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Volumn 1843, Issue 8, 2014, Pages 1529-1541

Everything old is new again: An update on current research on the Cpx envelope stress response

Author keywords

Post transcriptional regulation; Two component signal transduction

Indexed keywords

BETA LACTAM; CHLORAMPHENICOL; KANAMYCIN; NOVOBIOCIN; SPECTINOMYCIN;

EID: 84902314412     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2013.10.018     Document Type: Article
Times cited : (154)

References (129)
  • 1
    • 0018833244 scopus 로고
    • Chromosomal mutations of Escherichia coli that alter expression of conjugative plasmid functions
    • McEwen J., Silverman P. Chromosomal mutations of Escherichia coli that alter expression of conjugative plasmid functions. Proc. Natl. Acad. Sci. U. S. A. 1980, 77:513-517.
    • (1980) Proc. Natl. Acad. Sci. U. S. A. , vol.77 , pp. 513-517
    • McEwen, J.1    Silverman, P.2
  • 2
    • 0017262473 scopus 로고
    • Mutant of Escherichia coli defective in response to colicin K and in active transport
    • Plate C.A. Mutant of Escherichia coli defective in response to colicin K and in active transport. J. Bacteriol. 1976, 125:467-474.
    • (1976) J. Bacteriol. , vol.125 , pp. 467-474
    • Plate, C.A.1
  • 3
    • 0018088054 scopus 로고
    • Mutations determining generalized resistance to aminoglycoside antibiotics in Escherichia coli
    • Thorbjarnardottir S.H., Magnusdottir R.A., Eggertsson G. Mutations determining generalized resistance to aminoglycoside antibiotics in Escherichia coli. Mol. Gen. Genet. 1978, 161:89-98.
    • (1978) Mol. Gen. Genet. , vol.161 , pp. 89-98
    • Thorbjarnardottir, S.H.1    Magnusdottir, R.A.2    Eggertsson, G.3
  • 4
    • 0019221067 scopus 로고
    • Map location of the ssd mutation in Escherichia coli K-12
    • Morris J.F., Newman E.B. Map location of the ssd mutation in Escherichia coli K-12. J. Bacteriol. 1980, 143:1504-1505.
    • (1980) J. Bacteriol. , vol.143 , pp. 1504-1505
    • Morris, J.F.1    Newman, E.B.2
  • 5
    • 0019343015 scopus 로고
    • A mutation affecting L-serine and energy metabolism in E. coli K12
    • Newman E.B., Morris J.F., Walker C., Kapoor V. A mutation affecting L-serine and energy metabolism in E. coli K12. Mol. Gen. Genet. 1981, 182:143-147.
    • (1981) Mol. Gen. Genet. , vol.182 , pp. 143-147
    • Newman, E.B.1    Morris, J.F.2    Walker, C.3    Kapoor, V.4
  • 6
    • 0019980223 scopus 로고
    • Mutations in genes cpxA and cpxB of Escherichia coli K-12 cause a defect in acetohydroxyacid synthase I function in vivo
    • Sutton A., Newman T., McEwen J., Silverman P.M., Freundlich M. Mutations in genes cpxA and cpxB of Escherichia coli K-12 cause a defect in acetohydroxyacid synthase I function in vivo. J. Bacteriol. 1982, 151:976-982.
    • (1982) J. Bacteriol. , vol.151 , pp. 976-982
    • Sutton, A.1    Newman, T.2    McEwen, J.3    Silverman, P.M.4    Freundlich, M.5
  • 7
    • 0019119523 scopus 로고
    • Mutations in genes cpxA and cpxB of Escherichia coli K-12 cause a defect in isoleucine and valine syntheses
    • McEwen J., Silverman P.M. Mutations in genes cpxA and cpxB of Escherichia coli K-12 cause a defect in isoleucine and valine syntheses. J. Bacteriol. 1980, 144:68-73.
    • (1980) J. Bacteriol. , vol.144 , pp. 68-73
    • McEwen, J.1    Silverman, P.M.2
  • 8
    • 0020626403 scopus 로고
    • Synthesis of outer membrane proteins in cpxA cpxB mutants of Escherichia coli K-12
    • McEwen J., Sambucetti L., Silverman P.M. Synthesis of outer membrane proteins in cpxA cpxB mutants of Escherichia coli K-12. J. Bacteriol. 1983, 154:375-382.
    • (1983) J. Bacteriol. , vol.154 , pp. 375-382
    • McEwen, J.1    Sambucetti, L.2    Silverman, P.M.3
  • 9
    • 0020380048 scopus 로고
    • Mutations in genes cpxA and cpxB alter the protein composition of Escherichia coli inner and outer membranes
    • McEwen J., Silverman P.M. Mutations in genes cpxA and cpxB alter the protein composition of Escherichia coli inner and outer membranes. J. Bacteriol. 1982, 151:1553-1559.
    • (1982) J. Bacteriol. , vol.151 , pp. 1553-1559
    • McEwen, J.1    Silverman, P.M.2
  • 10
    • 0025355396 scopus 로고
    • The Cpx proteins of Escherichia coli K-12: evidence that cpxA, ecfB, ssd, and eup mutations all identify the same gene
    • Rainwater S., Silverman P.M. The Cpx proteins of Escherichia coli K-12: evidence that cpxA, ecfB, ssd, and eup mutations all identify the same gene. J. Bacteriol. 1990, 172:2456-2461.
    • (1990) J. Bacteriol. , vol.172 , pp. 2456-2461
    • Rainwater, S.1    Silverman, P.M.2
  • 11
    • 0027725286 scopus 로고
    • The deduced amino-acid sequence of the cloned cpxR gene suggests the protein is the cognate regulator for the membrane sensor, CpxA, in a two-component signal transduction system of Escherichia coli
    • Dong J., Iuchi S., Kwan H.S., Lu Z., Lin E.C. The deduced amino-acid sequence of the cloned cpxR gene suggests the protein is the cognate regulator for the membrane sensor, CpxA, in a two-component signal transduction system of Escherichia coli. Gene 1993, 136:227-230.
    • (1993) Gene , vol.136 , pp. 227-230
    • Dong, J.1    Iuchi, S.2    Kwan, H.S.3    Lu, Z.4    Lin, E.C.5
  • 12
    • 0023740169 scopus 로고
    • The Cpx proteins of Escherichia coli K-12: structure of the CpxA polypeptide as an inner membrane component
    • Weber R.F., Silverman P.J. The Cpx proteins of Escherichia coli K-12: structure of the CpxA polypeptide as an inner membrane component. J. Mol. Biol. 1988, 203:467-476.
    • (1988) J. Mol. Biol. , vol.203 , pp. 467-476
    • Weber, R.F.1    Silverman, P.J.2
  • 13
    • 0029589618 scopus 로고
    • Mutational activation of the Cpx signal transduction pathway of Escherichia coli suppresses the toxicity conferred by certain envelope-associated stresses
    • Cosma C.L., Danese P.N., Carlson J.H., Silhavy T.J., Snyder W.B. Mutational activation of the Cpx signal transduction pathway of Escherichia coli suppresses the toxicity conferred by certain envelope-associated stresses. Mol. Microbiol. 1995, 18:491-505.
    • (1995) Mol. Microbiol. , vol.18 , pp. 491-505
    • Cosma, C.L.1    Danese, P.N.2    Carlson, J.H.3    Silhavy, T.J.4    Snyder, W.B.5
  • 14
    • 0028983261 scopus 로고
    • Overproduction of NlpE, a new outer membrane lipoprotein, suppresses the toxicity of periplasmic LacZ by activation of the Cpx signal transduction pathway
    • Snyder W.B., Davis L.J., Danese P.N., Cosma C.L., Silhavy T.J. Overproduction of NlpE, a new outer membrane lipoprotein, suppresses the toxicity of periplasmic LacZ by activation of the Cpx signal transduction pathway. J. Bacteriol. 1995, 177:4216-4223.
    • (1995) J. Bacteriol. , vol.177 , pp. 4216-4223
    • Snyder, W.B.1    Davis, L.J.2    Danese, P.N.3    Cosma, C.L.4    Silhavy, T.J.5
  • 15
    • 0030998321 scopus 로고    scopus 로고
    • The sigma(E) and the Cpx signal transduction systems control the synthesis of periplasmic protein-folding enzymes in Escherichia coli
    • Danese P.N., Silhavy T.J. The sigma(E) and the Cpx signal transduction systems control the synthesis of periplasmic protein-folding enzymes in Escherichia coli. Genes Dev. 1997, 11:1183-1193.
    • (1997) Genes Dev. , vol.11 , pp. 1183-1193
    • Danese, P.N.1    Silhavy, T.J.2
  • 16
    • 0031905590 scopus 로고    scopus 로고
    • CpxP, a stress-combative member of the Cpx regulon
    • Danese P.N., Silhavy T.J. CpxP, a stress-combative member of the Cpx regulon. J. Bacteriol. 1998, 180:831-839.
    • (1998) J. Bacteriol. , vol.180 , pp. 831-839
    • Danese, P.N.1    Silhavy, T.J.2
  • 17
    • 0028951033 scopus 로고
    • The Cpx two-component signal transduction pathway of Escherichia coli regulates transcription of the gene specifying the stress-inducible periplasmic protease, DegP
    • Danese P.N., Snyder W.B., Cosma C.L., Davis L.J., Silhavy T.J. The Cpx two-component signal transduction pathway of Escherichia coli regulates transcription of the gene specifying the stress-inducible periplasmic protease, DegP. Genes Dev. 1995, 9:387-398.
    • (1995) Genes Dev. , vol.9 , pp. 387-398
    • Danese, P.N.1    Snyder, W.B.2    Cosma, C.L.3    Davis, L.J.4    Silhavy, T.J.5
  • 18
    • 0030992719 scopus 로고    scopus 로고
    • Regulation of Escherichia coli cell envelope proteins involved in protein folding and degradation by the Cpx two-component system
    • Pogliano J., Lynch A.S., Belin D., Lin E.C., Beckwith J. Regulation of Escherichia coli cell envelope proteins involved in protein folding and degradation by the Cpx two-component system. Genes Dev. 1997, 11:1169-1182.
    • (1997) Genes Dev. , vol.11 , pp. 1169-1182
    • Pogliano, J.1    Lynch, A.S.2    Belin, D.3    Lin, E.C.4    Beckwith, J.5
  • 19
    • 0033812832 scopus 로고    scopus 로고
    • Tethering of CpxP to the inner membrane prevents spheroplast induction of the Cpx envelope stress response
    • Raivio T.L., Laird M.W., Joly J.C., Silhavy T.J. Tethering of CpxP to the inner membrane prevents spheroplast induction of the Cpx envelope stress response. Mol. Microbiol. 2000, 37:1186-1197.
    • (2000) Mol. Microbiol. , vol.37 , pp. 1186-1197
    • Raivio, T.L.1    Laird, M.W.2    Joly, J.C.3    Silhavy, T.J.4
  • 20
    • 0033106492 scopus 로고    scopus 로고
    • The sigmaE and Cpx regulatory pathways: overlapping but distinct envelope stress responses
    • Raivio T.L., Silhavy T.J. The sigmaE and Cpx regulatory pathways: overlapping but distinct envelope stress responses. Curr. Opin. Microbiol. 1999, 2:159-165.
    • (1999) Curr. Opin. Microbiol. , vol.2 , pp. 159-165
    • Raivio, T.L.1    Silhavy, T.J.2
  • 21
    • 0001862358 scopus 로고    scopus 로고
    • Sensing and responding to envelope stress
    • ASM Press, Washington, DC, G. Storz, R. Hengge-Aronis (Eds.)
    • Raivio T.L., Silhavy T.J. Sensing and responding to envelope stress. Bacterial Stress Responses 2000, 19-32. ASM Press, Washington, DC. G. Storz, R. Hengge-Aronis (Eds.).
    • (2000) Bacterial Stress Responses , pp. 19-32
    • Raivio, T.L.1    Silhavy, T.J.2
  • 22
    • 0034780493 scopus 로고    scopus 로고
    • Periplasmic stress and ecf sigma factors
    • Raivio T.L., Silhavy T.J. Periplasmic stress and ecf sigma factors. Annu. Rev. Microbiol. 2001, 55:591-624.
    • (2001) Annu. Rev. Microbiol. , vol.55 , pp. 591-624
    • Raivio, T.L.1    Silhavy, T.J.2
  • 23
    • 83055178971 scopus 로고    scopus 로고
    • Just scratching the surface: an expanding view of the Cpx envelope stress response
    • Vogt S.L., Raivio T.L. Just scratching the surface: an expanding view of the Cpx envelope stress response. FEMS Microbiol. Lett. 2012, 326:2-11.
    • (2012) FEMS Microbiol. Lett. , vol.326 , pp. 2-11
    • Vogt, S.L.1    Raivio, T.L.2
  • 25
    • 0030775342 scopus 로고    scopus 로고
    • The chaperone-assisted membrane release and folding pathway is sensed by two signal transduction systems
    • Jones C.H., Danese P.N., Pinkner J.S., Silhavy T.J., Hultgren S.J. The chaperone-assisted membrane release and folding pathway is sensed by two signal transduction systems. EMBO J. 1997, 21:6394-6406.
    • (1997) EMBO J. , vol.21 , pp. 6394-6406
    • Jones, C.H.1    Danese, P.N.2    Pinkner, J.S.3    Silhavy, T.J.4    Hultgren, S.J.5
  • 26
    • 14644435718 scopus 로고    scopus 로고
    • CpxR/OmpR interplay regulates curli gene expression in response to osmolarity in Escherichia coli
    • Jubelin G., Vianney A., Beloin C., Ghigo J.M., Lazzaroni J.C., Lejeune P., Dorel C. CpxR/OmpR interplay regulates curli gene expression in response to osmolarity in Escherichia coli. J. Bacteriol. 2005, 187:2038-2049.
    • (2005) J. Bacteriol. , vol.187 , pp. 2038-2049
    • Jubelin, G.1    Vianney, A.2    Beloin, C.3    Ghigo, J.M.4    Lazzaroni, J.C.5    Lejeune, P.6    Dorel, C.7
  • 27
    • 0031039158 scopus 로고    scopus 로고
    • The Cpx two-component signal transduction pathway is activated in Escherichia coli mutant strains lacking phosphatidylethanolamine
    • Mileykovskaya E., Dowhan W. The Cpx two-component signal transduction pathway is activated in Escherichia coli mutant strains lacking phosphatidylethanolamine. J. Bacteriol. 1997, 179:1029-1034.
    • (1997) J. Bacteriol. , vol.179 , pp. 1029-1034
    • Mileykovskaya, E.1    Dowhan, W.2
  • 28
    • 4544222062 scopus 로고    scopus 로고
    • Effects of lipoprotein overproduction on the induction of DegP (HtrA) involved in quality control in the Escherichia coli periplasm
    • Miyadai H., Tanaka-Masuda K., Matsuyama S., Tokuda H. Effects of lipoprotein overproduction on the induction of DegP (HtrA) involved in quality control in the Escherichia coli periplasm. J. Biol. Chem. 2004, 279:39807-39813.
    • (2004) J. Biol. Chem. , vol.279 , pp. 39807-39813
    • Miyadai, H.1    Tanaka-Masuda, K.2    Matsuyama, S.3    Tokuda, H.4
  • 29
    • 11844292053 scopus 로고    scopus 로고
    • The Cpx Envelope Stress Response Affects Expression of the Type IV Bundle-Forming Pili of Enteropathogenic Escherichia coli
    • Nevesinjac A.Z., Raivio T.L. The Cpx Envelope Stress Response Affects Expression of the Type IV Bundle-Forming Pili of Enteropathogenic Escherichia coli. J. Bacteriol. 2005, 187:672-686.
    • (2005) J. Bacteriol. , vol.187 , pp. 672-686
    • Nevesinjac, A.Z.1    Raivio, T.L.2
  • 30
    • 0037133315 scopus 로고    scopus 로고
    • Surface sensing and adhesion of Escherichia coli controlled by the Cpx-signaling pathway
    • Otto K., Silhavy T.J. Surface sensing and adhesion of Escherichia coli controlled by the Cpx-signaling pathway. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:2287-2292.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 2287-2292
    • Otto, K.1    Silhavy, T.J.2
  • 31
    • 63049096052 scopus 로고    scopus 로고
    • Characterization of the Cpx regulon in Escherichia coli strain MC4100
    • Price N.L., Raivio T.L. Characterization of the Cpx regulon in Escherichia coli strain MC4100. J. Bacteriol. 2009, 191:1798-1815.
    • (2009) J. Bacteriol. , vol.191 , pp. 1798-1815
    • Price, N.L.1    Raivio, T.L.2
  • 32
    • 0036033555 scopus 로고    scopus 로고
    • A third envelope stress signal transduction pathway in Escherichia coli
    • Raffa R.G., Raivio T.L. A third envelope stress signal transduction pathway in Escherichia coli. Mol. Microbiol. 2002, 45:1599-1611.
    • (2002) Mol. Microbiol. , vol.45 , pp. 1599-1611
    • Raffa, R.G.1    Raivio, T.L.2
  • 33
    • 33746462208 scopus 로고    scopus 로고
    • Characterization of copper-inducible promoters regulated by CpxA/CpxR in Escherichia coli
    • Yamamoto K., Ishihama A. Characterization of copper-inducible promoters regulated by CpxA/CpxR in Escherichia coli. Biosci. Biotechnol. Biochem. 2006, 70:1688-1695.
    • (2006) Biosci. Biotechnol. Biochem. , vol.70 , pp. 1688-1695
    • Yamamoto, K.1    Ishihama, A.2
  • 34
    • 0030834844 scopus 로고    scopus 로고
    • Transduction of envelope stress in Escherichia coli by the Cpx two-component system
    • Raivio T.L., Silhavy T.J. Transduction of envelope stress in Escherichia coli by the Cpx two-component system. J. Bacteriol. 1997, 179:7724-7733.
    • (1997) J. Bacteriol. , vol.179 , pp. 7724-7733
    • Raivio, T.L.1    Silhavy, T.J.2
  • 35
    • 0037384456 scopus 로고    scopus 로고
    • Signal detection and target gene induction by the CpxRA two-component system
    • DiGiuseppe P.A., Silhavy T.J. Signal detection and target gene induction by the CpxRA two-component system. J. Bacteriol. 2003, 185:2432-2440.
    • (2003) J. Bacteriol. , vol.185 , pp. 2432-2440
    • DiGiuseppe, P.A.1    Silhavy, T.J.2
  • 36
    • 25144512854 scopus 로고    scopus 로고
    • Cpx signal transduction is influenced by a conserved N-terminal domain in the novel inhibitor CpxP and the periplasmic protease DegP
    • Buelow D.R., Raivio T.L. Cpx signal transduction is influenced by a conserved N-terminal domain in the novel inhibitor CpxP and the periplasmic protease DegP. J. Bacteriol. 2005, 187:6622-6630.
    • (2005) J. Bacteriol. , vol.187 , pp. 6622-6630
    • Buelow, D.R.1    Raivio, T.L.2
  • 37
  • 38
    • 0032851357 scopus 로고    scopus 로고
    • The Cpx envelope stress response is controlled by amplification and feedback inhibition
    • Raivio T.L., Popkin D.L., Silhavy T.J. The Cpx envelope stress response is controlled by amplification and feedback inhibition. J. Bacteriol. 1999, 181:5263-5272.
    • (1999) J. Bacteriol. , vol.181 , pp. 5263-5272
    • Raivio, T.L.1    Popkin, D.L.2    Silhavy, T.J.3
  • 39
    • 55949113873 scopus 로고    scopus 로고
    • Two-component signaling and gram negative envelope stress response systems
    • MacRitchie D.M., Buelow D.R., Price N.L., Raivio T.L. Two-component signaling and gram negative envelope stress response systems. Adv. Exp. Med. Biol. 2008, 631:80-110.
    • (2008) Adv. Exp. Med. Biol. , vol.631 , pp. 80-110
    • MacRitchie, D.M.1    Buelow, D.R.2    Price, N.L.3    Raivio, T.L.4
  • 40
    • 15744389448 scopus 로고    scopus 로고
    • Sensing external stress: watchdogs of the Escherichia coli cell envelope
    • Ruiz N., Silhavy T.J. Sensing external stress: watchdogs of the Escherichia coli cell envelope. Curr. Opin. Microbiol. 2005, 8:122-126.
    • (2005) Curr. Opin. Microbiol. , vol.8 , pp. 122-126
    • Ruiz, N.1    Silhavy, T.J.2
  • 41
    • 0019195917 scopus 로고
    • Genetic analysis of Escherichia coli K-12 chromosomal mutants defective in expression of F-plasmid functions: identification of genes cpxA and cpxB
    • McEwen J., Silverman P. Genetic analysis of Escherichia coli K-12 chromosomal mutants defective in expression of F-plasmid functions: identification of genes cpxA and cpxB. J. Bacteriol. 1980, 144:60-67.
    • (1980) J. Bacteriol. , vol.144 , pp. 60-67
    • McEwen, J.1    Silverman, P.2
  • 42
    • 77952802182 scopus 로고    scopus 로고
    • The Cpx envelope stress response both facilitates and inhibits elaboration of the enteropathogenic Escherichia coli bundle-forming pilus
    • Vogt S.L., Nevesinjac A.Z., Humphries R.M., Donnenberg M.S., Armstrong G.D., Raivio T.L. The Cpx envelope stress response both facilitates and inhibits elaboration of the enteropathogenic Escherichia coli bundle-forming pilus. Mol. Microbiol. 2010, 76:1095-1110.
    • (2010) Mol. Microbiol. , vol.76 , pp. 1095-1110
    • Vogt, S.L.1    Nevesinjac, A.Z.2    Humphries, R.M.3    Donnenberg, M.S.4    Armstrong, G.D.5    Raivio, T.L.6
  • 43
    • 84880694682 scopus 로고    scopus 로고
    • Activation of CpxRA in Haemophilus ducreyi Primarily Inhibits the Expression of Its Targets, Including Major Virulence Determinants
    • Gangaiah D., Zhang X., Fortney K.R., Baker B., Liu Y., Munson R.S., Spinola S.M. Activation of CpxRA in Haemophilus ducreyi Primarily Inhibits the Expression of Its Targets, Including Major Virulence Determinants. J. Bacteriol. 2013, 195:3486-3502.
    • (2013) J. Bacteriol. , vol.195 , pp. 3486-3502
    • Gangaiah, D.1    Zhang, X.2    Fortney, K.R.3    Baker, B.4    Liu, Y.5    Munson, R.S.6    Spinola, S.M.7
  • 44
    • 78049419108 scopus 로고    scopus 로고
    • Characterization of the CpxRA regulon in Haemophilus ducreyi
    • Labandeira-Rey M., Brautigam C.A., Hansen E.J. Characterization of the CpxRA regulon in Haemophilus ducreyi. Infect. Immun. 2010, 78:4779-4791.
    • (2010) Infect. Immun. , vol.78 , pp. 4779-4791
    • Labandeira-Rey, M.1    Brautigam, C.A.2    Hansen, E.J.3
  • 45
    • 84880011537 scopus 로고    scopus 로고
    • The Escherichia coli Cpx envelope stress response regulates genes of diverse function that impact antibiotic resistance and membrane integrity
    • Raivio T.L., Leblanc S.K., Price N.L. The Escherichia coli Cpx envelope stress response regulates genes of diverse function that impact antibiotic resistance and membrane integrity. J. Bacteriol. 2013, 195:2755-2767.
    • (2013) J. Bacteriol. , vol.195 , pp. 2755-2767
    • Raivio, T.L.1    Leblanc, S.K.2    Price, N.L.3
  • 46
    • 0037135593 scopus 로고    scopus 로고
    • Genome-wide profiling of promoter recognition by the two-component response regulator CpxR-P in Escherichia coli
    • De Wulf P., McGuire A.M., Liu X., Lin E.C. Genome-wide profiling of promoter recognition by the two-component response regulator CpxR-P in Escherichia coli. J. Biol. Chem. 2002, 277:26652-26661.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26652-26661
    • De Wulf, P.1    McGuire, A.M.2    Liu, X.3    Lin, E.C.4
  • 47
    • 67651227355 scopus 로고    scopus 로고
    • Regulation of expression of the Haemophilus ducreyi LspB and LspA2 proteins by CpxR
    • Labandeira-Rey M., Mock J.R., Hansen E.J. Regulation of expression of the Haemophilus ducreyi LspB and LspA2 proteins by CpxR. Infect. Immun. 2009, 77:3402-3411.
    • (2009) Infect. Immun. , vol.77 , pp. 3402-3411
    • Labandeira-Rey, M.1    Mock, J.R.2    Hansen, E.J.3
  • 48
    • 0017644533 scopus 로고
    • Effects of membrane-energy mutations and cations on streptomycin and gentamicin accumulation by bacteria: a model for entry of streptomycin and gentamicin in susceptible and resistant bacteria
    • Bryan L.E., Van Den Elzen H.M. Effects of membrane-energy mutations and cations on streptomycin and gentamicin accumulation by bacteria: a model for entry of streptomycin and gentamicin in susceptible and resistant bacteria. Antimicrob. Agents Chemother. 1977, 12:163-177.
    • (1977) Antimicrob. Agents Chemother. , vol.12 , pp. 163-177
    • Bryan, L.E.1    Van Den Elzen, H.M.2
  • 49
    • 0141928573 scopus 로고    scopus 로고
    • Beta-lactam resistance modulated by the overexpression of response regulators of two-component signal transduction systems in Escherichia coli
    • Hirakawa H., Nishino K., Yamada J., Hirata T., Yamaguchi A. Beta-lactam resistance modulated by the overexpression of response regulators of two-component signal transduction systems in Escherichia coli. J. Antimicrob. Chemother. 2003, 52:576-582.
    • (2003) J. Antimicrob. Chemother. , vol.52 , pp. 576-582
    • Hirakawa, H.1    Nishino, K.2    Yamada, J.3    Hirata, T.4    Yamaguchi, A.5
  • 50
    • 84882418522 scopus 로고    scopus 로고
    • KpnEF, a new member of the Klebsiella pneumoniae cell envelope stress response regulon is a SMR-type efflux pump involved in broad spectrum antimicrobial resistance
    • Srinivasan V.B., Rajamohan G. KpnEF, a new member of the Klebsiella pneumoniae cell envelope stress response regulon is a SMR-type efflux pump involved in broad spectrum antimicrobial resistance. Antimicrob. Agents Chemother. 2013, 57(9):4449-4462.
    • (2013) Antimicrob. Agents Chemother. , vol.57 , Issue.9 , pp. 4449-4462
    • Srinivasan, V.B.1    Rajamohan, G.2
  • 51
    • 84859355675 scopus 로고    scopus 로고
    • Role of the two component signal transduction system CpxAR in conferring cefepime and chloramphenicol resistance in Klebsiella pneumoniae NTUH-K2044
    • Srinivasan V.B., Vaidyanathan V., Mondal A., Rajamohan G. Role of the two component signal transduction system CpxAR in conferring cefepime and chloramphenicol resistance in Klebsiella pneumoniae NTUH-K2044. PLoS One 2012, 7:e33777.
    • (2012) PLoS One , vol.7
    • Srinivasan, V.B.1    Vaidyanathan, V.2    Mondal, A.3    Rajamohan, G.4
  • 53
  • 54
    • 55449126342 scopus 로고    scopus 로고
    • Mistranslation of membrane proteins and two-component system activation trigger antibiotic-mediated cell death
    • Kohanski M.A., Dwyer D.J., Wierzbowski J., Cottarel G., Collins J.J. Mistranslation of membrane proteins and two-component system activation trigger antibiotic-mediated cell death. Cell 2008, 135:679-690.
    • (2008) Cell , vol.135 , pp. 679-690
    • Kohanski, M.A.1    Dwyer, D.J.2    Wierzbowski, J.3    Cottarel, G.4    Collins, J.J.5
  • 55
    • 84876187408 scopus 로고    scopus 로고
    • The Cpx stress response confers resistance to some, but not all, bactericidal antibiotics
    • Mahoney T.F., Silhavy T.J. The Cpx stress response confers resistance to some, but not all, bactericidal antibiotics. J. Bacteriol. 2013, 195:1869-1874.
    • (2013) J. Bacteriol. , vol.195 , pp. 1869-1874
    • Mahoney, T.F.1    Silhavy, T.J.2
  • 56
    • 84877817268 scopus 로고    scopus 로고
    • The Cpx stress response system potentiates the fitness and virulence of uropathogenic Escherichia coli
    • Debnath I., Norton J.P., Barber A.E., Ott E.M., Dhakal B.K., Kulesus R.R., Mulvey M.A. The Cpx stress response system potentiates the fitness and virulence of uropathogenic Escherichia coli. Infect. Immun. 2013, 81:1450-1459.
    • (2013) Infect. Immun. , vol.81 , pp. 1450-1459
    • Debnath, I.1    Norton, J.P.2    Barber, A.E.3    Ott, E.M.4    Dhakal, B.K.5    Kulesus, R.R.6    Mulvey, M.A.7
  • 57
    • 0003830516 scopus 로고
    • Misread protein creates membrane channels: an essential step in the bactericidal action of aminoglycosides
    • Davis B.D., Chen L.L., Tai P.C. Misread protein creates membrane channels: an essential step in the bactericidal action of aminoglycosides. Proc. Natl. Acad. Sci. U. S. A. 1986, 83:6164-6168.
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 6164-6168
    • Davis, B.D.1    Chen, L.L.2    Tai, P.C.3
  • 59
    • 79958117263 scopus 로고    scopus 로고
    • Peptidoglycan recognition proteins kill bacteria by activating protein-sensing two-component systems
    • Kashyap D.R., Wang M., Liu L.H., Boons G.J., Gupta D., Dziarski R. Peptidoglycan recognition proteins kill bacteria by activating protein-sensing two-component systems. Nat. Med. 2011, 17:676-683.
    • (2011) Nat. Med. , vol.17 , pp. 676-683
    • Kashyap, D.R.1    Wang, M.2    Liu, L.H.3    Boons, G.J.4    Gupta, D.5    Dziarski, R.6
  • 60
    • 0032577263 scopus 로고    scopus 로고
    • Different pathways for protein degradation by the FtsH/HflKC membrane-embedded protease complex: an implication from the interference by a mutant form of a new substrate protein, YccA
    • Kihara A., Akiyama Y., Ito K. Different pathways for protein degradation by the FtsH/HflKC membrane-embedded protease complex: an implication from the interference by a mutant form of a new substrate protein, YccA. J. Mol. Biol. 1998, 279:175-188.
    • (1998) J. Mol. Biol. , vol.279 , pp. 175-188
    • Kihara, A.1    Akiyama, Y.2    Ito, K.3
  • 61
    • 0029017127 scopus 로고
    • FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit
    • Kihara A., Akiyama Y., Ito K. FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit. Proc. Natl. Acad. Sci. U. S. A. 1995, 92:4532-4536.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 4532-4536
    • Kihara, A.1    Akiyama, Y.2    Ito, K.3
  • 62
    • 68449090734 scopus 로고    scopus 로고
    • Effects of antibiotics and a proto-oncogene homolog on destruction of protein translocator SecY
    • van Stelten J., Silva F., Belin D., Silhavy T.J. Effects of antibiotics and a proto-oncogene homolog on destruction of protein translocator SecY. Science 2009, 325:753-756.
    • (2009) Science , vol.325 , pp. 753-756
    • van Stelten, J.1    Silva, F.2    Belin, D.3    Silhavy, T.J.4
  • 63
    • 80052539046 scopus 로고    scopus 로고
    • Membrane proteases and aminoglycoside antibiotic resistance
    • Hinz A., Lee S., Jacoby K., Manoil C. Membrane proteases and aminoglycoside antibiotic resistance. J. Bacteriol. 2011, 193:4790-4797.
    • (2011) J. Bacteriol. , vol.193 , pp. 4790-4797
    • Hinz, A.1    Lee, S.2    Jacoby, K.3    Manoil, C.4
  • 64
    • 34548213103 scopus 로고    scopus 로고
    • A common mechanism of cellular death induced by bactericidal antibiotics
    • Kohanski M.A., Dwyer D.J., Hayete B., Lawrence C.A., Collins J.J. A common mechanism of cellular death induced by bactericidal antibiotics. Cell 2007, 130:797-810.
    • (2007) Cell , vol.130 , pp. 797-810
    • Kohanski, M.A.1    Dwyer, D.J.2    Hayete, B.3    Lawrence, C.A.4    Collins, J.J.5
  • 65
    • 84874695302 scopus 로고    scopus 로고
    • Cell death from antibiotics without the involvement of reactive oxygen species
    • Liu Y., Imlay J.A. Cell death from antibiotics without the involvement of reactive oxygen species. Science 2013, 339:1210-1213.
    • (2013) Science , vol.339 , pp. 1210-1213
    • Liu, Y.1    Imlay, J.A.2
  • 66
    • 79953157864 scopus 로고    scopus 로고
    • Morigen, H. Andrews-Polymenis, M. McClelland, Y. Shi, The CpxR/CpxA Two-component System Up-regulates Two Tat-dependent Peptidoglycan Amidases to Confer Bacterial Resistance to Antimicrobial Peptide
    • Weatherspoon-Griffin N., Zhao G., Kong W., Kong Y. Morigen, H. Andrews-Polymenis, M. McClelland, Y. Shi, The CpxR/CpxA Two-component System Up-regulates Two Tat-dependent Peptidoglycan Amidases to Confer Bacterial Resistance to Antimicrobial Peptide. J. Biol. Chem. 2011, 286:5529-5539.
    • (2011) J. Biol. Chem. , vol.286 , pp. 5529-5539
    • Weatherspoon-Griffin, N.1    Zhao, G.2    Kong, W.3    Kong, Y.4
  • 67
    • 79958055551 scopus 로고    scopus 로고
    • Deletion of mtrC in Haemophilus ducreyi increases sensitivity to human antimicrobial peptides and activates the CpxRA regulon
    • Rinker S.D., Trombley M.P., Gu X., Fortney K.R., Bauer M.E. Deletion of mtrC in Haemophilus ducreyi increases sensitivity to human antimicrobial peptides and activates the CpxRA regulon. Infect. Immun. 2011, 79:2324-2334.
    • (2011) Infect. Immun. , vol.79 , pp. 2324-2334
    • Rinker, S.D.1    Trombley, M.P.2    Gu, X.3    Fortney, K.R.4    Bauer, M.E.5
  • 68
    • 84867423414 scopus 로고    scopus 로고
    • Similarities between Exogenously- and Endogenously-Induced Envelope Stress: The Effects of a New Antibacterial Molecule, TPI1609-10
    • Yitzhaki S., Rostron J.E., Xu Y., Rideout M.C., Authement R.N., Barlow S.B., Segall A.M. Similarities between Exogenously- and Endogenously-Induced Envelope Stress: The Effects of a New Antibacterial Molecule, TPI1609-10. PLoS One 2012, 7:e44896.
    • (2012) PLoS One , vol.7
    • Yitzhaki, S.1    Rostron, J.E.2    Xu, Y.3    Rideout, M.C.4    Authement, R.N.5    Barlow, S.B.6    Segall, A.M.7
  • 69
    • 0037336180 scopus 로고    scopus 로고
    • Comprehensive studies of drug resistance mediated by overexpression of response regulators of two-component signal transduction systems in Escherichia coli
    • Hirakawa H., Nishino K., Hirata T., Yamaguchi A. Comprehensive studies of drug resistance mediated by overexpression of response regulators of two-component signal transduction systems in Escherichia coli. J. Bacteriol. 2003, 185:1851-1856.
    • (2003) J. Bacteriol. , vol.185 , pp. 1851-1856
    • Hirakawa, H.1    Nishino, K.2    Hirata, T.3    Yamaguchi, A.4
  • 70
    • 23644456999 scopus 로고    scopus 로고
    • The Escherichia coli CpxA-CpxR envelope stress response system regulates expression of the porins ompF and ompC
    • Batchelor E., Walthers D., Kenney L.J., Goulian M. The Escherichia coli CpxA-CpxR envelope stress response system regulates expression of the porins ompF and ompC. J. Bacteriol. 2005, 187:5723-5731.
    • (2005) J. Bacteriol. , vol.187 , pp. 5723-5731
    • Batchelor, E.1    Walthers, D.2    Kenney, L.J.3    Goulian, M.4
  • 72
    • 78649367258 scopus 로고    scopus 로고
    • MzrA-EnvZ interactions in the periplasm influence the EnvZ/OmpR two-component regulon
    • Gerken H., Misra R. MzrA-EnvZ interactions in the periplasm influence the EnvZ/OmpR two-component regulon. J. Bacteriol. 2010, 192:6271-6278.
    • (2010) J. Bacteriol. , vol.192 , pp. 6271-6278
    • Gerken, H.1    Misra, R.2
  • 73
    • 14544286364 scopus 로고    scopus 로고
    • Indole induces the expression of multidrug exporter genes in Escherichia coli
    • Hirakawa H., Inazumi Y., Masaki T., Hirata T., Yamaguchi A. Indole induces the expression of multidrug exporter genes in Escherichia coli. Mol. Microbiol. 2005, 55:1113-1126.
    • (2005) Mol. Microbiol. , vol.55 , pp. 1113-1126
    • Hirakawa, H.1    Inazumi, Y.2    Masaki, T.3    Hirata, T.4    Yamaguchi, A.5
  • 74
    • 0023025772 scopus 로고
    • Evidence for a protonmotive force related regulatory system in Escherichia coli and its effects on lactose transport
    • Plate C.A., Seely S.A., Laffler T.G. Evidence for a protonmotive force related regulatory system in Escherichia coli and its effects on lactose transport. Biochemistry 1986, 25:6127-6132.
    • (1986) Biochemistry , vol.25 , pp. 6127-6132
    • Plate, C.A.1    Seely, S.A.2    Laffler, T.G.3
  • 75
    • 0019802520 scopus 로고
    • The eup genetic locus of Escherichia coli and its role in H+/solute symport
    • Plate C.A., Suit J.L. The eup genetic locus of Escherichia coli and its role in H+/solute symport. J. Biol. Chem. 1981, 256:12974-12980.
    • (1981) J. Biol. Chem. , vol.256 , pp. 12974-12980
    • Plate, C.A.1    Suit, J.L.2
  • 76
    • 84867374260 scopus 로고    scopus 로고
    • Conserved small protein associates with the multidrug efflux pump AcrB and differentially affects antibiotic resistance
    • Hobbs E.C., Yin X., Paul B.J., Astarita J.L., Storz G. Conserved small protein associates with the multidrug efflux pump AcrB and differentially affects antibiotic resistance. Proc. Natl. Acad. Sci. U. S. A. 2012, 109:16696-16701.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 16696-16701
    • Hobbs, E.C.1    Yin, X.2    Paul, B.J.3    Astarita, J.L.4    Storz, G.5
  • 77
    • 34247880509 scopus 로고    scopus 로고
    • Purification, reconstitution, and characterization of the CpxRAP envelope stress system of Escherichia coli
    • Fleischer R., Heermann R., Jung K., Hunke S. Purification, reconstitution, and characterization of the CpxRAP envelope stress system of Escherichia coli. J. Biol. Chem. 2007, 282:8583-8593.
    • (2007) J. Biol. Chem. , vol.282 , pp. 8583-8593
    • Fleischer, R.1    Heermann, R.2    Jung, K.3    Hunke, S.4
  • 78
    • 84867657727 scopus 로고    scopus 로고
    • Elevated CpxR P levels repress the Ysc-Yop type III secretion system of Yersinia pseudotuberculosis
    • Liu J., Thanikkal E.J., Obi I.R., Francis M.S. Elevated CpxR P levels repress the Ysc-Yop type III secretion system of Yersinia pseudotuberculosis. Res. Microbiol. 2012, 163:518-530.
    • (2012) Res. Microbiol. , vol.163 , pp. 518-530
    • Liu, J.1    Thanikkal, E.J.2    Obi, I.R.3    Francis, M.S.4
  • 79
    • 41549102957 scopus 로고    scopus 로고
    • Signal integration by the two-component signal transduction response regulator CpxR
    • Wolfe A.J., Parikh N., Lima B.P., Zemaitaitis B. Signal integration by the two-component signal transduction response regulator CpxR. J. Bacteriol. 2008, 190:2314-2322.
    • (2008) J. Bacteriol. , vol.190 , pp. 2314-2322
    • Wolfe, A.J.1    Parikh, N.2    Lima, B.P.3    Zemaitaitis, B.4
  • 81
    • 79953229542 scopus 로고    scopus 로고
    • Structural basis for two-component system inhibition and pilus sensing by the auxiliary CpxP protein
    • Zhou X., Keller R., Volkmer R., Krauss N., Scheerer P., Hunke S. Structural basis for two-component system inhibition and pilus sensing by the auxiliary CpxP protein. J. Biol. Chem. 2011, 286:9805-9814.
    • (2011) J. Biol. Chem. , vol.286 , pp. 9805-9814
    • Zhou, X.1    Keller, R.2    Volkmer, R.3    Krauss, N.4    Scheerer, P.5    Hunke, S.6
  • 82
    • 34547661799 scopus 로고    scopus 로고
    • Structural studies of the Cpx pathway activator NlpE on the outer membrane of Escherichia coli
    • Hirano Y., Hossain M.M., Takeda K., Tokuda H., Miki K. Structural studies of the Cpx pathway activator NlpE on the outer membrane of Escherichia coli. Structure 2007, 15:963-976.
    • (2007) Structure , vol.15 , pp. 963-976
    • Hirano, Y.1    Hossain, M.M.2    Takeda, K.3    Tokuda, H.4    Miki, K.5
  • 83
    • 67749135357 scopus 로고    scopus 로고
    • Genetic analysis of activation of the Vibrio cholerae Cpx pathway
    • Slamti L., Waldor M.K. Genetic analysis of activation of the Vibrio cholerae Cpx pathway. J. Bacteriol. 2009, 191:5044-5056.
    • (2009) J. Bacteriol. , vol.191 , pp. 5044-5056
    • Slamti, L.1    Waldor, M.K.2
  • 85
    • 84865419651 scopus 로고    scopus 로고
    • The crystal structure of the periplasmic domain of Vibrio parahaemolyticus CpxA
    • Kwon E., Kim D.Y., Ngo T.D., Gross C.A., Gross J.D., Kim K.K. The crystal structure of the periplasmic domain of Vibrio parahaemolyticus CpxA. Protein Sci. 2012, 21:1334-1343.
    • (2012) Protein Sci. , vol.21 , pp. 1334-1343
    • Kwon, E.1    Kim, D.Y.2    Ngo, T.D.3    Gross, C.A.4    Gross, J.D.5    Kim, K.K.6
  • 86
    • 24744452563 scopus 로고    scopus 로고
    • Control of expression of a periplasmic nickel efflux pump by periplasmic nickel concentrations
    • Grass G., Fricke B., Nies D.H. Control of expression of a periplasmic nickel efflux pump by periplasmic nickel concentrations. Biometals 2005, 18:437-448.
    • (2005) Biometals , vol.18 , pp. 437-448
    • Grass, G.1    Fricke, B.2    Nies, D.H.3
  • 87
    • 0342751307 scopus 로고    scopus 로고
    • Regulation of the cnr cobalt and nickel resistance determinant from Ralstonia sp. strain CH34
    • Grass G., Grosse C., Nies D.H. Regulation of the cnr cobalt and nickel resistance determinant from Ralstonia sp. strain CH34. J. Bacteriol. 2000, 182:1390-1398.
    • (2000) J. Bacteriol. , vol.182 , pp. 1390-1398
    • Grass, G.1    Grosse, C.2    Nies, D.H.3
  • 88
    • 84856303687 scopus 로고    scopus 로고
    • ZraP is a periplasmic molecular chaperone and a repressor of the zinc-responsive two-component regulator ZraSR
    • Appia-Ayme C., Hall A., Patrick E., Rajadurai S., Clarke T.A., Rowley G. ZraP is a periplasmic molecular chaperone and a repressor of the zinc-responsive two-component regulator ZraSR. Biochem. J. 2012, 442:85-93.
    • (2012) Biochem. J. , vol.442 , pp. 85-93
    • Appia-Ayme, C.1    Hall, A.2    Patrick, E.3    Rajadurai, S.4    Clarke, T.A.5    Rowley, G.6
  • 89
    • 84860470786 scopus 로고    scopus 로고
    • Activation of the Cpx phosphorelay signal transduction system in acidic phospholipid-deficient pgsA mutant cells of Escherichia coli
    • Itou A., Matsumoto K., Hara H. Activation of the Cpx phosphorelay signal transduction system in acidic phospholipid-deficient pgsA mutant cells of Escherichia coli. Biochem. Biophys. Res. Commun. 2012, 421:296-300.
    • (2012) Biochem. Biophys. Res. Commun. , vol.421 , pp. 296-300
    • Itou, A.1    Matsumoto, K.2    Hara, H.3
  • 90
    • 77950635752 scopus 로고    scopus 로고
    • Global change of gene expression and cell physiology in YidC-depleted Escherichia coli
    • Wang P., Kuhn A., Dalbey R.E. Global change of gene expression and cell physiology in YidC-depleted Escherichia coli. J. Bacteriol. 2010, 192:2193-2209.
    • (2010) J. Bacteriol. , vol.192 , pp. 2193-2209
    • Wang, P.1    Kuhn, A.2    Dalbey, R.E.3
  • 91
    • 0031765192 scopus 로고    scopus 로고
    • Accumulation of the enterobacterial common antigen lipid II biosynthetic intermediate stimulates degP transcription in Escherichia coli
    • Danese P.N., Oliver G.R., Barr K., Bowman G.D., Rick P.D., Silhavy T.J. Accumulation of the enterobacterial common antigen lipid II biosynthetic intermediate stimulates degP transcription in Escherichia coli. J. Bacteriol. 1998, 180:5875-5884.
    • (1998) J. Bacteriol. , vol.180 , pp. 5875-5884
    • Danese, P.N.1    Oliver, G.R.2    Barr, K.3    Bowman, G.D.4    Rick, P.D.5    Silhavy, T.J.6
  • 92
    • 78751491498 scopus 로고    scopus 로고
    • Characterization of combinatorial patterns generated by multiple two-component sensors in E. coli that respond to many stimuli
    • Clarke E.J., Voigt C.A. Characterization of combinatorial patterns generated by multiple two-component sensors in E. coli that respond to many stimuli. Biotechnol. Bioeng. 2011, 108:666-675.
    • (2011) Biotechnol. Bioeng. , vol.108 , pp. 666-675
    • Clarke, E.J.1    Voigt, C.A.2
  • 94
    • 33748804181 scopus 로고    scopus 로고
    • Expression and assembly of a functional type IV secretion system elicit extracytoplasmic and cytoplasmic stress responses in Escherichia coli
    • Zahrl D., Wagner M., Bischof K., Koraimann G. Expression and assembly of a functional type IV secretion system elicit extracytoplasmic and cytoplasmic stress responses in Escherichia coli. J. Bacteriol. 2006, 188:6611-6621.
    • (2006) J. Bacteriol. , vol.188 , pp. 6611-6621
    • Zahrl, D.1    Wagner, M.2    Bischof, K.3    Koraimann, G.4
  • 95
    • 3042610168 scopus 로고    scopus 로고
    • P pilus assembly motif necessary for activation of the CpxRA pathway by PapE in Escherichia coli
    • Lee Y.M., DiGiuseppe P.A., Silhavy T.J., Hultgren S.J. P pilus assembly motif necessary for activation of the CpxRA pathway by PapE in Escherichia coli. J. Bacteriol. 2004, 186:4326-4337.
    • (2004) J. Bacteriol. , vol.186 , pp. 4326-4337
    • Lee, Y.M.1    DiGiuseppe, P.A.2    Silhavy, T.J.3    Hultgren, S.J.4
  • 96
    • 77955127606 scopus 로고    scopus 로고
    • Managing membrane stress: the phage shock protein (Psp) response, from molecular mechanisms to physiology
    • Joly N., Engl C., Jovanovic G., Huvet M., Toni T., Sheng X., Stumpf M.P., Buck M. Managing membrane stress: the phage shock protein (Psp) response, from molecular mechanisms to physiology. FEMS Microbiol. Rev. 2010, 34:797-827.
    • (2010) FEMS Microbiol. Rev. , vol.34 , pp. 797-827
    • Joly, N.1    Engl, C.2    Jovanovic, G.3    Huvet, M.4    Toni, T.5    Sheng, X.6    Stumpf, M.P.7    Buck, M.8
  • 97
    • 79959326633 scopus 로고    scopus 로고
    • Characterization of the induction and cellular role of the BaeSR two-component envelope stress response of Escherichia coli
    • Leblanc S.K., Oates C.W., Raivio T.L. Characterization of the induction and cellular role of the BaeSR two-component envelope stress response of Escherichia coli. J. Bacteriol. 2011, 193:3367-3375.
    • (2011) J. Bacteriol. , vol.193 , pp. 3367-3375
    • Leblanc, S.K.1    Oates, C.W.2    Raivio, T.L.3
  • 98
    • 84873552933 scopus 로고    scopus 로고
    • Reduction of cellular stress by TolC-dependent efflux pumps in Escherichia coli indicated by BaeSR and CpxARP activation of spy in efflux mutants
    • Rosner J.L., Martin R.G. Reduction of cellular stress by TolC-dependent efflux pumps in Escherichia coli indicated by BaeSR and CpxARP activation of spy in efflux mutants. J. Bacteriol. 2013, 195:1042-1050.
    • (2013) J. Bacteriol. , vol.195 , pp. 1042-1050
    • Rosner, J.L.1    Martin, R.G.2
  • 99
    • 0032728835 scopus 로고    scopus 로고
    • The CpxRA signal transduction system of Escherichia coli: growth-related autoactivation and control of unanticipated target operons
    • De Wulf P., Kwon O., Lin E.C. The CpxRA signal transduction system of Escherichia coli: growth-related autoactivation and control of unanticipated target operons. J. Bacteriol. 1999, 181:6772-6778.
    • (1999) J. Bacteriol. , vol.181 , pp. 6772-6778
    • De Wulf, P.1    Kwon, O.2    Lin, E.C.3
  • 100
    • 80051937249 scopus 로고    scopus 로고
    • Involvement of protein acetylation in glucose-induced transcription of a stress-responsive promoter
    • Lima B.P., Antelmann H., Gronau K., Chi B.K., Becher D., Brinsmade S.R., Wolfe A.J. Involvement of protein acetylation in glucose-induced transcription of a stress-responsive promoter. Mol. Microbiol. 2011, 81:1190-1204.
    • (2011) Mol. Microbiol. , vol.81 , pp. 1190-1204
    • Lima, B.P.1    Antelmann, H.2    Gronau, K.3    Chi, B.K.4    Becher, D.5    Brinsmade, S.R.6    Wolfe, A.J.7
  • 101
    • 0035100582 scopus 로고    scopus 로고
    • Regulation of RpoS by a novel small RNA: the characterization of RprA
    • Majdalani N., Chen S., Murrow J., St John K., Gottesman S. Regulation of RpoS by a novel small RNA: the characterization of RprA. Mol. Microbiol. 2001, 39:1382-1394.
    • (2001) Mol. Microbiol. , vol.39 , pp. 1382-1394
    • Majdalani, N.1    Chen, S.2    Murrow, J.3    St John, K.4    Gottesman, S.5
  • 102
    • 84872012492 scopus 로고    scopus 로고
    • Multiple envelope stress response pathways are activated in an Escherichia coli strain with mutations in two members of the DedA membrane protein family
    • Sikdar R., Simmons A.R., Doerrler W.T. Multiple envelope stress response pathways are activated in an Escherichia coli strain with mutations in two members of the DedA membrane protein family. J. Bacteriol. 2013, 195:12-24.
    • (2013) J. Bacteriol. , vol.195 , pp. 12-24
    • Sikdar, R.1    Simmons, A.R.2    Doerrler, W.T.3
  • 103
    • 58649085492 scopus 로고    scopus 로고
    • The Crp-activated small noncoding regulatory RNA CyaR (RyeE) links nutritional status to group behavior
    • De Lay N., Gottesman S. The Crp-activated small noncoding regulatory RNA CyaR (RyeE) links nutritional status to group behavior. J. Bacteriol. 2009, 191:461-476.
    • (2009) J. Bacteriol. , vol.191 , pp. 461-476
    • De Lay, N.1    Gottesman, S.2
  • 104
    • 84879826686 scopus 로고    scopus 로고
    • Structure and signaling mechanism of a zinc-sensory diguanylate cyclase
    • Zahringer F., Lacanna E., Jenal U., Schirmer T., Boehm A. Structure and signaling mechanism of a zinc-sensory diguanylate cyclase. Structure 2013, 21:1149-1157.
    • (2013) Structure , vol.21 , pp. 1149-1157
    • Zahringer, F.1    Lacanna, E.2    Jenal, U.3    Schirmer, T.4    Boehm, A.5
  • 106
    • 51649096200 scopus 로고    scopus 로고
    • The RNA binding protein CsrA controls cyclic di-GMP metabolism by directly regulating the expression of GGDEF proteins
    • Jonas K., Edwards A.N., Simm R., Romeo T., Romling U., Melefors O. The RNA binding protein CsrA controls cyclic di-GMP metabolism by directly regulating the expression of GGDEF proteins. Mol. Microbiol. 2008, 70:236-257.
    • (2008) Mol. Microbiol. , vol.70 , pp. 236-257
    • Jonas, K.1    Edwards, A.N.2    Simm, R.3    Romeo, T.4    Romling, U.5    Melefors, O.6
  • 107
    • 33646072467 scopus 로고    scopus 로고
    • The Cpx system of Escherichia coli, a strategic signaling pathway for confronting adverse conditions and for settling biofilm communities?
    • Dorel C., Lejeune P., Rodrigue A. The Cpx system of Escherichia coli, a strategic signaling pathway for confronting adverse conditions and for settling biofilm communities?. Res. Microbiol. 2006, 157:306-314.
    • (2006) Res. Microbiol. , vol.157 , pp. 306-314
    • Dorel, C.1    Lejeune, P.2    Rodrigue, A.3
  • 108
    • 70349684496 scopus 로고    scopus 로고
    • OmpA influences Escherichia coli biofilm formation by repressing cellulose production through the CpxRA two-component system
    • Ma Q., Wood T.K. OmpA influences Escherichia coli biofilm formation by repressing cellulose production through the CpxRA two-component system. Environ. Microbiol. 2009, 11:2735-2746.
    • (2009) Environ. Microbiol. , vol.11 , pp. 2735-2746
    • Ma, Q.1    Wood, T.K.2
  • 110
  • 111
    • 0035205423 scopus 로고    scopus 로고
    • Complex regulatory network controls initial adhesion and biofilm formation in Escherichia coli via regulation of the csgD gene
    • Prigent-Combaret C., Brombacher E., Vidal O., Ambert A., Lejeune P., Landini P., Dorel C. Complex regulatory network controls initial adhesion and biofilm formation in Escherichia coli via regulation of the csgD gene. J. Bacteriol. 2001, 183:7213-7223.
    • (2001) J. Bacteriol. , vol.183 , pp. 7213-7223
    • Prigent-Combaret, C.1    Brombacher, E.2    Vidal, O.3    Ambert, A.4    Lejeune, P.5    Landini, P.6    Dorel, C.7
  • 112
    • 84858863122 scopus 로고    scopus 로고
    • Targeting of csgD by the small regulatory RNA RprA links stationary phase, biofilm formation and cell envelope stress in Escherichia coli
    • Mika F., Busse S., Possling A., Berkholz J., Tschowri N., Sommerfeldt N., Pruteanu M., Hengge R. Targeting of csgD by the small regulatory RNA RprA links stationary phase, biofilm formation and cell envelope stress in Escherichia coli. Mol. Microbiol. 2012, 84:51-65.
    • (2012) Mol. Microbiol. , vol.84 , pp. 51-65
    • Mika, F.1    Busse, S.2    Possling, A.3    Berkholz, J.4    Tschowri, N.5    Sommerfeldt, N.6    Pruteanu, M.7    Hengge, R.8
  • 113
    • 33644866120 scopus 로고    scopus 로고
    • Gene expression regulation by the Curli activator CsgD protein: modulation of cellulose biosynthesis and control of negative determinants for microbial adhesion
    • Brombacher E., Baratto A., Dorel C., Landini P. Gene expression regulation by the Curli activator CsgD protein: modulation of cellulose biosynthesis and control of negative determinants for microbial adhesion. J. Bacteriol. 2006, 188:2027-2037.
    • (2006) J. Bacteriol. , vol.188 , pp. 2027-2037
    • Brombacher, E.1    Baratto, A.2    Dorel, C.3    Landini, P.4
  • 114
    • 0036437019 scopus 로고    scopus 로고
    • Regulation and mode of action of the second small RNA activator of RpoS translation, RprA
    • Majdalani N., Hernandez D., Gottesman S. Regulation and mode of action of the second small RNA activator of RpoS translation, RprA. Mol. Microbiol. 2002, 46:813-826.
    • (2002) Mol. Microbiol. , vol.46 , pp. 813-826
    • Majdalani, N.1    Hernandez, D.2    Gottesman, S.3
  • 115
    • 0035014383 scopus 로고    scopus 로고
    • Mechanisms of biofilm resistance to antimicrobial agents
    • Mah T.F., O'Toole G.A. Mechanisms of biofilm resistance to antimicrobial agents. Trends Microbiol. 2001, 9:34-39.
    • (2001) Trends Microbiol. , vol.9 , pp. 34-39
    • Mah, T.F.1    O'Toole, G.A.2
  • 116
    • 84859996025 scopus 로고    scopus 로고
    • A mixed double negative feedback loop between the sRNA MicF and the global regulator Lrp
    • Holmqvist E., Unoson C., Reimegard J., Wagner E.G. A mixed double negative feedback loop between the sRNA MicF and the global regulator Lrp. Mol. Microbiol. 2012, 84:414-427.
    • (2012) Mol. Microbiol. , vol.84 , pp. 414-427
    • Holmqvist, E.1    Unoson, C.2    Reimegard, J.3    Wagner, E.G.4
  • 117
    • 0035850795 scopus 로고    scopus 로고
    • MicF: an antisense RNA gene involved in response of Escherichia coli to global stress factors
    • Delihas N., Forst S. MicF: an antisense RNA gene involved in response of Escherichia coli to global stress factors. J. Mol. Biol. 2001, 313:1-12.
    • (2001) J. Mol. Biol. , vol.313 , pp. 1-12
    • Delihas, N.1    Forst, S.2
  • 118
    • 25144451503 scopus 로고    scopus 로고
    • The Rcs phosphorelay: a complex signal transduction system
    • Majdalani N., Gottesman S. The Rcs phosphorelay: a complex signal transduction system. Annu. Rev. Microbiol. 2005, 59:379-405.
    • (2005) Annu. Rev. Microbiol. , vol.59 , pp. 379-405
    • Majdalani, N.1    Gottesman, S.2
  • 119
    • 84866784153 scopus 로고    scopus 로고
    • A connecter-like factor, CacA, links RssB/RpoS and the CpxR/CpxA two-component system in Salmonella
    • Kato A., Hayashi H., Nomura W., Emori H., Hagihara K., Utsumi R. A connecter-like factor, CacA, links RssB/RpoS and the CpxR/CpxA two-component system in Salmonella. BMC Microbiol. 2012, 12:224.
    • (2012) BMC Microbiol. , vol.12 , pp. 224
    • Kato, A.1    Hayashi, H.2    Nomura, W.3    Emori, H.4    Hagihara, K.5    Utsumi, R.6
  • 120
    • 79957530554 scopus 로고    scopus 로고
    • Engineered pathways for correct disulfide bond oxidation
    • Ren G., Bardwell J.C. Engineered pathways for correct disulfide bond oxidation. Antioxid. Redox Signal. 2011, 14:2399-2412.
    • (2011) Antioxid. Redox Signal. , vol.14 , pp. 2399-2412
    • Ren, G.1    Bardwell, J.C.2
  • 122
    • 0037436563 scopus 로고    scopus 로고
    • Dispelling the myths-biocatalysis in industrial synthesis
    • Schoemaker H.E., Mink D., Wubbolts M.G. Dispelling the myths-biocatalysis in industrial synthesis. Science 2003, 299:1694-1697.
    • (2003) Science , vol.299 , pp. 1694-1697
    • Schoemaker, H.E.1    Mink, D.2    Wubbolts, M.G.3
  • 123
    • 77953083400 scopus 로고    scopus 로고
    • Systematic screening of Escherichia coli single-gene knockout mutants for improving recombinant whole-cell biocatalysts
    • Zhou Y., Minami T., Honda K., Omasa T., Ohtake H. Systematic screening of Escherichia coli single-gene knockout mutants for improving recombinant whole-cell biocatalysts. Appl. Microbiol. Biotechnol. 2010, 87:647-655.
    • (2010) Appl. Microbiol. Biotechnol. , vol.87 , pp. 647-655
    • Zhou, Y.1    Minami, T.2    Honda, K.3    Omasa, T.4    Ohtake, H.5
  • 124
    • 77956651754 scopus 로고    scopus 로고
    • Enhancement of recombinant enzyme activity in cpxA-deficient mutant of Escherichia coli
    • Zhou Y., Minami T., Honda K., Omasa T., Ohtake H. Enhancement of recombinant enzyme activity in cpxA-deficient mutant of Escherichia coli. J. Biosci. Bioeng. 2010, 110:403-407.
    • (2010) J. Biosci. Bioeng. , vol.110 , pp. 403-407
    • Zhou, Y.1    Minami, T.2    Honda, K.3    Omasa, T.4    Ohtake, H.5
  • 126
    • 78650643942 scopus 로고    scopus 로고
    • Evolving a robust signal transduction pathway from weak cross-talk
    • Siryaporn A., Perchuk B.S., Laub M.T., Goulian M. Evolving a robust signal transduction pathway from weak cross-talk. Mol. Syst. Biol. 2010, 6:452.
    • (2010) Mol. Syst. Biol. , vol.6 , pp. 452
    • Siryaporn, A.1    Perchuk, B.S.2    Laub, M.T.3    Goulian, M.4
  • 127
    • 79953683989 scopus 로고    scopus 로고
    • Reconstitution of the Cpx signaling system from cell-free synthesized proteins
    • Miot M., Betton J.M. Reconstitution of the Cpx signaling system from cell-free synthesized proteins. New Biotechnol. 2011, 28:277-281.
    • (2011) New Biotechnol. , vol.28 , pp. 277-281
    • Miot, M.1    Betton, J.M.2
  • 128
    • 77957832226 scopus 로고    scopus 로고
    • Physiology, pathogenicity and immunogenicity of lon and/or cpxR deleted mutants of Salmonella Gallinarum as vaccine candidates for fowl typhoid
    • Matsuda K., Chaudhari A.A., Kim S.W., Lee K.M., Lee J.H. Physiology, pathogenicity and immunogenicity of lon and/or cpxR deleted mutants of Salmonella Gallinarum as vaccine candidates for fowl typhoid. Vet. Res. 2010, 41:59.
    • (2010) Vet. Res. , vol.41 , pp. 59
    • Matsuda, K.1    Chaudhari, A.A.2    Kim, S.W.3    Lee, K.M.4    Lee, J.H.5
  • 129
    • 78650582307 scopus 로고    scopus 로고
    • Evaluation of safety and protection efficacy on cpxR and lon deleted mutant of Salmonella Gallinarum as a live vaccine candidate for fowl typhoid
    • Matsuda K., Chaudhari A.A., Lee J.H. Evaluation of safety and protection efficacy on cpxR and lon deleted mutant of Salmonella Gallinarum as a live vaccine candidate for fowl typhoid. Vaccine 2011, 29:668-674.
    • (2011) Vaccine , vol.29 , pp. 668-674
    • Matsuda, K.1    Chaudhari, A.A.2    Lee, J.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.