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Volumn 74, Issue 5, 2011, Pages 849-864

An overview of molecular stress response mechanisms in escherichia coli contributing to survival of shiga toxin-producing escherichia coli during raw milk cheese production

Author keywords

[No Author keywords available]

Indexed keywords

SHIGA TOXIN;

EID: 79955582744     PISSN: 0362028X     EISSN: None     Source Type: Journal    
DOI: 10.4315/0362-028X.JFP-10-469     Document Type: Review
Times cited : (31)

References (213)
  • 1
    • 1842558298 scopus 로고    scopus 로고
    • E in Escherichia coli
    • DOI 10.1016/j.mib.2004.02.010, PII S1369527404000232
    • Ades, S. E. 2004. Control of the alternative sigma factor sigmaE in Escherichia coli. Curr. Opin. Microbiol. 7:157-162. (Pubitemid 38447049)
    • (2004) Current Opinion in Microbiology , vol.7 , Issue.2 , pp. 157-162
    • Ades, S.E.1
  • 2
    • 49949117088 scopus 로고    scopus 로고
    • Examination of stress and virulence gene expression in Escherichia coli O157:H7 using targeted microarray analysis
    • Allen, K. J., D. Lepp, R. C. McKellar, and M. W. Griffiths. 2008. Examination of stress and virulence gene expression in Escherichia coli O157:H7 using targeted microarray analysis. Foodborne Pathog. Dis. 5:437-447.
    • (2008) Foodborne Pathog. Dis. , vol.5 , pp. 437-447
    • Allen, K.J.1    Lepp, D.2    McKellar, R.C.3    Griffiths, M.W.4
  • 4
    • 0027083350 scopus 로고
    • A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli
    • Almiron, M., A. J. Link, D. Furlong, and R. Kolter. 1992. A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli. Genes Dev. 6:2646-2654. (Pubitemid 23052891)
    • (1992) Genes and Development , vol.6 , Issue.12 B , pp. 2646-2654
    • Almiron, M.1    Link, A.J.2    Furlong, D.3    Kolter, R.4
  • 5
    • 0027989420 scopus 로고
    • The sensor kinase KdpD and the response regulator KdpE control expression of the kdpFABC operon in Escherichia coli
    • DOI 10.1016/0923-2508(94)90084-1
    • Altendorf, K., P. Voelkner, and W. Puppe. 1994. The sensor kinase KdpD and the response regulator KdpE control expression of the kdpFABC operon in Escherichia coli. Res. Microbiol. 145:374-381. (Pubitemid 24281565)
    • (1994) Research in Microbiology , vol.145 , Issue.5-6 , pp. 374-381
    • Altendorf, K.1    Voelkner, P.2    Puppe, W.3
  • 6
    • 66149132248 scopus 로고    scopus 로고
    • Crystal structure of the acid-induced arginine decarboxylase from Escherichia coli: Reversible decamer assembly controls enzyme activity
    • Andrell, J., M. G. Hicks, T. Palmer, E. P. Carpenter, S. Iwata, and M. J. Maher. 2009. Crystal structure of the acid-induced arginine decarboxylase from Escherichia coli: Reversible decamer assembly controls enzyme activity. Biochemistry 48:3915-3927.
    • (2009) Biochemistry , vol.48 , pp. 3915-3927
    • Andrell, J.1    Hicks, M.G.2    Palmer, T.3    Carpenter, E.P.4    Iwata, S.5    Maher, M.J.6
  • 8
    • 0024028868 scopus 로고
    • Molecular cloning, physical mapping and expression of the bet genes governing the osmoregulatory choline-glycine betaine pathway of Escherichia coli
    • Andresen, P. A., I. Kaasen, O. B. Styrvold, G. Boulnois, and A. R. Strom. 1988. Molecular cloning, physical mapping and expression of the bet genes governing the osmoregulatory choline-glycine betaine pathway of Escherichia coli. J. Gen. Microbiol. 134:1737-1746.
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 1737-1746
    • Andresen, P.A.1    Kaasen, I.2    Styrvold, O.B.3    Boulnois, G.4    Strom, A.R.5
  • 9
    • 0030065869 scopus 로고    scopus 로고
    • Preservation microbiology and safety: Evidence that stress enhances virulence and triggers adaptive mutations
    • Archer, D. 1996. Preservation microbiology and safety: Evidence that stress enhances virulence and triggers adaptive mutations. Trends Food Sci. Technol. 7:91-95.
    • (1996) Trends Food Sci. Technol. , vol.7 , pp. 91-95
    • Archer, D.1
  • 10
    • 0029035948 scopus 로고
    • Starvation-and stationaryphase-induced acid tolerance in Escherichia coli O157: H7
    • Arnold, K. W., and C. W. Kaspar. 1995. Starvation-and stationaryphase-induced acid tolerance in Escherichia coli O157:H7. Appl. Environ. Microbiol. 61:2037-2039.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 2037-2039
    • Arnold, K.W.1    Kaspar, C.W.2
  • 11
    • 0037890192 scopus 로고    scopus 로고
    • The heat shock response of Escherichia coli
    • DOI 10.1016/S0168-1605(00)00206-3, PII S0168160500002063
    • Arsene, F., T. Tomoyasu, and B. Bukau. 2000. The heat shock response of Escherichia coli. Int. J. Food Microbiol. 55:3-9. (Pubitemid 30160797)
    • (2000) International Journal of Food Microbiology , vol.55 , Issue.1-3 , pp. 3-9
    • Arsene, F.1    Tomoyasu, T.2    Bukau, B.3
  • 12
    • 0030972952 scopus 로고    scopus 로고
    • H-NS: A modulator of environmentally regulated gene expression
    • Atlung, T., and H. Ingmer. 1997. H-NS: A modulator of environmentally regulated gene expression. Mol. Microbiol. 24: 7-17. (Pubitemid 27160834)
    • (1997) Molecular Microbiology , vol.24 , Issue.1 , pp. 7-17
    • Atlung, T.1    Ingmer, H.2
  • 13
    • 0029268463 scopus 로고
    • The fate of potentially pathogenic bacteria in Swiss hard and semihard cheeses made from raw milk
    • Bachmann, H. P., and U. Spahr. 1995. The fate of potentially pathogenic bacteria in Swiss hard and semihard cheeses made from raw milk. J. Dairy Sci. 78:476-483.
    • (1995) J. Dairy Sci. , vol.78 , pp. 476-483
    • Bachmann, H.P.1    Spahr, U.2
  • 14
    • 0035117825 scopus 로고    scopus 로고
    • The Escherichia coli histone-like protein HU regulates rpoS translation
    • DOI 10.1046/j.1365-2958.2001.02305.x
    • Balandina, A., L. Claret, R. Hengge-Aronis, and J. Rouviere-Yaniv. 2001. The Escherichia coli histone-like protein HU regulates rpoS translation. Mol. Microbiol. 39:1069-1079. (Pubitemid 32176349)
    • (2001) Molecular Microbiology , vol.39 , Issue.4 , pp. 1069-1079
    • Balandina, A.1    Claret, L.2    Hengge-Aronis, R.3    Rouviere-Yaniv, J.4
  • 15
    • 34248198768 scopus 로고    scopus 로고
    • The Kdp-ATPase system and its regulation
    • DOI 10.1007/s12038-007-0055-7
    • Ballal, A., B. Basu, and S. K. Apte. 2007. The Kdp-ATPase system and its regulation. J. Biosci. 32:559-568. (Pubitemid 46708706)
    • (2007) Journal of Biosciences , vol.32 , Issue.3 , pp. 559-568
    • Ballal, A.1    Basu, B.2    Apte, S.K.3
  • 16
    • 67949103493 scopus 로고    scopus 로고
    • Raw milk and raw milk cheeses as vehicles for infection by verocytotoxin producing Escherichia coli
    • Baylis, C. L. 2009. Raw milk and raw milk cheeses as vehicles for infection by verocytotoxin producing Escherichia coli. Int. J. Dairy Technol. 62:293-307.
    • (2009) Int. J. Dairy Technol. , vol.62 , pp. 293-307
    • Baylis, C.L.1
  • 17
    • 0031049325 scopus 로고    scopus 로고
    • Acid stress responses in enterobacteria
    • DOI 10.1016/S0378-1097(96)00503-4, PII S0378109796005034
    • Bearson, S., B. Bearson, and J. W. Foster. 1997. Acid stress responses in enterobacteria. FEMS Microbiol. Lett. 147:173-180. (Pubitemid 27105210)
    • (1997) FEMS Microbiology Letters , vol.147 , Issue.2 , pp. 173-180
    • Bearson, S.1    Bearson, B.2    Foster, J.W.3
  • 18
    • 0032989449 scopus 로고    scopus 로고
    • Regulation of RpoS proteolysis in Escherichia coli: The response regulator RssB is a recognition factor that interacts with the turnover element in RpoS
    • DOI 10.1073/pnas.96.11.6439
    • Becker, G., E. Klauck, and R. Hengge-Aronis. 1999. Regulation of RpoS proteolysis in Escherichia coli: The response regulator RssB is a recognition factor that interacts with the turnover element in RpoS. Proc. Natl. Acad. Sci. USA 96:6439-6444. (Pubitemid 29256684)
    • (1999) Proceedings of the National Academy of Sciences of the United States of America , vol.96 , Issue.11 , pp. 6439-6444
    • Becker, G.1    Klauck, E.2    Hengge-Aronis, R.3
  • 19
    • 0033951376 scopus 로고    scopus 로고
    • The response regulator RssB, a recognition factor for σ(S) proteolysis in Escherichia coli, can act like an anti-σ(S) factor
    • DOI 10.1046/j.1365-2958.2000.01736.x
    • Becker, G., E. Klauck, and R. Hengge-Aronis. 2000. The response regulator RssB, a recognition factor for sigmaS proteolysis in Escherichia coli, can act like an anti-sigmaS factor. Mol. Microbiol. 35:657-666. (Pubitemid 30085282)
    • (2000) Molecular Microbiology , vol.35 , Issue.3 , pp. 657-666
    • Becker, G.1    Klauck, E.2    Hengge-Aronis, R.3
  • 20
    • 0027218002 scopus 로고
    • Prevalence and some properties of verotoxin (Shiga-like toxin)-producing Escherichia coli in seven different species of healthy domestic animals
    • Beutin, L., D. Geier, H. Steinruck, S. Zimmermann, and F. Scheutz. 1993. Prevalence and some properties of verotoxin (Shiga-like toxin)-producing Escherichia coli in seven different species of healthy domestic animals. J. Clin. Microbiol. 31:2483-2488. (Pubitemid 23254221)
    • (1993) Journal of Clinical Microbiology , vol.31 , Issue.9 , pp. 2483-2488
    • Beutin, L.1    Geier, D.2    Steinruck, H.3    Zimmermann, S.4    Scheutz, F.5
  • 22
    • 0035237232 scopus 로고    scopus 로고
    • Protein stabilization by naturally occurring osmolytes
    • Bolen, D. W. 2001. Protein stabilization by naturally occurring osmolytes. Methods Mol. Biol. 168:17-36.
    • (2001) Methods Mol. Biol. , vol.168 , pp. 17-36
    • Bolen, D.W.1
  • 23
    • 0032853219 scopus 로고    scopus 로고
    • Cellular and molecular biology of the aquaporin water channels
    • DOI 10.1146/annurev.biochem.68.1.425
    • Borgnia, M., S. Nielsen, A. Engel, and P. Agre. 1999. Cellular and molecular biology of the aquaporin water channels. Annu. Rev. Biochem. 68:425-458. (Pubitemid 29449199)
    • (1999) Annual Review of Biochemistry , vol.68 , pp. 425-458
    • Borgnia, M.1    Nielsen, So.2    Engel, A.3    Agre, P.4
  • 24
    • 0036840677 scopus 로고    scopus 로고
    • Role of the RNA polymerase sigma subunit in transcription initiation
    • DOI 10.1016/S0923-2508(02)01368-2, PII S0923250802013682
    • Borukhov, S., and K. Severinov. 2002. Role of the RNA polymerase sigma subunit in transcription initiation. Res. Microbiol. 153:557-562. (Pubitemid 35223308)
    • (2002) Research in Microbiology , vol.153 , Issue.9 , pp. 557-562
    • Borukhov, S.1    Severinov, K.2
  • 26
    • 41049111259 scopus 로고    scopus 로고
    • S (RpoS) stability in Escherichia coli via the action of multiple anti-adaptors
    • DOI 10.1111/j.1365-2958.2008.06146.x
    • Bougdour, A., C. Cunning, P. J. Baptiste, T. Elliott, and S. Gottesman. 2008. Multiple pathways for regulation of sigmaS (RpoS) stability in Escherichia coli via the action of multiple antiadaptors. Mol. Microbiol. 68:298-313. (Pubitemid 351422952)
    • (2008) Molecular Microbiology , vol.68 , Issue.2 , pp. 298-313
    • Bougdour, A.1    Cunning, C.2    Baptiste, P.J.3    Elliott, T.4    Gottesman, S.5
  • 29
    • 0031015418 scopus 로고    scopus 로고
    • Mutations that increase expression of the rpoS gene and decrease its dependence on hfq function in Salmonella typhimurium
    • Brown, L., and T. Elliott. 1997. Mutations that increase expression of the rpoS gene and decrease its dependence on hfq function in Salmonella typhimurium. J. Bacteriol. 179:656-662. (Pubitemid 27051817)
    • (1997) Journal of Bacteriology , vol.179 , Issue.3 , pp. 656-662
    • Brown, L.1    Elliott, T.2
  • 30
    • 0027319272 scopus 로고
    • Regulation of the Escherichia coli heat-shock response
    • Bukau, B. 1993. Regulation of the Escherichia coli heat-shock response. Mol. Microbiol. 9:671-680. (Pubitemid 23253493)
    • (1993) Molecular Microbiology , vol.9 , Issue.4 , pp. 671-680
    • Bukau, B.1
  • 31
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • DOI 10.1016/S0092-8674(00)80928-9
    • Bukau, B., and A. L. Horwich. 1998. The Hsp70 and Hsp60 chaperone machines. Cell 92:351-366. (Pubitemid 28093013)
    • (1998) Cell , vol.92 , Issue.3 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 32
    • 0037025378 scopus 로고    scopus 로고
    • EnvZ-OmpR interaction and osmoregulation in Escherichia coli
    • DOI 10.1074/jbc.M110715200
    • Cai, S. J., and M. Inouye. 2002. EnvZ-OmpR interaction and osmoregulation in Escherichia coli. J. Biol. Chem. 277:24155-24161. (Pubitemid 34951930)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.27 , pp. 24155-24161
    • Cai, S.J.1    Inouye, M.2
  • 33
    • 0041465717 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of Escherichia coli glutamate decarboxylase
    • DOI 10.1093/emboj/cdg403
    • Capitani, G., D. De Biase, C. Aurizi, H. Gut, F. Bossa, and M. G. Grutter. 2003. Crystal structure and functional analysis of Escherichia coli glutamate decarboxylase. EMBO J. 22:4027-4037. (Pubitemid 37021732)
    • (2003) EMBO Journal , vol.22 , Issue.16 , pp. 4027-4037
    • Capitani, G.1    De Biase, D.2    Aurizi, C.3    Gut, H.4    Bossa, F.5    Grutter, M.G.6
  • 34
    • 34247096016 scopus 로고    scopus 로고
    • Occurrence of Shiga toxin-producing Escherichia coli in a Spanish raw ewe's milk cheese
    • DOI 10.1016/j.ijfoodmicro.2007.02.015, PII S0168160507001602
    • Caro, I., and M. R. Garcia-Armesto. 2007. Occurrence of Shiga toxin-producing Escherichia coli in a Spanish raw ewe's milk cheese. Int. J. Food Microbiol. 116:410-413. (Pubitemid 46602644)
    • (2007) International Journal of Food Microbiology , vol.116 , Issue.3 , pp. 410-413
    • Caro, I.1    Garcia-Armesto, M.R.2
  • 37
    • 0034028431 scopus 로고    scopus 로고
    • Biophysical characterization of changes in amounts and activity of Escherichia coli cell and compartment water and turgor pressure in response to osmotic stress
    • Cayley, D. S., H. J. Guttman, and M. T. Record, Jr. 2000. Biophysical characterization of changes in amounts and activity of Escherichia coli cell and compartment water and turgor pressure in response to osmotic stress. Biophys. J. 78:1748-1764. (Pubitemid 30183573)
    • (2000) Biophysical Journal , vol.78 , Issue.4 , pp. 1748-1764
    • Cayley, D.S.1    Guttman, H.J.2    Record Jr., M.T.3
  • 38
    • 0141754010 scopus 로고    scopus 로고
    • Role of the γ-phosphate of ATP in triggering protein folding by GroEL-GroES: Function, structure and energetics
    • DOI 10.1093/emboj/cdg477
    • Chaudhry, C., G. W. Farr, M. J. Todd, H. S. Rye, A. T. Brunger, P. D. Adams, A. L. Horwich, and P. B. Sigler. 2003. Role of the gamma-phosphate of ATP in triggering protein folding by GroELGroES: Function, structure and energetics. EMBO J. 22:4877-4887. (Pubitemid 37222010)
    • (2003) EMBO Journal , vol.22 , Issue.19 , pp. 4877-4887
    • Chaudhry, C.1    Farr, G.W.2    Todd, M.J.3    Rye, H.S.4    Brunger, A.T.5    Adams, P.D.6    Horwich, A.L.7    Sigler, P.B.8
  • 42
    • 0037457916 scopus 로고    scopus 로고
    • Osmosensor ProP of Escherichia coli responds to the concentration, chemistry, and molecular size of osmolytes in the proteoliposome lumen
    • DOI 10.1021/bi0264364
    • Culham, D. E., J. Henderson, R. A. Crane, and J. M. Wood. 2003. Osmosensor ProP of Escherichia coli responds to the concentration, chemistry, and molecular size of osmolytes in the proteoliposome lumen. Biochemistry 42:410-420. (Pubitemid 36105759)
    • (2003) Biochemistry , vol.42 , Issue.2 , pp. 410-420
    • Culham, D.E.1    Henderson, J.2    Crane, R.A.3    Wood, J.M.4
  • 43
    • 0024226563 scopus 로고
    • Thermal inactivation of Campylobacter species, Yersinia enterocolitica, and hemorrhagic Escherichia coli O157:H7 in fluid milk
    • D'Aoust, J. Y., C. E. Park, R. A. Szabo, E. C. Todd, D. B. Emmons, and R. C. McKellar. 1988. Thermal inactivation of Campylobacter species, Yersinia enterocolitica, and hemorrhagic Escherichia coli O157:H7 in fluid milk. J. Dairy Sci. 71:3230-3236.
    • (1988) J. Dairy Sci. , vol.71 , pp. 3230-3236
    • D'Aoust, J.Y.1    Park, C.E.2    Szabo, R.A.3    Todd, E.C.4    Emmons, D.B.5    McKellar, R.C.6
  • 44
    • 0024524097 scopus 로고
    • Osmoregulation in Escherichia coli: Complementation analysis and gene-protein relationships in the proU locus
    • Dattananda, C. S., and J. Gowrishankar. 1989. Osmoregulation in Escherichia coli: Complementation analysis and gene-protein relationships in the proU locus. J. Bacteriol. 171:1915-1922. (Pubitemid 19103955)
    • (1989) Journal of Bacteriology , vol.171 , Issue.4 , pp. 1915-1922
    • Dattananda, C.S.1    Gowrishankar, J.2
  • 47
    • 0023712118 scopus 로고
    • Transient accumulation of potassium glutamate and its replacement by trehalose during adaptation of growing cells of Escherichia coli K-12 to elevated sodium chloride concentrations
    • Dinnbier, U., E. Limpinsel, R. Schmid, and E. P. Bakker. 1988. Transient accumulation of potassium glutamate and its replacement by trehalose during adaptation of growing cells of Escherichia coli K-12 to elevated sodium chloride concentrations. Arch. Microbiol. 150:348-357.
    • (1988) Arch. Microbiol. , vol.150 , pp. 348-357
    • Dinnbier, U.1    Limpinsel, E.2    Schmid, R.3    Bakker, E.P.4
  • 48
    • 69249146924 scopus 로고    scopus 로고
    • Global effect of RpoS on gene expression in pathogenic Escherichia coli O157:H7 strain EDL933
    • Dong, T., and H. E. Schellhorn. 2009. Global effect of RpoS on gene expression in pathogenic Escherichia coli O157:H7 strain EDL933. BMC Genomics 10:349.
    • (2009) BMC Genomics , vol.10 , pp. 349
    • Dong, T.1    Schellhorn, H.E.2
  • 49
    • 34447528296 scopus 로고    scopus 로고
    • Microcins, gene-encoded antibacterial peptides from enterobacteria
    • DOI 10.1039/b516237h
    • Duquesne, S., D. Destoumieux-Garzon, J. Peduzzi, and S. Rebuffat. 2007. Microcins, gene-encoded antibacterial peptides from enterobacteria. Nat. Prod. Rep. 24:708-734. (Pubitemid 47108192)
    • (2007) Natural Product Reports , vol.24 , Issue.4 , pp. 708-734
    • Duquesne, S.1    Destoumieux-Garzon, D.2    Peduzzi, J.3    Rebuffat, S.4
  • 50
    • 0037122805 scopus 로고    scopus 로고
    • X-ray structure of a CIC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity
    • DOI 10.1038/415287a
    • Dutzler, R., E. B. Campbell, M. Cadene, B. T. Chait, and R. MacKinnon. 2002. X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity. Nature 415:287-294. (Pubitemid 34087544)
    • (2002) Nature , vol.415 , Issue.6869 , pp. 287-294
    • Dutzler, R.1    Campbell, E.B.2    Cadene, M.3    Chait, B.T.4    MacKinnon, R.5
  • 51
    • 0038056150 scopus 로고    scopus 로고
    • New insights on trehalose: A multifunctional molecule
    • DOI 10.1093/glycob/cwg047
    • Elbein, A. D., Y. T. Pan, I. Pastuszak, and D. Carroll. 2003. New insights on trehalose: A multifunctional molecule. Glycobiology 13: 17R-27R. (Pubitemid 36592310)
    • (2003) Glycobiology , vol.13 , Issue.4
    • Elbein, A.D.1    Pan, Y.T.2    Pastuszak, I.3    Carroll, D.4
  • 52
    • 1542570529 scopus 로고    scopus 로고
    • The Roles and Regulation of Potassium in Bacteria
    • DOI 10.1016/S0079-6603(03)75008-9, PII S0079660303750089
    • Epstein, W. 2003. The roles and regulation of potassium in bacteria. Prog. Nucleic Acid Res. Mol. Biol. 75:293-320. (Pubitemid 137639560)
    • (2003) Progress in Nucleic Acid Research and Molecular Biology , vol.75 , pp. 293-320
    • Epstein, W.1
  • 53
    • 27644580821 scopus 로고    scopus 로고
    • Response of Escherichia coli O157:H7, Listeria monocytogenes, Salmonella Typhimurium, and Staphylococcus aureus to the thermal stress occurring in model manufactures of Grana Padano cheese
    • Ercolini, D., V. Fusco, G. Blaiotta, F. Sarghini, and S. Coppola. 2005. Response of Escherichia coli O157:H7, Listeria monocytogenes, Salmonella Typhimurium, and Staphylococcus aureus to the thermal stress occurring in model manufactures of Grana Padano cheese. J. Dairy Sci. 88:3818-3825. (Pubitemid 41577596)
    • (2005) Journal of Dairy Science , vol.88 , Issue.11 , pp. 3818-3825
    • Ercolini, D.1    Fusco, V.2    Blaiotta, G.3    Sarghini, F.4    Coppola, S.5
  • 54
    • 0023367975 scopus 로고
    • Regulation of the promoters and transcripts of rpoH, the Escherichia coli heat shock regulatory gene
    • Erickson, J. W., V. Vaughn, W. A. Walter, F. C. Neidhardt, and C. A. Gross. 1987. Regulation of the promoters and transcripts of rpoH, the Escherichia coli heat shock regulatory gene. Genes Dev. 1:419-432.
    • (1987) Genes Dev. , vol.1 , pp. 419-432
    • Erickson, J.W.1    Vaughn, V.2    Walter, W.A.3    Neidhardt, F.C.4    Gross, C.A.5
  • 55
    • 0023692410 scopus 로고
    • Lac Fusion analysis of the bet genes of Escherichia coli: Regulation by osmolarity, temperature, oxygen, choline, and glycine betaine
    • Eshoo, M. W. 1988. lac Fusion analysis of the bet genes of Escherichia coli: Regulation by osmolarity, temperature, oxygen, choline, and glycine betaine. J. Bacteriol. 170:5208-5215. (Pubitemid 18259462)
    • (1988) Journal of Bacteriology , vol.170 , Issue.11 , pp. 5208-5215
    • Eshoo, M.W.1
  • 57
    • 0028113299 scopus 로고
    • Residues in chaperonin GroEL required for polypeptide binding and release
    • DOI 10.1038/371614a0
    • Fenton, W. A., Y. Kashi, K. Furtak, and A. L. Horwich. 1994. Residues in chaperonin GroEL required for polypeptide binding and release. Nature 371:614-619. (Pubitemid 24315744)
    • (1994) Nature , vol.371 , Issue.6498 , pp. 614-619
    • Fenton, W.A.1    Kashi, Y.2    Furtak, K.3    Horwich, A.L.4
  • 58
    • 0033118208 scopus 로고    scopus 로고
    • When protons attack: Microbial strategies of acid adaptation
    • DOI 10.1016/S1369-5274(99)80030-7
    • Foster, J. W. 1999. When protons attack: Microbial strategies of acid adaptation. Curr. Opin. Microbiol. 2:170-174. (Pubitemid 29176941)
    • (1999) Current Opinion in Microbiology , vol.2 , Issue.2 , pp. 170-174
    • Foster, J.W.1
  • 59
    • 9444285788 scopus 로고    scopus 로고
    • Escherichia coli acid resistance: Tales of an amateur acidophile
    • DOI 10.1038/nrmicro1021
    • Foster, J. W. 2004. Escherichia coli acid resistance: Tales of an amateur acidophile. Nat. Rev. Microbiol. 2:898-907. (Pubitemid 39561806)
    • (2004) Nature Reviews Microbiology , vol.2 , Issue.11 , pp. 898-907
    • Foster, J.W.1
  • 61
    • 0030044799 scopus 로고    scopus 로고
    • A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32
    • Gamer, J., G. Multhaup, T. Tomoyasu, J. S. McCarty, S. Rudiger, H. J. Schonfeld, C. Schirra, H. Bujard, and B. Bukau. 1996. A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32. EMBO J. 15:607-617.
    • (1996) EMBO J. , vol.15 , pp. 607-617
    • Gamer, J.1    Multhaup, G.2    Tomoyasu, T.3    McCarty, J.S.4    Rudiger, S.5    Schonfeld, H.J.6    Schirra, C.7    Bujard, H.8    Bukau, B.9
  • 62
    • 0027333423 scopus 로고
    • Role of the major heat shock proteins as molecular chaperones
    • Georgopoulos, C., and W. J. Welch. 1993. Role of the major heat shock proteins as molecular chaperones. Annu. Rev. Cell Biol. 9: 601-634.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 601-634
    • Georgopoulos, C.1    Welch, W.J.2
  • 63
    • 0024025446 scopus 로고
    • Biochemical and genetic characterization of osmoregulatory trehalose synthesis in Escherichia coli
    • Giaever, H. M., O. B. Styrvold, I. Kaasen, and A. R. Strom. 1988. Biochemical and genetic characterization of osmoregulatory trehalose synthesis in Escherichia coli. J. Bacteriol. 170:2841-2849.
    • (1988) J. Bacteriol. , vol.170 , pp. 2841-2849
    • Giaever, H.M.1    Styrvold, O.B.2    Kaasen, I.3    Strom, A.R.4
  • 64
    • 0030936847 scopus 로고    scopus 로고
    • Protein quality control: Triage by chaperones and proteases
    • Gottesman, S., S. Wickner, and M. R. Maurizi. 1997. Protein quality control: Triage by chaperones and proteases. Genes Dev. 11:815-823. (Pubitemid 27175289)
    • (1997) Genes and Development , vol.11 , Issue.7 , pp. 815-823
    • Gottesman, S.1    Wickner, S.2    Maurizi, M.R.3
  • 65
    • 18144426344 scopus 로고    scopus 로고
    • The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation
    • DOI 10.1074/jbc.M414124200
    • Gribun, A., M. S. Kimber, R. Ching, R. Sprangers, K. M. Fiebig, and W. A. Houry. 2005. The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation. J. Biol. Chem. 280:16185-16196. (Pubitemid 40616745)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.16 , pp. 16185-16196
    • Gribun, A.1    Kimber, M.S.2    Ching, R.3    Sprangers, R.4    Fiebig, K.M.5    Houry, W.A.6
  • 67
    • 0035794207 scopus 로고    scopus 로고
    • Reversible thermal transition in GrpE, the nucleotide exchange factor of the DnaK heat-shock system
    • Grimshaw, J. P., I. Jelesarov, H. J. Schonfeld, and P. Christen. 2001. Reversible thermal transition in GrpE, the nucleotide exchange factor of the DnaK heat-shock system. J. Biol. Chem. 276:6098-6104.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6098-6104
    • Grimshaw, J.P.1    Jelesarov, I.2    Schonfeld, H.J.3    Christen, P.4
  • 68
    • 0021225289 scopus 로고
    • The htpR gene product of E. coli is a sigma factor for heat-shock promoters
    • Grossman, A. D., J. W. Erickson, and C. A. Gross. 1984. The htpR gene product of E. coli is a sigma factor for heat-shock promoters. Cell 38:383-390. (Pubitemid 14022033)
    • (1984) Cell , vol.38 , Issue.2 , pp. 383-390
    • Grossman, A.D.1    Erickson, J.W.2    Gross, C.A.3
  • 69
    • 33745752814 scopus 로고    scopus 로고
    • Escherichia coli acid resistance: pH-sensing, activation by chloride and autoinhibition in GadB
    • DOI 10.1038/sj.emboj.7601107, PII 7601107
    • Gut, H., E. Pennacchietti, R. A. John, F. Bossa, G. Capitani, D. De Biase, and M. G. Grutter. 2006. Escherichia coli acid resistance: PH-sensing, activation by chloride and autoinhibition in GadB. EMBO J. 25:2643-2651. (Pubitemid 44012246)
    • (2006) EMBO Journal , vol.25 , Issue.11 , pp. 2643-2651
    • Gut, H.1    Pennacchietti, E.2    John, R.A.3    Bossa, F.4    Capitani, G.5    De Biase, D.6    Grutter, M.G.7
  • 70
    • 0025988008 scopus 로고
    • Genetic regulation of cardiolipin synthase in Escherichia coli
    • Heber, S., and B. E. Tropp. 1991. Genetic regulation of cardiolipin synthase in Escherichia coli. Biochim. Biophys. Acta 1129:1-12.
    • (1991) Biochim. Biophys. Acta , vol.1129 , pp. 1-12
    • Heber, S.1    Tropp, B.E.2
  • 71
    • 77149153391 scopus 로고    scopus 로고
    • The complexity of the 'simple' two-component system KdpD/KdpE in Escherichia coli
    • Heermann, R., and K. Jung. 2010. The complexity of the 'simple' two-component system KdpD/KdpE in Escherichia coli. FEMS Microbiol. Lett. 304:97-106.
    • (2010) FEMS Microbiol. Lett. , vol.304 , pp. 97-106
    • Heermann, R.1    Jung, K.2
  • 72
    • 71749093772 scopus 로고    scopus 로고
    • Proteolysis of sigmaS (RpoS) and the general stress response in Escherichia coli
    • Hengge, R. 2009. Proteolysis of sigmaS (RpoS) and the general stress response in Escherichia coli. Res. Microbiol. 160:667-676.
    • (2009) Res. Microbiol. , vol.160 , pp. 667-676
    • Hengge, R.1
  • 73
    • 0036198628 scopus 로고    scopus 로고
    • Recent insights into the general stress response regulatory network in Escherichia coli
    • Hengge-Aronis, R. 2002. Recent insights into the general stress response regulatory network in Escherichia coli. J. Mol. Microbiol. Biotechnol. 4:341-346. (Pubitemid 34256711)
    • (2002) Journal of Molecular Microbiology and Biotechnology , vol.4 , Issue.3 , pp. 341-346
    • Hengge-Aronis, R.1
  • 74
    • 0026330981 scopus 로고
    • Trehalose synthesis genes are controlled by the putative sigma factor encoded by rpoS and are involved in stationary-phase thermotolerance in Escherichia coli
    • Hengge-Aronis, R., W. Klein, R. Lange, M. Rimmele, and W. Boos. 1991. Trehalose synthesis genes are controlled by the putative sigma factor encoded by rpoS and are involved in stationary-phase thermotolerance in Escherichia coli. J. Bacteriol. 173:7918-7924.
    • (1991) J. Bacteriol. , vol.173 , pp. 7918-7924
    • Hengge-Aronis, R.1    Klein, W.2    Lange, R.3    Rimmele, M.4    Boos, W.5
  • 75
    • 0344211512 scopus 로고    scopus 로고
    • Lack of a robust unfoldase activity confers a unique level of substrate specificity to the universal AAA protease FtsH
    • DOI 10.1016/S1097-2765(03)00068-6
    • Herman, C., S. Prakash, C. Z. Lu, A. Matouschek, and C. A. Gross. 2003. Lack of a robust unfoldase activity confers a unique level of substrate specificity to the universal AAA protease FtsH. Mol. Cell 11:659-669. (Pubitemid 36385121)
    • (2003) Molecular Cell , vol.11 , Issue.3 , pp. 659-669
    • Herman, C.1    Prakash, S.2    Lu, C.Z.3    Matouschek, A.4    Gross, C.A.5
  • 76
    • 0027133440 scopus 로고
    • Active increase in cardiolipin synthesis in the stationary growth phase and its physiological significance in Escherichia coli
    • Hiraoka, S., H. Matsuzaki, and I. Shibuya. 1993. Active increase in cardiolipin synthesis in the stationary growth phase and its physiological significance in Escherichia coli. FEBS Lett. 336: 221-224.
    • (1993) FEBS Lett. , vol.336 , pp. 221-224
    • Hiraoka, S.1    Matsuzaki, H.2    Shibuya, I.3
  • 77
    • 16544391413 scopus 로고    scopus 로고
    • Weak organic acids: A panoply of effects on bacteria
    • Hirshfield, I. N., S. Terzulli, and C. O'Byrne. 2003. Weak organic acids: A panoply of effects on bacteria. Sci. Prog. 86:245-269.
    • (2003) Sci. Prog. , vol.86 , pp. 245-269
    • Hirshfield, I.N.1    Terzulli, S.2    O'Byrne, C.3
  • 78
    • 34547394297 scopus 로고    scopus 로고
    • New targets for the cyclic AMP receptor protein in the Escherichia coli K-12 genome
    • DOI 10.1111/j.1574-6968.2007.00826.x
    • Hollands, K., S. J. Busby, and G. S. Lloyd. 2007. New targets for the cyclic AMP receptor protein in the Escherichia coli K-12 genome. FEMS Microbiol. Lett. 274:89-94. (Pubitemid 47174318)
    • (2007) FEMS Microbiology Letters , vol.274 , Issue.1 , pp. 89-94
    • Hollands, K.1    Busby, S.J.W.2    Lloyd, G.S.3
  • 80
    • 33646907087 scopus 로고    scopus 로고
    • GroELGroES-mediated protein folding
    • Horwich, A. L., G. W. Farr, and W. A. Fenton. 2006. GroELGroES-mediated protein folding. Chem. Rev. 106:1917-1930.
    • (2006) Chem. Rev. , vol.106 , pp. 1917-1930
    • Horwich, A.L.1    Farr, G.W.2    Fenton, W.A.3
  • 81
    • 0001175140 scopus 로고    scopus 로고
    • Morphological and physiological changes during stationary phase
    • In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), 2nd ed. ASM Press, Washington, DC
    • Huisman, G., D. Siegele, M. Zambrano, and R. Kolter. 1996. Morphological and physiological changes during stationary phase, p. 1672-1682. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: Cellular and molecular biology, 2nd ed. ASM Press, Washington, DC.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology , pp. 1672-1682
    • Huisman, G.1    Siegele, D.2    Zambrano, M.3    Kolter, R.4
  • 82
    • 0030067634 scopus 로고    scopus 로고
    • The crystal structure of the GroES cochaperonin at 2.8 Å resolution
    • Hunt, J. F., A. J. Weaver, S. J. Landry, L. Gierasch, and J. Deisenhofer. 1996. The crystal structure of the GroES cochaperonin at 2.8 Å resolution. Nature 379:37-45.
    • (1996) Nature , vol.379 , pp. 37-45
    • Hunt, J.F.1    Weaver, A.J.2    Landry, S.J.3    Gierasch, L.4    Deisenhofer, J.5
  • 83
    • 25844525796 scopus 로고    scopus 로고
    • Cellular functions, mechanism of action, and regulation of FtsH protease
    • DOI 10.1146/annurev.micro.59.030804.121316
    • Ito, K., and Y. Akiyama. 2005. Cellular functions, mechanism of action, and regulation of FtsH protease. Annu. Rev. Microbiol. 59: 211-231. (Pubitemid 41507430)
    • (2005) Annual Review of Microbiology , vol.59 , pp. 211-231
    • Ito, K.1    Akiyama, Y.2
  • 85
    • 0242659209 scopus 로고    scopus 로고
    • Arginine-Agmatine Antiporter in Extreme Acid Resistance in Escherichia coli
    • DOI 10.1128/JB.185.22.6556-6561.2003
    • Iyer, R., C. Williams, and C. Miller. 2003. Arginine-agmatine antiporter in extreme acid resistance in Escherichia coli. J. Bacteriol. 185:6556-6561. (Pubitemid 37385874)
    • (2003) Journal of Bacteriology , vol.185 , Issue.22 , pp. 6556-6561
    • Iyer, R.1    Williams, C.2    Miller, C.3
  • 86
    • 0021716448 scopus 로고
    • Biosynthesis of membrane-derived oligosaccharides: Characterization of mdoB mutants defective in phosphoglycerol transferase I activity
    • Jackson, B. J., J. P. Bohin, and E. P. Kennedy. 1984. Biosynthesis of membrane-derived oligosaccharides: Characterization of mdoB mutants defective in phosphoglycerol transferase I activity. J. Bacteriol. 160:976-981. (Pubitemid 15219466)
    • (1984) Journal of Bacteriology , vol.160 , Issue.3 , pp. 976-981
    • Jackson, B.J.1    Bohin, J.-P.2    Kennedy, E.P.3
  • 87
    • 33644850534 scopus 로고    scopus 로고
    • Crystal structure of AqpZ tetramer reveals two distinct Arg-189 conformations associated with water permeation through the narrowest constriction of the water-conducting channel
    • DOI 10.1074/jbc.M508926200
    • Jiang, J., B. V. Daniels, and D. Fu. 2006. Crystal structure of AqpZ tetramer reveals two distinct Arg-189 conformations associated with water permeation through the narrowest constriction of the waterconducting channel. J. Biol. Chem. 281:454-460. (Pubitemid 43671207)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.1 , pp. 454-460
    • Jiang, J.1    Daniels, B.V.2    Fu, D.3
  • 88
    • 33845388167 scopus 로고    scopus 로고
    • The emerging clinical importance of non-O157 shiga toxin-producing Escherichia coli
    • DOI 10.1086/509573
    • Johnson, K. E., C. M. Thorpe, and C. L. Sears. 2006. The emerging clinical importance of non-O157 Shiga toxin-producing Escherichia coli. Clin. Infect. Dis. 43:1587-1595. (Pubitemid 44901903)
    • (2006) Clinical Infectious Diseases , vol.43 , Issue.12 , pp. 1587-1595
    • Johnson, K.E.1    Thorpe, C.M.2    Sears, C.L.3
  • 89
    • 0034989956 scopus 로고    scopus 로고
    • + concentration
    • DOI 10.1128/JB.183.12.3800-3803.2001
    • Jung, K., M. Krabusch, and K. Altendorf. 2001. Cs(z) induces the kdp operon of Escherichia coli by lowering the intracellular K(z) concentration. J. Bacteriol. 183:3800-3803. (Pubitemid 32510449)
    • (2001) Journal of Bacteriology , vol.183 , Issue.12 , pp. 3800-3803
    • Jung, K.1    Krabusch, M.2    Altendorf, K.3
  • 90
    • 0026541540 scopus 로고
    • Molecular cloning and physical mapping of the otsBA genes, which encode the osmoregulatory trehalose pathway of Escherichia coli: Evidence that transcription is activated by KatF (AppR)
    • Kaasen, I., P. Falkenberg, O. B. Styrvold, and A. R. Strom. 1992. Molecular cloning and physical mapping of the otsBA genes, which encode the osmoregulatory trehalose pathway of Escherichia coli: Evidence that transcription is activated by KatF (AppR). J. Bacteriol. 174:889-898.
    • (1992) J. Bacteriol , vol.174 , pp. 889-898
    • Kaasen, I.1    Falkenberg, P.2    Styrvold, O.B.3    Strom, A.R.4
  • 91
    • 0028360269 scopus 로고
    • Analysis of the otsBA operon for osmoregulatory trehalose synthesis in Escherichia coli and homology of the OtsA and OtsB proteins to the yeast trehalose-6-phosphate synthase/phosphatase complex
    • DOI 10.1016/0378-1119(94)90316-6
    • Kaasen, I., J. McDougall, and A. R. Strom. 1994. Analysis of the otsBA operon for osmoregulatory trehalose synthesis in Escherichia coli and homology of the OtsA and OtsB proteins to the yeast trehalose-6-phosphate synthase/phosphatase complex. Gene 145: 9-15. (Pubitemid 24224957)
    • (1994) Gene , vol.145 , Issue.1 , pp. 9-15
    • Kaasen, I.1    McDougall, J.2    Strom, A.R.3
  • 92
    • 63049110420 scopus 로고    scopus 로고
    • Characterization of the Escherichia coli O157:H7 Sakai GadE regulon
    • Kailasan Vanaja, S., T. M. Bergholz, and T. S. Whittam. 2009. Characterization of the Escherichia coli O157:H7 Sakai GadE regulon. J. Bacteriol. 191:1868-1877.
    • (2009) J. Bacteriol. , vol.191 , pp. 1868-1877
    • Kailasan Vanaja, S.1    Bergholz, T.M.2    Whittam, T.S.3
  • 93
    • 0026583203 scopus 로고
    • Excretion of putrescine by the putrescine-ornithine antiporter encoded by the potE gene of Escherichia coli
    • Kashiwagi, K., S. Miyamoto, F. Suzuki, H. Kobayashi, and K. Igarashi. 1992. Excretion of putrescine by the putrescine-ornithine antiporter encoded by the potE gene of Escherichia coli. Proc. Natl. Acad. Sci. USA 89:4529-4533.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4529-4533
    • Kashiwagi, K.1    Miyamoto, S.2    Suzuki, F.3    Kobayashi, H.4    Igarashi, K.5
  • 94
    • 0025720216 scopus 로고
    • Coexistence of the genes for putrescine transport protein and ornithine decarboxylase at 16 min on Escherichia coli chromosome
    • Kashiwagi, K., T. Suzuki, F. Suzuki, T. Furuchi, H. Kobayashi, and K. Igarashi. 1991. Coexistence of the genes for putrescine transport protein and ornithine decarboxylase at 16 min on Escherichia coli chromosome. J. Biol. Chem. 266:20922-20927. (Pubitemid 21908552)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.31 , pp. 20922-20927
    • Kashiwagi, K.1    Suzuki, T.2    Suzuki, F.3    Furuchi, T.4    Kobayashi, H.5    Igarashi, K.6
  • 96
    • 77954636793 scopus 로고    scopus 로고
    • Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations
    • Kimber, M. S., A. Y. Yu, M. Borg, E. Leung, H. S. Chan, and W. A. Houry. 2010. Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations. Structure 18:798-808.
    • (2010) Structure , vol.18 , pp. 798-808
    • Kimber, M.S.1    Yu, A.Y.2    Borg, M.3    Leung, E.4    Chan, H.S.5    Houry, W.A.6
  • 97
    • 4344633752 scopus 로고    scopus 로고
    • A regulatory trade-off as a source of strain variation in the species Escherichia coli
    • DOI 10.1128/JB.186.17.5614-5620.2004
    • King, T., A. Ishihama, A. Kori, and T. Ferenci. 2004. A regulatory trade-off as a source of strain variation in the species Escherichia coli. J. Bacteriol. 186:5614-5620. (Pubitemid 39128633)
    • (2004) Journal of Bacteriology , vol.186 , Issue.17 , pp. 5614-5620
    • King, T.1    Ishihama, A.2    Kori, A.3    Ferenci, T.4
  • 98
    • 0039016611 scopus 로고
    • Fate of nonpathogenic and enteropathogenic Escherichia coli during the manufacture of Colbylike cheese
    • Kornacki, J., and E. Marth. 1982. Fate of nonpathogenic and enteropathogenic Escherichia coli during the manufacture of Colbylike cheese. J. Food Prot. 45:310-316.
    • (1982) J. Food Prot. , vol.45 , pp. 310-316
    • Kornacki, J.1    Marth, E.2
  • 99
    • 77955112220 scopus 로고    scopus 로고
    • Bacterial stimulus perception and signal transduction: Response to osmotic stress
    • Kramer, R. 2010. Bacterial stimulus perception and signal transduction: Response to osmotic stress. Chem. Rec. 10:217-229.
    • (2010) Chem. Rec. , vol.10 , pp. 217-229
    • Kramer, R.1
  • 100
    • 0033057057 scopus 로고    scopus 로고
    • Protein ProQ influences osmotic activation of compatible solute transporter ProP in Escherichia coli K-12
    • Kunte, H. J., R. A. Crane, D. E. Culham, D. Richmond, and J. M. Wood. 1999. Protein ProQ influences osmotic activation of compatible solute transporter ProP in Escherichia coli K-12. J. Bacteriol. 181:1537-1543. (Pubitemid 29110814)
    • (1999) Journal of Bacteriology , vol.181 , Issue.5 , pp. 1537-1543
    • Kunte, H.J.1    Crane, R.A.2    Culham, D.E.3    Richmond, D.4    Wood, J.M.5
  • 101
    • 0033053006 scopus 로고    scopus 로고
    • The mdoC gene of Escherichia coli encodes a membrane protein that is required for succinylation of osmoregulated periplasmic glucans
    • Lacroix, J. M., E. Lanfroy, V. Cogez, Y. Lequette, A. Bohin, and J. P. Bohin. 1999. The mdoC gene of Escherichia coli encodes a membrane protein that is required for succinylation of osmoregulated periplasmic glucans. J. Bacteriol. 181:3626-3631. (Pubitemid 29283787)
    • (1999) Journal of Bacteriology , vol.181 , Issue.12 , pp. 3626-3631
    • Lacroix, J.-M.1    Lanfroy, E.2    Cogez, V.3    Lequette, Y.4    Bohin, A.5    Bohin, J.-P.6
  • 102
    • 0025769947 scopus 로고
    • The mdoA locus of Escherichia coli consists of an operon under osmotic control
    • Lacroix, J. M., I. Loubens, M. Tempete, B. Menichi, and J. P. Bohin. 1991. The mdoA locus of Escherichia coli consists of an operon under osmotic control. Mol. Microbiol. 5:1745-1753. (Pubitemid 21896206)
    • (1991) Molecular Microbiology , vol.5 , Issue.7 , pp. 1745-1753
    • Lacroix, J.-M.1    Loubens, I.2    Tempete, M.3    Menichi, B.4    Bohin, J.-P.5
  • 104
    • 0029965414 scopus 로고    scopus 로고
    • The complex bet promoters of Escherichia coli: Regulation by oxygen (ArcA), choline (BetI), and osmotic stress
    • Lamark, T., T. P. Rokenes, J. McDougall, and A. R. Strom. 1996. The complex bet promoters of Escherichia coli: Regulation by oxygen (ArcA), choline (BetI), and osmotic stress. J. Bacteriol. 178: 1655-1662. (Pubitemid 26085614)
    • (1996) Journal of Bacteriology , vol.178 , Issue.6 , pp. 1655-1662
    • Lamark, T.1    Rokenes, T.P.2    McDougall, J.3    Strom, A.R.4
  • 105
    • 0022503080 scopus 로고
    • Choline-glycine betaine pathway confers a high level of osmotic tolerance in Escherichia coli
    • Landfald, B., and A. R. Strom. 1986. Choline-glycine betaine pathway confers a high level of osmotic tolerance in Escherichia coli. J. Bacteriol. 165:849-855. (Pubitemid 16071415)
    • (1986) Journal of Bacteriology , vol.165 , Issue.3 , pp. 849-855
    • Landfald, B.1    Strom, A.R.2
  • 106
    • 0029082430 scopus 로고
    • Identification of transcriptional start sites and the role of ppGpp in the expression of rpoS, the structural gene for the sigma S subunit of RNA polymerase in Escherichia coli
    • Lange, R., D. Fischer, and R. Hengge-Aronis. 1995. Identification of transcriptional start sites and the role of ppGpp in the expression of rpoS, the structural gene for the sigma S subunit of RNA polymerase in Escherichia coli. J. Bacteriol. 177:4676-4680.
    • (1995) J. Bacteriol. , vol.177 , pp. 4676-4680
    • Lange, R.1    Fischer, D.2    Hengge-Aronis, R.3
  • 107
    • 0025769570 scopus 로고
    • Growth phase-regulated expression of bolA and morphology of stationary-phase Escherichia coli cells are controlled by the novel sigma factor sigma S
    • Lange, R., and R. Hengge-Aronis. 1991. Growth phase-regulated expression of bolA and morphology of stationary-phase Escherichia coli cells are controlled by the novel sigma factor sigma S. J. Bacteriol. 173:4474-4481.
    • (1991) J. Bacteriol. , vol.173 , pp. 4474-4481
    • Lange, R.1    Hengge-Aronis, R.2
  • 108
    • 0028176450 scopus 로고
    • The cellular concentration of the sigma S subunit of RNA polymerase in Escherichia coli is controlled at the levels of transcription, translation, and protein stability
    • Lange, R., and R. Hengge-Aronis. 1994. The cellular concentration of the sigma S subunit of RNA polymerase in Escherichia coli is controlled at the levels of transcription, translation, and protein stability. Genes Dev. 8:1600-1612.
    • (1994) Genes Dev. , vol.8 , pp. 1600-1612
    • Lange, R.1    Hengge-Aronis, R.2
  • 109
    • 0027092285 scopus 로고
    • Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity
    • Langer, T., G. Pfeifer, J. Martin, W. Baumeister, and F. U. Hartl. 1992. Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity. EMBO J. 11:4757-4765. (Pubitemid 23023418)
    • (1992) EMBO Journal , vol.11 , Issue.13 , pp. 4757-4765
    • Langer, T.1    Pfeifer, G.2    Martin, J.3    Baumeister, W.4    Hartl, F.-U.5
  • 110
    • 18444375008 scopus 로고    scopus 로고
    • Variation in acid resistance among shiga toxin-producing clones of pathogenic Escherichia coli
    • DOI 10.1128/AEM.71.5.2493-2500.2005
    • Large, T. M., S. T. Walk, and T. S. Whittam. 2005. Variation in acid resistance among Shiga toxin-producing clones of pathogenic Escherichia coli. Appl. Environ. Microbiol. 71:2493-2500. (Pubitemid 40646994)
    • (2005) Applied and Environmental Microbiology , vol.71 , Issue.5 , pp. 2493-2500
    • Large, T.M.1    Walk, S.T.2    Whittam, T.S.3
  • 112
    • 7044241302 scopus 로고    scopus 로고
    • How lipids affect the activities of integral membrane proteins
    • DOI 10.1016/j.bbamem.2004.05.012, PII S0005273604001592, Lipid-Protein Interactions
    • Lee, A. G. 2004. How lipids affect the activities of integral membrane proteins. Biochim. Biophys. Acta 1666:62-87. (Pubitemid 39425199)
    • (2004) Biochimica et Biophysica Acta - Biomembranes , vol.1666 , Issue.1-2 , pp. 62-87
    • Lee, A.G.1
  • 113
    • 77953694169 scopus 로고    scopus 로고
    • Control of substrate gating and translocation into ClpP by channel residues and ClpX binding
    • Lee, M. E., T. A. Baker, and R. T. Sauer. 2010. Control of substrate gating and translocation into ClpP by channel residues and ClpX binding. J. Mol. Biol. 399:707-718.
    • (2010) J. Mol. Biol. , vol.399 , pp. 707-718
    • Lee, M.E.1    Baker, T.A.2    Sauer, R.T.3
  • 114
    • 0034630095 scopus 로고    scopus 로고
    • Basic aspects of food preservation by hurdle technology
    • DOI 10.1016/S0168-1605(00)00161-6, PII S0168160500001616
    • Leistner, L. 2000. Basic aspects of food preservation by hurdle technology. Int. J. Food Microbiol. 55:181-186. (Pubitemid 30160828)
    • (2000) International Journal of Food Microbiology , vol.55 , Issue.1-3 , pp. 181-186
    • Leistner, L.1
  • 115
    • 0345196593 scopus 로고    scopus 로고
    • Protection of Escherichia coli cells against extreme turgor by activation of MscS and MscL mechanosensitive channels: Identification of genes required for MscS activity
    • Levina, N., S. Totemeyer, N. R. Stokes, P. Louis, M. A. Jones, and I. R. Booth. 1999. Protection of Escherichia coli cells against extreme turgor by activation of MscS and MscL mechanosensitive channels: Identification of genes required for MscS activity. EMBO J. 18:1730-1737. (Pubitemid 29158517)
    • (1999) EMBO Journal , vol.18 , Issue.7 , pp. 1730-1737
    • Levina, N.1    Totemeyer, S.2    Stokes, N.R.3    Louis, P.4    Jones, M.A.5    Booth, I.R.6
  • 116
    • 0028857775 scopus 로고
    • Acid adaptation of Escherichia coli O157:H7 increases survival in acidic foods
    • Leyer, G. J., L. L. Wang, and E. A. Johnson. 1995. Acid adaptation of Escherichia coli O157:H7 increases survival in acidic foods. Appl. Environ. Microbiol. 61:3752-3755.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 3752-3755
    • Leyer, G.J.1    Wang, L.L.2    Johnson, E.A.3
  • 118
    • 0028289538 scopus 로고
    • Adaptation of Escherichia coli to high osmolarity environments: Osmoregulation of the high-affinity glycine betaine transport system ProU
    • DOI 10.1016/0168-6445(94)90008-6
    • Lucht, J. M., and E. Bremer. 1994. Adaptation of Escherichia coli to high osmolarity environments: Osmoregulation of the high-affinity glycine betaine transport system proU. FEMS Microbiol. Rev. 14: 3-20. (Pubitemid 24188935)
    • (1994) FEMS Microbiology Reviews , vol.14 , Issue.1 , pp. 3-20
    • Lucht, J.M.1    Bremer, E.2
  • 119
    • 0034982311 scopus 로고    scopus 로고
    • Microbial molecular chaperones
    • DOI 10.1016/S0065-2911(01)44012-4
    • Lund, P. A. 2001. Microbial molecular chaperones. Adv. Microb. Physiol. 44:93-140. (Pubitemid 32500111)
    • (2001) Advances in Microbial Physiology , vol.44 , pp. 93-140
    • Lund, P.A.1
  • 120
    • 0346024121 scopus 로고    scopus 로고
    • Osmoregulatory Systems of Escherichia coli: Identification of Betaine-Carnitine-Choline Transporter Family Member BetU and Distributions of betU and trkG among Pathogenic and Nonpathogenic Isolates
    • DOI 10.1128/JB.186.2.296-306.2004
    • Ly, A., J. Henderson, A. Lu, D. E. Culham, and J. M. Wood. 2004. Osmoregulatory systems of Escherichia coli: Identification of betaine-carnitine-choline transporter family member BetU and distributions of betU and trkG among pathogenic and nonpathogenic isolates. J. Bacteriol. 186:296-306. (Pubitemid 38076418)
    • (2004) Journal of Bacteriology , vol.186 , Issue.2 , pp. 296-306
    • Ly, A.1    Henderson, J.2    Lu, A.3    Culham, D.E.4    Wood, J.M.5
  • 121
    • 0141566454 scopus 로고    scopus 로고
    • GadE (YhiE) activates glutamate decarboxylase-dependent acid resistance in Escherichia coli K-12
    • DOI 10.1046/j.1365-2958.2003.03633.x
    • Ma, Z., S. Gong, H. Richard, D. L. Tucker, T. Conway, and J. W. Foster. 2003. GadE (YhiE) activates glutamate decarboxylasedependent acid resistance in Escherichia coli K-12. Mol. Microbiol. 49:1309-1320. (Pubitemid 37153499)
    • (2003) Molecular Microbiology , vol.49 , Issue.5 , pp. 1309-1320
    • Ma, Z.1    Gong, S.2    Richard, H.3    Tucker, D.L.4    Conway, T.5    Foster, J.W.6
  • 123
    • 18044367581 scopus 로고    scopus 로고
    • PpGpp: A global regulator in Escherichia coli
    • DOI 10.1016/j.tim.2005.03.008
    • Magnusson, L. U., A. Farewell, and T. Nystrom. 2005. ppGpp: A global regulator in Escherichia coli. Trends Microbiol. 13:236-242. (Pubitemid 40603907)
    • (2005) Trends in Microbiology , vol.13 , Issue.5 , pp. 236-242
    • Magnusson, L.U.1    Farewell, A.2    Nystrom, T.3
  • 124
    • 0035135363 scopus 로고    scopus 로고
    • Growth and survival of E. coli O157:H7 during the manufacture and ripening of a smear-ripened cheese produced from raw milk
    • DOI 10.1046/j.1365-2672.2001.01232.x
    • Maher, M. M., K. N. Jordan, M. E. Upton, and A. Coffey. 2001. Growth and survival of E. coli O157:H7 during the manufacture and ripening of a smear-ripened cheese produced from raw milk. J. Appl. Microbiol. 90:201-207. (Pubitemid 32158739)
    • (2001) Journal of Applied Microbiology , vol.90 , Issue.2 , pp. 201-207
    • Maher, M.M.1    Jordan, K.N.2    Upton, M.E.3    Coffey, A.4
  • 126
    • 0028142574 scopus 로고
    • Evidence for involvement of proteins HU and RpoS in transcription of the osmoresponsive proU operon in Escherichia coli
    • Manna, D., and J. Gowrishankar. 1994. Evidence for involvement of proteins HU and RpoS in transcription of the osmoresponsive proU operon in Escherichia coli. J. Bacteriol. 176:5378-5384. (Pubitemid 24273526)
    • (1994) Journal of Bacteriology , vol.176 , Issue.17 , pp. 5378-5384
    • Manna, D.1    Gowrishankar, J.2
  • 127
    • 0026601663 scopus 로고
    • Proteases and protein degradation in Escherichia coli
    • Maurizi, M. R. 1992. Proteases and protein degradation in Escherichia coli. Experientia 48:178-201.
    • (1992) Experientia , vol.48 , pp. 178-201
    • Maurizi, M.R.1
  • 128
    • 0033936317 scopus 로고    scopus 로고
    • Multistep mechanism of substrate binding determines chaperone activity of Hsp70
    • DOI 10.1038/76819
    • Mayer, M. P., H. Schroder, S. Rudiger, K. Paal, T. Laufen, and B. Bukau. 2000. Multistep mechanism of substrate binding determines chaperone activity of Hsp70. Nat. Struct. Biol. 7:586-593. (Pubitemid 30445917)
    • (2000) Nature Structural Biology , vol.7 , Issue.7 , pp. 586-593
    • Mayer, M.P.1    Schroder, H.2    Rudiger, S.3    Paal, K.4    Laufen, T.5    Bukau, B.6
  • 129
    • 0028869981 scopus 로고
    • Two different Escherichia coli proP promoters respond to osmotic and growth phase signals
    • Mellies, J., A. Wise, and M. Villarejo. 1995. Two different Escherichia coli proP promoters respond to osmotic and growth phase signals. J. Bacteriol. 177:144-151.
    • (1995) J. Bacteriol. , vol.177 , pp. 144-151
    • Mellies, J.1    Wise, A.2    Villarejo, M.3
  • 130
    • 27744589294 scopus 로고    scopus 로고
    • S (RpoS) in E. coli
    • DOI 10.1101/gad.353705
    • Mika, F., and R. Hengge. 2005. A two-component phosphotransfer network involving ArcB, ArcA, and RssB coordinates synthesis and proteolysis of sigmaS (RpoS) in E. coli. Genes Dev. 19:2770-2781. (Pubitemid 41627942)
    • (2005) Genes and Development , vol.19 , Issue.22 , pp. 2770-2781
    • Mika, F.1    Hengge, R.2
  • 131
    • 0033956407 scopus 로고    scopus 로고
    • Visualization of phospholipid domains in Escherichia coli by using the cardiolipin-specific fluorescent dye 10-N-nonyl acridine orange
    • DOI 10.1128/JB.182.4.1172-1175.2000
    • Mileykovskaya, E., and W. Dowhan. 2000. Visualization of phospholipid domains in Escherichia coli by using the cardiolipinspecific fluorescent dye 10-N-nonyl acridine orange. J. Bacteriol. 182:1172-1175. (Pubitemid 30075045)
    • (2000) Journal of Bacteriology , vol.182 , Issue.4 , pp. 1172-1175
    • Mileykovskaya, E.1    Dowhan, W.2
  • 132
    • 59349116314 scopus 로고    scopus 로고
    • Fate of acid-resistant and non-acid resistant Shiga toxin-producing Escherichia coli strains in experimentally contaminated French fermented raw meat sausages
    • Montet, M. P., S. Christieans, D. Thevenot, V. Coppet, S. Ganet, M. L. Muller, L. Duniere, S. Miszczycha, and C. Vernozy-Rozand. 2009. Fate of acid-resistant and non-acid resistant Shiga toxin-producing Escherichia coli strains in experimentally contaminated French fermented raw meat sausages. Int. J. Food Microbiol. 129: 264-270.
    • (2009) Int. J. Food Microbiol. , vol.129 , pp. 264-270
    • Montet, M.P.1    Christieans, S.2    Thevenot, D.3    Coppet, V.4    Ganet, S.5    Muller, M.L.6    Duniere, L.7    Miszczycha, S.8    Vernozy-Rozand, C.9
  • 133
    • 75749102599 scopus 로고    scopus 로고
    • Growth and survival of acid-resistant and non-acid-resistant Shiga-toxin-producing Escherichia coli strains during the manufacture and ripening of Camembert cheese
    • doi:10.1155/2009/653481
    • Montet, M. P., E. Jamet, S. Ganet, M. Dizin, S. Miszczycha, L. Duniere, D. Thevenot, and C. Vernozy-Rozand. 2009. Growth and survival of acid-resistant and non-acid-resistant Shiga-toxin-producing Escherichia coli strains during the manufacture and ripening of Camembert cheese. Int. J. Microbiol. doi:10.1155/2009/ 653481.
    • (2009) Int. J. Microbiol.
    • Montet, M.P.1    Jamet, E.2    Ganet, S.3    Dizin, M.4    Miszczycha, S.5    Duniere, L.6    Thevenot, D.7    Vernozy-Rozand, C.8
  • 134
    • 33847296090 scopus 로고    scopus 로고
    • Phage types, virulence genes and PFGE profiles of Shiga toxin-producing Escherichia coli O157:H7 isolated from raw beef, soft cheese and vegetables in Lima (Peru)
    • DOI 10.1016/j.ijfoodmicro.2006.09.009, PII S0168160506005198
    • Mora, A., S. L. Leon, M. Blanco, J. E. Blanco, C. Lopez, G. Dahbi, A. Echeita, E. A. Gonzalez, and J. Blanco. 2007. Phage types, virulence genes and PFGE profiles of Shiga toxin-producing Escherichia coli O157:H7 isolated from raw beef, soft cheese and vegetables in Lima (Peru). Int. J. Food Microbiol. 114:204-210. (Pubitemid 46329173)
    • (2007) International Journal of Food Microbiology , vol.114 , Issue.2 , pp. 204-210
    • Mora, A.1    Leon, S.L.2    Blanco, M.3    Blanco, J.E.4    Lopez, C.5    Dahbi, G.6    Echeita, A.7    Gonzalez, E.A.8    Blanco, J.9
  • 135
    • 0031015478 scopus 로고    scopus 로고
    • 32 in Escherichia coli
    • Muffler, A., M. Barth, C. Marschall, and R. Hengge-Aronis. 1997. Heat shock regulation of sigmaS turnover: A role for DnaK and relationship between stress responses mediated by sigmaS and sigma32 in Escherichia coli. J. Bacteriol. 179:445-452. (Pubitemid 27030398)
    • (1997) Journal of Bacteriology , vol.179 , Issue.2 , pp. 445-452
    • Muffler, A.1    Barth, M.2    Marschall, C.3    Hengge-Aronis, R.4
  • 136
    • 0029990928 scopus 로고    scopus 로고
    • The response regulator RssB controls stability of the sigma(S) subunit of RNA polymerase in Escherichia coli
    • Muffler, A., D. Fischer, S. Altuvia, G. Storz, and R. Hengge-Aronis. 1996. The response regulator RssB controls stability of the sigma(S) subunit of RNA polymerase in Escherichia coli. EMBO J. 15:1333-1339.
    • (1996) EMBO J. , vol.15 , pp. 1333-1339
    • Muffler, A.1    Fischer, D.2    Altuvia, S.3    Storz, G.4    Hengge-Aronis, R.5
  • 137
    • 0029897937 scopus 로고    scopus 로고
    • The RNA-binding protein HF-I, known as a host factor for phage Qβ RNA replication, is essential for rpoS translation in Escherichia coli
    • Muffler, A., D. Fischer, and R. Hengge-Aronis. 1996. The RNAbinding protein HF-I, known as a host factor for phage Qbeta RNA replication, is essential for rpoS translation in Escherichia coli. Genes Dev. 10:1143-1151. (Pubitemid 26152855)
    • (1996) Genes and Development , vol.10 , Issue.9 , pp. 1143-1151
    • Muffler, A.1    Fischer, D.2    Hengge-Aronis, R.3
  • 139
    • 3042662444 scopus 로고    scopus 로고
    • Dps protects cells against multiple stresses during stationary phase
    • DOI 10.1128/JB.186.13.4192-4198.2004
    • Nair, S., and S. E. Finkel. 2004. Dps protects cells against multiple stresses during stationary phase. J. Bacteriol. 186:4192-4198. (Pubitemid 38802567)
    • (2004) Journal of Bacteriology , vol.186 , Issue.13 , pp. 4192-4198
    • Nair, S.1    Finkel, S.E.2
  • 141
    • 0029812095 scopus 로고    scopus 로고
    • Kinetics of expression of the Escherichia coli cad operon as a function of pH and lysine
    • Neely, M. N., and E. R. Olson. 1996. Kinetics of expression of the Escherichia coli cad operon as a function of pH and lysine. J. Bacteriol. 178:5522-5528. (Pubitemid 26304389)
    • (1996) Journal of Bacteriology , vol.178 , Issue.18 , pp. 5522-5528
    • Neely, M.N.1    Olson, E.R.2
  • 142
    • 9244230099 scopus 로고    scopus 로고
    • Stationary-phase physiology
    • DOI 10.1146/annurev.micro.58.030603.123818
    • Nystrom, T. 2004. Stationary-phase physiology. Annu. Rev. Microbiol. 58:161-181. (Pubitemid 39551983)
    • (2004) Annual Review of Microbiology , vol.58 , pp. 161-181
    • Nystrom, T.1
  • 143
    • 77954311600 scopus 로고    scopus 로고
    • Relative gene transcription and pathogenicity of enterohemorrhagic Escherichia coli after long-term adaptation to acid and salt stress
    • Olesen, I., and L. Jespersen. 2010. Relative gene transcription and pathogenicity of enterohemorrhagic Escherichia coli after long-term adaptation to acid and salt stress. Int. J. Food Microbiol. 141:248-253.
    • (2010) Int. J. Food Microbiol. , vol.141 , pp. 248-253
    • Olesen, I.1    Jespersen, L.2
  • 145
    • 0031848112 scopus 로고    scopus 로고
    • Pathogenesis and diagnosis of Shiga toxin-producing Escherichia coli infections
    • Paton, J. C., and A. W. Paton. 1998. Pathogenesis and diagnosis of Shiga toxin-producing Escherichia coli infections. Clin. Microbiol. Rev. 11:450-479. (Pubitemid 28379095)
    • (1998) Clinical Microbiology Reviews , vol.11 , Issue.3 , pp. 450-479
    • Paton, J.C.1    Paton, A.W.2
  • 146
    • 0028832576 scopus 로고
    • Physiological state of Escherichia coli BJ4 growing in the large intestines of streptomycin-treated mice
    • Poulsen, L. K., T. R. Licht, C. Rang, K. A. Krogfelt, and S. Molin. 1995. Physiological state of Escherichia coli BJ4 growing in the large intestines of streptomycin-treated mice. J. Bacteriol. 177: 5840-5845.
    • (1995) J. Bacteriol. , vol.177 , pp. 5840-5845
    • Poulsen, L.K.1    Licht, T.R.2    Rang, C.3    Krogfelt, K.A.4    Molin, S.5
  • 147
    • 41849136544 scopus 로고    scopus 로고
    • Anionic phospholipids affect the rate and extent of flux through the mechanosensitive channel of large conductance MscL
    • DOI 10.1021/bi702409t
    • Powl, A. M., J. M. East, and A. G. Lee. 2008. Anionic phospholipids affect the rate and extent of flux through the mechanosensitive channel of large conductance MscL. Biochemistry 47:4317-4328. (Pubitemid 351499887)
    • (2008) Biochemistry , vol.47 , Issue.14 , pp. 4317-4328
    • Powl, A.M.1    East, J.M.2    Lee, A.G.3
  • 148
    • 0034006405 scopus 로고    scopus 로고
    • Prevalence and characterization of Shiga toxin-producing Escherichia coli isolated from cattle, food, and children during a one-year prospective study in France
    • Pradel, N., V. Livrelli, C. De Champs, J. B. Palcoux, A. Reynaud, F. Scheutz, J. Sirot, B. Joly, and C. Forestier. 2000. Prevalence and characterization of Shiga toxin-producing Escherichia coli isolated from cattle, food, and children during a one-year prospective study in France. J. Clin. Microbiol. 38:1023-1031. (Pubitemid 30140553)
    • (2000) Journal of Clinical Microbiology , vol.38 , Issue.3 , pp. 1023-1031
    • Pradel, N.1    Livrelli, V.2    De Champs, C.3    Palcoux, J.-B.4    Reynaud, A.5    Scheutz, F.6    Sirot, J.7    Joly, B.8    Forestier, C.9
  • 149
    • 0029992419 scopus 로고    scopus 로고
    • From acids to osmZ: Multiple factors influence synthesis of the OmpF and OmpC porins in Escherichia coli
    • DOI 10.1111/j.1365-2958.1996.tb02532.x
    • Pratt, L. A., W. Hsing, K. E. Gibson, and T. J. Silhavy. 1996. From acids to osmZ: Multiple factors influence synthesis of the OmpF and OmpC porins in Escherichia coli. Mol. Microbiol. 20:911-917. (Pubitemid 26198264)
    • (1996) Molecular Microbiology , vol.20 , Issue.5 , pp. 911-917
    • Pratt, L.A.1    Hsing, W.2    Gibson, K.E.3    Silhavy, T.J.4
  • 151
    • 33745210122 scopus 로고    scopus 로고
    • Effect of rpoS gene knockout on the metabolism of Escherichia coli during exponential growth phase and early stationary phase based on gene expressions, enzyme activities and intracellular metabolite concentrations
    • Rahman, M., M. R. Hasan, T. Oba, and K. Shimizu. 2006. Effect of rpoS gene knockout on the metabolism of Escherichia coli during exponential growth phase and early stationary phase based on gene expressions, enzyme activities and intracellular metabolite concentrations. Biotechnol. Bioeng. 94:585-595.
    • (2006) Biotechnol. Bioeng. , vol.94 , pp. 585-595
    • Rahman, M.1    Hasan, M.R.2    Oba, T.3    Shimizu, K.4
  • 152
    • 0034780493 scopus 로고    scopus 로고
    • Periplasmic stress and ECF sigma factors
    • DOI 10.1146/annurev.micro.55.1.591
    • Raivio, T. L., and T. J. Silhavy. 2001. Periplasmic stress and ECF sigma factors. Annu. Rev. Microbiol. 55:591-624. (Pubitemid 32978117)
    • (2001) Annual Review of Microbiology , vol.55 , pp. 591-624
    • Raivio, T.L.1    Silhavy, T.J.2
  • 153
    • 77953689102 scopus 로고    scopus 로고
    • Molecular mechanism of polypeptide translocation catalyzed by the Escherichia coli ClpA protein translocase
    • Rajendar, B., and A. L. Lucius. 2010. Molecular mechanism of polypeptide translocation catalyzed by the Escherichia coli ClpA protein translocase. J. Mol. Biol. 399:665-679.
    • (2010) J. Mol. Biol. , vol.399 , pp. 665-679
    • Rajendar, B.1    Lucius, A.L.2
  • 154
    • 0032117745 scopus 로고    scopus 로고
    • Survival of bioluminescent Listeria monocytogenes and Escherichia coli O157:H7 in soft cheeses
    • Ramsaran, H., J. Chen, B. Brunke, A. Hill, and M. W. Griffiths. 1998. Survival of bioluminescent Listeria monocytogenes and Escherichia coli O157:H7 in soft cheeses. J. Dairy Sci. 81:1810-1817.
    • (1998) J. Dairy Sci. , vol.81 , pp. 1810-1817
    • Ramsaran, H.1    Chen, J.2    Brunke, B.3    Hill, A.4    Griffiths, M.W.5
  • 155
    • 67349284731 scopus 로고    scopus 로고
    • Interplay between the heat shock response and translation in Escherichia coli
    • Rasouly, A., and E. Z. Ron. 2009. Interplay between the heat shock response and translation in Escherichia coli. Res. Microbiol. 160: 288-296.
    • (2009) Res. Microbiol. , vol.160 , pp. 288-296
    • Rasouly, A.1    Ron, E.Z.2
  • 157
    • 0038187589 scopus 로고    scopus 로고
    • Small non-coding RNAs, co-ordinators of adaptation processes in Escherichia coli: The RpoS paradigm
    • DOI 10.1046/j.1365-2958.2003.03454.x
    • Repoila, F., N. Majdalani, and S. Gottesman. 2003. Small noncoding RNAs, co-ordinators of adaptation processes in Escherichia coli: The RpoS paradigm. Mol. Microbiol. 48:855-861. (Pubitemid 36628254)
    • (2003) Molecular Microbiology , vol.48 , Issue.4 , pp. 855-861
    • Repoila, F.1    Majdalani, N.2    Gottesman, S.3
  • 159
    • 0017276787 scopus 로고
    • Cation transport in Escherichia coli. VIII. Potassium transport mutants
    • Rhoads, D. B., F. B. Waters, and W. Epstein. 1976. Cation transport in Escherichia coli. VIII. Potassium transport mutants. J. Gen. Physiol. 67:325-341.
    • (1976) J. Gen. Physiol. , vol.67 , pp. 325-341
    • Rhoads, D.B.1    Waters, F.B.2    Epstein, W.3
  • 160
    • 4444226939 scopus 로고    scopus 로고
    • Escherichia coli glutamate- and arginine-dependent acid resistance systems increase internal pH and reverse transmembrane potential
    • DOI 10.1128/JB.186.18.6032-6041.2004
    • Richard, H., and J. W. Foster. 2004. Escherichia coli glutamate-and arginine-dependent acid resistance systems increase internal pH and reverse transmembrane potential. J. Bacteriol. 186:6032-6041. (Pubitemid 39186991)
    • (2004) Journal of Bacteriology , vol.186 , Issue.18 , pp. 6032-6041
    • Richard, H.1    Foster, J.W.2
  • 161
    • 0033214149 scopus 로고    scopus 로고
    • Genome-wide expression profiling in Escherichia coli K-12
    • DOI 10.1093/nar/27.19.3821
    • Richmond, C. S., J. D. Glasner, R. Mau, H. Jin, and F. R. Blattner. 1999. Genome-wide expression profiling in Escherichia coli K-12. Nucleic Acids Res. 27:3821-3835. (Pubitemid 29454430)
    • (1999) Nucleic Acids Research , vol.27 , Issue.19 , pp. 3821-3835
    • Richmond, C.S.1    Glasner, J.D.2    Mau, R.3    Jin, H.4    Blattner, F.R.5
  • 162
    • 0034034008 scopus 로고    scopus 로고
    • Effects of acid adaptation, product pH, and heating on survival of Escherichia coli O157:H7 in pepperoni
    • DOI 10.1128/AEM.66.4.1726-1729.2000
    • Riordan, D. C., G. Duffy, J. J. Sheridan, R. C. Whiting, I. S. Blair, and D. A. McDowell. 2000. Effects of acid adaptation, product pH, and heating on survival of Escherichia coli O157:H7 in pepperoni. Appl. Environ. Microbiol. 66:1726-1729. (Pubitemid 30185660)
    • (2000) Applied and Environmental Microbiology , vol.66 , Issue.4 , pp. 1726-1729
    • Riordan, D.C.R.1    Duffy, G.2    Sheridan, J.J.3    Whiting, R.C.4    Blair, I.S.5    McDowell, D.A.6
  • 163
    • 0023801241 scopus 로고
    • Accumulation of trehalose by Escherichia coli K-12 at high osmotic pressure depends on the presence of amber suppressors
    • Rod, M. L., K. Y. Alam, P. R. Cunningham, and D. P. Clark. 1988. Accumulation of trehalose by Escherichia coli K-12 at high osmotic pressure depends on the presence of amber suppressors. J. Bacteriol. 170:3601-3610.
    • (1988) J. Bacteriol. , vol.170 , pp. 3601-3610
    • Rod, M.L.1    Alam, K.Y.2    Cunningham, P.R.3    Clark, D.P.4
  • 164
  • 165
    • 0031882597 scopus 로고    scopus 로고
    • Perturbation of anion balance during inhibition of growth of Escherichia coli by weak acids
    • Roe, A. J., D. McLaggan, I. Davidson, C. O'Byrne, and I. R. Booth. 1998. Perturbation of anion balance during inhibition of growth of Escherichia coli by weak acids. J. Bacteriol. 180:767-772. (Pubitemid 28084199)
    • (1998) Journal of Bacteriology , vol.180 , Issue.4 , pp. 767-772
    • Roe, A.J.1    McLaggan, D.2    Davidson, I.3    O'Byrne, C.4    Booth, I.R.5
  • 166
    • 70349526143 scopus 로고    scopus 로고
    • Cardiolipin and the osmotic stress responses of bacteria
    • Romantsov, T., Z. Guan, and J. M. Wood. 2009. Cardiolipin and the osmotic stress responses of bacteria. Biochim. Biophys. Acta 1788: 2092-2100.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 2092-2100
    • Romantsov, T.1    Guan, Z.2    Wood, J.M.3
  • 167
    • 34250016257 scopus 로고    scopus 로고
    • Cardiolipin promotes polar localization of osmosensory transporter ProP in Escherichia coli
    • DOI 10.1111/j.1365-2958.2007.05727.x
    • Romantsov, T., S. Helbig, D. E. Culham, C. Gill, L. Stalker, and J. M. Wood. 2007. Cardiolipin promotes polar localization of osmosensory transporter ProP in Escherichia coli. Mol. Microbiol. 64:1455-1465. (Pubitemid 46889896)
    • (2007) Molecular Microbiology , vol.64 , Issue.6 , pp. 1455-1465
    • Romantsov, T.1    Helbig, S.2    Culham, D.E.3    Gill, C.4    Stalker, L.5    Wood, J.M.6
  • 168
    • 45549088082 scopus 로고    scopus 로고
    • Cardiolipin controls the osmotic stress response and the subcellular location of transporter ProP in Escherichia coli
    • Romantsov, T., L. Stalker, D. E. Culham, and J. M. Wood. 2008. Cardiolipin controls the osmotic stress response and the subcellular location of transporter ProP in Escherichia coli. J. Biol. Chem. 283: 12314-12323.
    • (2008) J. Biol. Chem. , vol.283 , pp. 12314-12323
    • Romantsov, T.1    Stalker, L.2    Culham, D.E.3    Wood, J.M.4
  • 169
    • 0017629285 scopus 로고
    • Localization of the HU protein on the Escherichia coli nucleoid. Cold Spring Harbor Symp
    • Rouviere-Yaniv, J. 1978. Localization of the HU protein on the Escherichia coli nucleoid. Cold Spring Harbor Symp. Quant. Biol. 42:439-447.
    • (1978) Quant. Biol. , vol.42 , pp. 439-447
    • Rouviere-Yaniv, J.1
  • 170
    • 0026651723 scopus 로고
    • Mechanisms of regulation of the biosynthesis of membranederived oligosaccharides in Escherichia coli
    • Rumley, M. K., H. Therisod, A. C. Weissborn, and E. P. Kennedy. 1992. Mechanisms of regulation of the biosynthesis of membranederived oligosaccharides in Escherichia coli. J. Biol. Chem. 267: 11806-11810.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11806-11810
    • Rumley, M.K.1    Therisod, H.2    Weissborn, A.C.3    Kennedy, E.P.4
  • 171
    • 0030804446 scopus 로고    scopus 로고
    • Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL
    • DOI 10.1038/42047
    • Rye, H. S., S. G. Burston, W. A. Fenton, J. M. Beechem, Z. Xu, P. B. Sigler, and A. L. Horwich. 1997. Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL. Nature 388: 792-798. (Pubitemid 27375160)
    • (1997) Nature , vol.388 , Issue.6644 , pp. 792-798
    • Rye, H.S.1    Burston, S.G.2    Fenton, W.A.3    Beechem, J.M.4    Xu, Z.5    Sigler, P.B.6    Horwich, A.L.7
  • 172
    • 0033617129 scopus 로고    scopus 로고
    • GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings
    • DOI 10.1016/S0092-8674(00)80742-4
    • Rye, H. S., A. M. Roseman, S. Chen, K. Furtak, W. A. Fenton, H. R. Saibil, and A. L. Horwich. 1999. GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings. Cell 97:325-338. (Pubitemid 29214589)
    • (1999) Cell , vol.97 , Issue.3 , pp. 325-338
    • Rye, H.S.1    Roseman, A.M.2    Chen, S.3    Furtak, K.4    Fenton, W.A.5    Saibil, H.R.6    Horwich, A.L.7
  • 173
    • 0015957627 scopus 로고
    • Purification and physical properties of inducible Escherichia coli lysine decarboxylase
    • Sabo, D. L., E. A. Boeker, B. Byers, H. Waron, and E. H. Fischer. 1974. Purification and physical properties of inducible Escherichia coli lysine decarboxylase. Biochemistry 13:662-670.
    • (1974) Biochemistry , vol.13 , pp. 662-670
    • Sabo, D.L.1    Boeker, E.A.2    Byers, B.3    Waron, H.4    Fischer, E.H.5
  • 174
    • 51449112852 scopus 로고    scopus 로고
    • Cardiolipin synthesis for the assembly of bacterial and mitochondrial membranes
    • Schlame, M. 2008. Cardiolipin synthesis for the assembly of bacterial and mitochondrial membranes. J. Lipid Res. 49:1607-1620.
    • (2008) J. Lipid Res. , vol.49 , pp. 1607-1620
    • Schlame, M.1
  • 175
    • 33646473824 scopus 로고    scopus 로고
    • Survival of a five-strain cocktail of Escherichia coli O157:H7 during the 60-day aging period of Cheddar cheese made from unpasteurized milk
    • Schlesser, J. E., R. Gerdes, S. Ravishankar, K. Madsen, J. Mowbray, and A. Y. Teo. 2006. Survival of a five-strain cocktail of Escherichia coli O157:H7 during the 60-day aging period of Cheddar cheese made from unpasteurized milk. J. Food Prot. 69: 990-998.
    • (2006) J. Food Prot. , vol.69 , pp. 990-998
    • Schlesser, J.E.1    Gerdes, R.2    Ravishankar, S.3    Madsen, K.4    Mowbray, J.5    Teo, A.Y.6
  • 176
    • 0030033933 scopus 로고    scopus 로고
    • Regulation of Escherichia coli starvation sigma factor (sigma s) by ClpXP protease
    • Schweder, T., K. H. Lee, O. Lomovskaya, and A. Matin. 1996. Regulation of Escherichia coli starvation sigma factor (sigma s) by ClpXP protease. J. Bacteriol. 178:470-476.
    • (1996) J. Bacteriol. , vol.178 , pp. 470-476
    • Schweder, T.1    Lee, K.H.2    Lomovskaya, O.3    Matin, A.4
  • 177
    • 0035136503 scopus 로고    scopus 로고
    • Differentiation of the effects of lethal pH and water activity: Food safety implications
    • DOI 10.1046/j.1472-765X.2001.00862.x
    • Shadbolt, C., T. Ross, and T. A. McMeekin. 2001. Differentiation of the effects of lethal pH and water activity: Food safety implications. Lett. Appl. Microbiol. 32:99-102. (Pubitemid 32158728)
    • (2001) Letters in Applied Microbiology , vol.32 , Issue.2 , pp. 99-102
    • Shadbolt, C.1    Ross, T.2    McMeekin, T.A.3
  • 178
    • 33845937366 scopus 로고    scopus 로고
    • Tuning of DnaK chaperone action by nonnative protein sensor DnaJ and thermosensor GrpE
    • DOI 10.1074/jbc.M606382200
    • Siegenthaler, R. K., and P. Christen. 2006. Tuning of DnaK chaperone action by nonnative protein sensor DnaJ and thermosensor GrpE. J. Biol. Chem. 281:34448-34456. (Pubitemid 46036652)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.45 , pp. 34448-34456
    • Siegenthaler, R.K.1    Christen, P.2
  • 179
    • 65149084160 scopus 로고    scopus 로고
    • The AAAz superfamily of functionally diverse proteins
    • Snider, J., G. Thibault, and W. A. Houry. 2008. The AAAz superfamily of functionally diverse proteins. Genome Biol. 9:216.
    • (2008) Genome Biol. , vol.9 , pp. 216
    • Snider, J.1    Thibault, G.2    Houry, W.A.3
  • 180
    • 1542721578 scopus 로고    scopus 로고
    • Excretion and uptake of cadaverine by CadB and its physiological functions in Escherichia coli
    • DOI 10.1046/j.1365-2958.2003.03913.x
    • Soksawatmaekhin, W., A. Kuraishi, K. Sakata, K. Kashiwagi, and K. Igarashi. 2004. Excretion and uptake of cadaverine by CadB and its physiological functions in Escherichia coli. Mol. Microbiol. 51: 1401-1412. (Pubitemid 38338901)
    • (2004) Molecular Microbiology , vol.51 , Issue.5 , pp. 1401-1412
    • Soksawatmaekhin, W.1    Kuraishi, A.2    Sakata, K.3    Kashiwagi, K.4    Igarashi, K.5
  • 181
    • 0036063918 scopus 로고    scopus 로고
    • Aquaporin Z of Escherichia coli: Reassessment of its regulation and physiological role
    • DOI 10.1128/JB.184.15.4304-4307.2002
    • Soupene, E., N. King, H. Lee, and S. Kustu. 2002. Aquaporin Z of Escherichia coli: Reassessment of its regulation and physiological role. J. Bacteriol. 184:4304-4307. (Pubitemid 34774313)
    • (2002) Journal of Bacteriology , vol.184 , Issue.15 , pp. 4304-4307
    • Soupene, E.1    King, N.2    Lee, H.3    Kustu, S.4
  • 182
    • 0033174242 scopus 로고    scopus 로고
    • Prevalence of verotoxin-producing Escherichia coli (VTEC) in bovine coli mastitis and their antibiotic resistance patterns
    • Stephan, R., and K. Kuhn. 1999. Prevalence of verotoxin-producing Escherichia coli (VTEC) in bovine coli mastitis and their antibiotic resistance patterns. Zentbl. Vetmed. B 46:423-427. (Pubitemid 129694373)
    • (1999) Journal of Veterinary Medicine, Series B , vol.46 , Issue.6 , pp. 423-427
    • Stephan, R.1    Kuhn, K.2
  • 183
    • 47149088288 scopus 로고    scopus 로고
    • Prevalence and characteristics of Shiga toxin-producing Escherichia coli in Swiss raw milk cheeses collected at producer level
    • DOI 10.3168/jds.2008-1055
    • Stephan, R., S. Schumacher, S. Corti, G. Krause, J. Danuser, and L. Beutin. 2008. Prevalence and characteristics of Shiga toxin-producing Escherichia coli in Swiss raw milk cheeses collected at producer level. J. Dairy Sci. 91:2561-2565. (Pubitemid 351976577)
    • (2008) Journal of Dairy Science , vol.91 , Issue.7 , pp. 2561-2565
    • Stephan, R.1    Schumacher, S.2    Corti, S.3    Krause, G.4    Danuser, J.5    Beutin, L.6
  • 185
    • 0023240043 scopus 로고
    • 32
    • DOI 10.1038/329348a0
    • Straus, D. B., W. A. Walter, and C. A. Gross. 1987. The heat shock response of E. coli is regulated by changes in the concentration of sigma 32. Nature 329:348-351. (Pubitemid 17134361)
    • (1987) Nature , vol.329 , Issue.6137 , pp. 348-351
    • Straus, D.B.1    Walter, W.A.2    Gross, C.A.3
  • 186
    • 64549106859 scopus 로고    scopus 로고
    • Controlled destruction: AAAz ATPases in protein degradation from bacteria to eukaryotes
    • Striebel, F., W. Kress, and E. Weber-Ban. 2009. Controlled destruction: AAAz ATPases in protein degradation from bacteria to eukaryotes. Curr. Opin. Struct. Biol. 19:209-217.
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 209-217
    • Striebel, F.1    Kress, W.2    Weber-Ban, E.3
  • 187
    • 0037134267 scopus 로고    scopus 로고
    • Control of the selectivity of the aquaporin water channel family by global orientational tuning
    • DOI 10.1126/science.1067778
    • Tajkhorshid, E., P. Nollert, M. O. Jensen, L. J. Miercke, J. O'Connell, R. M. Stroud, and K. Schulten. 2002. Control of the selectivity of the aquaporin water channel family by global orientational tuning. Science 296:525-530. (Pubitemid 34413590)
    • (2002) Science , vol.296 , Issue.5567 , pp. 525-530
    • Tajkhorshid, E.1    Nollert, P.2    Jensen, M.O.3    Miercke, L.J.W.4    O'Connell, J.5    Stroud, R.M.6    Schulten, K.7
  • 188
    • 15244348050 scopus 로고    scopus 로고
    • Shiga-toxin-producing Escherichia coli and haemolytic uraemic syndrome
    • DOI 10.1016/S0140-6736(05)71144-2
    • Tarr, P. I., C. A. Gordon, and W. L. Chandler. 2005. Shiga-toxin- producing Escherichia coli and haemolytic uraemic syndrome. Lancet 365:1073-1086. (Pubitemid 40386785)
    • (2005) Lancet , vol.365 , Issue.9464 , pp. 1073-1086
    • Tarr, P.I.1    Gordon, C.A.2    Chandler, W.L.3
  • 189
    • 0031737263 scopus 로고    scopus 로고
    • Heat shock regulation in the ftsH null mutant of Escherichia coli: Dissection of stability and activity control mechanisms of σ32 in vivo
    • DOI 10.1046/j.1365-2958.1998.01091.x
    • Tatsuta, T., T. Tomoyasu, B. Bukau, M. Kitagawa, H. Mori, K. Karata, and T. Ogura. 1998. Heat shock regulation in the ftsH null mutant of Escherichia coli: Dissection of stability and activity control mechanisms of sigma32 in vivo. Mol. Microbiol. 30:583-593. (Pubitemid 28497933)
    • (1998) Molecular Microbiology , vol.30 , Issue.3 , pp. 583-593
    • Tatsuta, T.1    Tomoyasu, T.2    Bukau, B.3    Kitagawa, M.4    Mori, H.5    Karata, K.6    Ogura, T.7
  • 190
    • 37749014565 scopus 로고    scopus 로고
    • The membrane-integrated transcriptional activator CadC of Escherichia coli senses lysine indirectly via the interaction with the lysine permease LysP
    • Tetsch, L., C. Koller, I. Haneburger, and K. Jung. 2008. The membrane-integrated transcriptional activator CadC of Escherichia coli senses lysine indirectly via the interaction with the lysine permease LysP. Mol. Microbiol. 67:570-583.
    • (2008) Mol. Microbiol. , vol.67 , pp. 570-583
    • Tetsch, L.1    Koller, C.2    Haneburger, I.3    Jung, K.4
  • 191
    • 33947416247 scopus 로고    scopus 로고
    • Membrane topology and mutational analysis of the osmotically activated BetT choline transporter of Escherichia coli
    • DOI 10.1099/mic.0.2006/003608-0
    • Tondervik, A., and A. R. Strom. 2007. Membrane topology and mutational analysis of the osmotically activated BetT choline transporter of Escherichia coli. Microbiology 153:803-813. (Pubitemid 46444378)
    • (2007) Microbiology , vol.153 , Issue.3 , pp. 803-813
    • Tondervik, A.1    Strom, A.R.2
  • 192
    • 29244463867 scopus 로고    scopus 로고
    • The osmotic activation of transporter ProP is tuned by both its C-terminal coiled-coil and osmotically induced changes in phospholipid composition
    • DOI 10.1074/jbc.M508362200
    • Tsatskis, Y., J. Khambati, M. Dobson, M. Bogdanov, W. Dowhan, and J. M. Wood. 2005. The osmotic activation of transporter ProP is tuned by both its C-terminal coiled-coil and osmotically induced changes in phospholipid composition. J. Biol. Chem. 280:41387-41394. (Pubitemid 41832197)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.50 , pp. 41387-41394
    • Tsatskis, Y.1    Khambati, J.2    Dobson, M.3    Bogdanov, M.4    Dowhan, W.5    Wood, J.M.6
  • 193
    • 77449130939 scopus 로고    scopus 로고
    • Differential expression of virulence and stress fitness genes between Escherichia coli O157:H7 strains with clinical or bovine-biased genotypes
    • Vanaja, S. K., A. C. Springman, T. E. Besser, T. S. Whittam, and S. D. Manning. 2010. Differential expression of virulence and stress fitness genes between Escherichia coli O157:H7 strains with clinical or bovine-biased genotypes. Appl. Environ. Microbiol. 76:60-68.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 60-68
    • Vanaja, S.K.1    Springman, A.C.2    Besser, T.E.3    Whittam, T.S.4    Manning, S.D.5
  • 194
    • 0030791975 scopus 로고    scopus 로고
    • Anionic phospholipids are determinants of membrane protein topology
    • DOI 10.1093/emboj/16.14.4261
    • van Klompenburg, W., I. Nilsson, G. von Heijne, and B. de Kruijff. 1997. Anionic phospholipids are determinants of membrane protein topology. EMBO J. 16:4261-4266. (Pubitemid 27298178)
    • (1997) EMBO Journal , vol.16 , Issue.14 , pp. 4261-4266
    • Van Klompenburg, W.1    Nilsson, I.2    Von Heijne, G.3    De Kruijff, B.4
  • 196
    • 24144437766 scopus 로고    scopus 로고
    • Isolation and characterization of Shiga toxin-producing Escherichia coli strains from raw milk cheeses in France
    • DOI 10.1111/j.1472-765X.2005.01756.x
    • Vernozy-Rozand, C., M. P. Montet, M. Berardin, C. Bavai, and L. Beutin. 2005. Isolation and characterization of Shiga toxin-producing Escherichia coli strains from raw milk cheeses in France. Lett. Appl. Microbiol. 41:235-241. (Pubitemid 41232368)
    • (2005) Letters in Applied Microbiology , vol.41 , Issue.3 , pp. 235-241
    • Vernozy-Rozand, C.1    Montet, M.P.2    Berardin, M.3    Bavai, C.4    Beutin, L.5
  • 197
    • 0030995008 scopus 로고    scopus 로고
    • Isolation of Vero cytotoxin-producing Escherichia coli O157 from wild birds
    • Wallace, J. S., T. Cheasty, and K. Jones. 1997. Isolation of vero cytotoxin-producing Escherichia coli O157 from wild birds. J. Appl. Microbiol. 82:399-404. (Pubitemid 27231024)
    • (1997) Journal of Applied Microbiology , vol.82 , Issue.3 , pp. 399-404
    • Wallace, J.S.1    Cheasty, T.2    Jones, K.3
  • 198
    • 0030691115 scopus 로고    scopus 로고
    • The structure of ClpP at 2.3 Å resolution suggests a model for ATP- dependent proteolysis
    • Wang, J., J. A. Hartling, and J. M. Flanagan. 1997. The structure of ClpP at 2.3 Å resolution suggests a model for ATP-dependent proteolysis. Cell 91:447-456. (Pubitemid 27508234)
    • (1997) Cell , vol.91 , Issue.4 , pp. 447-456
    • Wang, J.1    Hartling, J.A.2    Flanagan, J.M.3
  • 199
    • 14244256556 scopus 로고    scopus 로고
    • S-dependent genes, promoters, and sigma factor selectivity
    • DOI 10.1128/JB.187.5.1591-1603.2005
    • Weber, H., T. Polen, J. Heuveling, V. F. Wendisch, and R. Hengge. 2005. Genome-wide analysis of the general stress response network in Escherichia coli: SigmaS-dependent genes, promoters, and sigma factor selectivity. J. Bacteriol. 187:1591-1603. (Pubitemid 40289359)
    • (2005) Journal of Bacteriology , vol.187 , Issue.5 , pp. 1591-1603
    • Weber, H.1    Polen, T.2    Heuveling, J.3    Wendisch, V.F.4    Hengge, R.5
  • 200
    • 0037023851 scopus 로고    scopus 로고
    • Variation among Escherichia coli O157:H7 strains relative to their growth, survival, thermal inactivation, and toxin production in broth
    • DOI 10.1016/S0168-1605(02)00003-X, PII S016816050200003X
    • Whiting, R. C., and M. H. Golden. 2002. Variation among Escherichia coli O157:H7 strains relative to their growth, survival, thermal inactivation, and toxin production in broth. Int. J. Food Microbiol. 75:127-133. (Pubitemid 34226618)
    • (2002) International Journal of Food Microbiology , vol.75 , Issue.1-2 , pp. 127-133
    • Whiting, R.C.1    Golden, M.H.2
  • 201
    • 0033168858 scopus 로고    scopus 로고
    • DNA protection by stress-induced biocrystallization
    • DOI 10.1038/21918
    • Wolf, S. G., D. Frenkiel, T. Arad, S. E. Finkel, R. Kolter, and A. Minsky. 1999. DNA protection by stress-induced biocrystallization. Nature 400:83-85. (Pubitemid 29315116)
    • (1999) Nature , vol.400 , Issue.6739 , pp. 83-85
    • Wolf, S.G.1    Frenkiel, D.2    Arad, T.3    Finkeil, S.E.4    Kolter, R.5    Minsky, A.6
  • 202
    • 0024264744 scopus 로고
    • Proline porters effect of utilization of proline as nutrient or osmoprotectant for bacteria
    • DOI 10.1007/BF01872157
    • Wood, J. M. 1988. Proline porters effect the utilization of proline as nutrient or osmoprotectant for bacteria. J. Membr. Biol. 106:183-202. (Pubitemid 19020924)
    • (1988) Journal of Membrane Biology , vol.106 , Issue.3 , pp. 183-202
    • Wood, J.M.1
  • 203
    • 0033014719 scopus 로고    scopus 로고
    • Osmosensing by bacteria: Signals and membrane-based sensors
    • Wood, J. M. 1999. Osmosensing by bacteria: Signals and membrane-based sensors. Microbiol. Mol. Biol. Rev. 63:230-262. (Pubitemid 29116093)
    • (1999) Microbiology and Molecular Biology Reviews , vol.63 , Issue.1 , pp. 230-262
    • Wood, J.M.1
  • 204
    • 34250015848 scopus 로고    scopus 로고
    • Osmosensing by bacteria
    • Pe43. doi:10.1126/stke.3572006pe43
    • Wood, J. M. 2006. Osmosensing by bacteria. Sci. STKE 2006(357): Pe43. doi:10.1126/stke.3572006pe43.
    • (2006) Sci. STKE , vol.2006 , pp. 357
    • Wood, J.M.1
  • 205
    • 0030870719 scopus 로고    scopus 로고
    • The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
    • DOI 10.1038/41944
    • Xu, Z., A. L. Horwich, and P. B. Sigler. 1997. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature 388:741-750. (Pubitemid 27375147)
    • (1997) Nature , vol.388 , Issue.6644 , pp. 741-750
    • Xu, Z.1    Horwich, A.L.2    Sigler, P.B.3
  • 206
    • 34447511284 scopus 로고    scopus 로고
    • ClpP: A distinctive family of cylindrical energy-dependent serine proteases
    • DOI 10.1016/j.febslet.2007.04.076, PII S0014579307004735, Cellular Stress
    • Yu, A. Y., and W. A. Houry. 2007. ClpP: A distinctive family of cylindrical energy-dependent serine proteases. FEBS Lett. 581: 3749-3757. (Pubitemid 47082517)
    • (2007) FEBS Letters , vol.581 , Issue.19 , pp. 3749-3757
    • Yu, A.Y.H.1    Houry, W.A.2
  • 207
    • 0030089685 scopus 로고    scopus 로고
    • 32
    • Yura, T. 1996. Regulation and conservation of the heat-shock transcription factor sigma32. Genes Cells 1:277-284. (Pubitemid 126673124)
    • (1996) Genes to Cells , vol.1 , Issue.3 , pp. 277-284
    • Yura, T.1
  • 208
    • 0027385183 scopus 로고
    • Regulation of the heat-shock response in bacteria
    • Yura, T., H. Nagai, and H. Mori. 1993. Regulation of the heat-shock response in bacteria. Annu. Rev. Microbiol. 47:321-350. (Pubitemid 23302937)
    • (1993) Annual Review of Microbiology , vol.47 , pp. 321-350
    • Yura, T.1    Nagai, H.2    Mori, H.3
  • 209
    • 77950604350 scopus 로고    scopus 로고
    • Acid stress response in enteropathogenic gammaproteobacteria: An aptitude for survival
    • Zhao, B., and W. A. Houry. 2010. Acid stress response in enteropathogenic gammaproteobacteria: An aptitude for survival. Biochem. Cell. Biol. 88:301-314.
    • (2010) Biochem. Cell. Biol. , vol.88 , pp. 301-314
    • Zhao, B.1    Houry, W.A.2
  • 210
    • 0037008743 scopus 로고    scopus 로고
    • Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells. A ferritin-like DNA-binding protein of Escherichia coli
    • DOI 10.1074/jbc.M202094200
    • Zhao, G., P. Ceci, A. Ilari, L. Giangiacomo, T. M. Laue, E. Chiancone, and N. D. Chasteen. 2002. Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells. A ferritin-like DNA-binding protein of Escherichia coli. J. Biol. Chem. 277:27689-27696. (Pubitemid 34966712)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.31 , pp. 27689-27696
    • Zhao, G.1    Ceci, P.2    Ilari, A.3    Giangiacomo, L.4    Laue, T.M.5    Chiancone, E.6    Dennis Chasteen, N.7
  • 211
    • 33749350133 scopus 로고    scopus 로고
    • Modes of regulation of RpoS by H-NS
    • DOI 10.1128/JB.00687-06
    • Zhou, Y., and S. Gottesman. 2006. Modes of regulation of RpoS by H-NS. J. Bacteriol. 188:7022-7025. (Pubitemid 44497915)
    • (2006) Journal of Bacteriology , vol.188 , Issue.19 , pp. 7022-7025
    • Zhou, Y.1    Gottesman, S.2
  • 212
    • 75149177573 scopus 로고    scopus 로고
    • Hsp90 and co-chaperones twist the functions of diverse client proteins
    • Zuehlke, A., and J. L. Johnson. 2010. Hsp90 and co-chaperones twist the functions of diverse client proteins. Biopolymers 93:211-217.
    • (2010) Biopolymers , vol.93 , pp. 211-217
    • Zuehlke, A.1    Johnson, J.L.2
  • 213
    • 10444237944 scopus 로고    scopus 로고
    • Phenotypic and genotypic characteristics of non-O157 Shiga toxin-producing Escherichia coli (STEC) from Swiss cattle
    • DOI 10.1016/j.vetmic.2004.10.007, PII S0378113504003797
    • Zweifel, C., S. Schumacher, M. Blanco, J. E. Blanco, T. Tasara, J. Blanco, and R. Stephan. 2005. Phenotypic and genotypic characteristics of non-O157 Shiga toxin-producing Escherichia coli (STEC) from Swiss cattle. Vet. Microbiol. 105:37-45. (Pubitemid 39643419)
    • (2005) Veterinary Microbiology , vol.105 , Issue.1 , pp. 37-45
    • Zweifel, C.1    Schumacher, S.2    Blanco, M.3    Blanco, J.E.4    Tasara, T.5    Blanco, J.6    Stephan, R.7


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