메뉴 건너뛰기




Volumn 194, Issue 6, 2012, Pages 1552-1561

Physiology of resistant deinococcus geothermalis bacterium aerobically cultivated in low-manganese medium

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CARBON; CATALASE; CHAPERONE; IRON SULFUR PROTEIN; MANGANESE; OXYGEN; PEPTIDYLPROLYL ISOMERASE; PROTEOME; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SUCCINIC ACID; SUPEROXIDE DISMUTASE;

EID: 84857981938     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.06429-11     Document Type: Article
Times cited : (22)

References (61)
  • 2
    • 0020118402 scopus 로고
    • The scavenging of superoxide radical by manganeous complexes: in vitro
    • Archibald FS, Fridovich I. 1982. The scavenging of superoxide radical by manganeous complexes: in vitro. Arch. Biochem. Biophys. 214:452- 463.
    • (1982) Arch. Biochem. Biophys. , vol.214 , pp. 452-463
    • Archibald, F.S.1    Fridovich, I.2
  • 3
    • 38449089431 scopus 로고    scopus 로고
    • The Listeria monocytogenes homolog of the Escherichia coli era gene is involved in adhesion to inert surfaces
    • Auvray F, Chassaing D, Duprat C, Carpentier B. 2007. The Listeria monocytogenes homolog of the Escherichia coli era gene is involved in adhesion to inert surfaces. Appl. Environ. Microbiol. 73:7789 -7792.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 7789-7792
    • Auvray, F.1    Chassaing, D.2    Duprat, C.3    Carpentier, B.4
  • 4
    • 0029081870 scopus 로고
    • + oxidoreductase gene of Escherichia coli does not affect anaerobic growth but increases sensitivity to paraquat
    • Bianchi V, Haggård-Ljungquist E, Pontis E, Reichard P. 1995. Interruption of the ferredoxin(flavodoxin) NADP_ oxidoreductase gene of Escherichia coli does not affect anaerobic growth but increases sensitivity to paraquat. J. Bacteriol. 177:4528-4531.
    • (1995) J. Bacteriol. , vol.177 , pp. 4528-4531
    • Bianchi, V.1    Haggård-Ljungquist, E.2    Pontis, E.3    Reichard, P.4
  • 6
    • 0026026818 scopus 로고
    • The GTPase superfamily: conserved structure and molecular mechanism
    • Bourne HR, Sanders DA, McCormick F. 1991. The GTPase superfamily: conserved structure and molecular mechanism. Nature 349:117-127.
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 8
    • 0034837018 scopus 로고    scopus 로고
    • A comprehensive two-dimensional map of cytosolic proteins of Bacillus subtilis
    • Büttner K, et al. 2001. A comprehensive two-dimensional map of cytosolic proteins of Bacillus subtilis. Electrophoresis 22:2908 -2935.
    • (2001) Electrophoresis , vol.22 , pp. 2908-2935
    • Büttner, K.1
  • 9
    • 0034152767 scopus 로고    scopus 로고
    • Oxidative stress in bacteria and protein damage by reactive oxygen species
    • Cabiscol E, Tamarit J, Ros J. 1999. Oxidative stress in bacteria and protein damage by reactive oxygen species. Int. Microbiol. 3:3- 8.
    • (1999) Int. Microbiol. , vol.3 , pp. 3-8
    • Cabiscol, E.1    Tamarit, J.2    Ros, J.3
  • 10
    • 0032547711 scopus 로고    scopus 로고
    • Characterization of bacterial proteomes by twodimensional electrophoresis
    • Cash P. 1998. Characterization of bacterial proteomes by twodimensional electrophoresis. Anal. Chim. Acta 372:121-145.
    • (1998) Anal. Chim. Acta , vol.372 , pp. 121-145
    • Cash, P.1
  • 11
    • 0025268546 scopus 로고
    • Manganese(II) induces cell division and increases in superoxide dismutase and catalase activities in an aging deinococcal culture
    • Chou FI, Tan ST. 1990. Manganese(II) induces cell division and increases in superoxide dismutase and catalase activities in an aging deinococcal culture. J. Bacteriol. 172:2029 -2035.
    • (1990) J. Bacteriol. , vol.172 , pp. 2029-2035
    • Chou, F.I.1    Tan, S.T.2
  • 12
    • 8344278843 scopus 로고    scopus 로고
    • Accumulation of Mn(II) in Deinococcus radiodurans facilitates gamma-radiation resistance
    • Daly MJ, et al. 2004. Accumulation of Mn(II) in Deinococcus radiodurans facilitates gamma-radiation resistance. Science 306:1025-1028.
    • (2004) Science , vol.306 , pp. 1025-1028
    • Daly, M.J.1
  • 13
    • 34247375191 scopus 로고    scopus 로고
    • Protein oxidation implicated as the primary determinant of bacterial radioresistance
    • Daly MJ, et al. 2007. Protein oxidation implicated as the primary determinant of bacterial radioresistance. PLoS Biol. 5:e92.
    • (2007) PLoS Biol , vol.5
    • Daly, M.J.1
  • 14
    • 0032502811 scopus 로고    scopus 로고
    • The involvement of cell-to-cell signals in the development of a bacterial biofilm
    • Davies DG, et al. 1998. The involvement of cell-to-cell signals in the development of a bacterial biofilm. Science 280:295-298.
    • (1998) Science , vol.280 , pp. 295-298
    • Davies, D.G.1
  • 15
    • 0032213238 scopus 로고    scopus 로고
    • Bacterial senescence: stasis results in increased and differential oxidation of cytoplasmic proteins leading to developmental induction of the heat shock regulon
    • Dukan S, Nyström T. 1998. Bacterial senescence: stasis results in increased and differential oxidation of cytoplasmic proteins leading to developmental induction of the heat shock regulon. Genes Dev. 12:3431- 3441.
    • (1998) Genes Dev , vol.12 , pp. 3431-3441
    • Dukan, S.1    Nyström, T.2
  • 17
    • 0030808693 scopus 로고    scopus 로고
    • Deinococcus geothermalis sp. nov. and Deinococcus murrayi sp. nov., two extremely radiation-resistant and slightly thermophilic species from hot springs
    • Ferreira AC, et al. 1997. Deinococcus geothermalis sp. nov. and Deinococcus murrayi sp. nov., two extremely radiation-resistant and slightly thermophilic species from hot springs. Int. J. Syst. Bacteriol. 47:939 -947.
    • (1997) Int. J. Syst. Bacteriol. , vol.47 , pp. 939-947
    • Ferreira, A.C.1
  • 18
    • 42049105959 scopus 로고    scopus 로고
    • Protein Oxidation: key to bacterial desiccation resistance?
    • Fredrickson JK, et al. 2008. Protein Oxidation: key to bacterial desiccation resistance? ISME J. 2:393- 403.
    • (2008) ISME J , vol.2 , pp. 393-403
    • Fredrickson, J.K.1
  • 19
    • 20144388982 scopus 로고    scopus 로고
    • How radiation kills cells: survival of Deinococcus radiodurans and Shewanella oneidensis under oxidative stress
    • Ghosal D, et al. 2005. How radiation kills cells: survival of Deinococcus radiodurans and Shewanella oneidensis under oxidative stress. FEMS Microbiol. Rev. 29:361- 475.
    • (2005) FEMS Microbiol. Rev. , vol.29 , pp. 361-475
    • Ghosal, D.1
  • 20
    • 0029018721 scopus 로고
    • Metabolic sources of hydrogen peroxide in aerobically growing Escherichia coli
    • Gonzáles-Flecha B, 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
    • Gonzáles-Flecha, B.1    Demple, B.2
  • 21
    • 0031794743 scopus 로고    scopus 로고
    • Protein phylogenies and signature sequences: a reappraisal of evolutionary relationships among archaebacteria, eubacteria, and eukaryotes
    • Gupta RS. 1998. Protein phylogenies and signature sequences: a reappraisal of evolutionary relationships among archaebacteria, eubacteria, and eukaryotes. Microbiol. Mol. Biol. Rev. 62:1435-1491.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 1435-1491
    • Gupta, R.S.1
  • 22
    • 0029095434 scopus 로고
    • Twodimensional polyacrylamide gel electrophoresis with immobilized pH gradients in the first dimension (IPG-Dalt): the state of the art and the controversy of vertical versus horizontal systems
    • Görg A, Boguth G, Obermeier C, Posch A, Weiss W. 1995. Twodimensional polyacrylamide gel electrophoresis with immobilized pH gradients in the first dimension (IPG-Dalt): the state of the art and the controversy of vertical versus horizontal systems. Electrophoresis 16: 1079-1086.
    • (1995) Electrophoresis , vol.16 , pp. 1079-1086
    • Görg, A.1    Boguth, G.2    Obermeier, C.3    Posch, A.4    Weiss, W.5
  • 23
    • 0030052910 scopus 로고    scopus 로고
    • Roles of molecular chaperones in protein degradation
    • Hayes SA, Dice JF. 1996. Roles of molecular chaperones in protein degradation. J. Cell Biol. 132:255-258.
    • (1996) J. Cell Biol. , vol.132 , pp. 255-258
    • Hayes, S.A.1    Dice, J.F.2
  • 24
    • 63049097123 scopus 로고    scopus 로고
    • High cell density production of Deinococcus radiodurans under optimized conditions
    • He Y. 2009. High cell density production of Deinococcus radiodurans under optimized conditions. J. Ind. Microbiol. Biotechnol. 36:539 -546.
    • (2009) J. Ind. Microbiol. Biotechnol. , vol.36 , pp. 539-546
    • He, Y.1
  • 25
    • 84857932098 scopus 로고    scopus 로고
    • Proteomics of microorganisms: fundamental aspects and application
    • Scheper T (ed), Springer-Verlag, Berlin
    • Hecker M, Müllner S. 2003. Proteomics of microorganisms: fundamental aspects and application, p 27-140. In Scheper T (ed), Advances in biochemical engineering biotechnology. Springer-Verlag, Berlin, Germany.
    • (2003) Advances in biochemical engineering biotechnology , pp. 270-140
    • Hecker, M.1    Müllner, S.2
  • 26
    • 10644274361 scopus 로고    scopus 로고
    • Towards a comprehensive understanding of Bacillus subtilis cell physiology by physiological proteomics
    • Hecker M, Völker U. 2004. Towards a comprehensive understanding of Bacillus subtilis cell physiology by physiological proteomics. Proteomics 4:3727-3750.
    • (2004) Proteomics , vol.4 , pp. 3727-3750
    • Hecker, M.1    Völker, U.2
  • 28
    • 33645065589 scopus 로고    scopus 로고
    • Iron-sulfur clusters and the problem with oxygen
    • Imlay JA. 2006. Iron-sulfur clusters and the problem with oxygen. Mol. Microbiol. 59:1073-1082.
    • (2006) Mol. Microbiol. , vol.59 , pp. 1073-1082
    • Imlay, J.A.1
  • 29
    • 50649117912 scopus 로고    scopus 로고
    • Cellular defenses against superoxide and hydrogen peroxide
    • Imlay JA. 2008. Cellular defenses against superoxide and hydrogen peroxide. Annu. Rev. Biochem. 77:755-776.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 755-776
    • Imlay, J.A.1
  • 30
    • 0034916351 scopus 로고    scopus 로고
    • Out of iron age: new insights into the critical role of manganese homeostasis in bacteria
    • Jakubovich NS, Jenkinson HF. 2001. Out of iron age: new insights into the critical role of manganese homeostasis in bacteria. Microbiol. 147: 1709-1718.
    • (2001) Microbiol , vol.147 , pp. 1709-1718
    • Jakubovich, N.S.1    Jenkinson, H.F.2
  • 32
    • 0040643267 scopus 로고    scopus 로고
    • Cytochrome bd terminal oxidase
    • Jünemann S. 1997. Cytochrome bd terminal oxidase. Biochim. Biophys. Acta 1321:107-127.
    • (1997) Biochim. Biophys. Acta , vol.1321 , pp. 107-127
    • Jünemann, S.1
  • 33
    • 51649111614 scopus 로고    scopus 로고
    • Prokaryotic microbiota of recycled paper mills with low or zero effluent
    • Kanto Oqvist C, et al. 2008. Prokaryotic microbiota of recycled paper mills with low or zero effluent. J. Ind. Microbiol. Biotechnol. 35:1165- 1173.
    • (2008) J. Ind. Microbiol. Biotechnol. , vol.35 , pp. 1165-1173
    • Kanto Oqvist, C.1
  • 34
    • 0346034972 scopus 로고    scopus 로고
    • Distribution of microorganisms in the subsurface of the manus basin hydrothermal vent field in Papua New Guinea
    • Kimura H, Asada R, Masta A, Naganuma T. 2003. Distribution of microorganisms in the subsurface of the manus basin hydrothermal vent field in Papua New Guinea. Appl. Environ. Microbiol. 69:644-648.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 644-648
    • Kimura, H.1    Asada, R.2    Masta, A.3    Naganuma, T.4
  • 36
    • 0036175587 scopus 로고    scopus 로고
    • The flavoenzyme ferredoxin (flavodoxin)-NADP(H) Reductase modulates NADP(H) homeostasis during the soxRS response of Escherichia coli
    • Krapp AR, et al. 2002. The flavoenzyme ferredoxin (flavodoxin)-NADP(H) Reductase modulates NADP(H) homeostasis during the soxRS response of Escherichia coli. J. Bacteriol. 184:1474 -1480.
    • (2002) J. Bacteriol. , vol.184 , pp. 1474-1480
    • Krapp, A.R.1
  • 37
    • 0345708209 scopus 로고    scopus 로고
    • Structural and functional features of the Escherichia coli hydroperoxide resistance protein OsmC
    • Lesniak J, Barton WA, Nikolov DB. 2003. Structural and functional features of the Escherichia coli hydroperoxide resistance protein OsmC. Protein Sci. 12:2838 -2843.
    • (2003) Protein Sci , vol.12 , pp. 2838-2843
    • Lesniak, J.1    Barton, W.A.2    Nikolov, D.B.3
  • 38
    • 76649109593 scopus 로고    scopus 로고
    • Two-dimensional proteome reference map for the radiation resistant bacterium Deinococcus geothermalis
    • Liedert C, et al. 2010. Two-dimensional proteome reference map for the radiation resistant bacterium Deinococcus geothermalis. Proteomics 10: 1-9.
    • (2010) Proteomics , vol.10 , pp. 1-9
    • Liedert, C.1
  • 39
    • 0026778382 scopus 로고
    • Fumarase C, the stable fumarase of Escherichia coli, is controlled by the soxRS regulon
    • Liochev SI, Fridovich I. 1992. Fumarase C, the stable fumarase of Escherichia coli, is controlled by the soxRS regulon. Proc. Natl. Acad. Sci. U. S. A. 89:5892-5896.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 5892-5896
    • Liochev, S.I.1    Fridovich, I.2
  • 40
    • 0037388447 scopus 로고    scopus 로고
    • Transcriptome dynamics of Deinococcus radiodurans recovering from ionizing radiation
    • Liu Y, et al. 2003. Transcriptome dynamics of Deinococcus radiodurans recovering from ionizing radiation. Proc. Natl. Acad. Sci. U. S. A. 100: 4191-4196.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 4191-4196
    • Liu, Y.1
  • 41
    • 40149108041 scopus 로고    scopus 로고
    • The tricarboxylic acid cycle, an Ancient metabolic network with a novel twist
    • Mailloux RJ, et al. 2007. The tricarboxylic acid cycle, an Ancient metabolic network with a novel twist. PLoS One 2:e690.
    • (2007) PLoS One , vol.2
    • Mailloux, R.J.1
  • 42
    • 35948982966 scopus 로고    scopus 로고
    • Deinococcus geothermalis: the pool of extreme radiation resistance genes shrinks
    • Makarova KS, et al. 2007. Deinococcus geothermalis: the pool of extreme radiation resistance genes shrinks. PLoS One 2:e955.
    • (2007) PLoS One , vol.2
    • Makarova, K.S.1
  • 43
    • 0037415722 scopus 로고    scopus 로고
    • SufC: an unorthodox cytoplasmic ABC/ATPase required for [Fe-S] biogenesis under oxidative stress
    • Nachin L, Loiseau L, Expert D, Barras F. 2003. SufC: an unorthodox cytoplasmic ABC/ATPase required for [Fe-S] biogenesis under oxidative stress. EMBO 22:427- 437.
    • (2003) EMBO , vol.22 , pp. 427-437
    • Nachin, L.1    Loiseau, L.2    Expert, D.3    Barras, F.4
  • 44
    • 55949105767 scopus 로고    scopus 로고
    • Quantitative contributions of bacteria and of Deinococcus geothermalis to deposits and slimes in paper industry
    • Peltola M, et al. 2008. Quantitative contributions of bacteria and of Deinococcus geothermalis to deposits and slimes in paper industry. J. Ind. Microbiol. Biotechnol. 35:1651-1657.
    • (2008) J. Ind. Microbiol. Biotechnol. , vol.35 , pp. 1651-1657
    • Peltola, M.1
  • 45
    • 81055125747 scopus 로고    scopus 로고
    • Effects of polarization in the presence and absence of biocides on biofilms in a simulated paper machine water
    • Peltola M, et al. 2011. Effects of polarization in the presence and absence of biocides on biofilms in a simulated paper machine water. J. Ind. Microbiol. Biotechnol. 38:1719 -1727.
    • (2011) J. Ind. Microbiol. Biotechnol. , vol.38 , pp. 1719-1727
    • Peltola, M.1
  • 46
    • 0035205423 scopus 로고    scopus 로고
    • Complex regulatory network controls initial adhesion and biofilm formation in Escherichia coli via regulation of the csgD gene
    • Prigent-Combaret C, et al. 2001. Complex regulatory network controls initial adhesion and biofilm formation in Escherichia coli via regulation of the csgD gene. J. Bacteriol. 24:7213-7223.
    • (2001) J. Bacteriol. , vol.24 , pp. 7213-7223
    • Prigent-Combaret, C.1
  • 47
    • 0032486744 scopus 로고    scopus 로고
    • Microelectrode measurements of local mass transport rates in heterogenous biofilms
    • Rasmussen K, Lewandowski Z. 1997. Microelectrode measurements of local mass transport rates in heterogenous biofilms. Biotechnol. Bioeng. 59:302-309.
    • (1997) Biotechnol. Bioeng. , vol.59 , pp. 302-309
    • Rasmussen, K.1    Lewandowski, Z.2
  • 48
    • 33644765069 scopus 로고    scopus 로고
    • Destruction of Deinococcus geothermalis biofilm by photocatalytic ALD and sol-gel TiO2 surfaces
    • Raulio M, et al. 2006. Destruction of Deinococcus geothermalis biofilm by photocatalytic ALD and sol-gel TiO2 surfaces. J. Ind. Microbiol. Biotechnol. 33:261-268.
    • (2006) J. Ind. Microbiol. Biotechnol. , vol.33 , pp. 261-268
    • Raulio, M.1
  • 49
    • 33749335872 scopus 로고    scopus 로고
    • Characterization of adhesion threads of Deinococcus geothermalis as type IV pili
    • Saarimaa C, et al. 2006. Characterization of adhesion threads of Deinococcus geothermalis as type IV pili. J. Bacteriol. 188:7016 -7021.
    • (2006) J. Bacteriol. , vol.188 , pp. 7016-7021
    • Saarimaa, C.1
  • 50
    • 17844397959 scopus 로고    scopus 로고
    • The GTP binding protein Obg homolog ObgE is involved in ribosome maturation
    • Sato A, et al. 2005. The GTP binding protein Obg homolog ObgE is involved in ribosome maturation. Genes Cells 10:393- 408.
    • (2005) Genes Cells , vol.10 , pp. 393-408
    • Sato, A.1
  • 51
    • 18244402173 scopus 로고    scopus 로고
    • Global transcriptional and proteomic analysis of the Sig1 heat shock regulon of Deinococcus radiodurans
    • Schmid AK, Howel HA, Battista JR, Peterson SN, Lidstrom ME. 2005. Global transcriptional and proteomic analysis of the Sig1 heat shock regulon of Deinococcus radiodurans. J. Bacteriol. 187:3339 -3351.
    • (2005) J. Bacteriol. , vol.187 , pp. 3339-3351
    • Schmid, A.K.1    Howel, H.A.2    Battista, J.R.3    Peterson, S.N.4    Lidstrom, M.E.5
  • 52
    • 49949085210 scopus 로고    scopus 로고
    • A novel strategy involved anti-oxidative defense: the conversion ofNADHintoNADPHby a metabolic network
    • Singh R, Lemire J, Mailloux RJ, Appanna VD. 2008. A novel strategy involved anti-oxidative defense: the conversion ofNADHintoNADPHby a metabolic network. PLoS One 3:e2682.
    • (2008) PLoS One , vol.3
    • Singh, R.1    Lemire, J.2    Mailloux, R.J.3    Appanna, V.D.4
  • 53
    • 77956540473 scopus 로고    scopus 로고
    • Proteomic analysis of membrane proteins from a radioresistant and moderate thermophilic bacterium Deinococcus geothermalis
    • Tian B, et al. 2010. Proteomic analysis of membrane proteins from a radioresistant and moderate thermophilic bacterium Deinococcus geothermalis. Mol. Biosyst. 10:2068 -2077.
    • (2010) Mol. Biosyst. , vol.10 , pp. 2068-2077
    • Tian, B.1
  • 54
    • 38049119866 scopus 로고    scopus 로고
    • +/ATP ratio for ATP synthesis of prokaryotic V-ATPase from Thermus thermophilus
    • Toei M, et al. 2007. Dodecamer rotor ring defines H_ /ATP ratio for ATP synthesis of prokaryotic V-ATPase from Thermus thermophilus. Proc. Natl. Acad. Sci. U. S. A. 104:20256 -20261.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 20256-20261
    • Toei, M.1
  • 56
    • 0028979581 scopus 로고
    • Repair, refold, recycle: how bacteria can deal with spontaneous and environmental damage to proteins
    • Visick JE, Clarke S. 1995. Repair, refold, recycle: how bacteria can deal with spontaneous and environmental damage to proteins. Mol. Microbiol. 5:835- 845.
    • (1995) Mol. Microbiol. , vol.5 , pp. 835-845
    • Visick, J.E.1    Clarke, S.2
  • 58
    • 0031851909 scopus 로고    scopus 로고
    • Microbial communities of printing paper machines
    • Väisänen OM, et al. 1998. Microbial communities of printing paper machines. J. Appl. Microbiol. 84:1069 -1084.
    • (1998) J. Appl. Microbiol. , vol.84 , pp. 1069-1084
    • Väisänen, O.M.1
  • 59
    • 0037377827 scopus 로고    scopus 로고
    • Microarray analysis of Pseudomonas aeruginosa quorum-sensing regulons: effects of growth phase and environment
    • Wagner VE, Bushnell D, Passador L, Brooks AI, Iglewski BH. 2003. Microarray analysis of Pseudomonas aeruginosa quorum-sensing regulons: effects of growth phase and environment. J. Bacteriol. 7:2080 -2095.
    • (2003) J. Bacteriol. , vol.7 , pp. 2080-2095
    • Wagner, V.E.1    Bushnell, D.2    Passador, L.3    Brooks, A.I.4    Iglewski, B.H.5
  • 60
    • 0025695393 scopus 로고
    • Thermus thermophilus membrane-associated ATPase: indication of a eubacterial V-type ATPase
    • Yokoyama K, Oshima T, Yoshida M. 1990. Thermus thermophilus membrane-associated ATPase: indication of a eubacterial V-type ATPase. J. Biol. Chem. 265:21946 -21950.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21946-21950
    • Yokoyama, K.1    Oshima, T.2    Yoshida, M.3
  • 61
    • 0033988932 scopus 로고    scopus 로고
    • Induction of a futile Embden-Mayerhof-Parnas pathway in Deinococcus radiodurans by Mn: possible role of the pentose phosphate pathway in cell survival
    • Zhang YM, Wong TY, Chen LY, Lin CS, Liu JK. 2000. Induction of a futile Embden-Mayerhof-Parnas pathway in Deinococcus radiodurans by Mn: possible role of the pentose phosphate pathway in cell survival. Appl. Environ. Microbiol. 1:105-112.
    • (2000) Appl. Environ. Microbiol. , vol.1 , pp. 105-112
    • Zhang, Y.M.1    Wong, T.Y.2    Chen, L.Y.3    Lin, C.S.4    Liu, J.K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.