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Volumn 7, Issue , 2009, Pages 36-

Proteome analysis of the Escherichia coli heat shock response under steady-state conditions

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CELL PROTEIN; CHAPERONE; ENVELOPE PROTEIN; OXYGEN; PROTEIN DERIVATIVE; PROTEOME;

EID: 70449393144     PISSN: None     EISSN: 14775956     Source Type: Journal    
DOI: 10.1186/1477-5956-7-36     Document Type: Article
Times cited : (49)

References (107)
  • 1
    • 0027319272 scopus 로고
    • Regulation of the E. coli heat shock response
    • 10.1111/j.1365-2958.1993.tb01727.x, 7901731
    • Bukau B. Regulation of the E. coli heat shock response. Molecular Microbiology 1993, 9:671-680. 10.1111/j.1365-2958.1993.tb01727.x, 7901731.
    • (1993) Molecular Microbiology , vol.9 , pp. 671-680
    • Bukau, B.1
  • 2
    • 0003503903 scopus 로고    scopus 로고
    • Molecular Chaperones and Folding Catalysts-Regulation, Cellular Function and Mechanisms
    • Harwood Academic Publishers, Amsterdam
    • Bukau B. Molecular Chaperones and Folding Catalysts-Regulation, Cellular Function and Mechanisms. 1999, 690. Harwood Academic Publishers, Amsterdam.
    • (1999) , pp. 690
    • Bukau, B.1
  • 3
    • 0000757557 scopus 로고
    • Properties of the Heat Shock Proteins of Escherichia coli and the Autoregulation of the Heat Shock Response
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, Morimoto RI, Tissiéres A, Georgopoulos C
    • Georgopoulos C, Liberek K, Zylicz M, Ang D. Properties of the Heat Shock Proteins of Escherichia coli and the Autoregulation of the Heat Shock Response. The Biology of Heat Shock Proteins and Molecular Chaperones 1994, 209-250. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, Morimoto RI, Tissiéres A, Georgopoulos C.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 209-250
    • Georgopoulos, C.1    Liberek, K.2    Zylicz, M.3    Ang, D.4
  • 5
    • 8844219685 scopus 로고    scopus 로고
    • Roles and applications of small heat shock proteins in the production of recombinant proteins in Escherichia coli
    • 10.1002/bit.20227, 15382106
    • Han MJ, Park SJ, Park TJ, Lee SY. Roles and applications of small heat shock proteins in the production of recombinant proteins in Escherichia coli. Biotechnology and Bioengineering 2004, 88:426-436. 10.1002/bit.20227, 15382106.
    • (2004) Biotechnology and Bioengineering , vol.88 , pp. 426-436
    • Han, M.J.1    Park, S.J.2    Park, T.J.3    Lee, S.Y.4
  • 6
    • 0008872510 scopus 로고
    • New puffs induced by temperature shock. DNP and salicylate in salivary chromosomes of Drosophila melanogaster
    • Rotissa FM. New puffs induced by temperature shock. DNP and salicylate in salivary chromosomes of Drosophila melanogaster. Drosophila Information Service 1963, 37:122-123.
    • (1963) Drosophila Information Service , vol.37 , pp. 122-123
    • Rotissa, F.M.1
  • 7
    • 0004915153 scopus 로고
    • Specific loci in polytene chromosomes of Drosophila
    • 10.1016/0014-4827(64)90147-8, 14208747
    • Rotissa FM. Specific loci in polytene chromosomes of Drosophila. Experimental Cell Research 1964, 35:601-607. 10.1016/0014-4827(64)90147-8, 14208747.
    • (1964) Experimental Cell Research , vol.35 , pp. 601-607
    • Rotissa, F.M.1
  • 8
    • 34250561475 scopus 로고
    • A new puffing pattern induced by a temperature shock and DNP in Drosophila
    • Rotissa FM. A new puffing pattern induced by a temperature shock and DNP in Drosophila. Experientia 1962, 18:571-573.
    • (1962) Experientia , vol.18 , pp. 571-573
    • Rotissa, F.M.1
  • 9
    • 0017950371 scopus 로고
    • Transient rates of synthesis of individual polypeptides in E. coli following temperature shifts
    • 10.1016/0092-8674(78)90317-3, 350413
    • Lemaux PG, Herendeen SL, Bloch PL, Neidhardt FC. Transient rates of synthesis of individual polypeptides in E. coli following temperature shifts. Cell 1978, 13:427-434. 10.1016/0092-8674(78)90317-3, 350413.
    • (1978) Cell , vol.13 , pp. 427-434
    • Lemaux, P.G.1    Herendeen, S.L.2    Bloch, P.L.3    Neidhardt, F.C.4
  • 10
    • 0017859550 scopus 로고
    • Transient regulation of protein synthesis in Escherichia coli upon shift-up of growth temperature
    • Yamamori T, Ito K, Nakamura Y, Yura T. Transient regulation of protein synthesis in Escherichia coli upon shift-up of growth temperature. The Journal of Bacteriology 1978, 134:1133-1140.
    • (1978) The Journal of Bacteriology , vol.134 , pp. 1133-1140
    • Yamamori, T.1    Ito, K.2    Nakamura, Y.3    Yura, T.4
  • 11
    • 0028064780 scopus 로고
    • Rapid degradation of an abnormal protein in Escherichia coli involves the chaperones GroEL and GroES
    • Kandror O, Busconi L, Sherman M, Goldberg AL. Rapid degradation of an abnormal protein in Escherichia coli involves the chaperones GroEL and GroES. J Biol Chem 1994, 269:23575-23582.
    • (1994) J Biol Chem , vol.269 , pp. 23575-23582
    • Kandror, O.1    Busconi, L.2    Sherman, M.3    Goldberg, A.L.4
  • 12
    • 0026540796 scopus 로고
    • Involvement of the chaperonin DnaK in the rapid degradation of a mutant protein in Escherichia coli
    • 556427, 1740117
    • Sherman MY, Goldberg AL. Involvement of the chaperonin DnaK in the rapid degradation of a mutant protein in Escherichia coli. The EMBO Journal 1992, 11:71-77. 556427, 1740117.
    • (1992) The EMBO Journal , vol.11 , pp. 71-77
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 13
    • 0001897486 scopus 로고    scopus 로고
    • The heat-shock response: Regulation and function
    • Bacterial stress responses Washington: ASM Press, Stortz G, Hengge-Aronis R
    • Yura, Kanemori M, T MM. The heat-shock response: Regulation and function. 2000, 3-18. Bacterial stress responses Washington: ASM Press, Stortz G, Hengge-Aronis R.
    • (2000) , pp. 3-18
    • Yura1    Kanemori, M.2    T, M.M.3
  • 14
    • 0030611694 scopus 로고    scopus 로고
    • SigmaE is an essential sigma factor in Escherichia coli
    • 179621, 9352942
    • De Las Penas A, Connolly L, Gross CA. SigmaE is an essential sigma factor in Escherichia coli. J Bacteriol 1997, 179:6862-6864. 179621, 9352942.
    • (1997) J Bacteriol , vol.179 , pp. 6862-6864
    • De Las Penas, A.1    Connolly, L.2    Gross, C.A.3
  • 16
    • 0024051671 scopus 로고
    • Heat shock protein GroE of Escherichia coli: key protective roles against thermal stress
    • Kusukawa N, Yura T. Heat shock protein GroE of Escherichia coli: key protective roles against thermal stress. Genes & Development 1988, 2:874-882.
    • (1988) Genes & Development , vol.2 , pp. 874-882
    • Kusukawa, N.1    Yura, T.2
  • 17
    • 0023683820 scopus 로고
    • Isolation and characterization of Escherichia coli mutants that lack the heat shock sigma factor σ32
    • 211339, 2900239
    • Zhou YN, N K, JW E, CA G, Yura T. Isolation and characterization of Escherichia coli mutants that lack the heat shock sigma factor σ32. Journal of Bacteriology 1988, 170:3640-3649. 211339, 2900239.
    • (1988) Journal of Bacteriology , vol.170 , pp. 3640-3649
    • Zhou, Y.N.1    N, K.2    JW, E.3    CA, G.4    Yura, T.5
  • 18
    • 0015102446 scopus 로고
    • Growth Rate of Escherichia coli at Elevated Temperatures: Limitation by Methionine
    • Ron EZ, Davis BD. Growth Rate of Escherichia coli at Elevated Temperatures: Limitation by Methionine. The Journal of Bacteriology 1971, 107:391-396.
    • (1971) The Journal of Bacteriology , vol.107 , pp. 391-396
    • Ron, E.Z.1    Davis, B.D.2
  • 19
    • 0015101918 scopus 로고
    • Growth Rate of Escherichia coli at Elevated Temperatures: Reversible Inhibition of Homoserine Trans-Succinylase
    • Ron EZ, Shani M. Growth Rate of Escherichia coli at Elevated Temperatures: Reversible Inhibition of Homoserine Trans-Succinylase. The Journal of Bacteriology 1971, 107:397-400.
    • (1971) The Journal of Bacteriology , vol.107 , pp. 397-400
    • Ron, E.Z.1    Shani, M.2
  • 20
    • 33745127048 scopus 로고    scopus 로고
    • The Escherichia coli Proteome: Past, Present, and Future Prospects
    • 1489533, 16760308
    • Han MJ, Lee SY. The Escherichia coli Proteome: Past, Present, and Future Prospects. Microbiology and Molecular Biology Reviews 2006, 70:362-439. 1489533, 16760308.
    • (2006) Microbiology and Molecular Biology Reviews , vol.70 , pp. 362-439
    • Han, M.J.1    Lee, S.Y.2
  • 21
    • 70449460728 scopus 로고    scopus 로고
    • Effect of temperature up-shift on fermentation and metabolic characteristics in view of gene expressions in Escherichia coli
    • 2634768, 19055729
    • Hasan CM, Shimizu K. Effect of temperature up-shift on fermentation and metabolic characteristics in view of gene expressions in Escherichia coli. Microbial Cell Factories 2008, 7:35. 2634768, 19055729.
    • (2008) Microbial Cell Factories , vol.7 , pp. 35
    • Hasan, C.M.1    Shimizu, K.2
  • 22
    • 0003537303 scopus 로고
    • Biochemical Engineering Fundamentals
    • McGraw-Hill International Editions, Chemical Engineering Series, Singapore, 2
    • Bailey JE, Ollis DF. Biochemical Engineering Fundamentals. 1986, McGraw-Hill International Editions, Chemical Engineering Series, Singapore, 2.
    • (1986)
    • Bailey, J.E.1    Ollis, D.F.2
  • 23
    • 0003570376 scopus 로고
    • Chemical Reaction Engineering
    • John Wiley & Sons, Inc, USA, 2
    • Levenspiel O. Chemical Reaction Engineering. 1972, John Wiley & Sons, Inc, USA, 2.
    • (1972)
    • Levenspiel, O.1
  • 24
    • 0003634150 scopus 로고
    • Elementary Chemical Reactor Analysis
    • Prentice-Hall, Inc Englewood Cliffs, N J
    • Aris R. Elementary Chemical Reactor Analysis. 1969, Prentice-Hall, Inc Englewood Cliffs, N J.
    • (1969)
    • Aris, R.1
  • 25
    • 0019890564 scopus 로고
    • Positive regulatory gene for temperature-controlled proteins in Escherichia coli
    • Neidhardt FC, VanBogelen RA. Positive regulatory gene for temperature-controlled proteins in Escherichia coli. Biochem Biophys Res Commun 1981, 100:894-900.
    • (1981) Biochem Biophys Res Commun , vol.100 , pp. 894-900
    • Neidhardt, F.C.1    VanBogelen, R.A.2
  • 26
    • 0020092887 scopus 로고
    • Genetic control of heat-shock protein synthesis and its bearing on growth and thermal resistance in Escherichia coli K -12
    • 345852, 7038687
    • Yamamori T, Yura T. Genetic control of heat-shock protein synthesis and its bearing on growth and thermal resistance in Escherichia coli K -12. Proc Natl Acad Sci USA 1982, 79:860-864. 345852, 7038687.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 860-864
    • Yamamori, T.1    Yura, T.2
  • 27
    • 4544373143 scopus 로고    scopus 로고
    • Flux to acetate and lactate excretions in industrial fermentations: physiological and biochemical implications
    • El-Mansi M. Flux to acetate and lactate excretions in industrial fermentations: physiological and biochemical implications. Journal of Industrial Microbiology and Biotechnology 2004, 31:295-300.
    • (2004) Journal of Industrial Microbiology and Biotechnology , vol.31 , pp. 295-300
    • El-Mansi, M.1
  • 28
    • 0024416873 scopus 로고
    • Control of carbon flux to acetate excretion during growth of Escherichia coli in batch and continuous cultures
    • El-Mansi M, Holms WH. Control of carbon flux to acetate excretion during growth of Escherichia coli in batch and continuous cultures. J Gen Microbiol 1989, 135:2875-2883.
    • (1989) J Gen Microbiol , vol.135 , pp. 2875-2883
    • El-Mansi, M.1    Holms, W.H.2
  • 29
    • 0030463296 scopus 로고    scopus 로고
    • Flux analysis and control of the central metabolic pathways in Escherichia coli
    • Holms H. Flux analysis and control of the central metabolic pathways in Escherichia coli. FEMS Microbiology Reviews 1996, 19:85-116.
    • (1996) FEMS Microbiology Reviews , vol.19 , pp. 85-116
    • Holms, H.1
  • 30
    • 0025264582 scopus 로고
    • Comparison of growth, acetate production, and acetate inhibition of Escherichia coli strains in batch and fed-batch fermentations
    • 184335, 2187400
    • Luli GW, Strohl WR. Comparison of growth, acetate production, and acetate inhibition of Escherichia coli strains in batch and fed-batch fermentations. Appl Environ Microbiol 1990, 56:1004-1011. 184335, 2187400.
    • (1990) Appl Environ Microbiol , vol.56 , pp. 1004-1011
    • Luli, G.W.1    Strohl, W.R.2
  • 32
    • 0033062007 scopus 로고    scopus 로고
    • Glucose overflow metabolism and mixed-acid fermentation in aerobic large-scale fed-batch processes
    • 10390814
    • Xu B, Jahic M, Blomsten G, Enfors SO. Glucose overflow metabolism and mixed-acid fermentation in aerobic large-scale fed-batch processes. Applied Microbiology and Biotechnology 1999, 51:564-571. 10390814.
    • (1999) Applied Microbiology and Biotechnology , vol.51 , pp. 564-571
    • Xu, B.1    Jahic, M.2    Blomsten, G.3    Enfors, S.O.4
  • 33
    • 0033047059 scopus 로고    scopus 로고
    • Modeling of Overflow Metabolism in Batch and Fed-Batch Cultures of Escherichia coli
    • Xu B, Jahic M, Enfors S-O. Modeling of Overflow Metabolism in Batch and Fed-Batch Cultures of Escherichia coli. Biotechnology Progress 1999, 15:81-90.
    • (1999) Biotechnology Progress , vol.15 , pp. 81-90
    • Xu, B.1    Jahic, M.2    Enfors, S.-.O.3
  • 34
    • 0025700668 scopus 로고
    • Production of recombinant human growth hormone in Escherichia coli: Expression of different precursors and physiological effects of glucose, acetate, and salts
    • Jensen EB, Carlsen S. Production of recombinant human growth hormone in Escherichia coli: Expression of different precursors and physiological effects of glucose, acetate, and salts. Biotechnology and Bioengineering 1990, 36:1-11.
    • (1990) Biotechnology and Bioengineering , vol.36 , pp. 1-11
    • Jensen, E.B.1    Carlsen, S.2
  • 35
    • 0015837840 scopus 로고
    • Shigella flexneri Inhibition by Acetic Acid
    • 422815, 4578151
    • Baskett RC, Hentges DJ. Shigella flexneri Inhibition by Acetic Acid. Infect Immun 1973, 8:91-97. 422815, 4578151.
    • (1973) Infect Immun , vol.8 , pp. 91-97
    • Baskett, R.C.1    Hentges, D.J.2
  • 36
    • 0019456997 scopus 로고
    • Change in intracellular pH of Escherichia coli mediates the chemotactic response to certain attractants and repellents
    • Repaske DR, Adler J. Change in intracellular pH of Escherichia coli mediates the chemotactic response to certain attractants and repellents. The Journal of Bacteriology 1981, 145:1196-1208.
    • (1981) The Journal of Bacteriology , vol.145 , pp. 1196-1208
    • Repaske, D.R.1    Adler, J.2
  • 37
  • 38
    • 0027491617 scopus 로고
    • The inactivation of Fe-S cluster containing hydro-lyases by superoxide
    • Flint DH, Tuminello JF, Emptage MH. The inactivation of Fe-S cluster containing hydro-lyases by superoxide. J Biol Chem 1993, 268:9-2237.
    • (1993) J Biol Chem , vol.268 , pp. 9-2237
    • Flint, D.H.1    Tuminello, J.F.2    Emptage, M.H.3
  • 39
    • 0026045587 scopus 로고
    • Superoxide sensitivity of the Escherichia coli aconitase
    • Gardner PR, Fridovich I. Superoxide sensitivity of the Escherichia coli aconitase. J Biol Chem 1991, 266:8-1933.
    • (1991) J Biol Chem , vol.266 , pp. 8-1933
    • Gardner, P.R.1    Fridovich, I.2
  • 40
    • 0023886170 scopus 로고
    • DNA damage and oxygen radical toxicity
    • Imlay JA, Linn S. DNA damage and oxygen radical toxicity. 1988, 240:1302-1309.
    • (1988) , vol.240 , pp. 1302-1309
    • Imlay, J.A.1    Linn, S.2
  • 41
    • 0019804120 scopus 로고
    • Toxic drug effects associated with oxygen metabolism: redox cycling and lipid peroxidation
    • 7035210
    • Kappus H, Sies H. Toxic drug effects associated with oxygen metabolism: redox cycling and lipid peroxidation. Experientia 1981, 37:1233-1358. 7035210.
    • (1981) Experientia , vol.37 , pp. 1233-1358
    • Kappus, H.1    Sies, H.2
  • 42
    • 0027183423 scopus 로고
    • Oxidation of Free Amino Acids and Amino Acid Residues in Proteins by Radiolysis and by Metal-Catalyzed Reactions
    • Stadtman ER. Oxidation of Free Amino Acids and Amino Acid Residues in Proteins by Radiolysis and by Metal-Catalyzed Reactions. Annual Review of Biochemistry 1993, 62:797-821.
    • (1993) Annual Review of Biochemistry , vol.62 , pp. 797-821
    • Stadtman, E.R.1
  • 43
    • 0035209075 scopus 로고    scopus 로고
    • Alkyl Hydroperoxide Reductase Is the Primary Scavenger of Endogenous Hydrogen Peroxide in Escherichia coli
    • Seaver LC, Imlay JA. Alkyl Hydroperoxide Reductase Is the Primary Scavenger of Endogenous Hydrogen Peroxide in Escherichia coli. The Journal of Bacteriology 2001, 183:7173-7181.
    • (2001) The Journal of Bacteriology , vol.183 , pp. 7173-7181
    • Seaver, L.C.1    Imlay, J.A.2
  • 44
    • 0030811135 scopus 로고    scopus 로고
    • Protection of DNA during oxidative stress by the nonspecific DNA- binding protein Dps
    • 179379, 9260963
    • Martinez A, Kolter R. Protection of DNA during oxidative stress by the nonspecific DNA- binding protein Dps. J Bacteriol 1997, 179:5188-5194. 179379, 9260963.
    • (1997) J Bacteriol , vol.179 , pp. 5188-5194
    • Martinez, A.1    Kolter, R.2
  • 45
    • 3042662444 scopus 로고    scopus 로고
    • Dps Protects Cells against Multiple Stresses during Stationary Phase
    • 421617, 15205421
    • Nair S, Finkel SE. Dps Protects Cells against Multiple Stresses during Stationary Phase. J Bacteriol 2004, 186:4192-4198. 421617, 15205421.
    • (2004) J Bacteriol , vol.186 , pp. 4192-4198
    • Nair, S.1    Finkel, S.E.2
  • 46
    • 0033869982 scopus 로고    scopus 로고
    • Two types of localization of the DNA-binding proteins within the Escherichia coli nucleoid
    • Azam S, Hiraga S, Ishihama A. Two types of localization of the DNA-binding proteins within the Escherichia coli nucleoid. Genes to Cells 2000, 5:613-626.
    • (2000) Genes to Cells , vol.5 , pp. 613-626
    • Azam, S.1    Hiraga, S.2    Ishihama, A.3
  • 47
    • 0030819736 scopus 로고    scopus 로고
    • Nucleoid structure and distribution in thermophilic Archaea
    • Poplawski A, Bernander R. Nucleoid structure and distribution in thermophilic Archaea. The Journal of Bacteriology 1997, 179:7625-7630.
    • (1997) The Journal of Bacteriology , vol.179 , pp. 7625-7630
    • Poplawski, A.1    Bernander, R.2
  • 49
    • 0027083350 scopus 로고
    • A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli
    • Almiron M, Link AJ, Furlong D, Kolter R. A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli. Genes & Development 1992, 6:2646-2654.
    • (1992) Genes & Development , vol.6 , pp. 2646-2654
    • Almiron, M.1    Link, A.J.2    Furlong, D.3    Kolter, R.4
  • 50
    • 0033941953 scopus 로고    scopus 로고
    • The outer membrane protein, Antigen 43, mediates cell-to-cell interactions within Escherichia coli biofilms
    • Danese PN, Pratt LA, Dove SL, Kolter R. The outer membrane protein, Antigen 43, mediates cell-to-cell interactions within Escherichia coli biofilms. Molecular Microbiology 2000, 37:424-432.
    • (2000) Molecular Microbiology , vol.37 , pp. 424-432
    • Danese, P.N.1    Pratt, L.A.2    Dove, S.L.3    Kolter, R.4
  • 51
    • 0037423361 scopus 로고    scopus 로고
    • Three Highly Conserved Proteins Catalyze the Conversion of UDP-N-acetyl-D-glucosamine to Precursors for the Biosynthesis of O Antigen in Pseudomonas aeruginosa O11 and Capsule in Staphylococcus aureus Type 5. Implications for the UDP-N-Acetyl-L-Fucosoamine Biosynthetic Pathway
    • Kneidinger B, O'Riordan K, Li J, Brisson J-R, Lee JC, Lam JS. Three Highly Conserved Proteins Catalyze the Conversion of UDP-N-acetyl-D-glucosamine to Precursors for the Biosynthesis of O Antigen in Pseudomonas aeruginosa O11 and Capsule in Staphylococcus aureus Type 5. Implications for the UDP-N-Acetyl-L-Fucosoamine Biosynthetic Pathway. J Biol Chem 2003, 278:3615-3627.
    • (2003) J Biol Chem , vol.278 , pp. 3615-3627
    • Kneidinger, B.1    O'Riordan, K.2    Li, J.3    Brisson, J.-.R.4    Lee, J.C.5    Lam, J.S.6
  • 52
    • 0017671931 scopus 로고
    • Purification of protein A, an outer membrane component missing in Escherichia coli K-12 ompA mutants
    • Chai TJ, Foulds J. Purification of protein A, an outer membrane component missing in Escherichia coli K-12 ompA mutants. Biochem Biophys Acta 1977, 493:210-215.
    • (1977) Biochem Biophys Acta , vol.493 , pp. 210-215
    • Chai, T.J.1    Foulds, J.2
  • 53
    • 0017173775 scopus 로고
    • Influence of cultural conditions and mutations on the composition of the outer membrane proteins of Escherichia coli
    • Lugtenberg B, Peters R, Berheimer H, Berendsen W. Influence of cultural conditions and mutations on the composition of the outer membrane proteins of Escherichia coli. Molecular and General Genetics 1976, 147:251-262.
    • (1976) Molecular and General Genetics , vol.147 , pp. 251-262
    • Lugtenberg, B.1    Peters, R.2    Berheimer, H.3    Berendsen, W.4
  • 54
    • 0021202461 scopus 로고
    • Growth-rate dependent regulation of mRNA stability in Escherichia coli
    • 6387508
    • Nilsson G, Belasco JG, Cohen SN, von Gabain A. Growth-rate dependent regulation of mRNA stability in Escherichia coli. Nature 1984, 312:75-77. 6387508.
    • (1984) Nature , vol.312 , pp. 75-77
    • Nilsson, G.1    Belasco, J.G.2    Cohen, S.N.3    von Gabain, A.4
  • 55
    • 2442563573 scopus 로고    scopus 로고
    • Regulation of the Escherichia coli sigma-dependent envelope stress response
    • Alba B, Gross C. Regulation of the Escherichia coli sigma-dependent envelope stress response. Mol Microbiol 2004, 52:613-619.
    • (2004) Mol Microbiol , vol.52 , pp. 613-619
    • Alba, B.1    Gross, C.2
  • 56
    • 31144454629 scopus 로고    scopus 로고
    • Conserved and variable functions of the sigmaE stress response in related genomes
    • 1312014,1312014, 16336047
    • Rhodius V, Suh W, Nonaka G, West J, Gross C. Conserved and variable functions of the sigmaE stress response in related genomes. PLoS Biology 2006, 4:e2. 1312014,1312014, 16336047.
    • (2006) PLoS Biology , vol.4
    • Rhodius, V.1    Suh, W.2    Nonaka, G.3    West, J.4    Gross, C.5
  • 57
    • 34047094398 scopus 로고    scopus 로고
    • Sigma E controls biogenesis of the antisense RNA MicA
    • 1851643, 17267407
    • Udekwu KI, Wagner EGH. Sigma E controls biogenesis of the antisense RNA MicA. Nucleic Acids Research 2007, 35:1279-1288. 1851643, 17267407.
    • (2007) Nucleic Acids Research , vol.35 , pp. 1279-1288
    • Udekwu, K.I.1    Wagner, E.G.H.2
  • 58
    • 33750297745 scopus 로고    scopus 로고
    • Conserved Small Non-coding RNAs that belong to the sigmaE Regulon: Role in Down-regulation of Outer Membrane Proteins
    • Johansen J, Rasmussen AA, Overgaard M, Valentin-Hansen P. Conserved Small Non-coding RNAs that belong to the sigmaE Regulon: Role in Down-regulation of Outer Membrane Proteins. Journal of Molecular Biology 2006, 364:1-8.
    • (2006) Journal of Molecular Biology , vol.364 , pp. 1-8
    • Johansen, J.1    Rasmussen, A.A.2    Overgaard, M.3    Valentin-Hansen, P.4
  • 59
    • 0016589412 scopus 로고
    • The Major Proteins of the Escherichia coli Outer Cell Envelope Membrane. Preparative isolation of all major membrane proteins
    • Hindennach I, Henning U. The Major Proteins of the Escherichia coli Outer Cell Envelope Membrane. Preparative isolation of all major membrane proteins. European Journal of Biochemistry 1975, 59:207-213.
    • (1975) European Journal of Biochemistry , vol.59 , pp. 207-213
    • Hindennach, I.1    Henning, U.2
  • 60
    • 0019287045 scopus 로고
    • Proteins of the Outer Membrane of Gram-Negative Bacteria
    • 6254441
    • Osborn MJ, Wu HC. Proteins of the Outer Membrane of Gram-Negative Bacteria. Annual Review of Microbiology 1980, 34:369-422. 6254441.
    • (1980) Annual Review of Microbiology , vol.34 , pp. 369-422
    • Osborn, M.J.1    Wu, H.C.2
  • 61
    • 0027787823 scopus 로고
    • The activity of sigma E, an Escherichia coli heat-inducible sigma-factor, is modulated by expression of outer membrane proteins
    • Mecsas J, Rouviere PE, Erickson JW, Donohue TJ, Gross CA. The activity of sigma E, an Escherichia coli heat-inducible sigma-factor, is modulated by expression of outer membrane proteins. Genes & Development 1993, 7:2618-2628.
    • (1993) Genes & Development , vol.7 , pp. 2618-2628
    • Mecsas, J.1    Rouviere, P.E.2    Erickson, J.W.3    Donohue, T.J.4    Gross, C.A.5
  • 62
    • 0021989093 scopus 로고
    • Molecular bases of bacterial outer membrane permeability
    • 373015, 2580220
    • Nikaido H, Vaara M. Molecular bases of bacterial outer membrane permeability. Microbiological Reviews 1985, 49:1-32. 373015, 2580220.
    • (1985) Microbiological Reviews , vol.49 , pp. 1-32
    • Nikaido, H.1    Vaara, M.2
  • 63
    • 0036363003 scopus 로고    scopus 로고
    • The effect of starvation stress on the porin protein expression of Escherichia coli in lake water
    • Oezkanca R, Flint KP. The effect of starvation stress on the porin protein expression of Escherichia coli in lake water. Letters in Applied Microbiology 2002, 35:533-537.
    • (2002) Letters in Applied Microbiology , vol.35 , pp. 533-537
    • Oezkanca, R.1    Flint, K.P.2
  • 64
    • 0029684296 scopus 로고    scopus 로고
    • Involvement of molecular chaperones in intracellular protein breakdown
    • Sherman MY, Goldberg AL. Involvement of molecular chaperones in intracellular protein breakdown. EXS 1996, 77:57-78.
    • (1996) EXS , vol.77 , pp. 57-78
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 66
    • 0035877593 scopus 로고    scopus 로고
    • Characterization of the Escherichia coli sigma E Regulon
    • Dartigalongue C, Missiakas D, Raina S. Characterization of the Escherichia coli sigma E Regulon. J Biol Chem 2001, 276:6-2087.
    • (2001) J Biol Chem , vol.276 , pp. 6-2087
    • Dartigalongue, C.1    Missiakas, D.2    Raina, S.3
  • 67
    • 0344953579 scopus 로고    scopus 로고
    • OMP Peptide Signals Initiate the Envelope-Stress Response by Activating DegS Protease via Relief of Inhibition Mediated by Its PDZ Domain
    • Walsh NP, Alba BM, Bose B, Gross CA, Sauer RT. OMP Peptide Signals Initiate the Envelope-Stress Response by Activating DegS Protease via Relief of Inhibition Mediated by Its PDZ Domain. Cell 2003, 113:61-71.
    • (2003) Cell , vol.113 , pp. 61-71
    • Walsh, N.P.1    Alba, B.M.2    Bose, B.3    Gross, C.A.4    Sauer, R.T.5
  • 68
    • 0031004715 scopus 로고    scopus 로고
    • Chaperone Properties of the Bacterial Periplasmic Substrate-binding Proteins
    • Richarme G, Caldas TD. Chaperone Properties of the Bacterial Periplasmic Substrate-binding Proteins. Journal of Biological Chemistry 1997, 272:7-1561.
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 7-1561
    • Richarme, G.1    Caldas, T.D.2
  • 69
    • 0026596223 scopus 로고
    • Successive action of DnaK, DnaJ and GroEL along th pathway of chaperone-mediated protein folding
    • Langer T, Lu C, Echols H, Flanagan J, Hayer MK, Hartl FU. Successive action of DnaK, DnaJ and GroEL along th pathway of chaperone-mediated protein folding. Nature 1992, 356:683-689.
    • (1992) Nature , vol.356 , pp. 683-689
    • Langer, T.1    Lu, C.2    Echols, H.3    Flanagan, J.4    Hayer, M.K.5    Hartl, F.U.6
  • 70
    • 0018369994 scopus 로고
    • Aminoacyl-tRNA synthetases: general features and recognition of transfer RNAs
    • Schimmel PR, Söll D. Aminoacyl-tRNA synthetases: general features and recognition of transfer RNAs. Annual Review in Biochemistry 1979, 48:601-648.
    • (1979) Annual Review in Biochemistry , vol.48 , pp. 601-648
    • Schimmel, P.R.1    Söll, D.2
  • 71
    • 0029974453 scopus 로고    scopus 로고
    • Extraribosomal functions of ribosomal proteins
    • Wool IG. Extraribosomal functions of ribosomal proteins. Trends in Biochemical Sciences 1996, 21:164-165.
    • (1996) Trends in Biochemical Sciences , vol.21 , pp. 164-165
    • Wool, I.G.1
  • 73
    • 0022985811 scopus 로고
    • The central metabolic pathways of Escherichia coli: relationship between flux and control at a branch point, efficiency of conversion to biomass, and excretion of acetate
    • Holms H. The central metabolic pathways of Escherichia coli: relationship between flux and control at a branch point, efficiency of conversion to biomass, and excretion of acetate. Current Topics in Cellular Regulation 1986, 28:59-105.
    • (1986) Current Topics in Cellular Regulation , vol.28 , pp. 59-105
    • Holms, H.1
  • 74
    • 0000089325 scopus 로고
    • Observations on the carbohydrate metabolism of tumours
    • Crabtree HG. Observations on the carbohydrate metabolism of tumours. Biochemistry Journal 1929, 23:536-545.
    • (1929) Biochemistry Journal , vol.23 , pp. 536-545
    • Crabtree, H.G.1
  • 75
    • 0003127926 scopus 로고
    • Regulation of glucose metabolism in bacterial systems
    • Doelle HW, Ken NW, Hollywood NW. Regulation of glucose metabolism in bacterial systems. Adv Biochem Eng 1982, 23:1-35.
    • (1982) Adv Biochem Eng , vol.23 , pp. 1-35
    • Doelle, H.W.1    Ken, N.W.2    Hollywood, N.W.3
  • 76
    • 0021744435 scopus 로고
    • Uncoupling by Acetic Acid Limits Growth of and Acetogenesis by Clostridium thermoaceticum
    • 241699, 16346677
    • Baronofsky JJ, Schreurs WJ, Kashket ER. Uncoupling by Acetic Acid Limits Growth of and Acetogenesis by Clostridium thermoaceticum. Appl Environ Microbiol 1984, 48:1134-1139. 241699, 16346677.
    • (1984) Appl Environ Microbiol , vol.48 , pp. 1134-1139
    • Baronofsky, J.J.1    Schreurs, W.J.2    Kashket, E.R.3
  • 77
    • 0019395341 scopus 로고
    • Cytoplasmic pH mediates pH taxis and weak-acid repellent taxis of bacteria
    • 217121, 7009572
    • Kihara M, Macnab RM. Cytoplasmic pH mediates pH taxis and weak-acid repellent taxis of bacteria. J Bacteriol 1981, 145:1209-1221. 217121, 7009572.
    • (1981) J Bacteriol , vol.145 , pp. 1209-1221
    • Kihara, M.1    Macnab, R.M.2
  • 78
    • 0022349278 scopus 로고
    • Regulation of cytoplasmic pH in bacteria
    • Booth IR. Regulation of cytoplasmic pH in bacteria. Microbiol Mol Biol Rev 1985, 49:359-378.
    • (1985) Microbiol Mol Biol Rev , vol.49 , pp. 359-378
    • Booth, I.R.1
  • 79
    • 0031882597 scopus 로고    scopus 로고
    • Perturbation of Anion Balance during Inhibition of Growth of Escherichia coli by Weak Acids
    • Roe AJ, McLaggan D, Davidson I, O'Byrne C, Booth IR. Perturbation of Anion Balance during Inhibition of Growth of Escherichia coli by Weak Acids. The Journal of Bacteriology 1998, 180:767-772.
    • (1998) The Journal of Bacteriology , vol.180 , pp. 767-772
    • Roe, A.J.1    McLaggan, D.2    Davidson, I.3    O'Byrne, C.4    Booth, I.R.5
  • 80
    • 0036061941 scopus 로고    scopus 로고
    • Inhibition of Escherichia coli growth by acetic acid: a problem with methionine biosynthesis and homocysteine toxicity
    • Roe AJ, O'Byrne C, McLaggan D, Booth IR. Inhibition of Escherichia coli growth by acetic acid: a problem with methionine biosynthesis and homocysteine toxicity. Microbiology 2002, 148:2215-2222.
    • (2002) Microbiology , vol.148 , pp. 2215-2222
    • Roe, A.J.1    O'Byrne, C.2    McLaggan, D.3    Booth, I.R.4
  • 82
    • 0031844376 scopus 로고    scopus 로고
    • Negative regulation by RpoS: a case of sigma factor competition
    • Farewell A, Kvint K, Nystrom T. Negative regulation by RpoS: a case of sigma factor competition. Molecular Microbiology 1998, 29:1039-1051.
    • (1998) Molecular Microbiology , vol.29 , pp. 1039-1051
    • Farewell, A.1    Kvint, K.2    Nystrom, T.3
  • 83
    • 33846827387 scopus 로고    scopus 로고
    • Global gene expression analysis of glucose overflow metabolism in Escherichia coli and reduction of aerobic acetate formation
    • Veit A, Polen T, Wendisch VF. Global gene expression analysis of glucose overflow metabolism in Escherichia coli and reduction of aerobic acetate formation. Applied Microbiology and Biotechnology 2007, 74:406-421.
    • (2007) Applied Microbiology and Biotechnology , vol.74 , pp. 406-421
    • Veit, A.1    Polen, T.2    Wendisch, V.F.3
  • 84
    • 27744453102 scopus 로고    scopus 로고
    • Proteome analysis to assess physiological changes in Escherichia coli grown under glucose-limited fed-batch conditions
    • Raman B, Nandakumar MP, Muthuvijayan V, Marten MR. Proteome analysis to assess physiological changes in Escherichia coli grown under glucose-limited fed-batch conditions. Biotechnology and Bioengineering 2005, 92:384-392.
    • (2005) Biotechnology and Bioengineering , vol.92 , pp. 384-392
    • Raman, B.1    Nandakumar, M.P.2    Muthuvijayan, V.3    Marten, M.R.4
  • 85
    • 0000877111 scopus 로고
    • The glyoxylate cycle as a stage in the conversion of fat to carbohydrate in castor beans
    • Kornberg HL, Beevers H. The glyoxylate cycle as a stage in the conversion of fat to carbohydrate in castor beans. Biochimica et Biophysica Acta 1957, 26:531-537.
    • (1957) Biochimica et Biophysica Acta , vol.26 , pp. 531-537
    • Kornberg, H.L.1    Beevers, H.2
  • 86
    • 0000581636 scopus 로고
    • Synthesis of cell constituents from C2-units by a modified tricarboxylic acid cycle
    • Kornberg HL, Krebs HA. Synthesis of cell constituents from C2-units by a modified tricarboxylic acid cycle. Nature 1957, 179:988-991.
    • (1957) Nature , vol.179 , pp. 988-991
    • Kornberg, H.L.1    Krebs, H.A.2
  • 87
    • 0028340662 scopus 로고
    • Regulation of acetyl phosphate synthesis and degradation, and the control of flagellar expression in Escherichia coli
    • Pruess BM, Wolfe AJ. Regulation of acetyl phosphate synthesis and degradation, and the control of flagellar expression in Escherichia coli. Molecular Microbiology 1994, 12:973-984.
    • (1994) Molecular Microbiology , vol.12 , pp. 973-984
    • Pruess, B.M.1    Wolfe, A.J.2
  • 88
    • 0033621553 scopus 로고    scopus 로고
    • Sigma 70 Is the Principal Sigma Factor Responsible for Transcription of acs, Which Encodes Acetyl Coenzyme A Synthetase in Escherichia coli
    • 94314, 10629211
    • Kumari S, Simel EJ, Wolfe AJ. sigma 70 Is the Principal Sigma Factor Responsible for Transcription of acs, Which Encodes Acetyl Coenzyme A Synthetase in Escherichia coli. J Bacteriol 2000, 182:551-554. 94314, 10629211.
    • (2000) J Bacteriol , vol.182 , pp. 551-554
    • Kumari, S.1    Simel, E.J.2    Wolfe, A.J.3
  • 89
  • 90
    • 0015947712 scopus 로고
    • Transport Systems for L-Methionine in Escherichia coli
    • 246549, 4587605
    • Kadner RJ. Transport Systems for L-Methionine in Escherichia coli. J Bacteriol 1974, 117:232-241. 246549, 4587605.
    • (1974) J Bacteriol , vol.117 , pp. 232-241
    • Kadner, R.J.1
  • 91
    • 0016671558 scopus 로고
    • Regulation of methionine transport activity in Escherichia coli
    • 235647, 1091617
    • Kadner RJ. Regulation of methionine transport activity in Escherichia coli. J Bacteriol 1975, 122:110-119. 235647, 1091617.
    • (1975) J Bacteriol , vol.122 , pp. 110-119
    • Kadner, R.J.1
  • 92
    • 0003796783 scopus 로고    scopus 로고
    • Escherichia coli and Salmonella. Cellular and molecular Biology
    • ASM Press Washingtion, DC
    • Neidhardt FC. Escherichia coli and Salmonella. Cellular and molecular Biology. 1996, 1:542-560. ASM Press Washingtion, DC.
    • (1996) , vol.1 , pp. 542-560
    • Neidhardt, F.C.1
  • 94
    • 0016233136 scopus 로고
    • Evidence for the Involvement of Serine Transhydroxymethylase in Serine and Glycine Interconversions in Salmonella typhimurium
    • 1213123, 4603160
    • Stauffer GV, Brenchley JE. Evidence for the Involvement of Serine Transhydroxymethylase in Serine and Glycine Interconversions in Salmonella typhimurium. Genetics 1974, 77:185-198. 1213123, 4603160.
    • (1974) Genetics , vol.77 , pp. 185-198
    • Stauffer, G.V.1    Brenchley, J.E.2
  • 95
    • 0003830834 scopus 로고
    • The Biochemistry of Folic Acid and Related Pteridines
    • Elsevier/North-Holland Publishing Co, Amsterdam
    • Blakley RL. The Biochemistry of Folic Acid and Related Pteridines. 1969, Elsevier/North-Holland Publishing Co, Amsterdam.
    • (1969)
    • Blakley, R.L.1
  • 96
    • 0025778597 scopus 로고
    • Bipartite functional map of the E. coli polymerase α subunit: involvement of the C-terminal region in transcriptional activation by cAMP-CRP
    • Igarashi K, Ishihama A. Bipartite functional map of the E. coli polymerase α subunit: involvement of the C-terminal region in transcriptional activation by cAMP-CRP. Cell 1991, 65:1015-1022.
    • (1991) Cell , vol.65 , pp. 1015-1022
    • Igarashi, K.1    Ishihama, A.2
  • 97
    • 77956929400 scopus 로고
    • δ-Aminolevulinic acid synthetase
    • Academic Press Inc, New York, Boyer PD
    • Jordan PM, Shemin D. δ-Aminolevulinic acid synthetase. The Enzymes 1972, 7:339-356. Academic Press Inc, New York, Boyer PD.
    • (1972) The Enzymes , vol.7 , pp. 339-356
    • Jordan, P.M.1    Shemin, D.2
  • 98
    • 0034010828 scopus 로고    scopus 로고
    • Riding the sulfur cycle - metabolism of sulfonates and sulfate esters in Gram-negative bacteria
    • Kertesz MA. Riding the sulfur cycle - metabolism of sulfonates and sulfate esters in Gram-negative bacteria. FEMS Microbiology Reviews 2000, 24:135-175.
    • (2000) FEMS Microbiology Reviews , vol.24 , pp. 135-175
    • Kertesz, M.A.1
  • 99
    • 0021891891 scopus 로고
    • Biosynthesis and Metabolism of Tetrahydrobiopterin and Molybdopterin
    • Nichol CA, Smith GK, Duch DS. Biosynthesis and Metabolism of Tetrahydrobiopterin and Molybdopterin. Annual Review of Biochemistry 1985, 54:729-764.
    • (1985) Annual Review of Biochemistry , vol.54 , pp. 729-764
    • Nichol, C.A.1    Smith, G.K.2    Duch, D.S.3
  • 102
    • 0029075602 scopus 로고
    • Superoxide dismutase protects against aerobic heat shock in Escherichia coli
    • 177032, 7768839
    • Benov L, Fridovich I. Superoxide dismutase protects against aerobic heat shock in Escherichia coli. J Bacteriol 1995, 177:3344-3346. 177032, 7768839.
    • (1995) J Bacteriol , vol.177 , pp. 3344-3346
    • Benov, L.1    Fridovich, I.2
  • 104
    • 0035346790 scopus 로고    scopus 로고
    • A comparison between Sypro Ruby and ruthenium II tris (bathophenanthroline disulfonate) as fluorescent stains for protein detection in gels
    • 11678039
    • Rabilloud T, Strub JM, Luche S, van Dorsselaer A, Lunardi J. A comparison between Sypro Ruby and ruthenium II tris (bathophenanthroline disulfonate) as fluorescent stains for protein detection in gels. Proteomics 2001, 1:699-704. 11678039.
    • (2001) Proteomics , vol.1 , pp. 699-704
    • Rabilloud, T.1    Strub, J.M.2    Luche, S.3    van Dorsselaer, A.4    Lunardi, J.5
  • 105
    • 0019887744 scopus 로고
    • Phase Separation of Integral Membrane Proteins in Triton X-114 Solution
    • Bordier C. Phase Separation of Integral Membrane Proteins in Triton X-114 Solution. The Journal of Biological Chemistry 1981, 256:1604-1607.
    • (1981) The Journal of Biological Chemistry , vol.256 , pp. 1604-1607
    • Bordier, C.1
  • 106
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum
    • 2112113, 7068762
    • Fujiki Y, Hubbard AL, Fowler S, Lazarow PB. Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum. J Cell Biol 1982, 93:97-102. 2112113, 7068762.
    • (1982) J Cell Biol , vol.93 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.B.4
  • 107
    • 0042367748 scopus 로고    scopus 로고
    • Combined use of proteomic analysis and enzyme activity assays for metabolic pathway analysis of glycerol fermentation by Klebsiella pneumoniae
    • Wang W, Sun J, Hartlep M, Deckwer WD, Zeng AP. Combined use of proteomic analysis and enzyme activity assays for metabolic pathway analysis of glycerol fermentation by Klebsiella pneumoniae. Biotechnol Bioeng 2003, 83:525-536.
    • (2003) Biotechnol Bioeng , vol.83 , pp. 525-536
    • Wang, W.1    Sun, J.2    Hartlep, M.3    Deckwer, W.D.4    Zeng, A.P.5


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