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Volumn 7, Issue 8, 2012, Pages

Development of Quinoxaline 1, 4-Dioxides Resistance in Escherichia coli and Molecular Change under Resistance Selection

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; AMPICILLIN; ANTIINFECTIVE AGENT; CARBADOX; CEFTIOFUR; CHLORAMPHENICOL; CHLORTETRACYCLINE; CIADOX; CIPROFLOXACIN; COLISTIN; COMPLEMENTARY DNA; CYTIDINE TRIPHOSPHATE SYNTHASE; FLORFENICOL; FURAZOLIDONE; GENTAMICIN; IRON; LIPID A; MEQUIDOX; OLAQUINDOX; OXYTETRACYCLINE; QUINOXALINE 1,4 DIOXIDE DERIVATIVE; RIFAMPICIN; SULFAMETHOXAZOLE; SULFUR; TETRACYCLINE; THIOCTIC ACID; TREHALOSE; TRIMETHOPRIM; UNCLASSIFIED DRUG;

EID: 84865476102     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0043322     Document Type: Article
Times cited : (16)

References (69)
  • 2
    • 23844472369 scopus 로고    scopus 로고
    • Quinoxaline 1,4-dioxide: a versatile scaffold endowed with manifold activities
    • Carta A, Corona P, Loriga M, (2005) Quinoxaline 1,4-dioxide: a versatile scaffold endowed with manifold activities. Curr Med Chem 12: 2259-2272.
    • (2005) Curr Med Chem , vol.12 , pp. 2259-2272
    • Carta, A.1    Corona, P.2    Loriga, M.3
  • 3
    • 0034830902 scopus 로고    scopus 로고
    • Redox-activated, hypoxia-selective DNA cleavage by quinoxaline 1,4-di-N-oxide
    • Ganley B, Chowdhury G, Bhansali J, Daniels JS, Gates KS, (2001) Redox-activated, hypoxia-selective DNA cleavage by quinoxaline 1,4-di-N-oxide. Bioorg Med Chem 9: 2395-2401.
    • (2001) Bioorg Med Chem , vol.9 , pp. 2395-2401
    • Ganley, B.1    Chowdhury, G.2    Bhansali, J.3    Daniels, J.S.4    Gates, K.S.5
  • 4
    • 0019847072 scopus 로고
    • Mutagenicity of quindoxin, its metabolites, and two substituted quinoxaline-di-N-oxides
    • Beutin L, Preller E, Kowalski B, (1981) Mutagenicity of quindoxin, its metabolites, and two substituted quinoxaline-di-N-oxides. Antimicrob Agents Chemother 20: 336-343.
    • (1981) Antimicrob Agents Chemother , vol.20 , pp. 336-343
    • Beutin, L.1    Preller, E.2    Kowalski, B.3
  • 5
    • 67349125456 scopus 로고    scopus 로고
    • Olaquindox-induced genotoxicity and oxidative DNA damage in human hepatoma G2 (HepG2) cells
    • Zou J, Chen Q, Tang S, Jin X, Chen K, et al. (2009) Olaquindox-induced genotoxicity and oxidative DNA damage in human hepatoma G2 (HepG2) cells. Mutat Res 676: 27-33.
    • (2009) Mutat Res , vol.676 , pp. 27-33
    • Zou, J.1    Chen, Q.2    Tang, S.3    Jin, X.4    Chen, K.5
  • 6
    • 33646679840 scopus 로고    scopus 로고
    • Olaquindox and cyadox stimulate growth and decrease intestinal mucosal immunity of piglets orally inoculated with Escherichia coli
    • Ding MX, Yuan ZH, Wang YL, Zhu HL, Fan SX, (2006) Olaquindox and cyadox stimulate growth and decrease intestinal mucosal immunity of piglets orally inoculated with Escherichia coli. J Anim Physiol Anim Nutr (Berl) 90: 238-243.
    • (2006) J Anim Physiol Anim Nutr (Berl) , vol.90 , pp. 238-243
    • Ding, M.X.1    Yuan, Z.H.2    Wang, Y.L.3    Zhu, H.L.4    Fan, S.X.5
  • 7
    • 33748577356 scopus 로고    scopus 로고
    • Effects of cyadox and olaquindox on intestinal mucosal immunity and on fecal shedding of Escherichia coli in piglets
    • Ding MX, Wang YL, Zhu HL, Yuan ZH, (2006) Effects of cyadox and olaquindox on intestinal mucosal immunity and on fecal shedding of Escherichia coli in piglets. J Anim Sci 84: 2367-2373.
    • (2006) J Anim Sci , vol.84 , pp. 2367-2373
    • Ding, M.X.1    Wang, Y.L.2    Zhu, H.L.3    Yuan, Z.H.4
  • 8
    • 53249089990 scopus 로고    scopus 로고
    • Development of high performance liquid chromatographic methods for the determination of cyadox and its metabolites in plasma and tissues of chicken
    • Huang L, Wang Y, Tao Y, Chen D, Yuan Z, (2008) Development of high performance liquid chromatographic methods for the determination of cyadox and its metabolites in plasma and tissues of chicken. J Chromatogr B Analyt Technol Biomed Life Sci 874: 7-14.
    • (2008) J Chromatogr B Analyt Technol Biomed Life Sci , vol.874 , pp. 7-14
    • Huang, L.1    Wang, Y.2    Tao, Y.3    Chen, D.4    Yuan, Z.5
  • 10
    • 28844458799 scopus 로고    scopus 로고
    • Subchronic oral toxicity study with cyadox in Wistar rats
    • Fang G, He Q, Zhou S, Wang D, Zhang Y, et al. (2006) Subchronic oral toxicity study with cyadox in Wistar rats. Food Chem Toxicol 44: 36-41.
    • (2006) Food Chem Toxicol , vol.44 , pp. 36-41
    • Fang, G.1    He, Q.2    Zhou, S.3    Wang, D.4    Zhang, Y.5
  • 11
    • 44649083284 scopus 로고    scopus 로고
    • Associations of antimicrobial uses with antimicrobial resistance of fecal Escherichia coli from pigs on 47 farrow-to-finish farms in Ontario and British Columbia
    • Akwar HT, Poppe C, Wilson J, Reid-Smith RJ, Dyck M, et al. (2008b) Associations of antimicrobial uses with antimicrobial resistance of fecal Escherichia coli from pigs on 47 farrow-to-finish farms in Ontario and British Columbia. Can J Vet Res 72: 202-210.
    • (2008) Can J Vet Res , vol.72 , pp. 202-210
    • Akwar, H.T.1    Poppe, C.2    Wilson, J.3    Reid-Smith, R.J.4    Dyck, M.5
  • 12
    • 44649090219 scopus 로고    scopus 로고
    • Prevalence and patterns of antimicrobial resistance of fecal Escherichia coli among pigs on 47 farrow-to-finish farms with different in-feed medication policies in Ontario and British Columbia
    • Akwar HT, Poppe C, Wilson J, Reid-Smith RJ, Dyck M, et al. (2008) Prevalence and patterns of antimicrobial resistance of fecal Escherichia coli among pigs on 47 farrow-to-finish farms with different in-feed medication policies in Ontario and British Columbia. Can J Vet Res 72: 195-201.
    • (2008) Can J Vet Res , vol.72 , pp. 195-201
    • Akwar, H.T.1    Poppe, C.2    Wilson, J.3    Reid-Smith, R.J.4    Dyck, M.5
  • 13
    • 0032571027 scopus 로고    scopus 로고
    • Associations among antimicrobial drug treatments and antimicrobial resistance of fecal Escherichia coli of swine on 34 farrow-to-finish farms in Ontario, Canada
    • Dunlop RH, McEwen SA, Meek AH, Clarke RC, Black WD, et al. (1998) Associations among antimicrobial drug treatments and antimicrobial resistance of fecal Escherichia coli of swine on 34 farrow-to-finish farms in Ontario, Canada. Prev Vet Med 34: 283-305.
    • (1998) Prev Vet Med , vol.34 , pp. 283-305
    • Dunlop, R.H.1    McEwen, S.A.2    Meek, A.H.3    Clarke, R.C.4    Black, W.D.5
  • 16
    • 34447547677 scopus 로고    scopus 로고
    • Substrate specificity of the OqxAB multidrug resistance pump in Escherichia coli and selected enteric bacteria
    • Hansen LH, Jensen LB, Sorensen HI, Sorensen SJ, (2007) Substrate specificity of the OqxAB multidrug resistance pump in Escherichia coli and selected enteric bacteria. J Antimicrob Chemother 60: 145-147.
    • (2007) J Antimicrob Chemother , vol.60 , pp. 145-147
    • Hansen, L.H.1    Jensen, L.B.2    Sorensen, H.I.3    Sorensen, S.J.4
  • 17
    • 80053124273 scopus 로고    scopus 로고
    • Beyond serial passages: new methods for predicting the emergence of resistance to novel antibiotics
    • Martinez JL, Baquero F, Andersson DI, (2011) Beyond serial passages: new methods for predicting the emergence of resistance to novel antibiotics. Curr Opin Pharmacol 11: 439-445.
    • (2011) Curr Opin Pharmacol , vol.11 , pp. 439-445
    • Martinez, J.L.1    Baquero, F.2    Andersson, D.I.3
  • 18
    • 33751512976 scopus 로고    scopus 로고
    • Cut and move: protein machinery for DNA processing in bacterial conjugation
    • Gomis-Ruth FX, Coll M, (2006) Cut and move: protein machinery for DNA processing in bacterial conjugation. Curr Opin Struct Biol 16: 744-752.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 744-752
    • Gomis-Ruth, F.X.1    Coll, M.2
  • 19
    • 37849046638 scopus 로고    scopus 로고
    • Prokaryotic suppression subtractive hybridization PCR cDNA subtraction, a targeted method to identify differentially expressed genes
    • De Long SK, Kinney KA, Kirisits MJ, (2008) Prokaryotic suppression subtractive hybridization PCR cDNA subtraction, a targeted method to identify differentially expressed genes. Appl Environ Microbiol 74: 225-232.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 225-232
    • de Long, S.K.1    Kinney, K.A.2    Kirisits, M.J.3
  • 20
    • 19544387748 scopus 로고    scopus 로고
    • In vitro selection of resistance to clarithromycin in Streptococcus pneumoniae clinical isolates
    • Drago L, De Vecchi E, Nicola L, Legnani D, Prenna M, et al. (2005) In vitro selection of resistance to clarithromycin in Streptococcus pneumoniae clinical isolates. J Chemother 17: 161-168.
    • (2005) J Chemother , vol.17 , pp. 161-168
    • Drago, L.1    de Vecchi, E.2    Nicola, L.3    Legnani, D.4    Prenna, M.5
  • 21
    • 34249033759 scopus 로고    scopus 로고
    • Kinetics of plasmid transfer among Bacillus cereus group strains within lepidopteran larvae
    • Yuan YM, Hu XM, Liu HZ, Hansen BM, Yan JP, et al. (2007) Kinetics of plasmid transfer among Bacillus cereus group strains within lepidopteran larvae. Arch Microbiol 187: 425-431.
    • (2007) Arch Microbiol , vol.187 , pp. 425-431
    • Yuan, Y.M.1    Hu, X.M.2    Liu, H.Z.3    Hansen, B.M.4    Yan, J.P.5
  • 22
    • 53149153217 scopus 로고    scopus 로고
    • Riboprint and virulence gene patterns for Bacillus cereus and related species
    • Kim YR, Batt CA, (2008) Riboprint and virulence gene patterns for Bacillus cereus and related species. J Microbiol Biotechnol 18: 1146-1155.
    • (2008) J Microbiol Biotechnol , vol.18 , pp. 1146-1155
    • Kim, Y.R.1    Batt, C.A.2
  • 23
    • 0033775615 scopus 로고    scopus 로고
    • Absolute quantification of mRNA using real-time reverse transcription polymerase chain reaction assays
    • Bustin SA, (2000) Absolute quantification of mRNA using real-time reverse transcription polymerase chain reaction assays. J Mol Endocrinol 25: 169-193.
    • (2000) J Mol Endocrinol , vol.25 , pp. 169-193
    • Bustin, S.A.1
  • 24
    • 0023719363 scopus 로고
    • Olaquindox resistance in the coliform flora of pigs and their environment: an ecological study
    • Hedges AJ, Linton AH, (1988) Olaquindox resistance in the coliform flora of pigs and their environment: an ecological study. J Appl Bacteriol 64: 429-443.
    • (1988) J Appl Bacteriol , vol.64 , pp. 429-443
    • Hedges, A.J.1    Linton, A.H.2
  • 25
    • 0023908975 scopus 로고
    • Monitoring for the development of antimicrobial resistance during the use of olaquindox as a feed additive on commercial pig farms
    • Linton AH, Hedges AJ, Bennett PM, (1988) Monitoring for the development of antimicrobial resistance during the use of olaquindox as a feed additive on commercial pig farms. J Appl Bacteriol 64: 311-327.
    • (1988) J Appl Bacteriol , vol.64 , pp. 311-327
    • Linton, A.H.1    Hedges, A.J.2    Bennett, P.M.3
  • 26
    • 0019462262 scopus 로고
    • R plasmid with carbadox resistance from Escherichia coli of porcine origin
    • Ohmae K, Yonezawa S, Terakado N, (1981) R plasmid with carbadox resistance from Escherichia coli of porcine origin. Antimicrob Agents Chemother 19: 86-90.
    • (1981) Antimicrob Agents Chemother , vol.19 , pp. 86-90
    • Ohmae, K.1    Yonezawa, S.2    Terakado, N.3
  • 27
    • 77952884274 scopus 로고    scopus 로고
    • How antibiotics kill bacteria: from targets to networks
    • Kohanski MA, Dwyer DJ, Collins JJ, (2010) How antibiotics kill bacteria: from targets to networks. Nat Rev Microbiol 8: 423-435.
    • (2010) Nat Rev Microbiol , vol.8 , pp. 423-435
    • Kohanski, M.A.1    Dwyer, D.J.2    Collins, J.J.3
  • 28
    • 0035102909 scopus 로고    scopus 로고
    • The coordination and function of the redox centres of the membrane-bound nitrate reductases
    • Blasco F, Guigliarelli B, Magalon A, Asso M, Giordano G, et al. (2001) The coordination and function of the redox centres of the membrane-bound nitrate reductases. Cell Mol Life Sci 58: 179-193.
    • (2001) Cell Mol Life Sci , vol.58 , pp. 179-193
    • Blasco, F.1    Guigliarelli, B.2    Magalon, A.3    Asso, M.4    Giordano, G.5
  • 29
    • 0035341125 scopus 로고    scopus 로고
    • Electron transfer from heme bL to the [3Fe-4S] cluster of Escherichia coli nitrate reductase A (NarGHI)
    • Rothery RA, Blasco F, Weiner JH, (2001) Electron transfer from heme bL to the [3Fe-4S] cluster of Escherichia coli nitrate reductase A (NarGHI). Biochemistry 40: 5260-5268.
    • (2001) Biochemistry , vol.40 , pp. 5260-5268
    • Rothery, R.A.1    Blasco, F.2    Weiner, J.H.3
  • 30
    • 13444283630 scopus 로고    scopus 로고
    • Interaction network containing conserved and essential protein complexes in Escherichia coli
    • Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433: 531-537.
    • (2005) Nature , vol.433 , pp. 531-537
    • Butland, G.1    Peregrin-Alvarez, J.M.2    Li, J.3    Yang, W.4    Yang, X.5
  • 31
    • 0033971754 scopus 로고    scopus 로고
    • EcoGene: a genome sequence database for Escherichia coli K-12
    • Rudd KE, (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28: 60-64.
    • (2000) Nucleic Acids Res , vol.28 , pp. 60-64
    • Rudd, K.E.1
  • 32
    • 0028251157 scopus 로고
    • Diverse mechanisms for regulating ribosomal protein synthesis in Escherichia coli
    • Zengel JM, Lindahl L, (1994) Diverse mechanisms for regulating ribosomal protein synthesis in Escherichia coli. Prog Nucleic Acid Res Mol Biol 47: 331-370.
    • (1994) Prog Nucleic Acid Res Mol Biol , vol.47 , pp. 331-370
    • Zengel, J.M.1    Lindahl, L.2
  • 33
    • 0031028688 scopus 로고    scopus 로고
    • Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome
    • Rodnina MV, Savelsbergh A, Katunin VI, Wintermeyer W, (1997) Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome. Nature 385: 37-41.
    • (1997) Nature , vol.385 , pp. 37-41
    • Rodnina, M.V.1    Savelsbergh, A.2    Katunin, V.I.3    Wintermeyer, W.4
  • 34
    • 0037159243 scopus 로고    scopus 로고
    • Coupling of GTP hydrolysis by elongation factor G to translocation and factor recycling on the ribosome
    • Katunin VI, Savelsbergh A, Rodnina MV, Wintermeyer W, (2002) Coupling of GTP hydrolysis by elongation factor G to translocation and factor recycling on the ribosome. Biochemistry 41: 12806-12812.
    • (2002) Biochemistry , vol.41 , pp. 12806-12812
    • Katunin, V.I.1    Savelsbergh, A.2    Rodnina, M.V.3    Wintermeyer, W.4
  • 35
    • 0345120596 scopus 로고    scopus 로고
    • The lipoate synthase from Escherichia coli is an iron-sulfur protein
    • Ollagnier-de Choudens S, Fontecave M, (1999) The lipoate synthase from Escherichia coli is an iron-sulfur protein. FEBS Lett 453: 25-28.
    • (1999) FEBS Lett , vol.453 , pp. 25-28
    • Ollagnier-de Choudens, S.1    Fontecave, M.2
  • 36
    • 14844317304 scopus 로고    scopus 로고
    • Mechanistic investigations of lipoic acid biosynthesis in Escherichia coli: both sulfur atoms in lipoic acid are contributed by the same lipoyl synthase polypeptide
    • Cicchillo RM, Booker SJ, (2005) Mechanistic investigations of lipoic acid biosynthesis in Escherichia coli: both sulfur atoms in lipoic acid are contributed by the same lipoyl synthase polypeptide. J Am Chem Soc 127: 2860-2861.
    • (2005) J Am Chem Soc , vol.127 , pp. 2860-2861
    • Cicchillo, R.M.1    Booker, S.J.2
  • 37
    • 26444504579 scopus 로고    scopus 로고
    • Function, attachment and synthesis of lipoic acid in Escherichia coli
    • Cronan JE, Zhao X, Jiang Y, (2005) Function, attachment and synthesis of lipoic acid in Escherichia coli. Adv Microb Physiol 50: 103-146.
    • (2005) Adv Microb Physiol , vol.50 , pp. 103-146
    • Cronan, J.E.1    Zhao, X.2    Jiang, Y.3
  • 38
    • 34848890388 scopus 로고    scopus 로고
    • Lipoic acid and N-acetyl cysteine decrease mitochondrial-related oxidative stress in Alzheimer disease patient fibroblasts
    • Moreira PI, Harris PL, Zhu X, Santos MS, Oliveira CR, et al. (2007) Lipoic acid and N-acetyl cysteine decrease mitochondrial-related oxidative stress in Alzheimer disease patient fibroblasts. J Alzheimers Dis 12: 195-206.
    • (2007) J Alzheimers Dis , vol.12 , pp. 195-206
    • Moreira, P.I.1    Harris, P.L.2    Zhu, X.3    Santos, M.S.4    Oliveira, C.R.5
  • 39
    • 46849096052 scopus 로고    scopus 로고
    • Beneficial effect of alpha-lipoic acid on lipopolysaccharide-induced oxidative stress in bronchoalveolar lavage fluid
    • Goraca A, Skibska B, (2008) Beneficial effect of alpha-lipoic acid on lipopolysaccharide-induced oxidative stress in bronchoalveolar lavage fluid. J Physiol Pharmacol 59: 379-386.
    • (2008) J Physiol Pharmacol , vol.59 , pp. 379-386
    • Goraca, A.1    Skibska, B.2
  • 40
    • 65949106570 scopus 로고    scopus 로고
    • Effect of alpha-lipoic acid on LPS-induced oxidative stress in the heart
    • Goraca A, Piechota A, Huk-Kolega H, (2009) Effect of alpha-lipoic acid on LPS-induced oxidative stress in the heart. J Physiol Pharmacol 60: 61-68.
    • (2009) J Physiol Pharmacol , vol.60 , pp. 61-68
    • Goraca, A.1    Piechota, A.2    Huk-Kolega, H.3
  • 41
    • 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
    • Kaasen I, McDougall J, Strom AR, (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.
    • (1994) Gene , vol.145 , pp. 9-15
    • Kaasen, I.1    McDougall, J.2    Strom, A.R.3
  • 42
    • 0026030667 scopus 로고
    • Synthesis, accumulation, and excretion of trehalose in osmotically stressed Escherichia coli K-12 strains: influence of amber suppressors and function of the periplasmic trehalase
    • Styrvold OB, Strom AR, (1991) Synthesis, accumulation, and excretion of trehalose in osmotically stressed Escherichia coli K-12 strains: influence of amber suppressors and function of the periplasmic trehalase. J Bacteriol 173: 1187-1192.
    • (1991) J Bacteriol , vol.173 , pp. 1187-1192
    • Styrvold, O.B.1    Strom, A.R.2
  • 43
    • 0027166941 scopus 로고
    • Trehalose metabolism in Escherichia coli: stress protection and stress regulation of gene expression
    • Strom AR, Kaasen I, (1993) Trehalose metabolism in Escherichia coli: stress protection and stress regulation of gene expression. Mol Microbiol 8: 205-210.
    • (1993) Mol Microbiol , vol.8 , pp. 205-210
    • Strom, A.R.1    Kaasen, I.2
  • 45
    • 0035968318 scopus 로고    scopus 로고
    • Trehalose accumulation during cellular stress protects cells and cellular proteins from damage by oxygen radicals
    • Benaroudj N, Lee DH, Goldberg AL, (2001) Trehalose accumulation during cellular stress protects cells and cellular proteins from damage by oxygen radicals. J Biol Chem 276: 24261-24267.
    • (2001) J Biol Chem , vol.276 , pp. 24261-24267
    • Benaroudj, N.1    Lee, D.H.2    Goldberg, A.L.3
  • 46
    • 0035324440 scopus 로고    scopus 로고
    • Oxidative stress and mechanisms of protection against it in bacteria
    • Lushchak VI, (2001) Oxidative stress and mechanisms of protection against it in bacteria. Biochemistry (Mosc) 66: 476-489.
    • (2001) Biochemistry (Mosc) , vol.66 , pp. 476-489
    • Lushchak, V.I.1
  • 47
    • 84856224288 scopus 로고    scopus 로고
    • Central carbon metabolism influences fidelity of DNA replication in Escherichia coli
    • Maciag M, Nowicki D, Szalewska-Palasz A, Wegrzyn G, (2012) Central carbon metabolism influences fidelity of DNA replication in Escherichia coli. Mutat Res 731: 99-106.
    • (2012) Mutat Res , vol.731 , pp. 99-106
    • Maciag, M.1    Nowicki, D.2    Szalewska-Palasz, A.3    Wegrzyn, G.4
  • 48
    • 79953166468 scopus 로고    scopus 로고
    • Genetic response to metabolic fluctuations: correlation between central carbon metabolism and DNA replication in Escherichia coli
    • Maciag M, Nowicki D, Janniere L, Szalewska-Palasz A, Wegrzyn G, (2011) Genetic response to metabolic fluctuations: correlation between central carbon metabolism and DNA replication in Escherichia coli. Microb Cell Fact 10: 19.
    • (2011) Microb Cell Fact , vol.10 , pp. 19
    • Maciag, M.1    Nowicki, D.2    Janniere, L.3    Szalewska-Palasz, A.4    Wegrzyn, G.5
  • 49
    • 0037085010 scopus 로고    scopus 로고
    • The molecular mechanism of ATP synthesis by F1F0-ATP synthase
    • Senior AE, Nadanaciva S, Weber J, (2002) The molecular mechanism of ATP synthesis by F1F0-ATP synthase. Biochim Biophys Acta 1553: 188-211.
    • (2002) Biochim Biophys Acta , vol.1553 , pp. 188-211
    • Senior, A.E.1    Nadanaciva, S.2    Weber, J.3
  • 50
    • 0027508716 scopus 로고
    • Role of Clp protease subunits in degradation of carbon starvation proteins in Escherichia coli
    • Damerau K, St John AC, (1993) Role of Clp protease subunits in degradation of carbon starvation proteins in Escherichia coli. J Bacteriol 175: 53-63.
    • (1993) J Bacteriol , vol.175 , pp. 53-63
    • Damerau, K.1    St John, A.C.2
  • 51
    • 0029852402 scopus 로고    scopus 로고
    • Degradation by proteases Lon, Clp and HtrA, of Escherichia coli proteins aggregated in vivo by heat shock; HtrA protease action in vivo and in vitro
    • Laskowska E, Kuczynska-Wisnik D, Skorko-Glonek J, Taylor A, (1996) Degradation by proteases Lon, Clp and HtrA, of Escherichia coli proteins aggregated in vivo by heat shock; HtrA protease action in vivo and in vitro. Mol Microbiol 22: 555-571.
    • (1996) Mol Microbiol , vol.22 , pp. 555-571
    • Laskowska, E.1    Kuczynska-Wisnik, D.2    Skorko-Glonek, J.3    Taylor, A.4
  • 52
    • 0030033933 scopus 로고    scopus 로고
    • Regulation of Escherichia coli starvation sigma factor (sigma s) by ClpXP protease
    • Schweder T, Lee KH, Lomovskaya O, Matin A, (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
  • 53
    • 0031884182 scopus 로고    scopus 로고
    • Regulation of proteolysis of the stationary-phase sigma factor RpoS
    • Zhou Y, Gottesman S, (1998) Regulation of proteolysis of the stationary-phase sigma factor RpoS. J Bacteriol 180: 1154-1158.
    • (1998) J Bacteriol , vol.180 , pp. 1154-1158
    • Zhou, Y.1    Gottesman, S.2
  • 54
    • 0346882657 scopus 로고    scopus 로고
    • PepN is the major aminopeptidase in Escherichia coli: insights on substrate specificity and role during sodium-salicylate-induced stress
    • Chandu D, Nandi D, (2003) PepN is the major aminopeptidase in Escherichia coli: insights on substrate specificity and role during sodium-salicylate-induced stress. Microbiology 149: 3437-3447.
    • (2003) Microbiology , vol.149 , pp. 3437-3447
    • Chandu, D.1    Nandi, D.2
  • 55
    • 33846013178 scopus 로고    scopus 로고
    • Characterization and role of Peptidase N from Salmonella enterica serovar Typhimurium
    • Kumar A, Nandi D, (2007) Characterization and role of Peptidase N from Salmonella enterica serovar Typhimurium. Biochem Biophys Res Commun 353: 706-712.
    • (2007) Biochem Biophys Res Commun , vol.353 , pp. 706-712
    • Kumar, A.1    Nandi, D.2
  • 56
    • 57149093203 scopus 로고    scopus 로고
    • FKBP family proteins: immunophilins with versatile biological functions
    • Kang CB, Hong Y, Dhe-Paganon S, Yoon HS, (2008) FKBP family proteins: immunophilins with versatile biological functions. Neurosignals 16: 318-325.
    • (2008) Neurosignals , vol.16 , pp. 318-325
    • Kang, C.B.1    Hong, Y.2    Dhe-Paganon, S.3    Yoon, H.S.4
  • 57
    • 0026601663 scopus 로고
    • Proteases and protein degradation in Escherichia coli
    • Maurizi MR, (1992) Proteases and protein degradation in Escherichia coli. Experientia 48: 178-201.
    • (1992) Experientia , vol.48 , pp. 178-201
    • Maurizi, M.R.1
  • 58
    • 72949124219 scopus 로고    scopus 로고
    • Sense and sensibility: flagellum-mediated gene regulation
    • Anderson JK, Smith TG, Hoover TR, (2010) Sense and sensibility: flagellum-mediated gene regulation. Trends Microbiol 18: 30-37.
    • (2010) Trends Microbiol , vol.18 , pp. 30-37
    • Anderson, J.K.1    Smith, T.G.2    Hoover, T.R.3
  • 59
    • 0033787084 scopus 로고    scopus 로고
    • A new ABC transporter mediating the detachment of lipid-modified proteins from membranes
    • Yakushi T, Masuda K, Narita S, Matsuyama S, Tokuda H, (2000) A new ABC transporter mediating the detachment of lipid-modified proteins from membranes. Nat Cell Biol 2: 212-218.
    • (2000) Nat Cell Biol , vol.2 , pp. 212-218
    • Yakushi, T.1    Masuda, K.2    Narita, S.3    Matsuyama, S.4    Tokuda, H.5
  • 60
    • 0036175948 scopus 로고    scopus 로고
    • Disruption of lolCDE, encoding an ATP-binding cassette transporter, is lethal for Escherichia coli and prevents release of lipoproteins from the inner membrane
    • Narita S, Tanaka K, Matsuyama S, Tokuda H, (2002) Disruption of lolCDE, encoding an ATP-binding cassette transporter, is lethal for Escherichia coli and prevents release of lipoproteins from the inner membrane. J Bacteriol 184: 1417-1422.
    • (2002) J Bacteriol , vol.184 , pp. 1417-1422
    • Narita, S.1    Tanaka, K.2    Matsuyama, S.3    Tokuda, H.4
  • 61
    • 0038723310 scopus 로고    scopus 로고
    • A mutation in the membrane subunit of an ABC transporter LolCDE complex causing outer membrane localization of lipoproteins against their inner membrane-specific signals
    • Narita S, Kanamaru K, Matsuyama S, Tokuda H, (2003) A mutation in the membrane subunit of an ABC transporter LolCDE complex causing outer membrane localization of lipoproteins against their inner membrane-specific signals. Mol Microbiol 49: 167-177.
    • (2003) Mol Microbiol , vol.49 , pp. 167-177
    • Narita, S.1    Kanamaru, K.2    Matsuyama, S.3    Tokuda, H.4
  • 62
    • 79959523746 scopus 로고    scopus 로고
    • Traffic jam at the bacterial sec translocase: targeting the SecA nanomotor by small-molecule inhibitors
    • Segers K, Anne J, (2011) Traffic jam at the bacterial sec translocase: targeting the SecA nanomotor by small-molecule inhibitors. Chem Biol 18: 685-698.
    • (2011) Chem Biol , vol.18 , pp. 685-698
    • Segers, K.1    Anne, J.2
  • 63
    • 80053229280 scopus 로고    scopus 로고
    • The superoxide dismutase SodA is targeted to the periplasm in a SecA-dependent manner by a novel mechanism
    • Krehenbrink M, Edwards A, Downie JA, (2011) The superoxide dismutase SodA is targeted to the periplasm in a SecA-dependent manner by a novel mechanism. Mol Microbiol 82: 164-179.
    • (2011) Mol Microbiol , vol.82 , pp. 164-179
    • Krehenbrink, M.1    Edwards, A.2    Downie, J.A.3
  • 64
    • 78651477706 scopus 로고    scopus 로고
    • Syntheses, structures and antibiotic activities of LpxC inhibitors based on the diacetylene scaffold
    • Liang X, Lee CJ, Chen X, Chung HS, Zeng D, et al. (2011) Syntheses, structures and antibiotic activities of LpxC inhibitors based on the diacetylene scaffold. Bioorg Med Chem 19: 852-860.
    • (2011) Bioorg Med Chem , vol.19 , pp. 852-860
    • Liang, X.1    Lee, C.J.2    Chen, X.3    Chung, H.S.4    Zeng, D.5
  • 65
    • 77955418160 scopus 로고    scopus 로고
    • Assembly of the flagellum and its role in cell morphogenesis in Trypanosoma brucei
    • Vaughan S, (2010) Assembly of the flagellum and its role in cell morphogenesis in Trypanosoma brucei. Curr Opin Microbiol 13: 453-458.
    • (2010) Curr Opin Microbiol , vol.13 , pp. 453-458
    • Vaughan, S.1
  • 66
    • 77956546407 scopus 로고    scopus 로고
    • Genetic and functional analyses of the mob operon on conjugative transposon CTn341 from Bacteroides spp
    • Peed L, Parker AC, Smith CJ, (2010) Genetic and functional analyses of the mob operon on conjugative transposon CTn341 from Bacteroides spp. J Bacteriol 192: 4643-4650.
    • (2010) J Bacteriol , vol.192 , pp. 4643-4650
    • Peed, L.1    Parker, A.C.2    Smith, C.J.3
  • 67
  • 68
    • 0034977251 scopus 로고    scopus 로고
    • Genome-wide transcriptional profiling of the Escherichia coli responses to superoxide stress and sodium salicylate
    • Pomposiello PJ, Bennik MH, Demple B, (2001) Genome-wide transcriptional profiling of the Escherichia coli responses to superoxide stress and sodium salicylate. J Bacteriol 183: 3890-3902.
    • (2001) J Bacteriol , vol.183 , pp. 3890-3902
    • Pomposiello, P.J.1    Bennik, M.H.2    Demple, B.3
  • 69
    • 38649119145 scopus 로고    scopus 로고
    • Real-time PCR determination of rRNA gene copy number: absolute and relative quantification assays with Escherichia coli
    • Lee C, Lee S, Shin SG, Hwang S, (2008) Real-time PCR determination of rRNA gene copy number: absolute and relative quantification assays with Escherichia coli. Appl Microbiol Biotechnol 78: 371-376.
    • (2008) Appl Microbiol Biotechnol , vol.78 , pp. 371-376
    • Lee, C.1    Lee, S.2    Shin, S.G.3    Hwang, S.4


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