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Volumn 186, Issue 23, 2004, Pages 8123-8136

Regulation of iron transport in Streptococcus pneumoniae by RitR, an orphan response regulator

Author keywords

[No Author keywords available]

Indexed keywords

GENE PRODUCT; PROTEIN RITR; PROTEIN RR489; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 9244265524     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.186.23.8123-8136.2004     Document Type: Article
Times cited : (79)

References (59)
  • 1
    • 0036093097 scopus 로고    scopus 로고
    • Pharmacodynamics of the new fluoroquinolone gatifloxacin in murine thigh and lung infection models
    • Andes, D., and W. A. Craig. 2002. Pharmacodynamics of the new fluoroquinolone gatifloxacin in murine thigh and lung infection models. Antimicrob. Agents Chemother. 46:1665-1670.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 1665-1670
    • Andes, D.1    Craig, W.A.2
  • 3
    • 0028051713 scopus 로고
    • Molecular characterization of cap3A, a gene from the operon required for the synthesis of the capsule of Streptococcus pneumoniae type 3: Sequencing of mutations responsible for the unencapsulated phenotype and localization of the capsular cluster on the pneumococcal chromosome
    • Arrecubieta, C., R. Lopez, and E. Garcia. 1994. Molecular characterization of cap3A, a gene from the operon required for the synthesis of the capsule of Streptococcus pneumoniae type 3: sequencing of mutations responsible for the unencapsulated phenotype and localization of the capsular cluster on the pneumococcal chromosome. J. Bacteriol. 176:6375-6383.
    • (1994) J. Bacteriol. , vol.176 , pp. 6375-6383
    • Arrecubieta, C.1    Lopez, R.2    Garcia, E.3
  • 4
    • 0035104857 scopus 로고    scopus 로고
    • Genotoxicity of streptonigrin: A review
    • Bolzan, A. D., and M. S. Bianchi. 2001. Genotoxicity of streptonigrin: a review. Mutat. Res. 488:25-37.
    • (2001) Mutat. Res. , vol.488 , pp. 25-37
    • Bolzan, A.D.1    Bianchi, M.S.2
  • 5
    • 0035006337 scopus 로고    scopus 로고
    • A Streptococcus pneumoniae pathogenicity island encoding an ABC transporter involved in iron uptake and virulence
    • Brown, J. S., S. M. Gilliland, and D. W. Holden. 2001. A Streptococcus pneumoniae pathogenicity island encoding an ABC transporter involved in iron uptake and virulence. Mol. Microbiol. 40:572-585.
    • (2001) Mol. Microbiol. , vol.40 , pp. 572-585
    • Brown, J.S.1    Gilliland, S.M.2    Holden, D.W.3
  • 6
    • 0036070597 scopus 로고    scopus 로고
    • Characterization of pit, a Streptococcus pneumoniae iron uptake ABC transporter
    • Brown, J. S., S. M. Gilliland, J. Ruiz-Albert, and D. W. Holden. 2002. Characterization of pit, a Streptococcus pneumoniae iron uptake ABC transporter. Infect. Immun. 70:4389-4398.
    • (2002) Infect. Immun. , vol.70 , pp. 4389-4398
    • Brown, J.S.1    Gilliland, S.M.2    Ruiz-Albert, J.3    Holden, D.W.4
  • 7
    • 0036754957 scopus 로고    scopus 로고
    • Iron acquisition by Gram-positive bacterial pathogens
    • Brown, J. S., and D. W. Holden. 2002. Iron acquisition by Gram-positive bacterial pathogens. Microbes Infect. 4:1149-1156.
    • (2002) Microbes Infect. , vol.4 , pp. 1149-1156
    • Brown, J.S.1    Holden, D.W.2
  • 8
    • 0034778154 scopus 로고    scopus 로고
    • Immunization with components of two iron uptake ABC transporters protects mice against systemic Streptococcus pneumoniae infection
    • Brown J. S., A. D. Ogunniyi, M. C. Woodrow, D. W. Holden, and J. C. Paton. 2001. Immunization with components of two iron uptake ABC transporters protects mice against systemic Streptococcus pneumoniae infection. Infect. Immun. 69:6702-6706.
    • (2001) Infect. Immun. , vol.69 , pp. 6702-6706
    • Brown, J.S.1    Ogunniyi, A.D.2    Woodrow, M.C.3    Holden, D.W.4    Paton, J.C.5
  • 9
    • 0019640696 scopus 로고
    • The significance of iron in infection
    • Bullen, J. J. 1981. The significance of iron in infection. Rev. Infect. Dis. 3:1127-1138.
    • (1981) Rev. Infect. Dis. , vol.3 , pp. 1127-1138
    • Bullen, J.J.1
  • 10
    • 0029744688 scopus 로고    scopus 로고
    • Antisense RNA, fur, iron, and the regulation of iron transport genes in Vibrio anguillarum
    • Chen, Q., and J. H. Crosa. 1996. Antisense RNA, fur, iron, and the regulation of iron transport genes in Vibrio anguillarum. J. Biol. Chem. 271:18885-18891.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18885-18891
    • Chen, Q.1    Crosa, J.H.2
  • 11
    • 0033968782 scopus 로고    scopus 로고
    • Glutamate residues in the putative transmembrane region are required for the function of the VirS sensor histidine kinase from Clostridium perfringens
    • Cheung, J. K., and J. I. Rood. 2000. Glutamate residues in the putative transmembrane region are required for the function of the VirS sensor histidine kinase from Clostridium perfringens. Microbiology 146:517-525.
    • (2000) Microbiology , vol.146 , pp. 517-525
    • Cheung, J.K.1    Rood, J.I.2
  • 12
    • 0348230957 scopus 로고    scopus 로고
    • Quorum sensing and biofilm formation in streptococcal infections
    • Cvitkovitch, D. G., Y. H. Li, and R. P. Ellen. 2003. Quorum sensing and biofilm formation in streptococcal infections. J. Clin. Investig. 12:1626-1632.
    • (2003) J. Clin. Investig. , vol.12 , pp. 1626-1632
    • Cvitkovitch, D.G.1    Li, Y.H.2    Ellen, R.P.3
  • 13
    • 0031973704 scopus 로고    scopus 로고
    • Bacterial transcript imaging by hybridization of total RNA to oligonucleotide arrays
    • de Saizieu, A., U. Certa, J. Warrington, C. Gray, W. Keck, and J. Mous. 1998. Bacterial transcript imaging by hybridization of total RNA to oligonucleotide arrays. Nat. Biotechnol. 16:45-48.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 45-48
    • De Saizieu, A.1    Certa, U.2    Warrington, J.3    Gray, C.4    Keck, W.5    Mous, J.6
  • 14
    • 0027377225 scopus 로고
    • Identification of hydrogen peroxide as a Streptococcus pneumoniae toxin for rat alveolar epithelial cells
    • Duane, P. G., J. B. Rubins, H. R. Weisel, and E. N. Janoff. 1993. Identification of hydrogen peroxide as a Streptococcus pneumoniae toxin for rat alveolar epithelial cells. Infect. Immun. 61:4392-4397.
    • (1993) Infect. Immun. , vol.61 , pp. 4392-4397
    • Duane, P.G.1    Rubins, J.B.2    Weisel, H.R.3    Janoff, E.N.4
  • 15
    • 0042029733 scopus 로고    scopus 로고
    • Novel antioxidant role of alcohol dehydrogenase E from Escherichia coli
    • Echave, P., J. Tamarit, E. Cabiscol, and J. Ros. 2003. Novel antioxidant role of alcohol dehydrogenase E from Escherichia coli. J. Biol. Chem. 278:30193-30198.
    • (2003) J. Biol. Chem. , vol.278 , pp. 30193-30198
    • Echave, P.1    Tamarit, J.2    Cabiscol, E.3    Ros, J.4
  • 16
    • 0344172832 scopus 로고    scopus 로고
    • Opening the iron box: Transcriptional metalloregulation by the Fur protein
    • Escolar, L., J. Perez-Martin, and V. de Lorenzo. 1999. Opening the iron box: transcriptional metalloregulation by the Fur protein. J. Bacteriol. 181:6223-6229.
    • (1999) J. Bacteriol. , vol.181 , pp. 6223-6229
    • Escolar, L.1    Perez-Martin, J.2    De Lorenzo, V.3
  • 17
    • 1342304229 scopus 로고    scopus 로고
    • Structural basis for removal of adenine mispaired with 8-oxoguanine by MutY adenine DNA glycosylase
    • Fromme, J. C., A. Banerjee, S. J. Huang, and G. L. Verdine. 2004. Structural basis for removal of adenine mispaired with 8-oxoguanine by MutY adenine DNA glycosylase. Nature 427:652-656.
    • (2004) Nature , vol.427 , pp. 652-656
    • Fromme, J.C.1    Banerjee, A.2    Huang, S.J.3    Verdine, G.L.4
  • 18
    • 0027324378 scopus 로고
    • Mutagenesis by 8-oxoguanine: An enemy within
    • Grollman, A. P., and M. Moriya. 1993. Mutagenesis by 8-oxoguanine: an enemy within. Trends Genet. 9:246-249.
    • (1993) Trends Genet. , vol.9 , pp. 246-249
    • Grollman, A.P.1    Moriya, M.2
  • 19
    • 0035069457 scopus 로고    scopus 로고
    • Iron and metal regulation in bacteria
    • Hantke, K. 2002. Iron and metal regulation in bacteria. Curr. Opin. Microbiol. 4:172-177.
    • (2002) Curr. Opin. Microbiol. , vol.4 , pp. 172-177
    • Hantke, K.1
  • 20
    • 0028845364 scopus 로고
    • An unmodified heptadecapeptide pheromone induces competence for genetic transformation in Streptococcus pneumoniae
    • Havarstein, L. S., G. Coomaraswamy, and D. A. Morrison. 1995. An unmodified heptadecapeptide pheromone induces competence for genetic transformation in Streptococcus pneumoniae. Proc. Natl. Acad. Sci. USA 92:11140-11144.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11140-11144
    • Havarstein, L.S.1    Coomaraswamy, G.2    Morrison, D.A.3
  • 24
    • 0242608621 scopus 로고    scopus 로고
    • Pathways of oxidative damage
    • Imlay, J. A. 2003. Pathways of oxidative damage. Annu. Rev. Microbiol. 57:395-418.
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 395-418
    • Imlay, J.A.1
  • 25
    • 0346888587 scopus 로고    scopus 로고
    • On parametric empirical Bayes methods for comparing multiple groups using replicated gene expression profiles
    • Kendziorski, C. M., M. A. Newton, H. Lan, and M. N. Gould. 2003. On parametric empirical Bayes methods for comparing multiple groups using replicated gene expression profiles. Stat. Med. 22:3899-3914.
    • (2003) Stat. Med. , vol.22 , pp. 3899-3914
    • Kendziorski, C.M.1    Newton, M.A.2    Lan, H.3    Gould, M.N.4
  • 26
    • 0032854781 scopus 로고    scopus 로고
    • Domain organization and molecular characterization of 13 two-component systems identified by genome sequencing of Streptococcus pneumoniae
    • Lange R, C. Wagner, A. de Saizieu, N. Flint, J. Molnos, M. Stieger, P. Caspers, K. Kamber, W. Keck, and K. E. Amrein. 1999. Domain organization and molecular characterization of 13 two-component systems identified by genome sequencing of Streptococcus pneumoniae. Gene 237:223-234.
    • (1999) Gene , vol.237 , pp. 223-234
    • Lange, R.1    Wagner, C.2    De Saizieu, A.3    Flint, N.4    Molnos, J.5    Stieger, M.6    Caspers, P.7    Kamber, K.8    Keck, W.9    Amrein, K.E.10
  • 28
    • 0018421656 scopus 로고
    • Donor deoxyribonucleic acid length and marker effect in pneumococcal transformation
    • Lefevre, J. C., J. P. Claverys, and A. M. Sicard. 1979. Donor deoxyribonucleic acid length and marker effect in pneumococcal transformation. J. Bacteriol. 138:80-86.
    • (1979) J. Bacteriol. , vol.138 , pp. 80-86
    • Lefevre, J.C.1    Claverys, J.P.2    Sicard, A.M.3
  • 29
  • 30
    • 0034020990 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of CpsD negatively regulates capsular polysaccharide biosynthesis in Streptococcus pneumoniae
    • Morona, J. K., J. C. Paton, D. C. Miller, and R. Morona. 2000. Tyrosine phosphorylation of CpsD negatively regulates capsular polysaccharide biosynthesis in Streptococcus pneumoniae. Mol. Microbiol. 35:1431-1442.
    • (2000) Mol. Microbiol. , vol.35 , pp. 1431-1442
    • Morona, J.K.1    Paton, J.C.2    Miller, D.C.3    Morona, R.4
  • 31
    • 0031000618 scopus 로고    scopus 로고
    • Streptococcal competence for genetic transformation: Regulation by peptide pheromones
    • Morrison, D. A. 1997. Streptococcal competence for genetic transformation: regulation by peptide pheromones. Microb. Drug Resist. 3:27-37.
    • (1997) Microb. Drug Resist. , vol.3 , pp. 27-37
    • Morrison, D.A.1
  • 32
    • 0037240918 scopus 로고    scopus 로고
    • Control of the Salmonella ugd gene by three two component regulatory systems
    • Mouslim, C., and E. A. Groisman. 2003. Control of the Salmonella ugd gene by three two component regulatory systems. Mol. Microbiol. 47:335-344.
    • (2003) Mol. Microbiol. , vol.47 , pp. 335-344
    • Mouslim, C.1    Groisman, E.A.2
  • 34
    • 0036667415 scopus 로고    scopus 로고
    • A whole genome view of prokaryotic haem biosynthesis
    • Panek, H., and M. R. O'Brian. 2002. A whole genome view of prokaryotic haem biosynthesis. Microbiology 148:2273-2282.
    • (2002) Microbiology , vol.148 , pp. 2273-2282
    • Panek, H.1    O'Brian, M.R.2
  • 35
    • 0042324147 scopus 로고    scopus 로고
    • Two-component systems of Helicobacter pylori contribute to virulence in a mouse infection model
    • Panthel, K., P. Dietz, R. Haas, and D. Beier. 2003. Two-component systems of Helicobacter pylori contribute to virulence in a mouse infection model. Infect. Immun. 71:5381-5385.
    • (2003) Infect. Immun. , vol.71 , pp. 5381-5385
    • Panthel, K.1    Dietz, P.2    Haas, R.3    Beier, D.4
  • 36
    • 0033945724 scopus 로고    scopus 로고
    • Inhibitory and bactericidal effects of hydrogen peroxide production by Streptococcus pneumoniae on other inhabitants of the upper respiratory tract
    • Pericone, C. D., K. Overweg, P. W. Hermans, and J. N. Weiser. 2000. Inhibitory and bactericidal effects of hydrogen peroxide production by Streptococcus pneumoniae on other inhabitants of the upper respiratory tract. Infect. Immun. 68:3990-3997.
    • (2000) Infect. Immun. , vol.68 , pp. 3990-3997
    • Pericone, C.D.1    Overweg, K.2    Hermans, P.W.3    Weiser, J.N.4
  • 37
    • 0345687929 scopus 로고    scopus 로고
    • Factors contributing to hydrogen peroxide resistance in Streptococcus pneumoniae include pyruvate oxidase (SpxB) and avoidance of the toxic effects of the Fenton reaction
    • Pericone, C. D., S. Park, J. A. Imlay, and J. N. Weiser. 2003. Factors contributing to hydrogen peroxide resistance in Streptococcus pneumoniae include pyruvate oxidase (SpxB) and avoidance of the toxic effects of the Fenton reaction. J. Bacteriol. 185:6815-6825.
    • (2003) J. Bacteriol. , vol.185 , pp. 6815-6825
    • Pericone, C.D.1    Park, S.2    Imlay, J.A.3    Weiser, J.N.4
  • 38
    • 0031925161 scopus 로고    scopus 로고
    • Isolation and characterization of three Streptococcus pneumoniae transformation-specific loci by use of a lacZ reporter insertion vector
    • Pestova, E. V., and D. A. Morrison. 1998. Isolation and characterization of three Streptococcus pneumoniae transformation-specific loci by use of a lacZ reporter insertion vector. J. Bacteriol. 180:2701-2710.
    • (1998) J. Bacteriol. , vol.180 , pp. 2701-2710
    • Pestova, E.V.1    Morrison, D.A.2
  • 39
    • 0035283587 scopus 로고    scopus 로고
    • Redox-operated genetic switches: The SoxR and OxyR transcription factors
    • Pomposiello, P. J., and B. Demple. 2001. Redox-operated genetic switches: the SoxR and OxyR transcription factors. Trends Biotechnol. 19:109-114.
    • (2001) Trends Biotechnol. , vol.19 , pp. 109-114
    • Pomposiello, P.J.1    Demple, B.2
  • 40
    • 0032851843 scopus 로고    scopus 로고
    • Characterization of a manganese dependent regulatory protein, TroR, from Treponema pallidum
    • Posey, J. E., J. M. Hardham, S. J. Norris, and F. C. Gherardini. 1999. Characterization of a manganese dependent regulatory protein, TroR, from Treponema pallidum. Proc. Natl. Acad. Sci. USA 96:10887-10892.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10887-10892
    • Posey, J.E.1    Hardham, J.M.2    Norris, S.J.3    Gherardini, F.C.4
  • 41
    • 0034595617 scopus 로고    scopus 로고
    • Lack of a role for iron in the Lyme disease pathogen
    • Posey, J. E., and F. C. Gherardini. 2000. Lack of a role for iron in the Lyme disease pathogen. Science 288:1651-1653.
    • (2000) Science , vol.288 , pp. 1651-1653
    • Posey, J.E.1    Gherardini, F.C.2
  • 42
    • 0037424379 scopus 로고    scopus 로고
    • Molecular basis of H2O2 resistance mediated by streptococcal Dpr. Demonstration of the functional involvement of the putative ferroxidase center by site-directed mutagenesis in Streptococcus suis
    • Pulliainen, A. T., S. Haataja, S. Kahkonen, and J. Finne. 2003. Molecular basis of H2O2 resistance mediated by streptococcal Dpr. Demonstration of the functional involvement of the putative ferroxidase center by site-directed mutagenesis in Streptococcus suis. J. Biol. Chem. 278:7996-8005.
    • (2003) J. Biol. Chem. , vol.278 , pp. 7996-8005
    • Pulliainen, A.T.1    Haataja, S.2    Kahkonen, S.3    Finne, J.4
  • 44
    • 0034079940 scopus 로고    scopus 로고
    • Hyperrecombination in Streptococcus pneumoniae depends on an atypical mutY homologue
    • Samrakandi, M. M., and F. Pasta. 2000. Hyperrecombination in Streptococcus pneumoniae depends on an atypical mutY homologue. J. Bacteriol. 182:3353-3360.
    • (2000) J. Bacteriol. , vol.182 , pp. 3353-3360
    • Samrakandi, M.M.1    Pasta, F.2
  • 45
    • 0032833084 scopus 로고    scopus 로고
    • Identification of a two-component signal transduction system from Corynebacterium diphtheriae that activates gene expression in response to the presence of heme and hemoglobin
    • Schmitt, M. P. 1999. Identification of a two-component signal transduction system from Corynebacterium diphtheriae that activates gene expression in response to the presence of heme and hemoglobin. J. Bacteriol. 181:5330-5340.
    • (1999) J. Bacteriol. , vol.181 , pp. 5330-5340
    • Schmitt, M.P.1
  • 46
    • 0028884775 scopus 로고
    • Genetics of pentose-phosphate pathway enzymes of Escherichia coli K-12
    • Sprenger, G. A. 1995. Genetics of pentose-phosphate pathway enzymes of Escherichia coli K-12. Arch. Microbiol. 164:324-330.
    • (1995) Arch. Microbiol. , vol.164 , pp. 324-330
    • Sprenger, G.A.1
  • 47
    • 0033590613 scopus 로고    scopus 로고
    • Integrational plasmids for the tetracycline-regulated expression of genes in Streptococcus pneumoniae
    • Stieger, M., B. Wohlgensinger, M. Kamber, R. Lutz, and K. Keck. 1999. Integrational plasmids for the tetracycline-regulated expression of genes in Streptococcus pneumoniae. Gene 226:243-251.
    • (1999) Gene , vol.226 , pp. 243-251
    • Stieger, M.1    Wohlgensinger, B.2    Kamber, M.3    Lutz, R.4    Keck, K.5
  • 49
    • 0027363322 scopus 로고
    • Hemin utilization is related to virulence of Streptococcus pneumoniae
    • Tai, S. S., C. J. Lee, and R. E. Winter. 1993. Hemin utilization is related to virulence of Streptococcus pneumoniae. Infect. Immun. 61:5401-5405.
    • (1993) Infect. Immun. , vol.61 , pp. 5401-5405
    • Tai, S.S.1    Lee, C.J.2    Winter, R.E.3
  • 50
    • 0037470936 scopus 로고    scopus 로고
    • A solute binding protein of Streptococcus pneumoniae iron transport
    • Tai, S. S., C. Yu, and J. K. Lee. 2003. A solute binding protein of Streptococcus pneumoniae iron transport. FEMS Microbiol. Lett. 220:303-308.
    • (2003) FEMS Microbiol. Lett. , vol.220 , pp. 303-308
    • Tai, S.S.1    Yu, C.2    Lee, J.K.3
  • 51
    • 0028149973 scopus 로고
    • Iron, DtxR, and the regulation of diphtheria toxin expression
    • Tao, X., N. Schiering, H. Y. Zeng, D. Ringe, and J. R. Murphy. 1994. Iron, DtxR, and the regulation of diphtheria toxin expression. Mol. Microbiol. 14:191-197.
    • (1994) Mol. Microbiol. , vol.14 , pp. 191-197
    • Tao, X.1    Schiering, N.2    Zeng, H.Y.3    Ringe, D.4    Murphy, J.R.5
  • 54
    • 0036178058 scopus 로고    scopus 로고
    • Virulence of Streptococcus pneumoniae: PsaA mutants are hypersensitive to oxidative stress
    • Tseng, H. J., A. G. McEwan, J. C. Paton, and M. P. Jennings. 2002. Virulence of Streptococcus pneumoniae: PsaA mutants are hypersensitive to oxidative stress. Infect. Immun. 70:1635-1639.
    • (2002) Infect. Immun. , vol.70 , pp. 1635-1639
    • Tseng, H.J.1    McEwan, A.G.2    Paton, J.C.3    Jennings, M.P.4
  • 55
    • 0029972190 scopus 로고    scopus 로고
    • A vancomycin-inducible lacZ reporter system in Bacillus subtilis: Induction by antibiotics that inhibit cell wall synthesis and by lysozyme
    • Ulijasz, A. T., A. Grenader, and B. Weisblum. 1996. A vancomycin-inducible lacZ reporter system in Bacillus subtilis: induction by antibiotics that inhibit cell wall synthesis and by lysozyme. J. Bacteriol. 178:6305-6309.
    • (1996) J. Bacteriol. , vol.178 , pp. 6305-6309
    • Ulijasz, A.T.1    Grenader, A.2    Weisblum, B.3
  • 56
    • 0034687094 scopus 로고    scopus 로고
    • Peptide analogues of the VanS catalytic center inhibit VanR binding to its cognate promoter
    • Ulijasz, A. T., B. K. Kay, and B. Weisblum. 2000. Peptide analogues of the VanS catalytic center inhibit VanR binding to its cognate promoter. Biochemistry 39:11417-11424.
    • (2000) Biochemistry , vol.39 , pp. 11417-11424
    • Ulijasz, A.T.1    Kay, B.K.2    Weisblum, B.3
  • 58
    • 0020358807 scopus 로고
    • Iron requirement in the bactericidal mechanism of streptonigrin
    • Yeowell, H. N., and J. R. White. 1982. Iron requirement in the bactericidal mechanism of streptonigrin. Antimicrob. Agents Chemother. 22:961-968.
    • (1982) Antimicrob. Agents Chemother. , vol.22 , pp. 961-968
    • Yeowell, H.N.1    White, J.R.2
  • 59
    • 0038460063 scopus 로고    scopus 로고
    • The DNA excision repair system of the highly radio-resistant bacterium Deinococcus radiodurans is facilitated by the pentose phosphate pathway
    • Zhang, Y. M., J. K. Liu, and T. Y. Wong. 2003. The DNA excision repair system of the highly radio-resistant bacterium Deinococcus radiodurans is facilitated by the pentose phosphate pathway. Mol. Microbiol. 48:1317-1323.
    • (2003) Mol. Microbiol. , vol.48 , pp. 1317-1323
    • Zhang, Y.M.1    Liu, J.K.2    Wong, T.Y.3


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