitroarenes as mutagens in complex mixtures including diesel exhausts
    • Rosenkranz H.S., McCoy E.C., Mermelstein R., Speck W.T. A cautionary note the use of nitroreductase-deficient strains of Salmonella typhimurium for the detection of nitroarenes as mutagens in complex mixtures including diesel exhausts. Mutat. Res. 91:1981;103-105.
    • (1981) Mutat. Res. , vol.91 , pp. 103-105
    • Rosenkranz, H.S.1    McCoy, E.C.2    Mermelstein, R.3    Speck, W.T.4
  • 43
    • 0032847454 scopus 로고    scopus 로고
    • Unusual folded conformation of nicotinamide adenine dinucleotide bound to flavin reductase P
    • Tanner J.J., Tu S.C., Barbour L.J., Barnes C.L., Krause K.L. Unusual folded conformation of nicotinamide adenine dinucleotide bound to flavin reductase P. Protein Sci. 8:1999;1725-1732.
    • (1999) Protein Sci. , vol.8 , pp. 1725-1732
    • Tanner, J.J.1    Tu, S.C.2    Barbour, L.J.3    Barnes, C.L.4    Krause, K.L.5
  • 44
    • 0032174885 scopus 로고    scopus 로고
    • Purification and characterization of NfrA1, a Bacillus subtilis nitro/flavin reductase capable of interacting with the bacterial luciferase
    • Zenno S., Kobori T., Tanokura M., Saigo K. Purification and characterization of NfrA1, a Bacillus subtilis nitro/flavin reductase capable of interacting with the bacterial luciferase. Biosci. Biotechnol. Biochem. 62:1998;1978-1987.
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 1978-1987
    • Zenno, S.1    Kobori, T.2    Tanokura, M.3    Saigo, K.4
  • 45
    • 0030574274 scopus 로고    scopus 로고
    • Redox signaling and gene control in the Escherichia coli soxRS oxidative stress regulon - A review
    • Demple B. Redox signaling and gene control in the Escherichia coli soxRS oxidative stress regulon - a review. Gene. 179:1996;53-57.
    • (1996) Gene , vol.179 , pp. 53-57
    • Demple, B.1
  • 46
    • 0030912902 scopus 로고    scopus 로고
    • Redox signal transduction via iron-sulfur clusters in the SoxR transcription activator
    • Hidalgo E., Ding H., Demple B. Redox signal transduction via iron-sulfur clusters in the SoxR transcription activator. Trends Biochem. Sci. 22:1997;207-210.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 207-210
    • Hidalgo, E.1    Ding, H.2    Demple, B.3
  • 47
    • 0030631992 scopus 로고    scopus 로고
    • Regulation of bacterial responses to oxidative stress
    • Rosner J.L., Storz G. Regulation of bacterial responses to oxidative stress. Curr. Top. Cell. Regul. 35:1997;163-177.
    • (1997) Curr. Top. Cell. Regul. , vol.35 , pp. 163-177
    • Rosner, J.L.1    Storz, G.2
  • 48
    • 0033989893 scopus 로고    scopus 로고
    • Identification of SoxS-regulated genes in Salmonella enterica serovar Typhimurium
    • Pomposiello P.J., Demple B. Identification of SoxS-regulated genes in Salmonella enterica serovar Typhimurium. J. Bacteriol. 182:2000;23-29.
    • (2000) J. Bacteriol. , vol.182 , pp. 23-29
    • Pomposiello, P.J.1    Demple, B.2
  • 49
    • 0029091476 scopus 로고
    • A general genetic approach in Escherichia coli for determining the mechanism(s) of action of tumoricidal agents: Application to DMP 840, a tumoricidal agent
    • Chatterjee P.K., Sternberg N.L. A general genetic approach in Escherichia coli for determining the mechanism(s) of action of tumoricidal agents: application to DMP 840, a tumoricidal agent. Proc. Natl. Acad. Sci. U.S.A. 92:1995;8950-8954.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 8950-8954
    • Chatterjee, P.K.1    Sternberg, N.L.2


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