메뉴 건너뛰기




Volumn 196, Issue 15, 2014, Pages 2748-2761

Physiological and proteomic analysis of Escherichia coli iron-limited chemostat growth

Author keywords

[No Author keywords available]

Indexed keywords

GLUCOSE; GLYCOLYTIC ENZYME; IRON; LACTIC ACID; TRICARBOXYLIC ACID;

EID: 84903896000     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.01606-14     Document Type: Article
Times cited : (60)

References (80)
  • 1
    • 33845212090 scopus 로고    scopus 로고
    • Low micronutrient intake may accelerate the degenerative diseases of aging, allocation of scarce micronutrients by triage
    • Ames BN. 2006. Low micronutrient intake may accelerate the degenerative diseases of aging, allocation of scarce micronutrients by triage. Proc. Natl. Acad. Sci. U. S. A. 103: 17589-17594. http://dx.doi.org/10.1073/pnas .0608757103.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 17589-17594
    • Ames, B.N.1
  • 3
    • 82755162477 scopus 로고    scopus 로고
    • The impact of phos-phate scarcity on pharmaceutical protein production in S cerevisiae: linking transcriptomic insights to phenotypic responses
    • Kazemi Seresht A, Palmqvist EA, Olsson L. 2011. The impact of phos-phate scarcity on pharmaceutical protein production in S. cerevisiae: linking transcriptomic insights to phenotypic responses. Microb. Cell Fact. 10: 104. http://dx.doi.org/10.1186/1475-2859-10-104.
    • (2011) Microb. Cell Fact. , vol.10 , pp. 104
    • Kazemi Seresht, A.1    Palmqvist, E.A.2    Olsson, L.3
  • 4
    • 78650306221 scopus 로고    scopus 로고
    • Stoichiogenomics: the evolutionary ecology of macromolecular elemental composition
    • Elser JJ, Acquisti C, Kumar S. 2011. Stoichiogenomics: the evolutionary ecology of macromolecular elemental composition. Trends Ecol. Evol. 26: 38-44. http://dx.doi.org/10.1016/j.tree.2010.10.006.
    • (2011) Trends Ecol. Evol. , vol.26 , pp. 38-44
    • Elser, J.J.1    Acquisti, C.2    Kumar, S.3
  • 5
    • 85194761501 scopus 로고    scopus 로고
    • Ecological stoichiometry: the biology of elements from molecules to the biosphere
    • Princeton University Press, Princeton, NJ
    • Sterner RW, Elser JJ. 2002. Ecological stoichiometry: the biology of elements from molecules to the biosphere. Princeton University Press, Princeton, NJ.
    • (2002)
    • Sterner, R.W.1    Elser, J.J.2
  • 6
    • 0037296240 scopus 로고    scopus 로고
    • Are bacteria more like plants or animals? Growth rate and resource dependence of bacterial C: N: P stoichiometry
    • Makino W, Cotner JB, Sterner RW, Elser JJ. 2003. Are bacteria more like plants or animals? Growth rate and resource dependence of bacterial C: N: P stoichiometry. Funct. Ecol. 17: 121-130. http://dx.doi.org/10.1046/j.1365-2435.2003.00712.x.
    • (2003) Funct. Ecol. , vol.17 , pp. 121-130
    • Makino, W.1    Cotner, J.B.2    Sterner, R.W.3    Elser, J.J.4
  • 7
    • 4544388687 scopus 로고    scopus 로고
    • Dual nutrient limited growth: models, experimental observations, and applications
    • Zinn M, Witholt B, Egli T. 2004. Dual nutrient limited growth: models, experimental observations, and applications. J. Biotechnol. 113: 263-279. http://dx.doi.org/10.1016/j.jbiotec.2004.03.030.
    • (2004) J. Biotechnol. , vol.113 , pp. 263-279
    • Zinn, M.1    Witholt, B.2    Egli, T.3
  • 8
    • 0035854519 scopus 로고    scopus 로고
    • Molecular evolution of protein atomic composition
    • Baudouin-Cornu P, Surdin-Kerjan Y, Marlière P, Thomas D. 2001. Molecular evolution of protein atomic composition. Science 293: 297-300. http://dx.doi.org/10.1126/science.1061052.
    • (2001) Science , vol.293 , pp. 297-300
    • Baudouin-Cornu, P.1    Surdin-Kerjan, Y.2    Marlière, P.3    Thomas, D.4
  • 9
    • 58149354386 scopus 로고    scopus 로고
    • Protein material costs: single atoms can make an evolutionary difference
    • Bragg JG, Wagner A. 2009. Protein material costs: single atoms can make an evolutionary difference. Trends Genet. 25: 5-8. http://dx.doi.org/10 .1016/j.tig.2008.10.007.
    • (2009) Trends Genet. , vol.25 , pp. 5-8
    • Bragg, J.G.1    Wagner, A.2
  • 10
    • 0020553669 scopus 로고
    • Lactobacillus plantarum, an organism not requiring iron
    • Archibald F. 1983. Lactobacillus plantarum, an organism not requiring iron. FEMS Microbiol. Lett. 19: 29-32. http://dx.doi.org/10.1111/j.1574-6968.1983.tb00504.x.
    • (1983) FEMS Microbiol. Lett. , vol.19 , pp. 29-32
    • Archibald, F.1
  • 11
    • 0034595617 scopus 로고    scopus 로고
    • Lack of a role for iron in the Lyme disease pathogen
    • Posey JE, Gheridini FC. 2000. Lack of a role for iron in the Lyme disease pathogen. Science 288: 1651-1653. http://dx.doi.org/10.1126/science.288 .5471.1651.
    • (2000) Science , vol.288 , pp. 1651-1653
    • Posey, J.E.1    Gheridini, F.C.2
  • 12
    • 0033811814 scopus 로고    scopus 로고
    • Salicylic acid is not a bacterial siderophore: a theoretical study
    • Chipperfield JR, Ratledge C. 2000. Salicylic acid is not a bacterial siderophore: a theoretical study. BioMetals 13: 165-168. http://dx.doi.org/10 .1023/A: 1009227206890.
    • (2000) BioMetals , vol.13 , pp. 165-168
    • Chipperfield, J.R.1    Ratledge, C.2
  • 13
    • 0036888008 scopus 로고    scopus 로고
    • Chemical aspects of siderophore mediated iron transport
    • Boukhalfa H, Crumbliss AL. 2002. Chemical aspects of siderophore mediated iron transport. BioMetals 15: 325-339. http://dx.doi.org/10 .1023/A: 1020218608266.
    • (2002) BioMetals , vol.15 , pp. 325-339
    • Boukhalfa, H.1    Crumbliss, A.L.2
  • 14
    • 0019447069 scopus 로고
    • Regulation of ferric iron transport in Escherichia coli K12: isolation of a constitutive mutant
    • Hantke K. 1981. Regulation of ferric iron transport in Escherichia coli K12: isolation of a constitutive mutant. Mol. Gen. Genet. 182: 288-292. http://dx.doi.org/10.1007/BF00269672.
    • (1981) Mol. Gen. Genet. , vol.182 , pp. 288-292
    • Hantke, K.1
  • 15
    • 0016614384 scopus 로고
    • Nutritional immunity-host's attempt to withhold iron from microbial invaders
    • Weinberg ED. 1975. Nutritional immunity-host's attempt to withhold iron from microbial invaders. JAMA 231: 39-41. http://dx.doi.org/10 .1001/jama.1975.03240130021018.
    • (1975) JAMA , vol.231 , pp. 39-41
    • Weinberg, E.D.1
  • 16
    • 77949885386 scopus 로고    scopus 로고
    • Nutritional immunity beyond iron: a role for manganese and zinc
    • Kehl-Fie TE, Skaar EP. 2010. Nutritional immunity beyond iron: a role for manganese and zinc. Curr. Opin. Chem. Biol. 14: 218-224. http://dx .doi.org/10.1016/j.cbpa.2009.11.008.
    • (2010) Curr. Opin. Chem. Biol. , vol.14 , pp. 218-224
    • Kehl-Fie, T.E.1    Skaar, E.P.2
  • 17
    • 9444246510 scopus 로고    scopus 로고
    • Iron and microbial infection
    • Schaible UE, Kaufmann SHE. 2004. Iron and microbial infection. Nat. Rev. Microbiol. 2: 946-953. http://dx.doi.org/10.1038/nrmicro1046.
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 946-953
    • Schaible, U.E.1    Kaufmann, S.H.E.2
  • 18
    • 77958143617 scopus 로고    scopus 로고
    • The battle for iron between bacterial pathogens and their vertebrate hosts
    • Skaar EP. 2010. The battle for iron between bacterial pathogens and their vertebrate hosts. PLoS Pathog. 6: e1000949. http://dx.doi.org/10.1371/journal.ppat.1000949.
    • (2010) PLoS Pathog. , vol.6
    • Skaar, E.P.1
  • 19
  • 21
    • 1642506316 scopus 로고    scopus 로고
    • Adaptation of the photosynthetic electron transport chain in cyanobacteria to iron deficiency: the function of IdiA and IsiA
    • Michel KP, Pistorius EK. 2004. Adaptation of the photosynthetic electron transport chain in cyanobacteria to iron deficiency: the function of IdiA and IsiA. Physiol. Plant. 120: 36-50. http://dx.doi.org/10.1111/j.0031-9317.2004.0229.x.
    • (2004) Physiol. Plant. , vol.120 , pp. 36-50
    • Michel, K.P.1    Pistorius, E.K.2
  • 22
    • 0034010966 scopus 로고    scopus 로고
    • Sepsis: the critical role of iron
    • Bullen J, Griffiths E, Rogers H, Ward G. 2000. Sepsis: the critical role of iron. Microbes Infect. 2: 409-415. http://dx.doi.org/10.1016/S1286-4579 (00)00326-9.
    • (2000) Microbes Infect. , vol.2 , pp. 409-415
    • Bullen, J.1    Griffiths, E.2    Rogers, H.3    Ward, G.4
  • 24
    • 0033056654 scopus 로고    scopus 로고
    • Effect of loop deletions on the binding and transport of ferric enterobactin by FepA
    • Newton SMC, Igo JD, Scott DC, Klebba PE. 1999. Effect of loop deletions on the binding and transport of ferric enterobactin by FepA. Mol. Microbiol. 32: 1153-1165. http://dx.doi.org/10.1046/j.1365-2958 .1999.01424.x.
    • (1999) Mol. Microbiol. , vol.32 , pp. 1153-1165
    • Newton, S.M.C.1    Igo, J.D.2    Scott, D.C.3    Klebba, P.E.4
  • 25
    • 0037010152 scopus 로고    scopus 로고
    • Iron transport and signaling in Escherichia coli
    • Braun V, Braun M. 2002. Iron transport and signaling in Escherichia coli. FEBS Lett. 529: 78-85. http://dx.doi.org/10.1016/S0014-5793(02)03185-X.
    • (2002) FEBS Lett. , vol.529 , pp. 78-85
    • Braun, V.1    Braun, M.2
  • 26
    • 0037389797 scopus 로고    scopus 로고
    • Enterobactin: an archetype for microbial iron transport
    • Raymond KN, Dertz EA, Kim SS. 2003. Enterobactin: an archetype for microbial iron transport. Proc. Natl. Acad. Sci. U. S. A. 100: 3584-3588. http://dx.doi.org/10.1073/pnas.0630018100.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 3584-3588
    • Raymond, K.N.1    Dertz, E.A.2    Kim, S.S.3
  • 27
    • 77956653865 scopus 로고    scopus 로고
    • Iron starvation and siderophore-mediated iron transport
    • Smith AW. 1998. Iron starvation and siderophore-mediated iron transport. Methods Microbiol. 27: 331-342. http://dx.doi.org/10.1016/S0580-9517(08)70294-0.
    • (1998) Methods Microbiol. , vol.27 , pp. 331-342
    • Smith, A.W.1
  • 28
    • 0032719562 scopus 로고    scopus 로고
    • Ferredoxin and flavodoxin as biochemical indicators of iron limitation during open-ocean iron enrichment
    • Erdner DL, Anderson DM. 1999. Ferredoxin and flavodoxin as biochemical indicators of iron limitation during open-ocean iron enrichment. Limnol. Oceanogr. 44: 1609-1615. http://dx.doi.org/10.4319/lo.1999.44.7 .1609.
    • (1999) Limnol. Oceanogr. , vol.44 , pp. 1609-1615
    • Erdner, D.L.1    Anderson, D.M.2
  • 29
    • 0000228768 scopus 로고
    • The continuous culture of bacteria; a theoretical and experimental study
    • Herbert D, Elsworth R, Telling RC. 1956. The continuous culture of bacteria; a theoretical and experimental study. J. Gen. Microbiol. 14: 601-622. http://dx.doi.org/10.1099/00221287-14-3-601.
    • (1956) J. Gen. Microbiol. , vol.14 , pp. 601-622
    • Herbert, D.1    Elsworth, R.2    Telling, R.C.3
  • 30
    • 0001555399 scopus 로고
    • Description of the chemostat
    • Novick A, Szilard L. 1950. Description of the chemostat. Science 112: 715-716. http://dx.doi.org/10.1126/science.112.2920.715.
    • (1950) Science , vol.112 , pp. 715-716
    • Novick, A.1    Szilard, L.2
  • 31
    • 75649152860 scopus 로고    scopus 로고
    • Growth-limiting intracellular metabolites in yeast growing under diverse nutrient limitations
    • Boer VM, Crutchfield CA, Bradley PH, Botstein D, Rabinowitz JD. 2010. Growth-limiting intracellular metabolites in yeast growing under diverse nutrient limitations. Mol. Biol. Cell 21: 198-211. http://dx.doi.org/10.1091/mbc.E09-07-0597.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 198-211
    • Boer, V.M.1    Crutchfield, C.A.2    Bradley, P.H.3    Botstein, D.4    Rabinowitz, J.D.5
  • 32
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell PH. 1975. High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250: 4007-4021.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 34
    • 43049096460 scopus 로고    scopus 로고
    • Monitoring of transcriptome and proteome profiles to investigate the cellular response of E coli towards recombinant protein expression under defined chemostat conditions
    • Dürrschmid K, Reischer H, Schmidt-Heck W, Hrebicek T, Guthke R, Rizzi A, Bayer K. 2008. Monitoring of transcriptome and proteome profiles to investigate the cellular response of E. coli towards recombinant protein expression under defined chemostat conditions. J. Biotechnol. 135: 34-44. http://dx.doi.org/10.1016/j.jbiotec.2008.02.013.
    • (2008) J. Biotechnol. , vol.135 , pp. 34-44
    • Dürrschmid, K.1    Reischer, H.2    Schmidt-Heck, W.3    Hrebicek, T.4    Guthke, R.5    Rizzi, A.6    Bayer, K.7
  • 36
    • 70449393144 scopus 로고    scopus 로고
    • Proteome analysis of the Escherichia coli heat shock response under steady-state conditions
    • Lüders S, Fallet C, Franco-Lara E. 2009. Proteome analysis of the Escherichia coli heat shock response under steady-state conditions. Proteome Sci. 7: 36. http://dx.doi.org/10.1186/1477-5956-7-36.
    • (2009) Proteome Sci. , vol.7 , pp. 36
    • Lüders, S.1    Fallet, C.2    Franco-Lara, E.3
  • 37
    • 84867391844 scopus 로고    scopus 로고
    • The identification of global patterns and unique signatures of proteins across 14 environments using outer membrane proteomics of bacteria
    • Schliep M, Ryall B, Ferenci T. 2012. The identification of global patterns and unique signatures of proteins across 14 environments using outer membrane proteomics of bacteria. Mol. Biosyst. 8: 3017-3027. http://dx .doi.org/10.1039/c2mb25212k.
    • (2012) Mol. Biosyst. , vol.8 , pp. 3017-3027
    • Schliep, M.1    Ryall, B.2    Ferenci, T.3
  • 38
    • 0036225829 scopus 로고    scopus 로고
    • Escherichia coli aconitases and oxidative stress: post-transcriptional regulation of sodA expression
    • Tang Y, Quail MA, Artymiuk PJ, Green J. 2002. Escherichia coli aconitases and oxidative stress: post-transcriptional regulation of sodA expression. Microbiology 148: 1027-1037. http://mic.sgmjournals.org/content/148/4/1027.long.
    • (2002) Microbiology , vol.148 , pp. 1027-1037
    • Tang, Y.1    Quail, M.A.2    Artymiuk, P.J.3    Green, J.4
  • 39
    • 0035213758 scopus 로고    scopus 로고
    • Short-and long-term changes in proteome composition and kinetic properties in a culture of Escherichia coli during transition from glucose-excess to glucose limited growth conditions in continuous culture and vice versa
    • Wick LM, Quadroni M, Egli T. 2001. Short-and long-term changes in proteome composition and kinetic properties in a culture of Escherichia coli during transition from glucose-excess to glucose limited growth conditions in continuous culture and vice versa. Environ. Microbiol. 3: 588-599. http://dx.doi.org/10.1046/j.1462-2920.2001.00231.x.
    • (2001) Environ. Microbiol. , vol.3 , pp. 588-599
    • Wick, L.M.1    Quadroni, M.2    Egli, T.3
  • 40
    • 84875658113 scopus 로고    scopus 로고
    • Proteomic profiles and kinetics of development of bacteriophage T4 and its rI and rIII mutants in slowly growing Escherichia coli
    • Golec P, Karczewska-Golec J, Voigt B, Albrecht D, Schweder T, Hecker M, We{ogonek}grzyn G, ŁośM. 2013. Proteomic profiles and kinetics of development of bacteriophage T4 and its rI and rIII mutants in slowly growing Escherichia coli. J. Gen. Virol. 94: 896-905. http://dx.doi.org/10.1099/vir.0 .048686-0.
    • (2013) J. Gen. Virol. , vol.94 , pp. 896-905
    • Golec, P.1    Karczewska-Golec, J.2    Voigt, B.3    Albrecht, D.4    Schweder, T.5    Hecker, M.6    Wegrzyn, G.7    Łoś, M.8
  • 42
    • 0037007078 scopus 로고    scopus 로고
    • A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli
    • MasséE, Gottesman S. 2002. A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 99: 4620-4625. http://dx.doi.org/10.1073/pnas.032066599.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 4620-4625
    • Massé, E.1    Gottesman, S.2
  • 43
    • 3142675034 scopus 로고    scopus 로고
    • Specific growth rate and not cell density controls the general stress response in Escherichia coli
    • Ihssen J, Egli T. 2004. Specific growth rate and not cell density controls the general stress response in Escherichia coli. Microbiology 150: 1637-1648. http://dx.doi.org/10.1099/mic.0.26849-0.
    • (2004) Microbiology , vol.150 , pp. 1637-1648
    • Ihssen, J.1    Egli, T.2
  • 44
    • 25144518340 scopus 로고    scopus 로고
    • Global physiological analysis of carbon-and energy-limited growing Escherichia coli confirms a high degree of catabolic flexibility and preparedness for mixed substrate utilization
    • Ihssen J, Egli T. 2005. Global physiological analysis of carbon-and energy-limited growing Escherichia coli confirms a high degree of catabolic flexibility and preparedness for mixed substrate utilization. Environ. Microbiol. 7: 1568-1581. http://dx.doi.org/10.1111/j.1462-2920 .2005.00846.x.
    • (2005) Environ. Microbiol. , vol.7 , pp. 1568-1581
    • Ihssen, J.1    Egli, T.2
  • 45
    • 34447317252 scopus 로고    scopus 로고
    • Metabolic systems cost-benefit analysis for interpreting network structure and regulation
    • Carlson RP. 2007. Metabolic systems cost-benefit analysis for interpreting network structure and regulation. Bioinformatics 23: 1258-1264. http://dx.doi.org/10.1093/bioinformatics/btm082.
    • (2007) Bioinformatics , vol.23 , pp. 1258-1264
    • Carlson, R.P.1
  • 46
    • 58049200682 scopus 로고    scopus 로고
    • Decomposition of complex microbial behaviors into resource-based stress responses
    • Carlson RP. 2009. Decomposition of complex microbial behaviors into resource-based stress responses. Bioinformatics 25: 90-97. http://dx.doi .org/10.1093/bioinformatics/btn589.
    • (2009) Bioinformatics , vol.25 , pp. 90-97
    • Carlson, R.P.1
  • 47
  • 48
    • 73149109962 scopus 로고    scopus 로고
    • Shifts in growth strategies reflect tradeoffs in cellular economics
    • Molenaar D, van Berlo R, de Ridder D, Teusink B. 2009. Shifts in growth strategies reflect tradeoffs in cellular economics. Mol. Syst. Biol. 5: 323. http://dx.doi.org/10.1038/msb.2009.82.
    • (2009) Mol. Syst. Biol. , vol.5 , pp. 323
    • Molenaar, D.1    van Berlo, R.2    de Ridder, D.3    Teusink, B.4
  • 49
    • 3242795003 scopus 로고    scopus 로고
    • The principle of flux minimization and its application to estimate stationary fluxes in metabolic networks
    • Holzhutter HG. 2004. The principle of flux minimization and its application to estimate stationary fluxes in metabolic networks. Eur. J. Biochem. 271: 2905-2922. http://dx.doi.org/10.1111/j.1432-1033.2004 .04213.x.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 2905-2922
    • Holzhutter, H.G.1
  • 50
    • 0004265596 scopus 로고
    • Short protocols in molecular biology
    • 2nd ed. Greene Publishing Associates and John Wiley & Sons, New York, NY
    • Ausubel F, Brent R, Kingston R, Moore D, Seidman JG, Smith JA, Struhl K (ed). 1992. Short protocols in molecular biology, 2nd ed. Greene Publishing Associates and John Wiley & Sons, New York, NY.
    • (1992)
    • Ausubel, F.1    Brent, R.2    Kingston, R.3    Moore, D.4    Seidman, J.G.5    Smith, J.A.6    Struhl, K.7
  • 51
    • 3242657100 scopus 로고    scopus 로고
    • Colorimetric ferrozine-based assay for the quantitation of iron in cultured cells
    • Riemer J, Hoepken HH, Czerwinska H, Robinson SR, Dringen R. 2004. Colorimetric ferrozine-based assay for the quantitation of iron in cultured cells. Anal. Biochem. 331: 370-375. http://dx.doi.org/10.1016/j.ab.2004 .03.049.
    • (2004) Anal. Biochem. , vol.331 , pp. 370-375
    • Riemer, J.1    Hoepken, H.H.2    Czerwinska, H.3    Robinson, S.R.4    Dringen, R.5
  • 52
    • 0031859738 scopus 로고    scopus 로고
    • Regulation of porin-mediated outer membrane permeability by nutrient limitation in Escherichia coli
    • Liu X, Ferenci T. 1998. Regulation of porin-mediated outer membrane permeability by nutrient limitation in Escherichia coli. J. Bacteriol. 180: 3917-3922.
    • (1998) J. Bacteriol. , vol.180 , pp. 3917-3922
    • Liu, X.1    Ferenci, T.2
  • 53
    • 0028116314 scopus 로고
    • The growth of Escherichia coli in glucose-limited chemostat cultures: a re-examination of the kinetics
    • Senn H, Lendenmann U, Snozzi M, Hamer G, Egli T. 1994. The growth of Escherichia coli in glucose-limited chemostat cultures: a re-examination of the kinetics. Biochim. Biophys. Acta 1201: 424-436. http://dx.doi.org/10.1016/0304-4165(94)90072-8.
    • (1994) Biochim. Biophys. Acta , vol.1201 , pp. 424-436
    • Senn, H.1    Lendenmann, U.2    Snozzi, M.3    Hamer, G.4    Egli, T.5
  • 54
    • 37049093005 scopus 로고
    • The Berthelot or indophenol reaction and its use in the analytical chemistry of nitrogen: a review
    • Searle PL. 1984. The Berthelot or indophenol reaction and its use in the analytical chemistry of nitrogen: a review. Analyst 109: 549-568. http://dx .doi.org/10.1039/an9840900549.
    • (1984) Analyst , vol.109 , pp. 549-568
    • Searle, P.L.1
  • 55
    • 84903882044 scopus 로고    scopus 로고
    • 4500-NH3 F phenate method
    • In Eaton AD, Clesceri LS, Rice EW, Greenberg AE, Franson MAH (ed), 21st (centennial) ed. American Public Health Association/American Water Works Association/Water Environment Federation, Washington, DC
    • Stieg S. 2005. 4500-NH3 F phenate method, p 4-114. In Eaton AD, Clesceri LS, Rice EW, Greenberg AE, Franson MAH (ed), Standard methods for the examination of water and wastewater, 21st (centennial) ed. American Public Health Association/American Water Works Association/Water Environment Federation, Washington, DC.
    • (2005) Standard methods for the examination of water and wastewater , pp. 4-114
    • Stieg, S.1
  • 56
    • 0023127806 scopus 로고
    • Universal chemical assay for the detection and determination of siderophores
    • Schwyn B, Neilands JB. 1987. Universal chemical assay for the detection and determination of siderophores. Anal. Biochem. 160: 47-56. http://dx .doi.org/10.1016/0003-2697(87)90612-9.
    • (1987) Anal. Biochem. , vol.160 , pp. 47-56
    • Schwyn, B.1    Neilands, J.B.2
  • 57
    • 84903888955 scopus 로고    scopus 로고
    • Zwitterionic dyes for labeling in proteomic and other biological analyses
    • 582+260, January
    • Dratz EA, Grieco PA. January 2004. Zwitterionic dyes for labeling in proteomic and other biological analyses. US patent 7,582,260.
    • (2004) US patent , vol.7
    • Dratz, E.A.1    Grieco, P.A.2
  • 58
    • 84866412649 scopus 로고    scopus 로고
    • Proteomic and systems biology analysis of monocytes exposed to securinine, a GABAA receptor antagonist and immune adjuvant
    • Shipman M, Lubick K, Fouchard D, Guram R, Grieco P, Jutila M, Dratz EA. 2012. Proteomic and systems biology analysis of monocytes exposed to securinine, a GABAA receptor antagonist and immune adjuvant. PLoS One 7: e41278. http://dx.doi.org/10.1371/journal.pone.0041278.
    • (2012) PLoS One , vol.7
    • Shipman, M.1    Lubick, K.2    Fouchard, D.3    Guram, R.4    Grieco, P.5    Jutila, M.6    Dratz, E.A.7
  • 60
    • 0019801599 scopus 로고
    • Iron uptake and iron limited growth of Escherichia coli K-12
    • Hartmann A, Braun V. 1981. Iron uptake and iron limited growth of Escherichia coli K-12. Arch. Microbiol. 130: 353-356. http://dx.doi.org/10 .1007/BF00414599.
    • (1981) Arch. Microbiol. , vol.130 , pp. 353-356
    • Hartmann, A.1    Braun, V.2
  • 61
    • 0026222925 scopus 로고
    • Cybernetic modeling of iron limited growth and siderophore production
    • Alexander ML, Ramkrishna D. 1991. Cybernetic modeling of iron limited growth and siderophore production. Biotechnol. Bioeng. 38: 637-652. http://dx.doi.org/10.1002/bit.260380609.
    • (1991) Biotechnol. Bioeng. , vol.38 , pp. 637-652
    • Alexander, M.L.1    Ramkrishna, D.2
  • 62
    • 0035809231 scopus 로고    scopus 로고
    • Formate accumulation due to DNA release in aerobic cultivations of Escherichia coli
    • Castan A, Sven-Olof E. 2002. Formate accumulation due to DNA release in aerobic cultivations of Escherichia coli. Biotechnol. Bioeng. 77: 324-328. http://dx.doi.org/10.1002/bit.1198.
    • (2002) Biotechnol. Bioeng. , vol.77 , pp. 324-328
    • Castan, A.1    Sven-Olof, E.2
  • 63
    • 33750973382 scopus 로고    scopus 로고
    • Metabolic characterization of E coli citrate synthase and phosphoenolpyruvate carboxylase mutants in aerobic cultures
    • De Maeseneire SL, De Mey M, Vandedrinck S, Vandamme EJ. 2006. Metabolic characterization of E. coli citrate synthase and phosphoenolpyruvate carboxylase mutants in aerobic cultures. Biotechnol. Lett. 28: 1945-1953. http://dx.doi.org/10.1007/s10529-006-9182-8.
    • (2006) Biotechnol. Lett. , vol.28 , pp. 1945-1953
    • De Maeseneire, S.L.1    Vandedrinck, S.2    Vandamme, E.J.3
  • 64
    • 0033895840 scopus 로고    scopus 로고
    • Effects of limited aeration and of the ArcAB system on intermediary pyruvate catabolism in Escherichia coli
    • Alexeeva S, de Kort B, Sawers G, Hellingwerf KJ, Teixeira JM. 2000. Effects of limited aeration and of the ArcAB system on intermediary pyruvate catabolism in Escherichia coli. J. Bacteriol. 182: 4934-4940. http://dx.doi.org/10.1128/JB.182.17.4934-4940.2000.
    • (2000) J. Bacteriol. , vol.182 , pp. 4934-4940
    • Alexeeva, S.1    de Kort, B.2    Sawers, G.3    Hellingwerf, K.J.4    Teixeira, J.M.5
  • 65
    • 0036177861 scopus 로고    scopus 로고
    • Quantitative assessment of oxygen availability: perceived aerobiosis and its effect on flux distribution in the respiratory chain of Escherichia coli
    • Alexeeva S, Hellingwerf KJ, de Mattos MJT. 2002. Quantitative assessment of oxygen availability: perceived aerobiosis and its effect on flux distribution in the respiratory chain of Escherichia coli. J. Bacteriol. 184: 1402-1406. http://dx.doi.org/10.1128/JB.184.5.1402-1406.2002.
    • (2002) J. Bacteriol. , vol.184 , pp. 1402-1406
    • Alexeeva, S.1    Hellingwerf, K.J.2    De Mattos, M.J.T.3
  • 66
    • 0032753923 scopus 로고    scopus 로고
    • Metabolic flux ratio analysis of genetic and environmental modulations of Escherichia coli central carbon metabolism
    • Sauer U, Lasko DR, Fiaux J, Hochuli M, Glaser R, Szyperski T, Wüthrich K, Bailey JE. 1999. Metabolic flux ratio analysis of genetic and environmental modulations of Escherichia coli central carbon metabolism. J. Bacteriol. 181: 6679-6688.
    • (1999) J. Bacteriol. , vol.181 , pp. 6679-6688
    • Sauer, U.1    Lasko, D.R.2    Fiaux, J.3    Hochuli, M.4    Glaser, R.5    Szyperski, T.6    Wüthrich, K.7    Bailey, J.E.8
  • 68
    • 33947136225 scopus 로고    scopus 로고
    • The lysine decarboxylase CadA protects Escherichia coli starved of phosphate against fermentation acids
    • Moreau PL. 2007. The lysine decarboxylase CadA protects Escherichia coli starved of phosphate against fermentation acids. J. Bacteriol. 189: 2249-2261. http://dx.doi.org/10.1128/JB.01306-06.
    • (2007) J. Bacteriol. , vol.189 , pp. 2249-2261
    • Moreau, P.L.1
  • 69
    • 0023578514 scopus 로고
    • Cloning and promoter identification of the iron-regulated cir gene of Escherichia coli
    • Griggs DW, Tharp BB, Konisky J. 1987. Cloning and promoter identification of the iron-regulated cir gene of Escherichia coli. J. Bacteriol. 169: 5343-5352.
    • (1987) J. Bacteriol. , vol.169 , pp. 5343-5352
    • Griggs, D.W.1    Tharp, B.B.2    Konisky, J.3
  • 70
    • 34249881603 scopus 로고    scopus 로고
    • Quantitative profile of the uropathogenic Escherichia coli outer membrane proteome during growth in human urine
    • Alteri CJ, Mobley HLT. 2007. Quantitative profile of the uropathogenic Escherichia coli outer membrane proteome during growth in human urine. Infect. Immun. 75: 2679-2688. http://dx.doi.org/10.1128/IAI .00076-06.
    • (2007) Infect. Immun. , vol.75 , pp. 2679-2688
    • Alteri, C.J.1    Mobley, H.L.T.2
  • 71
    • 34547637894 scopus 로고    scopus 로고
    • Uropathogenic Escherichia coli outer membrane antigens expressed during urinary tract infection
    • Hagan EC, Mobley HLT. 2007. Uropathogenic Escherichia coli outer membrane antigens expressed during urinary tract infection. Infect. Immun. 75: 3941-3949. http://dx.doi.org/10.1128/IAI.00337-07.
    • (2007) Infect. Immun. , vol.75 , pp. 3941-3949
    • Hagan, E.C.1    Mobley, H.L.T.2
  • 73
    • 0344443759 scopus 로고    scopus 로고
    • A novel metabolic cycle catalyzes glucose oxidation and anaplerosis in hungry Escherichia coli
    • Fischer E, Sauer U. 2003. A novel metabolic cycle catalyzes glucose oxidation and anaplerosis in hungry Escherichia coli. J. Biol. Chem. 278: 46446-46451. http://dx.doi.org/10.1074/jbc.M307968200.
    • (2003) J. Biol. Chem. , vol.278 , pp. 46446-46451
    • Fischer, E.1    Sauer, U.2
  • 74
    • 14244270260 scopus 로고    scopus 로고
    • Analysis of gene expression in Escherichia coli in response to changes of growth-limiting nutrient in chemostat cultures
    • Hua Q, Yang C, Oshima T, Mori H, Shimizu K. 2004. Analysis of gene expression in Escherichia coli in response to changes of growth-limiting nutrient in chemostat cultures. Appl. Environ. Microbiol. 70: 2354-2366. http://dx.doi.org/10.1128/AEM.70.4.2354-2366.2004.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 2354-2366
    • Hua, Q.1    Yang, C.2    Oshima, T.3    Mori, H.4    Shimizu, K.5
  • 75
    • 77957347506 scopus 로고    scopus 로고
    • Molecular-level tradeoffs and metabolic adaptation to simultaneous stressors
    • Carlson RP, Taffs RL. 2010. Molecular-level tradeoffs and metabolic adaptation to simultaneous stressors. Curr. Opin. Biotechnol. 21: 670-676. http://dx.doi.org/10.1016/j.copbio.2010.05.011.
    • (2010) Curr. Opin. Biotechnol. , vol.21 , pp. 670-676
    • Carlson, R.P.1    Taffs, R.L.2
  • 76
    • 26444505976 scopus 로고    scopus 로고
    • Effect of RyhB small RNA on global iron use in Escherichia coli
    • MasséE, Vanderpool CK, Gottesman S. 2005. Effect of RyhB small RNA on global iron use in Escherichia coli. J. Bacteriol. 187: 6962-6971. http://dx.doi.org/10.1128/JB.187.20.6962-6971.2005.
    • (2005) J. Bacteriol. , vol.187 , pp. 6962-6971
    • Massé, E.1    Vanderpool, C.K.2    Gottesman, S.3
  • 77
    • 0036148845 scopus 로고    scopus 로고
    • AcnC of Escherichia coli is a 2-methylcitrate dehydratase (PrpD) that can use citrate and isocitrate as substrates
    • Blank L, Green J, Guest JR. 2002. AcnC of Escherichia coli is a 2-methylcitrate dehydratase (PrpD) that can use citrate and isocitrate as substrates. Microbiology 148: 133-146. http://mic.sgmjournals.org/content/148/1/1 33.long.
    • (2002) Microbiology , vol.148 , pp. 133-146
    • Blank, L.1    Green, J.2    Guest, J.R.3
  • 78
    • 0028113546 scopus 로고
    • Two genetically-distinct and differentiallyregulated aconitases (AcnA and AcnB) in Escherichia coli
    • Gruer MJ, Guest JR. 1994. Two genetically-distinct and differentiallyregulated aconitases (AcnA and AcnB) in Escherichia coli. Microbiology 140: 2531-2541. http://dx.doi.org/10.1099/00221287-140-10-2531.
    • (1994) Microbiology , vol.140 , pp. 2531-2541
    • Gruer, M.J.1    Guest, J.R.2
  • 79
    • 0037214441 scopus 로고    scopus 로고
    • Contrasting sensitivities of Escherichia coli aconitases A and B to oxidation and iron depletion
    • Varghese S, Tang Y, Imlay JA. 2003. Contrasting sensitivities of Escherichia coli aconitases A and B to oxidation and iron depletion. J. Bacteriol. 185: 221-230. http://dx.doi.org/10.1128/JB.185.1.221-230.2003.
    • (2003) J. Bacteriol. , vol.185 , pp. 221-230
    • Varghese, S.1    Tang, Y.2    Imlay, J.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.