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Volumn 35, Issue 1, 2000, Pages 150-160

A developmentally regulated catalase required for proper differentiation and osmoprotection of Streptomyces coelicolor

Author keywords

[No Author keywords available]

Indexed keywords

ACTINORHODINE; BACTERIAL PROTEIN; CATALASE; PRODIGIOSIN;

EID: 0033971399     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2000.01685.x     Document Type: Article
Times cited : (47)

References (58)
  • 1
    • 0025292818 scopus 로고
    • Mutations in a new Streptomyces coelicolor locus which globally block antibiotic biosynthesis but not sporulation
    • Adamidis, T., Riggle, P., and Champness, W.C. (1990) Mutations in a new Streptomyces coelicolor locus which globally block antibiotic biosynthesis but not sporulation. J Bacteriol 172: 2962-2969.
    • (1990) J Bacteriol , vol.172 , pp. 2962-2969
    • Adamidis, T.1    Riggle, P.2    Champness, W.C.3
  • 3
    • 0031899704 scopus 로고    scopus 로고
    • F and KatX is essential for hydrogen peroxide resistance of the germinating spore
    • F and KatX is essential for hydrogen peroxide resistance of the germinating spore. J Bacteriol 180: 2057-2062.
    • (1998) J Bacteriol , vol.180 , pp. 2057-2062
    • Bagyan, I.1    Casillas-Martinez, L.2    Setlow, P.3
  • 4
    • 0021710537 scopus 로고
    • The relationship between base composition and codon usage in bacterial genes and its use for the simple and reliable identification of protein-coding sequences
    • Bibb, M.J., Findlay, P.R., and Johnson, M.W. (1984) The relationship between base composition and codon usage in bacterial genes and its use for the simple and reliable identification of protein-coding sequences. Gene 30: 157-166.
    • (1984) Gene , vol.30 , pp. 157-166
    • Bibb, M.J.1    Findlay, P.R.2    Johnson, M.W.3
  • 5
    • 0026645203 scopus 로고
    • Plasmid cloning vectors for the conjugal transfer of DNA from Escherichia coli to Streptomyces spp
    • Bierman, M., Logan, R., O'Brien, K., Seno, E.T., Rao, R.N., and Schoner, B.E. (1992) Plasmid cloning vectors for the conjugal transfer of DNA from Escherichia coli to Streptomyces spp. Gene 116: 43-49.
    • (1992) Gene , vol.116 , pp. 43-49
    • Bierman, M.1    Logan, R.2    O'Brien, K.3    Seno, E.T.4    Rao, R.N.5    Schoner, B.E.6
  • 6
    • 0025720743 scopus 로고
    • The isolation, cloning and identification of a vegetative catalase gene from Bacillus subtilis
    • Bol, D.K., and Yasbin, R.E. (1991) The isolation, cloning and identification of a vegetative catalase gene from Bacillus subtilis. Gene 109: 31-37.
    • (1991) Gene , vol.109 , pp. 31-37
    • Bol, D.K.1    Yasbin, R.E.2
  • 7
    • 0028034844 scopus 로고
    • Analysis of the dual regulatory mechanisms controlling expression of the vegetative catalase gene of Bacillus subtilis
    • Bol, D.K., and Yasbin, R.E. (1994) Analysis of the dual regulatory mechanisms controlling expression of the vegetative catalase gene of Bacillus subtilis. J Bacteriol 176: 6744-6748.
    • (1994) J Bacteriol , vol.176 , pp. 6744-6748
    • Bol, D.K.1    Yasbin, R.E.2
  • 8
    • 0030690926 scopus 로고    scopus 로고
    • Alkyl hydroperoxide reductase, catalase, MrgA, and superoxide dismutase are not involved in resistance of Bacillus subtilis spores to heat or oxidizing agents
    • Casillas-Martinez, L., and Setlow, P. (1997) Alkyl hydroperoxide reductase, catalase, MrgA, and superoxide dismutase are not involved in resistance of Bacillus subtilis spores to heat or oxidizing agents. J Bacteriol 179: 7420-7425.
    • (1997) J Bacteriol , vol.179 , pp. 7420-7425
    • Casillas-Martinez, L.1    Setlow, P.2
  • 9
    • 0031747318 scopus 로고    scopus 로고
    • Taking a genetic scalpel to the Streptomyces colony
    • Chater, K.F. (1998) Taking a genetic scalpel to the Streptomyces colony. Microbiology 144: 1465-1478.
    • (1998) Microbiology , vol.144 , pp. 1465-1478
    • Chater, K.F.1
  • 11
    • 0008916169 scopus 로고
    • Cloning and characterization of two catalase genes from Streptomyces coelicolor Müller
    • Cho, Y.-H., and Roe, J.-H. (1994) Cloning and characterization of two catalase genes from Streptomyces coelicolor Müller. Kor J Microbiol 32: 486-494.
    • (1994) Kor J Microbiol , vol.32 , pp. 486-494
    • Cho, Y.-H.1    Roe, J.-H.2
  • 12
    • 0030911601 scopus 로고    scopus 로고
    • Isolation and expression of the catA gene encoding the major vegetative catalase in Streptomyces coelicolor Müller
    • Cho, Y.-H., and Roe, J.-H. (1997) Isolation and expression of the catA gene encoding the major vegetative catalase in Streptomyces coelicolor Müller. J Bacteriol 179: 4049-4052.
    • (1997) J Bacteriol , vol.179 , pp. 4049-4052
    • Cho, Y.-H.1    Roe, J.-H.2
  • 13
    • 0018367454 scopus 로고
    • Purification of the odianisidine peroxidase from Escherichia coli B
    • Claiborne, A., and Fridovich, I. (1979) Purification of the odianisidine peroxidase from Escherichia coli B. J Biol Chem 254: 4245-4252.
    • (1979) J Biol Chem , vol.254 , pp. 4245-4252
    • Claiborne, A.1    Fridovich, I.2
  • 14
    • 0018639058 scopus 로고
    • Purification and characterization of hydroperoxidase II of Escherichia coli B
    • Claiborne, A., Malinowski, D.P., and Fridovich, I. (1979) Purification and characterization of hydroperoxidase II of Escherichia coli B. J Biol Chem 254: 11664-11668.
    • (1979) J Biol Chem , vol.254 , pp. 11664-11668
    • Claiborne, A.1    Malinowski, D.P.2    Fridovich, I.3
  • 15
    • 0021139249 scopus 로고
    • Effects of molecular oxygen on detection of superoxide radical with nitroblue tetrazolium and on activity stains for catalase
    • Clare, D.A., Duong, M.H., Darr, D., Archibald, F., and Fridovich, I. (1984) Effects of molecular oxygen on detection of superoxide radical with nitroblue tetrazolium and on activity stains for catalase. Anal Biochem 140: 532-537.
    • (1984) Anal Biochem , vol.140 , pp. 532-537
    • Clare, D.A.1    Duong, M.H.2    Darr, D.3    Archibald, F.4    Fridovich, I.5
  • 16
    • 0030589073 scopus 로고    scopus 로고
    • Impaired oxidative stress resistance of Bacillus subtilis sigB mutants and the role of katA and katE
    • Engelmann, S., and Hecker, M. (1996) Impaired oxidative stress resistance of Bacillus subtilis sigB mutants and the role of katA and katE. FEMS Microbiol Lett 145: 63-69.
    • (1996) FEMS Microbiol Lett , vol.145 , pp. 63-69
    • Engelmann, S.1    Hecker, M.2
  • 18
    • 0025899144 scopus 로고
    • The act cluster contains regulatory and antibiotic export genes, direct targets for translational control by the bldA tRNA gene of Streptomyces
    • Fernández-Moreno, M.A., Caballero, J.L., Hopwood, D.A., and Malpartida, F. (1991) The act cluster contains regulatory and antibiotic export genes, direct targets for translational control by the bldA tRNA gene of Streptomyces. Cell 66: 769-780.
    • (1991) Cell , vol.66 , pp. 769-780
    • Fernández-Moreno, M.A.1    Caballero, J.L.2    Hopwood, D.A.3    Malpartida, F.4
  • 19
    • 0029018721 scopus 로고
    • Metabolic sources of hydrogen peroxide in aerobically growing Escherichia coli
    • González-Flecha, B., and Demple, B. (1995) Metabolic sources of hydrogen peroxide in aerobically growing Escherichia coli. J Biol Chem 270: 13681-13687.
    • (1995) J Biol Chem , vol.270 , pp. 13681-13687
    • González-Flecha, B.1    Demple, B.2
  • 20
    • 0023990992 scopus 로고
    • Promoter determining the timing and spatial localization of transcription of a cloned Streptomyces coelicolor gene encoding a spore-associated polypeptide
    • Guijarro, J., Santamaria, R., Schauer, A., and Losick, R. (1988) Promoter determining the timing and spatial localization of transcription of a cloned Streptomyces coelicolor gene encoding a spore-associated polypeptide. J Bacteriol 170: 1985-1901.
    • (1988) J Bacteriol , vol.170 , pp. 1985-11901
    • Guijarro, J.1    Santamaria, R.2    Schauer, A.3    Losick, R.4
  • 21
    • 0026605537 scopus 로고
    • Clustal V: Improved software for multiple sequence alignment
    • Higgins, D.G., Bleasby, A.T., and Fuchs, R. (1992) Clustal V: improved software for multiple sequence alignment. Comput Appl Biosci 8: 189-191.
    • (1992) Comput Appl Biosci , vol.8 , pp. 189-191
    • Higgins, D.G.1    Bleasby, A.T.2    Fuchs, R.3
  • 22
    • 0025971441 scopus 로고
    • Gene disruption and gene replacement in Streptomyces via single stranded DNA transformation of integration vectors
    • Hillemann, D., Pühler, A., and Wohlleben, W. (1991) Gene disruption and gene replacement in Streptomyces via single stranded DNA transformation of integration vectors. Nucleic Acids Res 19: 727-731.
    • (1991) Nucleic Acids Res , vol.19 , pp. 727-731
    • Hillemann, D.1    Pühler, A.2    Wohlleben, W.3
  • 23
    • 0025037357 scopus 로고
    • Pigmented antibiotic production by Streptomyces coelicolor A3(2): Kinetics and the influence of nutrients
    • Hobbs, G., Frazer, C.M., Gardner, D.C.J., Flett, F., and Oliver, S.G. (1990) Pigmented antibiotic production by Streptomyces coelicolor A3(2): kinetics and the influence of nutrients. J Gen Microbiol 136: 2291-2296.
    • (1990) J Gen Microbiol , vol.136 , pp. 2291-2296
    • Hobbs, G.1    Frazer, C.M.2    Gardner, D.C.J.3    Flett, F.4    Oliver, S.G.5
  • 24
    • 0026668498 scopus 로고
    • Molecular genetic analysis of proline and tryptophan biosynthesis in Streptomyces coelicolor A3(2): Interaction between primary and secondary metabolism - A review
    • Hood, D.W., Heidstra, R., Swoboda, U.K., and Hodgson, D.A. (1992) Molecular genetic analysis of proline and tryptophan biosynthesis in Streptomyces coelicolor A3(2): interaction between primary and secondary metabolism - a review. Gene 115: 5-12.
    • (1992) Gene , vol.115 , pp. 5-12
    • Hood, D.W.1    Heidstra, R.2    Swoboda, U.K.3    Hodgson, D.A.4
  • 26
    • 0028245940 scopus 로고
    • Role of rpoS (katF) in oxyR-independent regulation of hydroperoxidase I in Escherichia coli
    • Ivanova, A., Miller, C., Glinsky, G., and Eisenstark, A. (1994) Role of rpoS (katF) in oxyR-independent regulation of hydroperoxidase I in Escherichia coli. Mol Microbiol 12: 571-578.
    • (1994) Mol Microbiol , vol.12 , pp. 571-578
    • Ivanova, A.1    Miller, C.2    Glinsky, G.3    Eisenstark, A.4
  • 27
    • 0025144155 scopus 로고
    • Similar organization of the sigB and spollA operons encoding alternative sigma factors of Bacillus subtilis RNA polymerase
    • Kalman, S.M., Duncan, M.L., Thomas, S.M., and Price, C.W. (1990) Similar organization of the sigB and spollA operons encoding alternative sigma factors of Bacillus subtilis RNA polymerase. J Bacteriol 172: 5575-5585.
    • (1990) J Bacteriol , vol.172 , pp. 5575-5585
    • Kalman, S.M.1    Duncan, M.L.2    Thomas, S.M.3    Price, C.W.4
  • 29
    • 0030995326 scopus 로고    scopus 로고
    • Two divergent catalase genes are differentially regulated during Aspergillus nidulans development and oxidative stress
    • Kawasaki, L., Wysong, D., Diamond, R., and Aguirre, J. (1997) Two divergent catalase genes are differentially regulated during Aspergillus nidulans development and oxidative stress. J Bacteriol 179: 3284-3292.
    • (1997) J Bacteriol , vol.179 , pp. 3284-3292
    • Kawasaki, L.1    Wysong, D.2    Diamond, R.3    Aguirre, J.4
  • 30
    • 0029787353 scopus 로고    scopus 로고
    • The positions of the sigma-factor genes, whiG and sigF in the hierarchy controlling the development of spore chains in the aerial mycelial hyphae of Streptomyces coelicolor A3(2)
    • Kelemen, G.H., Brown, G.L., Kormanec, J., Potúčková L., Chater, K.F., and Buttner, M.J. (1996) The positions of the sigma-factor genes, whiG and sigF in the hierarchy controlling the development of spore chains in the aerial mycelial hyphae of Streptomyces coelicolor A3(2). Mol Microbiol 21: 593-693.
    • (1996) Mol Microbiol , vol.21 , pp. 593-693
    • Kelemen, G.H.1    Brown, G.L.2    Kormanec, J.3    Potúčková, L.4    Chater, K.F.5    Buttner, M.J.6
  • 31
    • 0021330492 scopus 로고
    • Salt stress control of intracellular solutes in streptomycetes indigenous to saline soils
    • Killham, K., and Firestone, M.K. (1984) Salt stress control of intracellular solutes in streptomycetes indigenous to saline soils. Appl Environ Mircobiol 47: 301-306.
    • (1984) Appl Environ Mircobiol , vol.47 , pp. 301-306
    • Killham, K.1    Firestone, M.K.2
  • 32
    • 0028588511 scopus 로고
    • Characterization of the major catalase from Streptomyces coelicolor ATCC 10147
    • Kim, H.-P., Lee, J.-S., Hah, Y.-C., and Roe, J.-H. (1994) Characterization of the major catalase from Streptomyces coelicolor ATCC 10147. Microbiology 140: 3391-3397.
    • (1994) Microbiology , vol.140 , pp. 3391-3397
    • Kim, H.-P.1    Lee, J.-S.2    Hah, Y.-C.3    Roe, J.-H.4
  • 33
    • 0029132272 scopus 로고
    • Cloning, characterization and phenotypic expression in Escherichia coli of catF, which encodes the catalytic subunit of catalase isozyme CatF of Pseudomonas syringae
    • Klotz, M.G., Kim, Y.C., Katsuwon, J., and Anderson, A.J. (1995) Cloning, characterization and phenotypic expression in Escherichia coli of catF, which encodes the catalytic subunit of catalase isozyme CatF of Pseudomonas syringae. Appl Microbiol Biotechnol 43: 656-666.
    • (1995) Appl Microbiol Biotechnol , vol.43 , pp. 656-666
    • Klotz, M.G.1    Kim, Y.C.2    Katsuwon, J.3    Anderson, A.J.4
  • 34
    • 0030854046 scopus 로고    scopus 로고
    • Phylogenetic relationships among prokaryotic and eukaryotic catalases
    • Klotz, M.G., Klassen, F.R., and Loewen, P.C. (1997) Phylogenetic relationships among prokaryotic and eukaryotic catalases. Mol Biol Evol 14: 951-958.
    • (1997) Mol Biol Evol , vol.14 , pp. 951-958
    • Klotz, M.G.1    Klassen, F.R.2    Loewen, P.C.3
  • 35
    • 0026624778 scopus 로고
    • Identification of heat-stable A-factor from Myxococcus xanthus
    • Kuspa, A., Plamann, L., and Kaiser, D. (1992) Identification of heat-stable A-factor from Myxococcus xanthus. J Bacteriol 174: 3319-3326.
    • (1992) J Bacteriol , vol.174 , pp. 3319-3326
    • Kuspa, A.1    Plamann, L.2    Kaiser, D.3
  • 36
    • 0002097003 scopus 로고
    • Regulation of bacterial catalase synthesis
    • Scandalios, J. (ed.). Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Loewen, P.C. (1992) Regulation of bacterial catalase synthesis. In Molecular Biology of Free Radical Scavenging Systems. Scandalios, J. (ed.). Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, pp. 96-116.
    • (1992) Molecular Biology of Free Radical Scavenging Systems , pp. 96-116
    • Loewen, P.C.1
  • 37
    • 0023449164 scopus 로고
    • Purification and characterization of catalase-1 from Bacillus subtilis
    • Loewen, P.C., and Switala, J. (1987a) Purification and characterization of catalase-1 from Bacillus subtilis. Biochem Cell Biol 65: 939-947.
    • (1987) Biochem Cell Biol , vol.65 , pp. 939-947
    • Loewen, P.C.1    Switala, J.2
  • 38
    • 0024044027 scopus 로고
    • Purification and characterization of spore-specific catalase-2 from Bacillus subtilis
    • Loewen, P.C., and Switala, J. (1987b) Purification and characterization of spore-specific catalase-2 from Bacillus subtilis. Biochem Cell Biol 66: 707-714.
    • (1987) Biochem Cell Biol , vol.66 , pp. 707-714
    • Loewen, P.C.1    Switala, J.2
  • 39
    • 0024225034 scopus 로고
    • Characterization of a unique methyl-specific restriction system in Streptomyces avermitilis
    • MacNeil, D.J. (1988) Characterization of a unique methyl-specific restriction system in Streptomyces avermitilis. J Bacteriol 170: 5607-5612.
    • (1988) J Bacteriol , vol.170 , pp. 5607-5612
    • MacNeil, D.J.1
  • 40
    • 0024327340 scopus 로고
    • Intergenic conjugation between Escherichia coli and Streptomyces species
    • Mazodier, P., Petter, R., and Thompson, C. (1989) Intergenic conjugation between Escherichia coli and Streptomyces species. J Bacteriol 171: 3538-3585.
    • (1989) J Bacteriol , vol.171 , pp. 3538-3585
    • Mazodier, P.1    Petter, R.2    Thompson, C.3
  • 41
    • 0016723556 scopus 로고
    • Role of amino acids in osmoregulation of non-halophilic bacteria
    • Measures, J.C. (1975) Role of amino acids in osmoregulation of non-halophilic bacteria. Nature 257: 398-400.
    • (1975) Nature , vol.257 , pp. 398-400
    • Measures, J.C.1
  • 43
    • 0029869234 scopus 로고    scopus 로고
    • catA, a new Aspergillus nidulans gene encoding a developmentally regulated catalase
    • Navarro, R.E., Stringer, M.A., Hansberg, W., Timberlake, W.E., and Aguirre, J. (1996) catA, a new Aspergillus nidulans gene encoding a developmentally regulated catalase. Curr Genet 29: 352-359.
    • (1996) Curr Genet , vol.29 , pp. 352-359
    • Navarro, R.E.1    Stringer, M.A.2    Hansberg, W.3    Timberlake, W.E.4    Aguirre, J.5
  • 44
    • 0026074553 scopus 로고
    • Nucleotide sequence of Escherichia coli katE, which encodes catalase HPII
    • von Ossowski, I., Mulvey, M.R., Leco, P.A., Borys, A., and Loewen, P.C. (1991) Nucleotide sequence of Escherichia coli katE, which encodes catalase HPII. J Bacteriol 173: 514-520.
    • (1991) J Bacteriol , vol.173 , pp. 514-520
    • Von Ossowski, I.1    Mulvey, M.R.2    Leco, P.A.3    Borys, A.4    Loewen, P.C.5
  • 45
    • 0031875675 scopus 로고    scopus 로고
    • Regulation of compatible solute accumulation in bacteria
    • Poolman, B., and Glaasker, E. (1998) Regulation of compatible solute accumulation in bacteria. Mol Microbiol 29: 397-407.
    • (1998) Mol Microbiol , vol.29 , pp. 397-407
    • Poolman, B.1    Glaasker, E.2
  • 47
    • 0021799340 scopus 로고
    • Mutations that affect utilization of a promoter in stationary-phase Bacillus subtilis
    • Ray, C., Hay, R.E., Carter, H.L., and Moran, Jr, C.P. (1985) Mutations that affect utilization of a promoter in stationary-phase Bacillus subtilis. J Bacteriol 163: 610-614.
    • (1985) J Bacteriol , vol.163 , pp. 610-614
    • Ray, C.1    Hay, R.E.2    Carter, H.L.3    Moran C.P., Jr.4
  • 48
    • 0019809562 scopus 로고
    • Expression of the Streptomyces enzyme endoglycosidase H in Escherichia coli
    • Robbins, P.W., Wirth, D.F., and Hering, C. (1981) Expression of the Streptomyces enzyme endoglycosidase H in Escherichia coli. J Biol Chem 256: 10640-10644.
    • (1981) J Biol Chem , vol.256 , pp. 10640-10644
    • Robbins, P.W.1    Wirth, D.F.2    Hering, C.3
  • 49
    • 0021252858 scopus 로고
    • Primary structure of the Streptomyces enzyme endo-beta-N-acetylglucosaminidase H
    • Robbins, P.W., Trimble, R.B., Wirth, D.F., Hering, C., Maley, F., Maley, G.F., et al. (1984) Primary structure of the Streptomyces enzyme endo-beta-N-acetylglucosaminidase H. J Biol Chem 259: 7577-7583.
    • (1984) J Biol Chem , vol.259 , pp. 7577-7583
    • Robbins, P.W.1    Trimble, R.B.2    Wirth, D.F.3    Hering, C.4    Maley, F.5    Maley, G.F.6
  • 51
    • 0031940127 scopus 로고    scopus 로고
    • Thioredoxin is an essential protein induced by multiple stresses in Bacillus subtilis
    • Scharf, C., Riethdorf, S., Ernst, H., Engelmann, S., Völker, U., and Hecker, M. (1998) Thioredoxin is an essential protein induced by multiple stresses in Bacillus subtilis. J Bacteriol 180: 1869-1877.
    • (1998) J Bacteriol , vol.180 , pp. 1869-1877
    • Scharf, C.1    Riethdorf, S.2    Ernst, H.3    Engelmann, S.4    Völker, U.5    Hecker, M.6
  • 52
    • 0021740996 scopus 로고
    • Promoter recognition by sigma-37 RNA polymerase from Bacillus subtilis
    • Tatti, K.M., and Moran, Jr, C.P. (1984) Promoter recognition by sigma-37 RNA polymerase from Bacillus subtilis. J Mol Biol 175: 285-297.
    • (1984) J Mol Biol , vol.175 , pp. 285-297
    • Tatti, K.M.1    Moran C.P., Jr.2
  • 53
    • 0031794754 scopus 로고    scopus 로고
    • A surface active protein involved in aerial hyphae formation in the filamentous fungus Schizophillum commune restores the capacity of a bald mutant of the filamentous bacterium Streptomyces coelicolor to erect aerial structures
    • Tillotson, R.D., Wosten, H.A., Richter, M., and Willey, J.M. (1998) A surface active protein involved in aerial hyphae formation in the filamentous fungus Schizophillum commune restores the capacity of a bald mutant of the filamentous bacterium Streptomyces coelicolor to erect aerial structures. Mol Microbiol 30: 595-602.
    • (1998) Mol Microbiol , vol.30 , pp. 595-602
    • Tillotson, R.D.1    Wosten, H.A.2    Richter, M.3    Willey, J.M.4
  • 55
    • 0021968633 scopus 로고
    • RNA polymerase heterogeneity in Streptomyces coelicolor
    • Westpheling, J., Ranes, M., and Losick, R. (1985) RNA polymerase heterogeneity in Streptomyces coelicolor. Nature 313: 22-27.
    • (1985) Nature , vol.313 , pp. 22-27
    • Westpheling, J.1    Ranes, M.2    Losick, R.3
  • 56
    • 0025883573 scopus 로고
    • Extracellular complementation of a developmental mutation implicates a small sporulation protein in aerial mycelium formation by Streptomyces coelicolor
    • Willey, J., Santamaria, R., Guijaro, J., and Losick, R. (1991) Extracellular complementation of a developmental mutation implicates a small sporulation protein in aerial mycelium formation by Streptomyces coelicolor. Cell 65: 641-650.
    • (1991) Cell , vol.65 , pp. 641-650
    • Willey, J.1    Santamaria, R.2    Guijaro, J.3    Losick, R.4
  • 57
    • 0032515092 scopus 로고    scopus 로고
    • Identification and subcellular localization of a novel Cu,Zn superoxide dismutase of Mycobacterium tuberculosis
    • Wu, C.H., Tsai-Wu, J.J., Huang, Y.T., Lin, C.Y., Lioua, G.G., and Lee, F.J. (1998) Identification and subcellular localization of a novel Cu,Zn superoxide dismutase of Mycobacterium tuberculosis. FEBS Lett 439: 192-196.
    • (1998) FEBS Lett , vol.439 , pp. 192-196
    • Wu, C.H.1    Tsai-Wu, J.J.2    Huang, Y.T.3    Lin, C.Y.4    Lioua, G.G.5    Lee, F.J.6


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