메뉴 건너뛰기




Volumn 84, Issue 7, 2003, Pages 801-814

Escherichia coli - A Model System That Benefits from and Contributes to the Evolution of Proteomics

Author keywords

2DE map; MALDI TOFTOF; Proteomics

Indexed keywords

BIOTECHNOLOGY; DATABASE SYSTEMS; ELECTROPHORESIS; MASS SPECTROMETRY; PROTEINS;

EID: 0347132485     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/bit.10848     Document Type: Review
Times cited : (43)

References (120)
  • 1
    • 0023430927 scopus 로고
    • Internal amino-acid sequence-analysis of proteins separated by one-dimensional or two-dimensional gel-electrophoresis after in situ protease digestion on nitrocellulose
    • Aebersold RH, Leavitt J, Saavedra RA, Hood LE, Kent SBH. 1987. Internal amino-acid sequence-analysis of proteins separated by one-dimensional or two-dimensional gel-electrophoresis after in situ protease digestion on nitrocellulose. Proc Natl Acad Sci USA 84:6970-6974.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 6970-6974
    • Aebersold, R.H.1    Leavitt, J.2    Saavedra, R.A.3    Hood, L.E.4    Kent, S.B.H.5
  • 2
    • 0022522851 scopus 로고
    • Overproduction, isolation and determination of the amino-terminal sequence of the Sec Y protein, a membrane protein involved in protein export in Escherichia coli
    • Akiyama Y, Ito K. 1986. Overproduction, isolation and determination of the amino-terminal sequence of the Sec Y protein, a membrane protein involved in protein export in Escherichia coli. Eur J Biochem 159:263-266.
    • (1986) Eur J Biochem , vol.159 , pp. 263-266
    • Akiyama, Y.1    Ito, K.2
  • 3
    • 0017225203 scopus 로고
    • Two-dimensional gel electrophoresis of membrane proteins
    • Ames GF, Nikaido K. 1976. Two-dimensional gel electrophoresis of membrane proteins. Biochemistry 15:616-623.
    • (1976) Biochemistry , vol.15 , pp. 616-623
    • Ames, G.F.1    Nikaido, K.2
  • 4
    • 0019126631 scopus 로고
    • Identification and quantitation of elongation factor EF-P in Escherichia coli cell-free extracts
    • An G, Glick BR, Friesen JD, Ganoza MC. 1980. Identification and quantitation of elongation factor EF-P in Escherichia coli cell-free extracts. Can J Biochem 58:1312-1314.
    • (1980) Can J Biochem , vol.58 , pp. 1312-1314
    • An, G.1    Glick, B.R.2    Friesen, J.D.3    Ganoza, M.C.4
  • 5
    • 0029018797 scopus 로고
    • Role for the histone-like protein H-NS in growth phase-dependent and osmotic regulation of sigma S and many sigma S-dependent genes in Escherichia coli
    • Barth M, Marschall C, Muffler A, Fischer D, Hengge-Aronis R. 1995. Role for the histone-like protein H-NS in growth phase-dependent and osmotic regulation of sigma S and many sigma S-dependent genes in Escherichia coli. J Bacteriol 177:3455-3464.
    • (1995) J Bacteriol , vol.177 , pp. 3455-3464
    • Barth, M.1    Marschall, C.2    Muffler, A.3    Fischer, D.4    Hengge-Aronis, R.5
  • 6
    • 0035943486 scopus 로고    scopus 로고
    • Affinity-reversed-phase liquid chromatography assay to quantitate recombinant antibodies and antibody fragments in fermentation broth
    • Battersby JE, Snedecor B, Chen C, Champion KM, Riddle L, Vanderlaan M. 2001. Affinity-reversed-phase liquid chromatography assay to quantitate recombinant antibodies and antibody fragments in fermentation broth. J Chromatogr A 927:61-76.
    • (2001) J Chromatogr A , vol.927 , pp. 61-76
    • Battersby, J.E.1    Snedecor, B.2    Chen, C.3    Champion, K.M.4    Riddle, L.5    Vanderlaan, M.6
  • 7
    • 0033230904 scopus 로고    scopus 로고
    • Toward a clinical molecular scanner for proteome research: Parallel protein chemical processing before and during western blot
    • Bienvenut WV, Sanchez JC, Karmime A, Rouge V, Rose K, Binz PA, Hochstrasser DF. 1999. Toward a clinical molecular scanner for proteome research: Parallel protein chemical processing before and during western blot. Anal Chem 71:4800-4807.
    • (1999) Anal Chem , vol.71 , pp. 4800-4807
    • Bienvenut, W.V.1    Sanchez, J.C.2    Karmime, A.3    Rouge, V.4    Rose, K.5    Binz, P.A.6    Hochstrasser, D.F.7
  • 8
    • 0026416683 scopus 로고
    • Plasmid presence changes the relative levels of many host-cell proteins and ribosome components in recombinant Escherichia coli
    • Birnbaum S, Bailey JE. 1991. Plasmid presence changes the relative levels of many host-cell proteins and ribosome components in recombinant Escherichia coli. Biotechnol Bioeng 37:736-745.
    • (1991) Biotechnol Bioeng , vol.37 , pp. 736-745
    • Birnbaum, S.1    Bailey, J.E.2
  • 9
    • 0027763435 scopus 로고
    • A nonlinear wide-range immobilized pH gradient for 2-dimensional electrophoresis and its definition in A relevant pH scale
    • Bjellqvist B, Pasquali C, Ravier F, Sanchez JC, Hochstrasser D. 1993. A nonlinear wide-range immobilized pH gradient for 2-dimensional electrophoresis and its definition in A relevant pH scale. Electrophoresis 14:1357-1365.
    • (1993) Electrophoresis , vol.14 , pp. 1357-1365
    • Bjellqvist, B.1    Pasquali, C.2    Ravier, F.3    Sanchez, J.C.4    Hochstrasser, D.5
  • 10
    • 0021955321 scopus 로고
    • Long-chain fatty acid transport in Escherichia coli. Cloning, mapping, and expression of the fadL gene
    • Black PN, Kianian SF, DiRusso CC, Nunn WD. 1985. Long-chain fatty acid transport in Escherichia coli. Cloning, mapping, and expression of the fadL gene. J Biol Chem 260:1780-1789.
    • (1985) J Biol Chem , vol.260 , pp. 1780-1789
    • Black, P.N.1    Kianian, S.F.2    DiRusso, C.C.3    Nunn, W.D.4
  • 11
    • 0023153689 scopus 로고
    • Purification and characterization of an outer membrane-bound protein involved in long-chain fatty acid transport in Escherichia coli
    • Black PN, Said B, Ghosn CR, Beach JV, Nunn WD. 1987. Purification and characterization of an outer membrane-bound protein involved in long-chain fatty acid transport in Escherichia coli. J Biol Chem 262:1412-1419.
    • (1987) J Biol Chem , vol.262 , pp. 1412-1419
    • Black, P.N.1    Said, B.2    Ghosn, C.R.3    Beach, J.V.4    Nunn, W.D.5
  • 13
    • 0018908906 scopus 로고
    • Protein identifications of O'Farrell two-dimensional gels: Locations of 81 Escherichia coli proteins
    • Bloch PL, Phillips TA, Neidhardt FC. 1980. Protein identifications of O'Farrell two-dimensional gels: Locations of 81 Escherichia coli proteins. J Bacteriol 141:1409-1420.
    • (1980) J Bacteriol , vol.141 , pp. 1409-1420
    • Bloch, P.L.1    Phillips, T.A.2    Neidhardt, F.C.3
  • 14
    • 0027195391 scopus 로고
    • Two-dimensional gel selection of protein binding sites on DNA
    • Boffini A, Prentki P. 1993. Two-dimensional gel selection of protein binding sites on DNA. Electrophoresis 14:259-265.
    • (1993) Electrophoresis , vol.14 , pp. 259-265
    • Boffini, A.1    Prentki, P.2
  • 17
    • 0037040607 scopus 로고    scopus 로고
    • Global internal standard technology for comparative proteomics
    • Chakraborty A, Regnier FE. 2002. Global internal standard technology for comparative proteomics. J Chromatogr A 949:173-184.
    • (2002) J Chromatogr A , vol.949 , pp. 173-184
    • Chakraborty, A.1    Regnier, F.E.2
  • 18
    • 0042665851 scopus 로고    scopus 로고
    • Comparison of the Escherichia coli proteomes for recombinant human growth hormone producing and nonproducing fermentations
    • Champion KM, Nishihara JC, Aldor IS, Moreno GT, Andersen D, Stults KL, Vanderlaan M. 2003. Comparison of the Escherichia coli proteomes for recombinant human growth hormone producing and nonproducing fermentations. Proteomics 3:1365-1373.
    • (2003) Proteomics , vol.3 , pp. 1365-1373
    • Champion, K.M.1    Nishihara, J.C.2    Aldor, I.S.3    Moreno, G.T.4    Andersen, D.5    Stults, K.L.6    Vanderlaan, M.7
  • 19
    • 85047683547 scopus 로고    scopus 로고
    • Similarity of the Escherichia coli proteome upon completion of different biopharmaceutical fermentation processes
    • Champion KM, Nishihara JC, Joly JC, Arnott D. 2001. Similarity of the Escherichia coli proteome upon completion of different biopharmaceutical fermentation processes. Proteomics 1:1133-1148.
    • (2001) Proteomics , vol.1 , pp. 1133-1148
    • Champion, K.M.1    Nishihara, J.C.2    Joly, J.C.3    Arnott, D.4
  • 20
    • 0027960812 scopus 로고
    • Role of the AGA/AGG codons, the rarest codons in global gene expression in Escherichia coli
    • Chen GFT, Inouye M. 1994. Role of the AGA/AGG codons, the rarest codons in global gene expression in Escherichia coli. Genes Dev 8:2641-2652.
    • (1994) Genes Dev , vol.8 , pp. 2641-2652
    • Chen, G.F.T.1    Inouye, M.2
  • 21
    • 0032903914 scopus 로고    scopus 로고
    • Proteome analysis of factor for inversion stimulation (Fis) overproduction in Escherichia coli
    • Choe LH, Chen W, Lee KH. 1999. Proteome analysis of factor for inversion stimulation (Fis) overproduction in Escherichia coli. Electrophoresis 20:798-805.
    • (1999) Electrophoresis , vol.20 , pp. 798-805
    • Choe, L.H.1    Chen, W.2    Lee, K.H.3
  • 22
    • 0034013175 scopus 로고    scopus 로고
    • Subproteomics based upon protein cellular location and relative solubilities in conjunction with composite two-dimensional electrophoresis gels
    • Cordwell SJ, Nouwens AS, Verrills NM, Basseal DJ, Walsh BJ. 2000. Subproteomics based upon protein cellular location and relative solubilities in conjunction with composite two-dimensional electrophoresis gels. Electrophoresis 21:1094-1103.
    • (2000) Electrophoresis , vol.21 , pp. 1094-1103
    • Cordwell, S.J.1    Nouwens, A.S.2    Verrills, N.M.3    Basseal, D.J.4    Walsh, B.J.5
  • 23
    • 0022774381 scopus 로고
    • Characterization of the phosphoproteins of Escherichia coli cells by electrophoretic analysis
    • Cortay JC, Rieul C, Duclos B, Cozzone AJ. 1986. Characterization of the phosphoproteins of Escherichia coli cells by electrophoretic analysis. Eur J Biochem 159:227-237.
    • (1986) Eur J Biochem , vol.159 , pp. 227-237
    • Cortay, J.C.1    Rieul, C.2    Duclos, B.3    Cozzone, A.J.4
  • 24
    • 0019878585 scopus 로고
    • Identification of proteins at the subunit interface of the Escherichia coli ribosome by cross-linking with dimethyl 3,3′ -dithiobis(propionimidate)
    • Cover JA, Lambert JM, Norman CM, Traut RR. 1981. Identification of proteins at the subunit interface of the Escherichia coli ribosome by cross-linking with dimethyl 3,3′-dithiobis(propionimidate). Biochemistry 20:2843-2852.
    • (1981) Biochemistry , vol.20 , pp. 2843-2852
    • Cover, J.A.1    Lambert, J.M.2    Norman, C.M.3    Traut, R.R.4
  • 25
    • 0021756293 scopus 로고
    • Two-dimensional analysis of proteins phosphorylated in E. coli cells
    • Desmarquets G, Cortay JC, Cozzone AJ. 1984. Two-dimensional analysis of proteins phosphorylated in E. coli cells. FEBS Lett 173:337-341.
    • (1984) FEBS Lett , vol.173 , pp. 337-341
    • Desmarquets, G.1    Cortay, J.C.2    Cozzone, A.J.3
  • 26
    • 0033543618 scopus 로고    scopus 로고
    • Oxidative stress defense and deterioration of growth-arrested Escherichia coli cells
    • Dukan S, Nystrom T. 1999. Oxidative stress defense and deterioration of growth-arrested Escherichia coli cells. J Biol Chem 274:26027-26032.
    • (1999) J Biol Chem , vol.274 , pp. 26027-26032
    • Dukan, S.1    Nystrom, T.2
  • 27
    • 0026505534 scopus 로고
    • Characterization of the regulon controlled by the leucine-responsive regulatory protein in Escherichia coli
    • Ernsting BR, Atkinson MR, Ninfa AJ, Matthews RG. 1992. Characterization of the regulon controlled by the leucine-responsive regulatory protein in Escherichia coli. J Bacteriol 174:1109-1118.
    • (1992) J Bacteriol , vol.174 , pp. 1109-1118
    • Ernsting, B.R.1    Atkinson, M.R.2    Ninfa, A.J.3    Matthews, R.G.4
  • 28
    • 0019451125 scopus 로고
    • Phosphate-containing proteins of Salmonella typhimurium and Escherichia coli: Analysis by a new two-dimensional gel system
    • Ferro-Luzzi Ames G, Nikaido K. 1981. Phosphate-containing proteins of Salmonella typhimurium and Escherichia coli: Analysis by a new two-dimensional gel system. Eur J Biochem 115:525-531.
    • (1981) Eur J Biochem , vol.115 , pp. 525-531
    • Ferro-Luzzi Ames, G.1    Nikaido, K.2
  • 29
    • 0347764580 scopus 로고    scopus 로고
    • A comparison of automated in-gel digest methods for femtomole level samples
    • Finehout EJ, Lee KH. A comparison of automated in-gel digest methods for femtomole level samples. Electrophoresis 24:3508-3516.
    • Electrophoresis , vol.24 , pp. 3508-3516
    • Finehout, E.J.1    Lee, K.H.2
  • 30
    • 0031555475 scopus 로고    scopus 로고
    • The universal stress protein, UspA, of Escherichia coli is phosphorylated in response to stasis
    • Freestone P, Nystrom T, Trinei M, Norris V. 1997. The universal stress protein, UspA, of Escherichia coli is phosphorylated in response to stasis. J Mol Biol 274:318-324.
    • (1997) J Mol Biol , vol.274 , pp. 318-324
    • Freestone, P.1    Nystrom, T.2    Trinei, M.3    Norris, V.4
  • 32
    • 0022363158 scopus 로고
    • Evidence for RecA protein association with the cell membrane and for changes in the levels of major outer membrane proteins in SOS-induced Escherichia coli cells
    • Garvey N, St John AC, Witkin EM. 1985. Evidence for RecA protein association with the cell membrane and for changes in the levels of major outer membrane proteins in SOS-induced Escherichia coli cells. J Bacteriol 163:870-876.
    • (1985) J Bacteriol , vol.163 , pp. 870-876
    • Garvey, N.1    St. John, A.C.2    Witkin, E.M.3
  • 35
    • 0022356423 scopus 로고
    • Detection of host-derived contaminants in products of recombinant DNA technology in E. coli: A comparison of silver-staining and immunoblotting
    • Gooding RP, Bristow AF. 1985. Detection of host-derived contaminants in products of recombinant DNA technology in E. coli: A comparison of silver-staining and immunoblotting. J Pharm Pharmacol 37:781-786.
    • (1985) J Pharm Pharmacol , vol.37 , pp. 781-786
    • Gooding, R.P.1    Bristow, A.F.2
  • 36
    • 0025078495 scopus 로고
    • Positive control of a global antioxidant defense regulon activated by superoxide-generating agents in Escherichia coli
    • Greenberg JT, Monach P, Chou JH, Josephy PD, Demple B. 1990. Positive control of a global antioxidant defense regulon activated by superoxide-generating agents in Escherichia coli. Proc Natl Acad Sci USA 87:6181-6185.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6181-6185
    • Greenberg, J.T.1    Monach, P.2    Chou, J.H.3    Josephy, P.D.4    Demple, B.5
  • 37
    • 0022972149 scopus 로고
    • Starvation proteins in Escherichia coli-kinetics of synthesis and role in starvation survival
    • Groat RG, Schultz JE, Zychlinsky E, Bockman A, Matin A. 1986. Starvation proteins in Escherichia coli-kinetics of synthesis and role in starvation survival. J Bacteriol 168:486-493.
    • (1986) J Bacteriol , vol.168 , pp. 486-493
    • Groat, R.G.1    Schultz, J.E.2    Zychlinsky, E.3    Bockman, A.4    Matin, A.5
  • 38
    • 0018389658 scopus 로고
    • Studies on bacterial chemotaxis. II. Effect of cheB and cheZ mutations on the methylation of methyl-accepting chemotaxis protein of Escherichia coli
    • Hayashi H, Koiwai O, Kozuka M. 1979. Studies on bacterial chemotaxis. II. Effect of cheB and cheZ mutations on the methylation of methyl-accepting chemotaxis protein of Escherichia coli. Biochem 85:1213-1223.
    • (1979) Biochem , vol.85 , pp. 1213-1223
    • Hayashi, H.1    Koiwai, O.2    Kozuka, M.3
  • 39
    • 0033672478 scopus 로고    scopus 로고
    • A turning point in proteome analysis: Sample prefractionation via multicompartment electrolyzers with isoelectric membranes
    • Herbert B, Righetti PG. 2000. A turning point in proteome analysis: Sample prefractionation via multicompartment electrolyzers with isoelectric membranes. Electrophoresis 21:3639-3648.
    • (2000) Electrophoresis , vol.21 , pp. 3639-3648
    • Herbert, B.1    Righetti, P.G.2
  • 40
    • 0025425980 scopus 로고
    • Acid shock proteins of Escherichia coli
    • Heyde M, Portalier R. 1990. Acid shock proteins of Escherichia coli. FEMS Microbiol Lett 57:19-26.
    • (1990) FEMS Microbiol Lett , vol.57 , pp. 19-26
    • Heyde, M.1    Portalier, R.2
  • 41
    • 0025455839 scopus 로고
    • Patterns of protein synthesis in a growth delay mutant (nuv) of Escherichia coli after treatment by near-UV radiation or hydrogen peroxide
    • Hoerter J, Eisenstark A. 1990. Patterns of protein synthesis in a growth delay mutant (nuv) of Escherichia coli after treatment by near-UV radiation or hydrogen peroxide. J Photochem Photobiol B 6:283-289.
    • (1990) J Photochem Photobiol B , vol.6 , pp. 283-289
    • Hoerter, J.1    Eisenstark, A.2
  • 42
    • 0035829831 scopus 로고    scopus 로고
    • On-line estimation of the metabolic burden resulting from the synthesis of plasmid-encoded and heat-shock proteins by monitoring respiratory energy generation
    • Hoffmann F, Rinas U. 2001. On-line estimation of the metabolic burden resulting from the synthesis of plasmid-encoded and heat-shock proteins by monitoring respiratory energy generation. Biotechnol Bioeng 76:333-340.
    • (2001) Biotechnol Bioeng , vol.76 , pp. 333-340
    • Hoffmann, F.1    Rinas, U.2
  • 43
    • 0037027382 scopus 로고    scopus 로고
    • Metabolic adaptation of Escherichia coli during temperature-induced recombinant protein production: 1. Readjustment of metabolic enzyme synthesis
    • Hoffmann F, Weber J, Rinas U. 2002. Metabolic adaptation of Escherichia coli during temperature-induced recombinant protein production: 1. Readjustment of metabolic enzyme synthesis. Biotechnol Bioeng 80:313-319
    • (2002) Biotechnol Bioeng , vol.80 , pp. 313-319
    • Hoffmann, F.1    Weber, J.2    Rinas, U.3
  • 44
    • 0020574745 scopus 로고
    • Initiation factor and ribosome levels are coordinately controlled in Escherichia coli growing at different rates
    • Howe JG, Hershey JW. 1983. Initiation factor and ribosome levels are coordinately controlled in Escherichia coli growing at different rates. J Biol Chem 258:1954-1959.
    • (1983) J Biol Chem , vol.258 , pp. 1954-1959
    • Howe, J.G.1    Hershey, J.W.2
  • 45
    • 0033151997 scopus 로고    scopus 로고
    • Probing proteomes using capillary isoelectric focusing-electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry
    • Jensen PK, Pasa-Tolic L, Anderson GA, Horner JA, Lipton MS, Bruce JE, Smith RD. 1999. Probing proteomes using capillary isoelectric focusing-electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry. Anal Chem 71:2076-2084.
    • (1999) Anal Chem , vol.71 , pp. 2076-2084
    • Jensen, P.K.1    Pasa-Tolic, L.2    Anderson, G.A.3    Horner, J.A.4    Lipton, M.S.5    Bruce, J.E.6    Smith, R.D.7
  • 47
    • 0016593169 scopus 로고
    • Two-dimensional polyacylamide gel electrophoresis of envelope proteins of Escherichia coli
    • Johnson WC, Silhavy TJ, Boos W. 1975. Two-dimensional polyacylamide gel electrophoresis of envelope proteins of Escherichia coli. Appl Microbiol 29:405-413.
    • (1975) Appl Microbiol , vol.29 , pp. 405-413
    • Johnson, W.C.1    Silhavy, T.J.2    Boos, W.3
  • 48
    • 0030043216 scopus 로고    scopus 로고
    • Cold shock induces a major ribosomal-associated protein that unwinds double-stranded RNA in Escherichia coli
    • Jones PG, Mitta M, Kim Y, Jiang W, Inouye M. 1996. Cold shock induces a major ribosomal-associated protein that unwinds double-stranded RNA in Escherichia coli. Proc Natl Acad Sci USA 93:76-80.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 76-80
    • Jones, P.G.1    Mitta, M.2    Kim, Y.3    Jiang, W.4    Inouye, M.5
  • 49
    • 0023186464 scopus 로고
    • Induction of proteins in response to low temperature in Escherichia coli
    • Jones PG, Vanbogelen RA, Neidhardt FC. 1987. Induction of proteins in response to low temperature in Escherichia coli. J Bacteriol 169:2092-2095.
    • (1987) J Bacteriol , vol.169 , pp. 2092-2095
    • Jones, P.G.1    Vanbogelen, R.A.2    Neidhardt, F.C.3
  • 50
    • 0036130438 scopus 로고    scopus 로고
    • Characterization of up-regulated proteases in an industrial recombinant Escherichia coli fermentation
    • Jordan GL, Harcum SW. 2002. Characterization of up-regulated proteases in an industrial recombinant Escherichia coli fermentation. J Indust Microbiol Biotechnol 28:74-80.
    • (2002) J Indust Microbiol Biotechnol , vol.28 , pp. 74-80
    • Jordan, G.L.1    Harcum, S.W.2
  • 51
    • 0016637146 scopus 로고
    • Protein mapping by combined isoelectric focusing and electrophoresis of mouse tissues-novel approach to testing for induced point mutations in mammals
    • Klose J. 1975. Protein mapping by combined isoelectric focusing and electrophoresis of mouse tissues-novel approach to testing for induced point mutations in mammals. Humangenetik 26:231-243.
    • (1975) Humangenetik , vol.26 , pp. 231-243
    • Klose, J.1
  • 52
    • 0033918391 scopus 로고    scopus 로고
    • Mass spectrometry: A tool for the identification of proteins separated by gels
    • Lahm HW, Langen H. 2000. Mass spectrometry: A tool for the identification of proteins separated by gels. Electrophoresis 21:2105-2114.
    • (2000) Electrophoresis , vol.21 , pp. 2105-2114
    • Lahm, H.W.1    Langen, H.2
  • 53
    • 0026020230 scopus 로고
    • Identification of a central regulator of stationary-phase gene expression in Escherichia coli
    • Lange R, Hengge-Aronis R. 1991. Identification of a central regulator of stationary-phase gene expression in Escherichia coli. Mol Microbiol 5:49-59.
    • (1991) Mol Microbiol , vol.5 , pp. 49-59
    • Lange, R.1    Hengge-Aronis, R.2
  • 54
    • 0028888071 scopus 로고
    • The Escherichia coli DNA-binding protein H-NS is one of the first proteins to be synthesized after a nutritional upshift
    • Laurent-Winter C, Lejeune P, Danchin A. 1995. The Escherichia coli DNA-binding protein H-NS is one of the first proteins to be synthesized after a nutritional upshift. Res Microbiol 146:5-16.
    • (1995) Res Microbiol , vol.146 , pp. 5-16
    • Laurent-Winter, C.1    Lejeune, P.2    Danchin, A.3
  • 55
    • 0030983671 scopus 로고    scopus 로고
    • Role of Escherichia coli histone-like nucleoid-structuring protein in bacterial metabolism and stress response: Identification of targets by two-dimensional electrophoresis
    • Laurent-Winter C, Ngo S, Danchin A, Bertin P. 1997. Role of Escherichia coli histone-like nucleoid-structuring protein in bacterial metabolism and stress response: identification of targets by two-dimensional electrophoresis. Eur J Biochem 244:767-773.
    • (1997) Eur J Biochem , vol.244 , pp. 767-773
    • Laurent-Winter, C.1    Ngo, S.2    Danchin, A.3    Bertin, P.4
  • 56
    • 0025832506 scopus 로고
    • UV induction of LexA independent proteins which could be involved in SOS repair
    • Lesca C, Petit C, Defais M. 1991. UV induction of LexA independent proteins which could be involved in SOS repair. Biochimie 73:407-409.
    • (1991) Biochimie , vol.73 , pp. 407-409
    • Lesca, C.1    Petit, C.2    Defais, M.3
  • 57
    • 0023114826 scopus 로고
    • Multiple SecA protein isoforms in Escherichia coli
    • Liebke HH. 1987. Multiple SecA protein isoforms in Escherichia coli. J Bacteriol 169:1174-1181.
    • (1987) J Bacteriol , vol.169 , pp. 1174-1181
    • Liebke, H.H.1
  • 59
    • 0030805979 scopus 로고    scopus 로고
    • Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12
    • Link AJ, Robison K, Church GM. 1997. Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis 18:1259-1313.
    • (1997) Electrophoresis , vol.18 , pp. 1259-1313
    • Link, A.J.1    Robison, K.2    Church, G.M.3
  • 61
    • 0019407288 scopus 로고
    • Identification of the AraE transport protein of Escherichia coli
    • MacPherson AJ, Jones-Mortimer MC, Henderson PJ. 1981. Identification of the AraE transport protein of Escherichia coli. Biochem J 196:269-283.
    • (1981) Biochem J , vol.196 , pp. 269-283
    • MacPherson, A.J.1    Jones-Mortimer, M.C.2    Henderson, P.J.3
  • 62
    • 0018579767 scopus 로고
    • Regulation of synthesis of a major outer membrane protein: Cyclic AMP represses Escherichia coli protein III synthesis
    • Mallick U, Herrlich P. 1979. Regulation of synthesis of a major outer membrane protein: Cyclic AMP represses Escherichia coli protein III synthesis. Proc Natl Acad Sci USA 76:5520-5523.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 5520-5523
    • Mallick, U.1    Herrlich, P.2
  • 63
    • 0025785253 scopus 로고
    • The putative sigma factor KatF has a central role in development of starvation-mediated general resistance in Escherichia coli
    • McCann MP, Kidwell JP, Matin A. 1991. The putative sigma factor KatF has a central role in development of starvation-mediated general resistance in Escherichia coli. J Bacteriol 173:4188-4194.
    • (1991) J Bacteriol , vol.173 , pp. 4188-4194
    • McCann, M.P.1    Kidwell, J.P.2    Matin, A.3
  • 64
    • 0026529433 scopus 로고
    • Identification of intermolecular RNA cross-links at the subunit interface of the Escherichia coli ribosome
    • Mitchell P, Osswald M, Brimacombe R. 1992. Identification of intermolecular RNA cross-links at the subunit interface of the Escherichia coli ribosome. Biochemistry 31:3004-3011.
    • (1992) Biochemistry , vol.31 , pp. 3004-3011
    • Mitchell, P.1    Osswald, M.2    Brimacombe, R.3
  • 65
    • 0033573135 scopus 로고    scopus 로고
    • Identification of thermolabile Escherichia coli proteins: Prevention and reversion of aggregation by DnaK and ClpB
    • Mogk A, Tomoyasu T, Goloubinoff P, Rudiger S, Roder D, Langen H, Bukau B. 1999. Identification of thermolabile Escherichia coli proteins: Prevention and reversion of aggregation by DnaK and ClpB. EMBO J 18:6934-6949.
    • (1999) EMBO J , vol.18 , pp. 6934-6949
    • Mogk, A.1    Tomoyasu, T.2    Goloubinoff, P.3    Rudiger, S.4    Roder, D.5    Langen, H.6    Bukau, B.7
  • 68
    • 0032589276 scopus 로고    scopus 로고
    • Extraction of Escherichia coli proteins with organic solvents prior to two-dimensional electrophoresis
    • Molloy MP, Herbert BR, Williams KL, Gooley AA. 1999. Extraction of Escherichia coli proteins with organic solvents prior to two-dimensional electrophoresis. Electrophoresis 20:701-704.
    • (1999) Electrophoresis , vol.20 , pp. 701-704
    • Molloy, M.P.1    Herbert, B.R.2    Williams, K.L.3    Gooley, A.A.4
  • 69
    • 38149080325 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis and peptide mass fingerprinting of bacterial outer membrane proteins
    • Molloy MP, Phadke ND, Maddock JR, Andrews PC. 2001. Two-dimensional electrophoresis and peptide mass fingerprinting of bacterial outer membrane proteins. Electrophoresis 22:1686-1696.
    • (2001) Electrophoresis , vol.22 , pp. 1686-1696
    • Molloy, M.P.1    Phadke, N.D.2    Maddock, J.R.3    Andrews, P.C.4
  • 70
    • 0031028155 scopus 로고    scopus 로고
    • The RNA-binding protein HF-I plays a global regulatory role which is largely, but not exclusively, due to its role in expression of the sigmaS subunit of RNA polymerase in Escherichia coli
    • Muffler A, Traulsen DD, Fischer D, Lange R, Hengge-Aronis R. 1997. The RNA-binding protein HF-I plays a global regulatory role which is largely, but not exclusively, due to its role in expression of the sigmaS subunit of RNA polymerase in Escherichia coli. J Bacteriol 179:297-300.
    • (1997) J Bacteriol , vol.179 , pp. 297-300
    • Muffler, A.1    Traulsen, D.D.2    Fischer, D.3    Lange, R.4    Hengge-Aronis, R.5
  • 71
    • 0024504492 scopus 로고
    • Genomically linked cellular protein databases derived from two-dimensional polyacrylamide gel electrophoresis
    • Neidhardt FC, Appleby DB, Sankar P, Hutton ME, Phillips TA. 1989. Genomically linked cellular protein databases derived from two-dimensional polyacrylamide gel electrophoresis. Electrophoresis 10:116-122.
    • (1989) Electrophoresis , vol.10 , pp. 116-122
    • Neidhardt, F.C.1    Appleby, D.B.2    Sankar, P.3    Hutton, M.E.4    Phillips, T.A.5
  • 73
    • 0028335964 scopus 로고
    • The glucose-starvation stimulon of Escherichia coli: Induced and repressed synthesis of enzymes of central metabolic pathways and role of acetyl phosphate in gene expression and starvation survival
    • Nystrom T. 1994a. The glucose-starvation stimulon of Escherichia coli: Induced and repressed synthesis of enzymes of central metabolic pathways and role of acetyl phosphate in gene expression and starvation survival. Mol Microbiol 12:833-843
    • (1994) Mol Microbiol , vol.12 , pp. 833-843
    • Nystrom, T.1
  • 74
    • 0027985236 scopus 로고
    • Role of guanosine tetraphosphate in gene expression and the survival of glucose or seryl-transfer-RNA starved cells of Escherichia coli K-12
    • Nystrom T. 1994b. Role of guanosine tetraphosphate in gene expression and the survival of glucose or seryl-transfer-RNA starved cells of Escherichia coli K-12. Mol Gen Genet 245:355-362.
    • (1994) Mol Gen Genet , vol.245 , pp. 355-362
    • Nystrom, T.1
  • 75
    • 0030035132 scopus 로고    scopus 로고
    • Bacterial defense against aging: Role of the Escherichia coli ArcA regulator in gene expression, readjusted energy flux and survival during stasis
    • Nystrom T, Larsson C, Gustafsson L. 1996. Bacterial defense against aging: Role of the Escherichia coli ArcA regulator in gene expression, readjusted energy flux and survival during stasis. EMBO J 15:3219-3228.
    • (1996) EMBO J , vol.15 , pp. 3219-3228
    • Nystrom, T.1    Larsson, C.2    Gustafsson, L.3
  • 76
    • 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
  • 77
    • 0017986804 scopus 로고
    • The suppression of defective translation by ppGpp and its role in the stringent response
    • O'Farrell PH. 1978. The suppression of defective translation by ppGpp and its role in the stringent response. Cell 14:545-557.
    • (1978) Cell , vol.14 , pp. 545-557
    • O'Farrell, P.H.1
  • 79
    • 0037326081 scopus 로고    scopus 로고
    • Mass spectrometric-based approaches in quantitative proteomics
    • Ong SE, Foster LJ, Mann M. 2003. Mass spectrometric-based approaches in quantitative proteomics. Methods 29:124-130.
    • (2003) Methods , vol.29 , pp. 124-130
    • Ong, S.E.1    Foster, L.J.2    Mann, M.3
  • 81
    • 0032079807 scopus 로고    scopus 로고
    • Comprehensive two-dimensional high-performance liquid chromatography for the isolation of overexpressed proteins and proteome mapping
    • Opiteck GJ, Ramirez SM, Jorgenson JW, Moseley MA. 1998. Comprehensive two-dimensional high-performance liquid chromatography for the isolation of overexpressed proteins and proteome mapping. Anal Biochem 258:349-361.
    • (1998) Anal Biochem , vol.258 , pp. 349-361
    • Opiteck, G.J.1    Ramirez, S.M.2    Jorgenson, J.W.3    Moseley, M.A.4
  • 82
    • 0018387174 scopus 로고
    • Protein interactions in the outer membrane of Escherichia coli
    • Palva ET. 1979. Protein interactions in the outer membrane of Escherichia coli. Eur J Biochem 93:495-503.
    • (1979) Eur J Biochem , vol.93 , pp. 495-503
    • Palva, E.T.1
  • 83
    • 0017861127 scopus 로고
    • Patterns of protein synthesis in E. coli: A catalog of the amount of 140 individual proteins at different growth rates
    • Pedersen S, Bloch PL, Reeh S, Neidhardt FC. 1978. Patterns of protein synthesis in E. coli: A catalog of the amount of 140 individual proteins at different growth rates. Cell 14:179-190.
    • (1978) Cell , vol.14 , pp. 179-190
    • Pedersen, S.1    Bloch, P.L.2    Reeh, S.3    Neidhardt, F.C.4
  • 84
    • 0017251082 scopus 로고
    • The use of a cleavable crosslinking reagent to identify neighboring proteins in the 30s ribosomal subunit of Escherichia coli
    • Peretz H, Towbin H, Elson D. 1976. The use of a cleavable crosslinking reagent to identify neighboring proteins in the 30s ribosomal subunit of Escherichia coli. Eur J Biochem 63:83-92.
    • (1976) Eur J Biochem , vol.63 , pp. 83-92
    • Peretz, H.1    Towbin, H.2    Elson, D.3
  • 85
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins DN, Pappin DJC, Creasy DM, Cottrell JS. 1999. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20:3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.C.2    Creasy, D.M.3    Cottrell, J.S.4
  • 87
    • 0019170299 scopus 로고
    • Protein identifications on O'Farrell two-dimensional gels: Locations of 55 additional Escherichia coli proteins
    • Phillips TA, Bloch PL, Neidhardt FC. 1980. Protein identifications on O'Farrell two-dimensional gels: Locations of 55 additional Escherichia coli proteins. J Bacteriol 144:1024-1033.
    • (1980) J Bacteriol , vol.144 , pp. 1024-1033
    • Phillips, T.A.1    Bloch, P.L.2    Neidhardt, F.C.3
  • 88
    • 0021266784 scopus 로고
    • Lon gene product of Escherichia coli is a heat-shock protein
    • Phillips TA, VanBogelen RA, Neidhardt FC. 1984. Lon gene product of Escherichia coli is a heat-shock protein. J Bacteriol 159:283-287.
    • (1984) J Bacteriol , vol.159 , pp. 283-287
    • Phillips, T.A.1    VanBogelen, R.A.2    Neidhardt, F.C.3
  • 89
    • 0037147266 scopus 로고    scopus 로고
    • Cysteine is exported from the Escherichia coli cytoplasm by CydDC, an ATP-binding cassette-type transporter required for cytochrome assembly
    • Pittman MS, Corker H, Wu G, Binet MB, Moir AJ, Poole RK. 2002. Cysteine is exported from the Escherichia coli cytoplasm by CydDC, an ATP-binding cassette-type transporter required for cytochrome assembly. J Biol Chem 277:49841-49849.
    • (2002) J Biol Chem , vol.277 , pp. 49841-49849
    • Pittman, M.S.1    Corker, H.2    Wu, G.3    Binet, M.B.4    Moir, A.J.5    Poole, R.K.6
  • 90
    • 0019876874 scopus 로고
    • Incorporation of photosensitive fatty acids into phospholipids of Escherichia coli and irradiation-dependent cross-linking of phospholipids to membrane proteins
    • Quay SC, Radhakrishnan R, Khorana HG. 1981. Incorporation of photosensitive fatty acids into phospholipids of Escherichia coli and irradiation-dependent cross-linking of phospholipids to membrane proteins. J Biol Chem 256:4444-4449.
    • (1981) J Biol Chem , vol.256 , pp. 4444-4449
    • Quay, S.C.1    Radhakrishnan, R.2    Khorana, H.G.3
  • 91
    • 0018666812 scopus 로고
    • Post-translational modification of Escherichia coli ribosomal protein S6
    • Reeh S, Pedersen S. 1979. Post-translational modification of Escherichia coli ribosomal protein S6. Mol Gen Genet 173:183-187.
    • (1979) Mol Gen Genet , vol.173 , pp. 183-187
    • Reeh, S.1    Pedersen, S.2
  • 92
    • 0017353226 scopus 로고
    • Cross-linking of the proteins in the outer membrane of Escherichia coli
    • Reithmeier RA, Bragg PD. 1977. Cross-linking of the proteins in the outer membrane of Escherichia coli. Biochim Biophys Acta 466:245-256.
    • (1977) Biochim Biophys Acta , vol.466 , pp. 245-256
    • Reithmeier, R.A.1    Bragg, P.D.2
  • 93
    • 0030088490 scopus 로고    scopus 로고
    • Synthesis rates of cellular proteins involved in translation and protein folding are strongly altered in response to overproduction of basic fibroblast growth factor by recombinant Escherichia coli
    • Rinas U. 1996. Synthesis rates of cellular proteins involved in translation and protein folding are strongly altered in response to overproduction of basic fibroblast growth factor by recombinant Escherichia coli. Biotechnol Progr 12:196-200.
    • (1996) Biotechnol Progr , vol.12 , pp. 196-200
    • Rinas, U.1
  • 94
    • 0027470134 scopus 로고
    • Characterization of inclusion bodies in recombinant Escherichia coli producing high levels of porcine somatotropin
    • Rinas U, Boone TC, Bailey JE. 1993. Characterization of inclusion bodies in recombinant Escherichia coli producing high levels of porcine somatotropin. J Biotechnol 28:313-320.
    • (1993) J Biotechnol , vol.28 , pp. 313-320
    • Rinas, U.1    Boone, T.C.2    Bailey, J.E.3
  • 95
    • 0028175657 scopus 로고
    • Phosphorylation of elongation factor G and ribosomal protein S6 in bacteriophage T7-infected Escherichia coli
    • Robertson ES, Aggison LA, Nicholson AW. 1994. Phosphorylation of elongation factor G and ribosomal protein S6 in bacteriophage T7-infected Escherichia coli. Mol Microbiol 11:1045-1057.
    • (1994) Mol Microbiol , vol.11 , pp. 1045-1057
    • Robertson, E.S.1    Aggison, L.A.2    Nicholson, A.W.3
  • 96
    • 0026650807 scopus 로고
    • Phosphorylation of Escherichia coli translation initiation-factors by the bacteriophage-T7 protein-kinase
    • Robertson ES, Nicholson AW. 1992. Phosphorylation of Escherichia coli translation initiation-factors by the bacteriophage-T7 protein-kinase. Biochemistry 31:4822-4827.
    • (1992) Biochemistry , vol.31 , pp. 4822-4827
    • Robertson, E.S.1    Nicholson, A.W.2
  • 98
    • 0017659827 scopus 로고
    • Membrane proteins of Escherichia coli K-12: Two-dimensional polyacrylamide gel electrophoresis of inner and outer membranes
    • Sato T, Ito K, Yura T. 1977. Membrane proteins of Escherichia coli K-12: Two-dimensional polyacrylamide gel electrophoresis of inner and outer membranes. Eur J Biochem 78:557-567.
    • (1977) Eur J Biochem , vol.78 , pp. 557-567
    • Sato, T.1    Ito, K.2    Yura, T.3
  • 100
    • 0025980680 scopus 로고
    • Molecular and functional-characterization of a carbon starvation gene of Escherichia coli
    • Schultz JE, Matin A. 1991. Molecular and functional-characterization of a carbon starvation gene of Escherichia coli. J Mol Biol 218:129-140.
    • (1991) J Mol Biol , vol.218 , pp. 129-140
    • Schultz, J.E.1    Matin, A.2
  • 102
    • 0017163756 scopus 로고
    • Periplasmic protein related to the sn-glycerol-3-phosphate transport system of Escherichia coli
    • Silhavy TJ, Hartig-Beecken I, Boos W. 1976. Periplasmic protein related to the sn-glycerol-3-phosphate transport system of Escherichia coli. J Bacteriol 126:951-958.
    • (1976) J Bacteriol , vol.126 , pp. 951-958
    • Silhavy, T.J.1    Hartig-Beecken, I.2    Boos, W.3
  • 103
    • 0020491416 scopus 로고
    • Precise localisation of three intra-RNA cross-links in 23S RNA and one in 5S RNA, induced by treatment of Escherichia coli 50S ribosomal subunits with bis-(2-chloroethyl)-methylamine
    • Stiege W, Zwieb C, Brimacombe R. 1982. Precise localisation of three intra-RNA cross-links in 23S RNA and one in 5S RNA, induced by treatment of Escherichia coli 50S ribosomal subunits with bis-(2-chloroethyl)-methylamine. Nucl Acids Res 10:7211-7229.
    • (1982) Nucl Acids Res , vol.10 , pp. 7211-7229
    • Stiege, W.1    Zwieb, C.2    Brimacombe, R.3
  • 104
    • 0032946957 scopus 로고    scopus 로고
    • Using native gel in two-dimensional PAGE for the detection of protein interactions in protein extract
    • Sun H, Pan YC. 1999. Using native gel in two-dimensional PAGE for the detection of protein interactions in protein extract. J Biochem Biophys Meth 39:143-151.
    • (1999) J Biochem Biophys Meth , vol.39 , pp. 143-151
    • Sun, H.1    Pan, Y.C.2
  • 105
    • 0020530936 scopus 로고
    • Identification of the heat-inducible protein c15.4 as the groES gene product in Escherichia coli
    • Tilly K, VanBogelen RA, Georgopoulos C, Neidhardt FC. 1983. Identification of the heat-inducible protein c15.4 as the groES gene product in Escherichia coli. J Bacteriol 154:1505-1507.
    • (1983) J Bacteriol , vol.154 , pp. 1505-1507
    • Tilly, K.1    VanBogelen, R.A.2    Georgopoulos, C.3    Neidhardt, F.C.4
  • 107
    • 0025328743 scopus 로고
    • Ribosomes as sensors of heat and cold shock in Escherichia coli
    • Vanbogelen RA, Neidhardt FC. 1990. Ribosomes as sensors of heat and cold shock in Escherichia coli. Proc Natl Acad Sci USA 87:5589-5593.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5589-5593
    • Vanbogelen, R.A.1    Neidhardt, F.C.2
  • 108
    • 0029418629 scopus 로고
    • Application of two-dimensional protein gels in biotechnology
    • VanBogelen RA, Olson ER. 1995. Application of two-dimensional protein gels in biotechnology. Biotechnol Annu Rev 1:69-103.
    • (1995) Biotechnol Annu Rev , vol.1 , pp. 69-103
    • VanBogelen, R.A.1    Olson, E.R.2
  • 109
    • 0029779668 scopus 로고    scopus 로고
    • Global analysis of proteins synthesized during phosphorus restriction in Escherichia coli
    • VanBogelen RA, Olson ER, Wanner BL, Neidhardt FC. 1996. Global analysis of proteins synthesized during phosphorus restriction in Escherichia coli. J Bacteriol 178:4344-4366.
    • (1996) J Bacteriol , vol.178 , pp. 4344-4366
    • VanBogelen, R.A.1    Olson, E.R.2    Wanner, B.L.3    Neidhardt, F.C.4
  • 111
    • 0035055142 scopus 로고    scopus 로고
    • Mass spectrometric imaging of immobilized pHgradient gels and creation of "virtual" two-dimensional gels
    • Walker AK, Rymar G, Andrews PC. 2001. Mass spectrometric imaging of immobilized pHgradient gels and creation of "virtual" two-dimensional gels. Electrophoresis 22:933-945.
    • (2001) Electrophoresis , vol.22 , pp. 933-945
    • Walker, A.K.1    Rymar, G.2    Andrews, P.C.3
  • 112
    • 0037040565 scopus 로고    scopus 로고
    • Quantitative proteomics strategy involving the selection of peptides containing both cysteine and histidine from tryptic digests of cell lysates
    • Wang SH, Zhang X, Regnier FE. 2002. Quantitative proteomics strategy involving the selection of peptides containing both cysteine and histidine from tryptic digests of cell lysates. J Chromatogr A 949:153-162.
    • (2002) J Chromatogr A , vol.949 , pp. 153-162
    • Wang, S.H.1    Zhang, X.2    Regnier, F.E.3
  • 113
    • 0037216549 scopus 로고    scopus 로고
    • Global role for clpP-containing proteases in stationary-phase adaptation of Escherichia coli
    • Weichart D, Querfurth N, Dreger M, Hengge-Aronis R. 2003. Global role for clpP-containing proteases in stationary-phase adaptation of Escherichia coli. J Bacteriol 185:115-125.
    • (2003) J Bacteriol , vol.185 , pp. 115-125
    • Weichart, D.1    Querfurth, N.2    Dreger, M.3    Hengge-Aronis, R.4
  • 114
    • 0036748438 scopus 로고    scopus 로고
    • Tagless extraction-retentate chromatography: A new global protein digestion strategy for monitoring differential protein expression
    • Weinberger SR, Viner RI, Ho P. 2002. Tagless extraction-retentate chromatography: A new global protein digestion strategy for monitoring differential protein expression. Electrophoresis 23:3182-3192.
    • (2002) Electrophoresis , vol.23 , pp. 3182-3192
    • Weinberger, S.R.1    Viner, R.I.2    Ho, P.3
  • 115
    • 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.
    • (2001) Environ Microbiol , vol.3 , pp. 588-599
    • Wick, L.M.1    Quadroni, M.2    Egli, T.3
  • 118
    • 0036907867 scopus 로고    scopus 로고
    • Fluorescence two-dimensional difference gel electrophoresis and mass spectrometry based proteomic analysis of Escherichia coli
    • Yan JX, Devenish AT, Wait R, Stone T, Lewis S, Fowler S. 2002. Fluorescence two-dimensional difference gel electrophoresis and mass spectrometry based proteomic analysis of Escherichia coli. Proteomics 2:1682-1698.
    • (2002) Proteomics , vol.2 , pp. 1682-1698
    • Yan, J.X.1    Devenish, A.T.2    Wait, R.3    Stone, T.4    Lewis, S.5    Fowler, S.6
  • 119
    • 0034213595 scopus 로고    scopus 로고
    • Profound: An expert system for protein identification using mass spectrometric peptide mapping information
    • Zhang WZ, Chait BT. 2000. Profound: An expert system for protein identification using mass spectrometric peptide mapping information. Anal Chem 72:2482-2489.
    • (2000) Anal Chem , vol.72 , pp. 2482-2489
    • Zhang, W.Z.1    Chait, B.T.2
  • 120
    • 0023622594 scopus 로고
    • The grpE protein of Escherichia coli. Purification and properties
    • Zylicz M, Ang D, Georgopoulos C. 1987. The grpE protein of Escherichia coli. Purification and properties. J Biol Chem 262:17437-17442.
    • (1987) J Biol Chem , vol.262 , pp. 17437-17442
    • Zylicz, M.1    Ang, D.2    Georgopoulos, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.