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Volumn 12, Issue 3, 2013, Pages 297-310

Indole: A novel signaling molecule and its applications

Author keywords

Biofilm; Indole signaling; Multidrug efflux pump; Plasmid stability; Tryptophanase

Indexed keywords

7 FLUOROINDOLE; INDOLE; INDOLEACETIC ACID; TRYPTOPHANASE; UNCLASSIFIED DRUG;

EID: 84886041845     PISSN: 09725849     EISSN: 09750967     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (27)

References (133)
  • 1
    • 0029051543 scopus 로고
    • The bacterial 'enigma': Cracking the code of cell-cell communication
    • Salmond G P, Bycroft B W, Stewart G S&Williams P,. The bacterial 'enigma': Cracking the code of cell-cell communication, Mol Microbiol, 16 (1995) 615-624.
    • (1995) Mol Microbiol , vol.16 , pp. 615-624
    • Salmond, G.P.1    Bycroft, B.W.2    Stewart, G.S.3    Williams, P.4
  • 2
    • 0027479479 scopus 로고
    • Agrobacterium conjugation and gene regulation by N-acyl-homoserine lactones
    • Zhang L, Murphy P J, Kerr A&Tate M E,. Agrobacterium conjugation and gene regulation by N-acyl-homoserine lactones, Nature (Lond), 362 (1993) 446-448.
    • (1993) Nature (Lond) , vol.362 , pp. 446-448
    • Zhang, L.1    Murphy, P.J.2    Kerr, A.3    Tate, M.E.4
  • 3
    • 0029959768 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular peptide factor that affects two different developmental pathways in Bacillus subtilis
    • Solomon J M, Lazazzera B A&Grossman A D,. Purification and characterization of an extracellular peptide factor that affects two different developmental pathways in Bacillus subtilis, Genes Dev, 10 (1996) 2014-2024.
    • (1996) Genes Dev , vol.10 , pp. 2014-2024
    • Solomon, J.M.1    Lazazzera, B.A.2    Grossman, A.D.3
  • 4
    • 0025883573 scopus 로고
    • Extracellular complementation of a developmental mutation implicates a small sporulation protein in aerial mycelium formation by S. coelicolor
    • Willey J, Santamaria R J, Guijarro M, Geistlich&Losick R,. Extracellular complementation of a developmental mutation implicates a small sporulation protein in aerial mycelium formation by S. coelicolor, Cell, 65 (1991) 641-650.
    • (1991) Cell , vol.65 , pp. 641-650
    • Willey, J.1    Santamaria, R.2    Guijarro, J.3    Geistlich, M.4    Losick, R.5
  • 5
    • 0027252653 scopus 로고
    • A small diffusible signal molecule is responsible for the global control of virulence and exoenzyme production in the plant pathogen Erwinia carotovora
    • Pirhonen M, Flego D, Heikinheimo R&Palva E,. A small diffusible signal molecule is responsible for the global control of virulence and exoenzyme production in the plant pathogen Erwinia carotovora, EMBO J, 12 (1993) 2467-2476.
    • (1993) EMBO J , vol.12 , pp. 2467-2476
    • Pirhonen, M.1    Flego, D.2    Heikinheimo, R.3    Palva, E.4
  • 6
    • 0033978494 scopus 로고    scopus 로고
    • Indole-inducible proteins in bacteria suggest membrane and oxidant toxicity
    • Garbe T R, Kobayashi M&Yukawa H,. Indole-inducible proteins in bacteria suggest membrane and oxidant toxicity, Arch Microbiol, 173 (2000) 78-82.
    • (2000) Arch Microbiol , vol.173 , pp. 78-82
    • Garbe, T.R.1    Kobayashi, M.2    Yukawa, H.3
  • 7
    • 0000119739 scopus 로고
    • A contribution to the chemistry of proteids: Part II. The constitution of trypyophan and the action of bacteria upon it
    • Hopkins F G&Cole S W A,. A contribution to the chemistry of proteids: Part II. The constitution of trypyophan and the action of bacteria upon it, J Physiol, 29 (1903) 451-466.
    • (1903) J Physiol , vol.29 , pp. 451-466
    • Hopkins, F.G.1    Cole, S.W.A.2
  • 8
    • 14444288481 scopus 로고
    • Formation and interrelationships of tryptophanase and tryptophan synthetases in Escherichia coli
    • Newton W A&Snell E E,. Formation and interrelationships of tryptophanase and tryptophan synthetases in Escherichia coli, J Bacteriol, 89 (1965) 355-364.
    • (1965) J Bacteriol , vol.89 , pp. 355-364
    • Newton, W.A.1    Snell, E.E.2
  • 9
    • 14544286364 scopus 로고    scopus 로고
    • Indole induces the expression of multidrug exporter genes in Escherichia coli
    • Hirakawa H, Inazumi Y, Masaki T, HirataT&Yamaguchi A,. Indole induces the expression of multidrug exporter genes in Escherichia coli, Mol Microbiol, 55 (2005) 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
  • 10
    • 0036009525 scopus 로고    scopus 로고
    • Isolation of an Escherichia coli strain mutant unable to form biofilm on polystrene and to adhere to human pneumocyte cells: Involvement of tryptophanase
    • Di Martino P, Merieau A, Phillips R, Orange N&Hulen C,. Isolation of an Escherichia coli strain mutant unable to form biofilm on polystrene and to adhere to human pneumocyte cells: Involvement of tryptophanase, Can J Microbiol, 48 (2002) 132-137.
    • (2002) Can J Microbiol , vol.48 , pp. 132-137
    • Di Martino, P.1    Merieau, A.2    Phillips, R.3    Orange, N.4    Hulen, C.5
  • 11
    • 53849116437 scopus 로고    scopus 로고
    • Indole cell signaling occurs primarily at low temperatures in Escherichia coli
    • Lee J, Zhang X S, Hegde M, Bentley W E, Jayaraman A et al,. Indole cell signaling occurs primarily at low temperatures in Escherichia coli, ISME J, 2 (2008) 1007-1023.
    • (2008) ISME J , vol.2 , pp. 1007-1023
    • Lee, J.1    Zhang, X.S.2    Hegde, M.3    Bentley, W.E.4    Jayaraman, A.5
  • 12
    • 0027285737 scopus 로고
    • Induction of myxospores in Stigmatella aurantiaca (myxobacteria): Inducers and inhibitors of myxospore formation, and mutants with a changed sporulation behavior
    • Gerth K, Metzger R&Reichenbach H,. Induction of myxospores in Stigmatella aurantiaca (myxobacteria): Inducers and inhibitors of myxospore formation, and mutants with a changed sporulation behavior, J Gen Microbiol, 139 (1993) 865-871.
    • (1993) J Gen Microbiol , vol.139 , pp. 865-871
    • Gerth, K.1    Metzger, R.2    Reichenbach, H.3
  • 13
    • 0028844453 scopus 로고
    • Localization of the stress protein SP21 in indole induced spores and fruiting bodies and heat shocked cells of Stigmatella aurantiaca
    • Lunsdorf H, Schairer H U&Heidelbach M,. Localization of the stress protein SP21 in indole induced spores and fruiting bodies and heat shocked cells of Stigmatella aurantiaca, J Bacterial, 177 (1995) 7092-7099.
    • (1995) J Bacterial , vol.177 , pp. 7092-7099
    • Lunsdorf, H.1    Schairer, H.U.2    Heidelbach, M.3
  • 14
    • 0029809436 scopus 로고    scopus 로고
    • Quorum sensing in Vibrio fischeri: Evidence that S-adenosylmethionine is the amino acid substrate for autoinducer synthesis
    • Henzelka B L&Greenberg E P,. Quorum sensing in Vibrio fischeri: Evidence that S-adenosylmethionine is the amino acid substrate for autoinducer synthesis, J Bacteriol, 178 (1996) 5291-5294.
    • (1996) J Bacteriol , vol.178 , pp. 5291-5294
    • Henzelka, B.L.1    Greenberg, E.P.2
  • 15
    • 0021997246 scopus 로고
    • Diffusion of autoinducer is involved in regulation of the Vibrio fischeri luminescence system
    • Kaplan H B&Greenberg E P,. Diffusion of autoinducer is involved in regulation of the Vibrio fischeri luminescence system, J Bacteriol, 163 (1985) 1210-1214.
    • (1985) J Bacteriol , vol.163 , pp. 1210-1214
    • Kaplan, H.B.1    Greenberg, E.P.2
  • 16
    • 3142764130 scopus 로고    scopus 로고
    • Cell to cell signaling in Escherichia coli and Salmonella enterica
    • Ahmer B M,. Cell to cell signaling in Escherichia coli and Salmonella enterica, Mol Microbiol, 52 (2004) 933-945.
    • (2004) Mol Microbiol , vol.52 , pp. 933-945
    • Ahmer, B.M.1
  • 17
    • 0034810591 scopus 로고    scopus 로고
    • SdiA of Salmonella enterica is a LuxR homolog that detects mixed microbial communities
    • Michael B, Smith J N, Swift S, Hefferon F&Ahmer B M,. SdiA of Salmonella enterica is a LuxR homolog that detects mixed microbial communities, J Bacteriol, 183 (19) (2001) 5733-5742.
    • (2001) J Bacteriol , vol.183 , Issue.19 , pp. 5733-5742
    • Michael, B.1    Smith, J.N.2    Swift, S.3    Hefferon, F.4    Ahmer, B.M.5
  • 18
    • 4243965222 scopus 로고
    • rd edn
    • edited by B D Davis, R Dulbecco, H N Eisen&H S Ginsberg (Harper and Row, Publishers, Inc., Philadelphia, PA, USA)
    • rd edn, edited by B D Davis, R Dulbecco, H N Eisen&H S Ginsberg (Harper and Row, Publishers, Inc., Philadelphia, PA, USA) 1980, 645-672.
    • (1980) , pp. 645-672
    • Sonnenworth, A.C.1
  • 19
    • 0016418469 scopus 로고
    • Tryptophanase: Structure, catalytic activities and mechanism of action
    • Snell E E,. Tryptophanase: Structure, catalytic activities and mechanism of action, Adv Enzymol Relat Areas Mol Bio, 42 (1975) 287-333.
    • (1975) Adv Enzymol Relat Areas Mol Bio , vol.42 , pp. 287-333
    • Snell, E.E.1
  • 20
    • 0026006958 scopus 로고
    • Physiological studies of tryptophan transport and tryptophanase operon induction in Escherichia coli
    • Yanofusky C, Horn V&Gollnick P,. Physiological studies of tryptophan transport and tryptophanase operon induction in Escherichia coli, J Bacteriol, 173 (1991) 6009-6017.
    • (1991) J Bacteriol , vol.173 , pp. 6009-6017
    • Yanofusky, C.1    Horn, V.2    Gollnick, P.3
  • 22
    • 0037690463 scopus 로고    scopus 로고
    • Origins of root-mediated pH changes in the rhizosphere and their responses to environmental constraints: A review
    • Hinsinger P, Plassard C, Tang C X&Jaillard B,. Origins of root-mediated pH changes in the rhizosphere and their responses to environmental constraints: A review, Plant Soil, 248 (2003) 43-59.
    • (2003) Plant Soil , vol.248 , pp. 43-59
    • Hinsinger, P.1    Plassard, C.2    Tang, C.X.3    Jaillard, B.4
  • 23
    • 30744454039 scopus 로고    scopus 로고
    • YdgG (TqsA) controls biofilm formation in Escherichia coli K-12 through autoinducer 2 transport
    • Herberg M, Kaye I K, Peti W&Wood T K,. YdgG (TqsA) controls biofilm formation in Escherichia coli K-12 through autoinducer 2 transport, J Bacteriol, 188 (2006) 587-598.
    • (2006) J Bacteriol , vol.188 , pp. 587-598
    • Herberg, M.1    Kaye, I.K.2    Peti, W.3    Wood, T.K.4
  • 24
    • 0035087832 scopus 로고    scopus 로고
    • Multidrug efflux pumps and antimicrobial resistance in Pseudomonas aeruginosa and related organisms
    • Poole K,. Multidrug efflux pumps and antimicrobial resistance in Pseudomonas aeruginosa and related organisms, J Mol Microbiol Biotechnol, 3 (2001) 255-264.
    • (2001) J Mol Microbiol Biotechnol , vol.3 , pp. 255-264
    • Poole, K.1
  • 25
    • 77953206694 scopus 로고    scopus 로고
    • Indole as an intercellular signal in microbial communities
    • Lee J&Lee J,. Indole as an intercellular signal in microbial communities, FEMS Microbiol Rev, 34 (2010) 426-444.
    • (2010) FEMS Microbiol Rev , vol.34 , pp. 426-444
    • Lee, J.1    Lee, J.2
  • 26
    • 66149128846 scopus 로고    scopus 로고
    • Indole acts as an extracellular cue regulating gene expression in Vibrio cholera
    • Mueller R S, Beyhan S, Saini S G, Yildiz F H&Bartlett D H,. Indole acts as an extracellular cue regulating gene expression in Vibrio cholera, J Bacteriol, 191 (2009) 3504-3516.
    • (2009) J Bacteriol , vol.191 , pp. 3504-3516
    • Mueller, R.S.1    Beyhan, S.2    Saini, S.G.3    Yildiz, F.H.4    Bartlett, D.H.5
  • 27
    • 0031974011 scopus 로고    scopus 로고
    • The tryptophanase gene cluster of Haemophilus influenzae type b: Evidence for horizontal gene transfer
    • Martin K, Morlin G, Smith A, Nordyke A, Eisenstark A et al,. The tryptophanase gene cluster of Haemophilus influenzae type b: Evidence for horizontal gene transfer, J Bacteriol, 180 (1998) 107-118.
    • (1998) J Bacteriol , vol.180 , pp. 107-118
    • Martin, K.1    Morlin, G.2    Smith, A.3    Nordyke, A.4    Eisenstark, A.5
  • 29
    • 0035798158 scopus 로고    scopus 로고
    • Fungal auxin antagonist hypaphorine competitively inhibits indole-3-acetic acid-dependent superoxide generation by horse radish peroxidase
    • Kawano T, Kawano N, Hosoya H&Lapeyrie F,. Fungal auxin antagonist hypaphorine competitively inhibits indole-3-acetic acid-dependent superoxide generation by horse radish peroxidase, Biochem Biophys Res Commun, 288 (2001) 546-551.
    • (2001) Biochem Biophys Res Commun , vol.288 , pp. 546-551
    • Kawano, T.1    Kawano, N.2    Hosoya, H.3    Lapeyrie, F.4
  • 30
    • 0005548147 scopus 로고
    • Bacterial dissimilation of indole acetic acid- New route of breakdown of the indole nucleus
    • Procter M H,. Bacterial dissimilation of indole acetic acid- New route of breakdown of the indole nucleus, Nature (Lond), 181 (1958) 1345-1345.
    • (1958) Nature (Lond) , vol.181 , pp. 1345-1345
    • Procter, M.H.1
  • 31
    • 18444366567 scopus 로고
    • Studies on destruction of indole-3-acetic acid by a species of Arthrobacter IV. Decomposition products
    • Mino Y,. Studies on destruction of indole-3-acetic acid by a species of Arthrobacter IV. Decomposition products, Plant Cell Physiol, 11 (1970) 129-138.
    • (1970) Plant Cell Physiol , vol.11 , pp. 129-138
    • Mino, Y.1
  • 32
    • 18444393086 scopus 로고    scopus 로고
    • Uilization of the plant hormone Indole-3-acetic acid for growth by Pseudomonas putida strain 1290
    • Leveau J H J&Lindlow S E,. Uilization of the plant hormone Indole-3-acetic acid for growth by Pseudomonas putida strain 1290, Appl Environ Microbiol, 71 (2005) 2365-2371.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 2365-2371
    • Leveau, J.H.J.1    Lindlow, S.E.2
  • 33
    • 33746300232 scopus 로고    scopus 로고
    • Auxin transport: A field in flux
    • Kramer E M&Bennett M J,. Auxin transport: A field in flux, Trends Plant Sci, 11 (1999) 382-386.
    • (1999) Trends Plant Sci , vol.11 , pp. 382-386
    • Kramer, E.M.1    Bennett, M.J.2
  • 34
    • 0030027987 scopus 로고    scopus 로고
    • Comparison of mechanisms controlling uptake and accumulation of 2,4-dichlorophenoxy acetic acid, naphthalene-1-acetic acid, and indole-3-acetic acid in suspension-cultured tobacco cells
    • Delbarre A, Muller P, ImhoffV&Guern J,. Comparison of mechanisms controlling uptake and accumulation of 2,4-dichlorophenoxy acetic acid, naphthalene-1-acetic acid, and indole-3-acetic acid in suspension-cultured tobacco cells, Planta, 198 (1996) 532-541.
    • (1996) Planta , vol.198 , pp. 532-541
    • Delbarre, A.1    Muller, P.2    Imhoff, V.3    Guern, J.4
  • 35
    • 33845708038 scopus 로고    scopus 로고
    • Indole signaling contributes to the stable maintenance of Escherichia coli multicopy plasmids
    • Chant E L&Summers D K,. Indole signaling contributes to the stable maintenance of Escherichia coli multicopy plasmids, Mol Microbiol, 63 (2007) 35-43.
    • (2007) Mol Microbiol , vol.63 , pp. 35-43
    • Chant, E.L.1    Summers, D.K.2
  • 36
    • 62149113666 scopus 로고    scopus 로고
    • Reconfiguring the quorum-sensing regulator sdiA of Escherichia coli to control biofilm formation via indole and N-acylhomoserine lactones
    • Lee J, Maeda T, Hong S H&Wood T K,. Reconfiguring the quorum-sensing regulator sdiA of Escherichia coli to control biofilm formation via indole and N-acylhomoserine lactones, Appl Environ Microbiol, 75 (2009) 1703-1716.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 1703-1716
    • Lee, J.1    Maeda, T.2    Hong, S.H.3    Wood, T.K.4
  • 37
    • 0027422093 scopus 로고
    • Two related recombinases are required for site-specific recombination at dif and cer in E. coli K12
    • Blakely G, May G, McCulloch R, Arciszewska L K, Burke M et al,. Two related recombinases are required for site-specific recombination at dif and cer in E. coli K12, Cell, 75 (1993) 351-361.
    • (1993) Cell , vol.75 , pp. 351-361
    • Blakely, G.1    May, G.2    McCulloch, R.3    Arciszewska, L.K.4    Burke, M.5
  • 38
    • 0037053345 scopus 로고    scopus 로고
    • Analysis of tryptophanase operon expression in vitro: Accumulation of TnaC-peptidyl-tRNA in a release factor 2-depleted S-30 extract prevents Rho factor action, simulating induction
    • Gong F&Yanofsky C,. Analysis of tryptophanase operon expression in vitro: Accumulation of TnaC-peptidyl-tRNA in a release factor 2-depleted S-30 extract prevents Rho factor action, simulating induction, J Biol Chem, 277 (2002) 17095-17100.
    • (2002) J Biol Chem , vol.277 , pp. 17095-17100
    • Gong, F.1    Yanofsky, C.2
  • 39
    • 51149093453 scopus 로고    scopus 로고
    • Diffusible signals and interspecies communication in bacteria
    • Ryan R P&Dow J M,. Diffusible signals and interspecies communication in bacteria, Microbiology, 154 (2008) 1845-1858.
    • (2008) Microbiology , vol.154 , pp. 1845-1858
    • Ryan, R.P.1    Dow, J.M.2
  • 40
    • 0027418427 scopus 로고
    • Indole acetic acid production by the rhizosphere bacterium Azospirillum brasilense Cd under in vitro conditions
    • Omay S H, Schmidt W A Martin P&Bangerth F,. Indole acetic acid production by the rhizosphere bacterium Azospirillum brasilense Cd under in vitro conditions, Can J Microbiol, 39 (1993) 187-192.
    • (1993) Can J Microbiol , vol.39 , pp. 187-192
    • Omay, S.H.1    Schmidt, W.A.2    Martin, P.3    Bangerth, F.4
  • 41
    • 0028872551 scopus 로고
    • Occurrence of enzymes involved in biosynthesis of indole-3-acetic acid from indole-3-acetonitrile in plant-associated bacteria, Agrobacterium and Rhizobium
    • Kobayashi M, Suzuki T, Fujita T, Masuda M&Shimizu S,. Occurrence of enzymes involved in biosynthesis of indole-3-acetic acid from indole-3-acetonitrile in plant-associated bacteria, Agrobacterium and Rhizobium, Proc Natl Acad Sci USA, 92 (1995) 714-718.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 714-718
    • Kobayashi, M.1    Suzuki, T.2    Fujita, T.3    Masuda, M.4    Shimizu, S.5
  • 42
    • 0029804964 scopus 로고    scopus 로고
    • Cloning and characterization of a locus encoding an indole pyruvate decarboxylase involved in indole-3-acetic acid synthesis in Erwinia herbicola
    • Brandl M T&Lindow S E,. Cloning and characterization of a locus encoding an indole pyruvate decarboxylase involved in indole-3-acetic acid synthesis in Erwinia herbicola, Appl Environ Microbiol, 62 (1996) 4121-4128.
    • (1996) Appl Environ Microbiol , vol.62 , pp. 4121-4128
    • Brandl, M.T.1    Lindow, S.E.2
  • 43
    • 0026050912 scopus 로고
    • Indole-3-acetic-acid (IAA) synthesis in the biocontrol strain CHA0 of Pseudomonas fluorescens-Role of tryptophan side-chain oxidase
    • Oberhansli T, Defago G&Haas D,. Indole-3-acetic-acid (IAA) synthesis in the biocontrol strain CHA0 of Pseudomonas fluorescens-Role of tryptophan side-chain oxidase, J Gen Microbiol, 137 (1991) 2273-2279.
    • (1991) J Gen Microbiol , vol.137 , pp. 2273-2279
    • Oberhansli, T.1    Defago, G.2    Haas, D.3
  • 44
    • 0037324714 scopus 로고    scopus 로고
    • Tales from the underground: Molecular plant-rhizobacteria interactions
    • Persello-Cartieaux F, Nussaume L&Robaglia C,. Tales from the underground: Molecular plant-rhizobacteria interactions, Plant Cell Environ, 26 (2003) 189-199.
    • (2003) Plant Cell Environ , vol.26 , pp. 189-199
    • Persello-Cartieaux, F.1    Nussaume, L.2    Robaglia, C.3
  • 45
    • 0032122522 scopus 로고    scopus 로고
    • Differential involvement of indole-3-acetic acid biosynthetic pathways in pathogenecity and epiphytic fitness of Erwinia herbicola pv. gypsophilae
    • Manulis S, Haviv-Chesner A, Brandle M T, Lindlow S E&Barash I,. Differential involvement of indole-3-acetic acid biosynthetic pathways in pathogenecity and epiphytic fitness of Erwinia herbicola pv. gypsophilae, Mol Plant Microbe Interact, 11 (1998) 634-642.
    • (1998) Mol Plant Microbe Interact , vol.11 , pp. 634-642
    • Manulis, S.1    Haviv-Chesner, A.2    Brandle, M.T.3    Lindlow, S.E.4    Barash, I.5
  • 46
    • 0032519985 scopus 로고    scopus 로고
    • Indole-3-acetic acid biosynthesis by Xanthomonas axonopodis pv. citri is increased in the presence of plant leaf extracts
    • Costacurta A, Mazzafera P&Rosato Y B,. Indole-3-acetic acid biosynthesis by Xanthomonas axonopodis pv. citri is increased in the presence of plant leaf extracts, FEMS Microbiol Lett, 159 (1998) 215-220.
    • (1998) FEMS Microbiol Lett , vol.159 , pp. 215-220
    • Costacurta, A.1    Mazzafera, P.2    Rosato, Y.B.3
  • 47
    • 0001605760 scopus 로고
    • Isolation and characterization of Azospirillum mutants excreting high amounts of indoleacetic acid
    • Hartmann A, Singh M&Klingmüller W,. Isolation and characterization of Azospirillum mutants excreting high amounts of indoleacetic acid, Can J Microbiol, 29 (1983) 916-923.
    • (1983) Can J Microbiol , vol.29 , pp. 916-923
    • Hartmann, A.1    Singh, M.2    Klingmüller, W.3
  • 48
    • 0027525856 scopus 로고
    • Nitrilase in biosynthesis of the plant hormone indole-3-acetic acid from indole-3-acetonitrile-Cloning of the Alcaligenes gene and site directed mutagenesis of cysteine residues
    • Kobayashi M, Izui H, Nagasawa T&Yamada H,. Nitrilase in biosynthesis of the plant hormone indole-3-acetic acid from indole-3-acetonitrile-Cloning of the Alcaligenes gene and site directed mutagenesis of cysteine residues, Proc Natl Acad Sci USA, 90 (1993) 247-251.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 247-251
    • Kobayashi, M.1    Izui, H.2    Nagasawa, T.3    Yamada, H.4
  • 49
    • 4544385299 scopus 로고    scopus 로고
    • Flavonoids, NodD1, NodD2, and nod-box NB15 modulate expression of the y4wEFG locus that is required for indole-3-acetic acid synthesis in Rhizobium sp. strain NGR234
    • Theunis M, Kobayashi H, Broughton W J&Prinsen E,. Flavonoids, NodD1, NodD2, and nod-box NB15 modulate expression of the y4wEFG locus that is required for indole-3-acetic acid synthesis in Rhizobium sp. strain NGR234, Mol Plant Microbe Interact, 17 (2004) 1153-1161.
    • (2004) Mol Plant Microbe Interact , vol.17 , pp. 1153-1161
    • Theunis, M.1    Kobayashi, H.2    Broughton, W.J.3    Prinsen, E.4
  • 50
    • 18444389292 scopus 로고
    • Bradyrhizobial indoleacetic acid metabolism and its significance for root nodule development, in Molecular genetics of plant-microbe interactions
    • edited by R Palacios&D P S Verma (APS Press, St. Paul, Minn, USA)
    • Nielsen S V S, Egebo L A&Jochimsen B,. Bradyrhizobial indoleacetic acid metabolism and its significance for root nodule development, in Molecular genetics of plant-microbe interactions, edited by R Palacios&D P S Verma (APS Press, St. Paul, Minn, USA) 1988, 151-152.
    • (1988) , pp. 151-152
    • Nielsen, S.V.S.1    Egebo, L.A.2    Jochimsen, B.3
  • 51
    • 0022617930 scopus 로고
    • Cloning of the gene for indole acetic acid -lysine synthetase from Pseudomonas syrangiae subs.savastoni
    • Glass NL&Kouge Y,. Cloning of the gene for indole acetic acid -lysine synthetase from Pseudomonas syrangiae subs.savastoni, J Bacteriol,166 (1986) 598-603
    • (1986) J Bacteriol , vol.166 , pp. 598-603
    • Glass, N.L.1    Kouge, Y.2
  • 52
    • 0020612907 scopus 로고
    • Expression of naphthalene oxidation genes in Escherichia coli results in the biosynthesis of indigo
    • Ensley B D, Ratzkin B J, Oslund T D, Simon M J, Wackett L P&Gibson D T,. Expression of naphthalene oxidation genes in Escherichia coli results in the biosynthesis of indigo, Science, 222 (1983) 167-169.
    • (1983) Science , vol.222 , pp. 167-169
    • Ensley, B.D.1    Ratzkin, B.J.2    Oslund, T.D.3    Simon, M.J.4    Wackett, L.P.5    Gibson, D.T.6
  • 53
    • 28344455582 scopus 로고    scopus 로고
    • Degradation of indole by enrichment culture and Pseudomonas aeruginosa Gs isolated from mangrove sediment
    • Yin B, Gu J-D&Wan N,. Degradation of indole by enrichment culture and Pseudomonas aeruginosa Gs isolated from mangrove sediment, Int Biodeter Biodegr, 56 (2005) 243-248.
    • (2005) Int Biodeter Biodegr , vol.56 , pp. 243-248
    • Yin, B.1    Gu, J.-D.2    Wan, N.3
  • 54
    • 0031129944 scopus 로고    scopus 로고
    • Biodegradation of indole at high concentration by per solvent fermentation with Pseudomonas sp. ST-200
    • Doukyu N&Aono R,. Biodegradation of indole at high concentration by per solvent fermentation with Pseudomonas sp. ST-200, Extremophiles, 1 (1997) 100-105.
    • (1997) Extremophiles , vol.1 , pp. 100-105
    • Doukyu, N.1    Aono, R.2
  • 55
    • 34047136753 scopus 로고    scopus 로고
    • Cruciferous vegetables and human cancer risk: Epidemiologic evidence and mechanistic basis
    • Higdon J V, Delage B, Williams D E&Dashwood R H,. Cruciferous vegetables and human cancer risk: Epidemiologic evidence and mechanistic basis, Pharmacol Res, 55 (2007) 224-236.
    • (2007) Pharmacol Res , vol.55 , pp. 224-236
    • Higdon, J.V.1    Delage, B.2    Williams, D.E.3    Dashwood, R.H.4
  • 56
    • 68049137923 scopus 로고    scopus 로고
    • Low concentrations of diindolylmethane, a metabolite of indole-3-carbinol, protect against oxidative stress in a BRCA1-dependent manner
    • Fan S, Meng Q, Saha T, Sarkar F H&Rosen E M,. Low concentrations of diindolylmethane, a metabolite of indole-3-carbinol, protect against oxidative stress in a BRCA1-dependent manner, Cancer Res, 69 (2009) 6083-6091.
    • (2009) Cancer Res , vol.69 , pp. 6083-6091
    • Fan, S.1    Meng, Q.2    Saha, T.3    Sarkar, F.H.4    Rosen, E.M.5
  • 57
    • 34948893955 scopus 로고    scopus 로고
    • A novel indole compound that inhibits Pseudomonas aeruginosa growth by targeting mreB is a substrate for MexAB-OprM
    • Robertson G T, Doyle T B, Du Q, Duncan L, Mdluli K E et al,. A novel indole compound that inhibits Pseudomonas aeruginosa growth by targeting mreB is a substrate for MexAB-OprM, J Bacteriol, 189 (2007) 6870-6881.
    • (2007) J Bacteriol , vol.189 , pp. 6870-6881
    • Robertson, G.T.1    Doyle, T.B.2    Du, Q.3    Duncan, L.4    Mdluli, K.E.5
  • 58
    • 0033605031 scopus 로고    scopus 로고
    • Indole positive Vibrio vulnificus isolated from disease outbreaks on a Danish eel farm
    • Dalsgaard I, Hoi L, Siebeling R J&Dalsgaard A,. Indole positive Vibrio vulnificus isolated from disease outbreaks on a Danish eel farm, Dis Aquat Organ, 35 (1999) 187-194.
    • (1999) Dis Aquat Organ , vol.35 , pp. 187-194
    • Dalsgaard, I.1    Hoi, L.2    Siebeling, R.J.3    Dalsgaard, A.4
  • 60
    • 0020117421 scopus 로고
    • Increased indole detection for Pasteurella multocida
    • Clemons K V&Gadberry J L,. Increased indole detection for Pasteurella multocida, J Clin Microbiol, 15 (1982) 731-732.
    • (1982) J Clin Microbiol , vol.15 , pp. 731-732
    • Clemons, K.V.1    Gadberry, J.L.2
  • 61
    • 6044242148 scopus 로고    scopus 로고
    • Molecular basis of the indole-negative reaction in Shigella strains: Extensive damages to the tna operon by insertion sequences
    • Rezwan F, Lan R&Reeves P R,. Molecular basis of the indole-negative reaction in Shigella strains: Extensive damages to the tna operon by insertion sequences, J Bacteriol, 186 (2004) 7460-7465.
    • (2004) J Bacteriol , vol.186 , pp. 7460-7465
    • Rezwan, F.1    Lan, R.2    Reeves, P.R.3
  • 62
    • 0030838574 scopus 로고    scopus 로고
    • Identification of clinical isolates of indole-positive Klebsiella spp. including Klebsiella planticola, and a genetic and molecular analysis of their β-lactamases
    • Liu Y, Mee B J&Mulgrave L,. Identification of clinical isolates of indole-positive Klebsiella spp., including Klebsiella planticola, and a genetic and molecular analysis of their β-lactamases, J Clin Microbiol, 35 (1997) 2365-2369.
    • (1997) J Clin Microbiol , vol.35 , pp. 2365-2369
    • Liu, Y.1    Mee, B.J.2    Mulgrave, L.3
  • 63
    • 0014504162 scopus 로고
    • Tryptophanase in diverse bacterial species
    • DeMoss R D&Moser K,. Tryptophanase in diverse bacterial species, J Bacteriol, 98 (1969) 161-171.
    • (1969) J Bacteriol , vol.98 , pp. 161-171
    • DeMoss, R.D.1    Moser, K.2
  • 64
    • 77953182407 scopus 로고
    • Physiological effects of aconstitutive tryptophanase in Bacillus alvei
    • Hoch J A&DeMoss R D,. Physiological effects of aconstitutive tryptophanase in Bacillus alvei, J Bacteriol, 90 (1965) 604-610.
    • (1965) J Bacteriol , vol.90 , pp. 604-610
    • Hoch, J.A.1    DeMoss, R.D.2
  • 65
    • 0021480444 scopus 로고
    • Relatedness and classification of Streptococcus mutans and 'mutans-like' streptococci
    • Schleifer K H, Kilpper-Balz R, Kraus J&Gehring F,. Relatedness and classification of Streptococcus mutans and 'mutans-like' streptococci, J Dent Res, 63 (1984) 1047-1050.
    • (1984) J Dent Res , vol.63 , pp. 1047-1050
    • Schleifer, K.H.1    Kilpper-Balz, R.2    Kraus, J.3    Gehring, F.4
  • 66
    • 0018771487 scopus 로고
    • Cytotoxic enterotoxin produced by Aeromonas hydrophila: Relationship of toxigenic isolates to diarrheal disease
    • Cumberbatch N, Gurwith M J, Langston C, Sack R B&Brunton J L,. Cytotoxic enterotoxin produced by Aeromonas hydrophila: Relationship of toxigenic isolates to diarrheal disease, Infct Immun, 239 (1979) 829-837.
    • (1979) Infct Immun , vol.239 , pp. 829-837
    • Cumberbatch, N.1    Gurwith, M.J.2    Langston, C.3    Sack, R.B.4    Brunton, J.L.5
  • 67
    • 0032900505 scopus 로고    scopus 로고
    • The phn genes of Burkholderia sp. strain RP007 constitute a divergent gene cluster for polycyclic aromatic hydrocarbon catabolism
    • Laurie A D&Llyod-Jones G,. The phn genes of Burkholderia sp. strain RP007 constitute a divergent gene cluster for polycyclic aromatic hydrocarbon catabolism, J Bacteriol, 181 (1999) 531-540.
    • (1999) J Bacteriol , vol.181 , pp. 531-540
    • Laurie, A.D.1    Llyod-Jones, G.2
  • 68
    • 0024833240 scopus 로고
    • Effect of growth conditions on production of violacein by Chromobacterium violaceum (BB-78 strain)
    • Riveros R, Haun M&Duran N,. Effect of growth conditions on production of violacein by Chromobacterium violaceum (BB-78 strain), Braz J Med Biol Res, 22 (1989) 569-577.
    • (1989) Braz J Med Biol Res , vol.22 , pp. 569-577
    • Riveros, R.1    Haun, M.2    Duran, N.3
  • 69
    • 0033855441 scopus 로고    scopus 로고
    • A novel protein-deamidating enzymes from Chryseobacterium proteolyticum sp. nov., a newly isolated bacterium from soil
    • Yamaguchi S&Yokoe M A,. A novel protein-deamidating enzymes from Chryseobacterium proteolyticum sp. nov., a newly isolated bacterium from soil, Appl Environ Microbiol, 9 (2000) 3337-3343.
    • (2000) Appl Environ Microbiol , vol.9 , pp. 3337-3343
    • Yamaguchi, S.1    Yokoe, M.A.2
  • 70
    • 0016284014 scopus 로고
    • Sensitivity of Citrobacter freundi and Citrobacter koseri to cephalosporins and penicillins
    • Holmes B, King A, Phillip I&Lapage S P,. Sensitivity of Citrobacter freundi and Citrobacter koseri to cephalosporins and penicillins, J Clin Pathol, 27 (1974) 729-733.
    • (1974) J Clin Pathol , vol.27 , pp. 729-733
    • Holmes, B.1    King, A.2    Phillip, I.3    Lapage, S.P.4
  • 72
    • 0015075476 scopus 로고
    • R-B enteric differential system for identification of Enterobacteriaceae
    • Smith P B, Rhoden D L, Tomfohrde K M, Dunn C R, Balows A et al,. R-B enteric differential system for identification of Enterobacteriaceae, Appl Microbiol, 21 (1971) 1036-1039.
    • (1971) Appl Microbiol , vol.21 , pp. 1036-1039
    • Smith, P.B.1    Rhoden, D.L.2    Tomfohrde, K.M.3    Dunn, C.R.4    Balows, A.5
  • 73
    • 77953218909 scopus 로고
    • A modification of the method for determining the production of indole by bacteria
    • Smith T,. A modification of the method for determining the production of indole by bacteria, J Exp Med, 2 (1987) 543-547.
    • (1987) J Exp Med , vol.2 , pp. 543-547
    • Smith, T.1
  • 74
    • 0024440006 scopus 로고
    • Methods for identification of flavobacteria
    • Picket M J,. Methods for identification of flavobacteria, J Clin Microbiol, 27 (1989) 2309-2315.
    • (1989) J Clin Microbiol , vol.27 , pp. 2309-2315
    • Picket, M.J.1
  • 75
    • 0017401553 scopus 로고
    • Fusobacterium necrophorum: Its characteristics and role as an animal pathogen
    • Langworth B F,. Fusobacterium necrophorum: Its characteristics and role as an animal pathogen, Bacteriol Rev, 41 (1977) 373-390.
    • (1977) Bacteriol Rev , vol.41 , pp. 373-390
    • Langworth, B.F.1
  • 76
    • 0017253675 scopus 로고
    • A taxonomic study of the genus Haemophilus, with the proposal of a new species
    • Kilian M,. A taxonomic study of the genus Haemophilus, with the proposal of a new species, J Gen Microbiol, 93 (1976) 9-62.
    • (1976) J Gen Microbiol , vol.93 , pp. 9-62
    • Kilian, M.1
  • 77
    • 0019349159 scopus 로고
    • The biology of Hyphomicrobium and other prosthecate, budding bacteria
    • Moore R L,. The biology of Hyphomicrobium and other prosthecate, budding bacteria, Annu Rev Microbiol, 359 (1981) 567-594.
    • (1981) Annu Rev Microbiol , vol.359 , pp. 567-594
    • Moore, R.L.1
  • 78
    • 0024362786 scopus 로고
    • Transfer of Enterobacter agglomerance (Beijrinck 1988) Ewing and Fife 1972 to Pantoea gen. nov. as Pantoea agglomerans comb. nov. and description of Pantoea dispersa sp. nov.
    • Gavini F, Mergaert J, Beji A, Mielcarek C, Izard D et al,. Transfer of Enterobacter agglomerance (Beijrinck 1988) Ewing and Fife 1972 to Pantoea gen. nov. as Pantoea agglomerans comb. nov. and description of Pantoea dispersa sp. nov., Int J Syst Bacteriol, 39 (1989) 337-345.
    • (1989) Int J Syst Bacteriol , vol.39 , pp. 337-345
    • Gavini, F.1    Mergaert, J.2    Beji, A.3    Mielcarek, C.4    Izard, D.5
  • 79
    • 0025989354 scopus 로고
    • Rapid presumptive identification of black-pigmented Gramnegative anaerobic bacteria by using 4-methylumbelliferone derivatives
    • Moncla B J, Braham P, Rabe L K&Hillier S L,. Rapid presumptive identification of black-pigmented Gramnegative anaerobic bacteria by using 4-methylumbelliferone derivatives, J Clin Microbiol, 29 (1991) 1955-1958.
    • (1991) J Clin Microbiol , vol.29 , pp. 1955-1958
    • Moncla, B.J.1    Braham, P.2    Rabe, L.K.3    Hillier, S.L.4
  • 80
    • 0033786377 scopus 로고    scopus 로고
    • Classification, identification, and clinical significance of Proteus, Provodencia and Morgenella
    • O'Hara C M, Brenner F W&Miller J M,. Classification, identification, and clinical significance of Proteus, Provodencia and Morgenella, Clin Microbiol Rev, 13 (2000) 534-546.
    • (2000) Clin Microbiol Rev , vol.13 , pp. 534-546
    • O'Hara, C.M.1    Brenner, F.W.2    Miller, J.M.3
  • 82
    • 0014529652 scopus 로고
    • Morphological and biochemical differentiation of three types of small oral spirochaetes
    • Socransky S S, Listgarten M, Hubersak C, Cotmore J&Clark A,. Morphological and biochemical differentiation of three types of small oral spirochaetes, J Bacteriol, 98 (1969) 878-882.
    • (1969) J Bacteriol , vol.98 , pp. 878-882
    • Socransky, S.S.1    Listgarten, M.2    Hubersak, C.3    Cotmore, J.4    Clark, A.5
  • 84
    • 0011118274 scopus 로고
    • Isolation of toxigenic strains of Clostridium novyi from soil
    • Nishida S&Nakagawara G,. Isolation of toxigenic strains of Clostridium novyi from soil, J Bacteriol, 88 (1964) 1636-1640.
    • (1964) J Bacteriol , vol.88 , pp. 1636-1640
    • Nishida, S.1    Nakagawara, G.2
  • 85
    • 0017129337 scopus 로고
    • The end products of the metabolism of aromatic amino acids by Clostridia
    • Elsden S R, Hilton M G&Waller J M,. The end products of the metabolism of aromatic amino acids by Clostridia, Arch Microbiol, 107 (1976) 283-288.
    • (1976) Arch Microbiol , vol.107 , pp. 283-288
    • Elsden, S.R.1    Hilton, M.G.2    Waller, J.M.3
  • 86
    • 0032941995 scopus 로고    scopus 로고
    • Formation of hydride-Meisenheimer complexes of picric acid (2,4,6-trinitrophenol) and 2,4-dinitrophenol during mineralization of picric acid by Nocardioides sp. strain CB 22-12
    • Behrend C&Heesche-Wagner K,. Formation of hydride-Meisenheimer complexes of picric acid (2,4,6-trinitrophenol) and 2,4-dinitrophenol during mineralization of picric acid by Nocardioides sp. strain CB 22-12, Appl Environ Microbiol, 65 (1999) 1372-1377.
    • (1999) Appl Environ Microbiol , vol.65 , pp. 1372-1377
    • Behrend, C.1    Heesche-Wagner, K.2
  • 87
    • 6744237460 scopus 로고    scopus 로고
    • Severe infections caused by Propionibacterium acnes: An underestimated pathogen in late postoperative infections
    • Jakab E, Zbinden R, Gubler J, Ruef C, von Graevenitz A et al,. Severe infections caused by Propionibacterium acnes: An underestimated pathogen in late postoperative infections, Yale J Biol Med, 69 (1996) 477-482.
    • (1996) Yale J Biol Med , vol.69 , pp. 477-482
    • Jakab, E.1    Zbinden, R.2    Gubler, J.3    Ruef, C.4    von Graevenitz, A.5
  • 88
    • 5444269195 scopus 로고    scopus 로고
    • Oribacterium sinus gen. nov., sp. nov., with the family 'Lachnospiraceae' (phylum Fimicutes)
    • Carlier J-P, K'ouas G, Bonne I, Lozniewski A&Mory F,. Oribacterium sinus gen. nov., sp. nov., with the family 'Lachnospiraceae' (phylum Fimicutes), Int J Syst Evol Microbiol, 54 (2004) 1611-1615.
    • (2004) Int J Syst Evol Microbiol , vol.54 , pp. 1611-1615
    • Carlier, J.-P.1    K'ouas, G.2    Bonne, I.3    Lozniewski, A.4    Mory, F.5
  • 89
    • 0030053347 scopus 로고    scopus 로고
    • Introduction of a de-novo bioremediation activity into anaerobic granular sludge using the dechlorinating bacterium DCB-2
    • Christiansen N&Ahring B K,. Introduction of a de-novo bioremediation activity into anaerobic granular sludge using the dechlorinating bacterium DCB-2, Antonie van Leeunhoek, 69 (1996) 61-66.
    • (1996) Antonie van Leeunhoek , vol.69 , pp. 61-66
    • Christiansen, N.1    Ahring, B.K.2
  • 90
    • 47249087842 scopus 로고    scopus 로고
    • Discovery of a bacterial gene cluster for catabolism of the plant hormone indole acetic acid
    • Leveau J H J&Gerards S,. Discovery of a bacterial gene cluster for catabolism of the plant hormone indole acetic acid, FEMS Microbiol Ecol, 65 (2008) 238-250.
    • (2008) FEMS Microbiol Ecol , vol.65 , pp. 238-250
    • Leveau, J.H.J.1    Gerards, S.2
  • 91
    • 15444362611 scopus 로고    scopus 로고
    • Biosynthesis of auxin by the Gram-positive phytopathogen Rhodococcus fascians is controlled by compounds specific to infected plant tissues
    • Vandeputte O, Oden S, Mol A, Vereecke D, Goethals K et al,. Biosynthesis of auxin by the Gram-positive phytopathogen Rhodococcus fascians is controlled by compounds specific to infected plant tissues, Appl Environ Microbiol, 71 (2005) 1169-1177.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 1169-1177
    • Vandeputte, O.1    Oden, S.2    Mol, A.3    Vereecke, D.4    Goethals, K.5
  • 92
    • 0043271394 scopus 로고
    • Endogenous indoles and the biosynthesis and metabolism of indole-3-acetic acid in cultures of Rhizobium phaseoli
    • Ernstsen A, Sandberg G, Crozier A&Wheeler C T,. Endogenous indoles and the biosynthesis and metabolism of indole-3-acetic acid in cultures of Rhizobium phaseoli, Planta, 171 (1987) 422-428.
    • (1987) Planta , vol.171 , pp. 422-428
    • Ernstsen, A.1    Sandberg, G.2    Crozier, A.3    Wheeler, C.T.4
  • 93
    • 85007904738 scopus 로고
    • Factors influencing the production and further metabolism of indole-3-acetic acid by Pseudomonas savastonoi
    • Kuo T T&Kosuge T,. Factors influencing the production and further metabolism of indole-3-acetic acid by Pseudomonas savastonoi, J Gen Microbiol, 15 (1969) 51-63.
    • (1969) J Gen Microbiol , vol.15 , pp. 51-63
    • Kuo, T.T.1    Kosuge, T.2
  • 94
    • 0020622839 scopus 로고
    • Degradation of indole by Alcaligenes sp.
    • Claus G&Kutzner H J,. Degradation of indole by Alcaligenes sp., Syst Appl Microbiol, 4 (1983) 169-180.
    • (1983) Syst Appl Microbiol , vol.4 , pp. 169-180
    • Claus, G.1    Kutzner, H.J.2
  • 95
    • 9044222365 scopus 로고
    • The bacterial decomposition of indole acetic acid
    • Tsubokura S, Sakamoto Y&Ichihara K,. The bacterial decomposition of indole acetic acid, J Biochem, 49 (1961) 38-42.
    • (1961) J Biochem , vol.49 , pp. 38-42
    • Tsubokura, S.1    Sakamoto, Y.2    Ichihara, K.3
  • 96
    • 0028785995 scopus 로고
    • Catabolism of indole-3-acetic acid and 4-and 5-chloroindole-3-acetic acids in Bradyrhizobium japonicum
    • Jensen J B, Egsgaard H, Van Onckelen H&Jochimsen B U,. Catabolism of indole-3-acetic acid and 4-and 5-chloroindole-3-acetic acids in Bradyrhizobium japonicum, J Bacteriol, 177 (1995) 5762-5766.
    • (1995) J Bacteriol , vol.177 , pp. 5762-5766
    • Jensen, J.B.1    Egsgaard, H.2    Van Onckelen, H.3    Jochimsen, B.U.4
  • 97
    • 0017692513 scopus 로고
    • Isolation and chatracteristics of a skatole producing Lactobacillus sp. from the bovine rumen
    • Yokoyama M T, Carlson J R&Holdeman L V,. Isolation and chatracteristics of a skatole producing Lactobacillus sp. from the bovine rumen, Appl Environ Microbiol, 34 (1977) 837-842.
    • (1977) Appl Environ Microbiol , vol.34 , pp. 837-842
    • Yokoyama, M.T.1    Carlson, J.R.2    Holdeman, L.V.3
  • 98
    • 0034787723 scopus 로고    scopus 로고
    • Review of microbiological and biochemical effects of skatole on animal production
    • Deslandes B, Gariepy C&Houde A,. Review of microbiological and biochemical effects of skatole on animal production, Livest Prod Sci, 71 (2001) 193-200.
    • (2001) Livest Prod Sci , vol.71 , pp. 193-200
    • Deslandes, B.1    Gariepy, C.2    Houde, A.3
  • 99
    • 0030053413 scopus 로고    scopus 로고
    • Carbazole degradation by Pseudomonas sp. LD2: Metabolic characteristics and the identification of some metabolites
    • Gieg L M, Otter A&Fedorak P M,. Carbazole degradation by Pseudomonas sp. LD2: Metabolic characteristics and the identification of some metabolites, Environ Sci Technol, 30 (1996) 575-585.
    • (1996) Environ Sci Technol , vol.30 , pp. 575-585
    • Gieg, L.M.1    Otter, A.2    Fedorak, P.M.3
  • 100
    • 0029795374 scopus 로고    scopus 로고
    • The β-ketoadipate pathway and the biology of self-identity
    • Harwood C S&Parales R E,. The β-ketoadipate pathway and the biology of self-identity, Ann Rev Microbiol, 50 (1996) 553-590.
    • (1996) Ann Rev Microbiol , vol.50 , pp. 553-590
    • Harwood, C.S.1    Parales, R.E.2
  • 101
    • 0043271394 scopus 로고
    • Endogenous indoles and the biosynthesis and metabolism of indole-3-acetic acid in cultures of Rhizobium phaseoli
    • Ernstsen A, Sandberg G, Crozier A&Wheeler C T,. Endogenous indoles and the biosynthesis and metabolism of indole-3-acetic acid in cultures of Rhizobium phaseoli, Planta, 171 (1987) 422-428.
    • (1987) Planta , vol.171 , pp. 422-428
    • Ernstsen, A.1    Sandberg, G.2    Crozier, A.3    Wheeler, C.T.4
  • 102
    • 0034069085 scopus 로고    scopus 로고
    • Manipulation of hormone biosynthetic genes in transgenic plants
    • Hedden P&Phillips A L,. Manipulation of hormone biosynthetic genes in transgenic plants, Curr Opin Biotechnol, 11 (2000) 130-137.
    • (2000) Curr Opin Biotechnol , vol.11 , pp. 130-137
    • Hedden, P.1    Phillips, A.L.2
  • 103
    • 22344440794 scopus 로고    scopus 로고
    • Electrostatic contributions to indole-lipid interactions
    • Gaede H C, Yau W M&Gawrisch K,. Electrostatic contributions to indole-lipid interactions, J Phys Chem B, 109 (2005) 13014-13023.
    • (2005) J Phys Chem B , vol.109 , pp. 13014-13023
    • Gaede, H.C.1    Yau, W.M.2    Gawrisch, K.3
  • 104
    • 0000712189 scopus 로고
    • Chemistry and physiology of the bound auxins
    • Cohen J D&Bandurski R S,. Chemistry and physiology of the bound auxins, Annu Rev Plant Physiol, 33 (1982) 403-430.
    • (1982) Annu Rev Plant Physiol , vol.33 , pp. 403-430
    • Cohen, J.D.1    Bandurski, R.S.2
  • 105
    • 33744965045 scopus 로고    scopus 로고
    • Indole-3-acetic acid protein conjugates: Novel players in auxin homeostasis
    • Seidel C, Walz A, Park S, Cohen J D&Ludwig-Muller J,. Indole-3-acetic acid protein conjugates: Novel players in auxin homeostasis, Plant Biol, 8 (2006) 340-345.
    • (2006) Plant Biol , vol.8 , pp. 340-345
    • Seidel, C.1    Walz, A.2    Park, S.3    Cohen, J.D.4    Ludwig-Muller, J.5
  • 106
    • 24644464894 scopus 로고    scopus 로고
    • Indole-3-acetic acid: A reciprocal signalling molecule in bacteria-plant interactions
    • Lambrecht M, Okon Y, Vande Broek A&Vanderleyden J,. Indole-3-acetic acid: A reciprocal signalling molecule in bacteria-plant interactions, Trends Microbiol, 298 (2000) 1-3.
    • (2000) Trends Microbiol , vol.298 , pp. 1-3
    • Lambrecht, M.1    Okon, Y.2    Vande Broek, A.3    Vanderleyden, J.4
  • 107
    • 0001590140 scopus 로고
    • Influence of bacterial source of indole-3-acetic acid on root elongation of sugar beet
    • Loper J E, Schroth M N,. Influence of bacterial source of indole-3-acetic acid on root elongation of sugar beet, Phytopathology, 76 (1986) 386-389.
    • (1986) Phytopathology , vol.76 , pp. 386-389
    • Loper, J.E.1    Schroth, M.N.2
  • 108
    • 33645967758 scopus 로고    scopus 로고
    • A plant miRNA contributes to antibacterial resistance by repressing auxin signaling
    • Navarro L, Dunoyer P, Jay F, Arnold B, Dharmasiri N et al,. A plant miRNA contributes to antibacterial resistance by repressing auxin signaling, Science, 312 (2006) 436-439.
    • (2006) Science , vol.312 , pp. 436-439
    • Navarro, L.1    Dunoyer, P.2    Jay, F.3    Arnold, B.4    Dharmasiri, N.5
  • 110
    • 0030048903 scopus 로고    scopus 로고
    • Isolation and characterization of mutants of the plant growth-promoting rhizobacterium Pseudomonas putida CR12-2 that overproduce indole acetic acid
    • Xie H, Pasternak J J&Glick B R,. Isolation and characterization of mutants of the plant growth-promoting rhizobacterium Pseudomonas putida CR12-2 that overproduce indole acetic acid, Curr Microbiol, 32 (1996) 67-71.
    • (1996) Curr Microbiol , vol.32 , pp. 67-71
    • Xie, H.1    Pasternak, J.J.2    Glick, B.R.3
  • 111
    • 0025727999 scopus 로고
    • Stimulation of indole-3-acetic acid production in Rhizobium by flavonoids
    • Prinsen E, Chauvaux N, Schmidt J, John M, Wieneke U et al,. Stimulation of indole-3-acetic acid production in Rhizobium by flavonoids, FEBS Lett, 282(1991) 53-55.
    • (1991) FEBS Lett , vol.282 , pp. 53-55
    • Prinsen, E.1    Chauvaux, N.2    Schmidt, J.3    John, M.4    Wieneke, U.5
  • 112
    • 0141489163 scopus 로고
    • Presence of gibberellin-like substances and their possible role in auxin bioproduction in root nodules and roots of Lupinus luteus L.
    • Dullaart J&Duba L,. Presence of gibberellin-like substances and their possible role in auxin bioproduction in root nodules and roots of Lupinus luteus L., Acta Bot Neerl, 19 (1970) 290-297.
    • (1970) Acta Bot Neerl , vol.19 , pp. 290-297
    • Dullaart, J.1    Duba, L.2
  • 113
    • 33750319399 scopus 로고    scopus 로고
    • Production and metabolism of indole acetic acid in roots and root nodules of Phaseolus mungo
    • Ghosh S&Basu P S,. Production and metabolism of indole acetic acid in roots and root nodules of Phaseolus mungo, Microbiol Res, 161 (2006) 362-366.
    • (2006) Microbiol Res , vol.161 , pp. 362-366
    • Ghosh, S.1    Basu, P.S.2
  • 114
    • 33748065649 scopus 로고    scopus 로고
    • Integrated regulation of the Type III secretion system and other virulence determinants in Ralstonia solanacearum
    • Valls M, Genin S&Boucher C,. Integrated regulation of the Type III secretion system and other virulence determinants in Ralstonia solanacearum, PLoS Pathog, 2 (2006) 798-807.
    • (2006) PLoS Pathog , vol.2 , pp. 798-807
    • Valls, M.1    Genin, S.2    Boucher, C.3
  • 115
    • 0026006958 scopus 로고
    • Physiological studies of tryptophan transport and tryptophanase operon induction in Escherichia coli
    • Yanofusky C, Horn V&Gollnick P,. Physiological studies of tryptophan transport and tryptophanase operon induction in Escherichia coli, J Bacteriol, 173 (1991) 6009-6017.
    • (1991) J Bacteriol , vol.173 , pp. 6009-6017
    • Yanofusky, C.1    Horn, V.2    Gollnick, P.3
  • 116
    • 34347237865 scopus 로고    scopus 로고
    • Indole is an interspecies biofilm signal mediated by SdiA
    • Lee J, Jayaraman A&Wood T K,. Indole is an interspecies biofilm signal mediated by SdiA, BMC Microbiol, 7 (2007) 42.
    • (2007) BMC Microbiol , vol.7 , pp. 42
    • Lee, J.1    Jayaraman, A.2    Wood, T.K.3
  • 117
    • 0037053345 scopus 로고    scopus 로고
    • Analysis of tryptophanase operon expression in vitro: Accumulation of TnaC-peptidyl-tRNA in a release factor 2-depleted S-30 extractprevents Rho-factor action, simulating induction
    • Gong F&Yanofsky C,. Analysis of tryptophanase operon expression in vitro: Accumulation of TnaC-peptidyl-tRNA in a release factor 2-depleted S-30 extractprevents Rho-factor action, simulating induction, J Biol Chem, 277 (2002) 17095-17100.
    • (2002) J Biol Chem , vol.277 , pp. 17095-17100
    • Gong, F.1    Yanofsky, C.2
  • 118
    • 34548500624 scopus 로고    scopus 로고
    • Differential effects of epinephrine, norepinephrine, and indole on Escherichia coli O157:H7 chemotaxis, colonization, and gene expression
    • Bansal T, Englert D, Lee J, Hegde M, Wood T K et al,. Differential effects of epinephrine, norepinephrine, and indole on Escherichia coli O157:H7 chemotaxis, colonization, and gene expression, Infect Immun, 75 (2007) 4597-4607.
    • (2007) Infect Immun , vol.75 , pp. 4597-4607
    • Bansal, T.1    Englert, D.2    Lee, J.3    Hegde, M.4    Wood, T.K.5
  • 119
    • 34250331207 scopus 로고    scopus 로고
    • Indole-3-acetic acid in microbial and microorganism-plant signalling
    • Spaepen S, Vanderleyden J&Remans R,. Indole-3-acetic acid in microbial and microorganism-plant signalling, FEMS Microbiol Rev, 31 (2007) 425-448.
    • (2007) FEMS Microbiol Rev , vol.31 , pp. 425-448
    • Spaepen, S.1    Vanderleyden, J.2    Remans, R.3
  • 120
    • 34447552975 scopus 로고
    • Genes specifying auxin and cytokinin biosynthesis in prokaryotes, in Plant hormones and their role in plant growth and development
    • edited by P J Davies (Kluwer Academic Publishers, Dordrecht, The Netherlands)
    • Morris R O,. Genes specifying auxin and cytokinin biosynthesis in prokaryotes, in Plant hormones and their role in plant growth and development, edited by P J Davies (Kluwer Academic Publishers, Dordrecht, The Netherlands) 1987, 636-656.
    • (1987) , pp. 636-656
    • Morris, R.O.1
  • 122
    • 0034966692 scopus 로고    scopus 로고
    • Indole can act as an extracellular signal in Escherichia coli
    • Wang D, Ding X&Rather P N,. Indole can act as an extracellular signal in Escherichia coli, J Bacteriol, 183 (2001) 4210-4216.
    • (2001) J Bacteriol , vol.183 , pp. 4210-4216
    • Wang, D.1    Ding, X.2    Rather, P.N.3
  • 123
    • 33646092295 scopus 로고    scopus 로고
    • YliH (BssR) and YceP (BssS) regulate Escherichia coli K-12 biofilm formation by influencing cell signaling
    • Domka J, Lee J&Wood T K,. YliH (BssR) and YceP (BssS) regulate Escherichia coli K-12 biofilm formation by influencing cell signaling, Appl Environ Microbiol, 72 (2006) 2449-2459.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 2449-2459
    • Domka, J.1    Lee, J.2    Wood, T.K.3
  • 124
    • 0037076596 scopus 로고    scopus 로고
    • An attractive surface: Gram-negative bacterial biofilms, Sci STKE
    • [DOI: 10.1126/scisignal.1322002re6]
    • Schembri M A, Givskov M&Klemm P,. An attractive surface: Gram-negative bacterial biofilms, Sci STKE, (2002) re6. [DOI: 10.1126/scisignal.1322002re6]
    • (2002)
    • Schembri, M.A.1    Givskov, M.2    Klemm, P.3
  • 125
    • 0037226597 scopus 로고    scopus 로고
    • Contributions of antibiotic penetration, oxygen limitation and low metabolic activity to tolerance of P. aeruginosa biofilms to ciprofloxacin and tobromycin
    • Walters M C III, Roe F, Bugnicourt A, Franklin M J&Stewart P S,. Contributions of antibiotic penetration, oxygen limitation and low metabolic activity to tolerance of P. aeruginosa biofilms to ciprofloxacin and tobromycin, Antimicrob Agents Chemother, 47 (2003) 317-323.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 317-323
    • Walters, M.C.1    Roe, F.2    Bugnicourt, A.3    Franklin, M.J.4    Stewart, P.S.5
  • 126
    • 34247850885 scopus 로고    scopus 로고
    • YcfR (BhsA) influences Escherichia coli biofilm Formation through stress response and surface hydrophobicity
    • Zhang X, Garcia-Contreras R&Wood T K,. YcfR (BhsA) influences Escherichia coli biofilm Formation through stress response and surface hydrophobicity, J Bacteriol, (2007) 3051-3062.
    • (2007) J Bacteriol , pp. 3051-3062
    • Zhang, X.1    Garcia-Contreras, R.2    Wood, T.K.3
  • 127
    • 0034462751 scopus 로고    scopus 로고
    • Alternative transcription factor s B is involved in regulation of biofilm expression in a Staphylococcus aureus mucosal isolate
    • Rachid S, Ohlsen K, Wallner U, Hecker U, Heckker M et al,. Alternative transcription factor s B is involved in regulation of biofilm expression in a Staphylococcus aureus mucosal isolate, J Bacteriol, 182 (2000) 6824-6826.
    • (2000) J Bacteriol , vol.182 , pp. 6824-6826
    • Rachid, S.1    Ohlsen, K.2    Wallner, U.3    Hecker, U.4    Heckker, M.5
  • 128
    • 11144342769 scopus 로고    scopus 로고
    • Trigger factor in Streptococcus mutans is involved in stress tolerence, competence development and biofilm formation
    • Wen Z T, Suntharaligham P, Cvitkovitch D G&Burne R A,. Trigger factor in Streptococcus mutans is involved in stress tolerence, competence development and biofilm formation, Infect Immunol, 7 (2005) 219-225.
    • (2005) Infect Immunol , vol.7 , pp. 219-225
    • Wen, Z.T.1    Suntharaligham, P.2    Cvitkovitch, D.G.3    Burne, R.A.4
  • 129
    • 0035087098 scopus 로고    scopus 로고
    • Global impact of sdiA amplification revealed by comprehensive gene expression profiling of Escherichia coli
    • Wei Y, Lee J M, Smulski D R&LaRossa R A,. Global impact of sdiA amplification revealed by comprehensive gene expression profiling of Escherichia coli, J Bacteriol, 183 (2001) 2265-227.
    • (2001) J Bacteriol , vol.183 , pp. 2265-227
    • Wei, Y.1    Lee, J.M.2    Smulski, D.R.3    LaRossa, R.A.4
  • 130
    • 23844449036 scopus 로고    scopus 로고
    • Cell lysis directed by sigma E in early stationary phase and effect of induction of the rpoE gene on global gene expression in Escherichia coli
    • Kabir M S, Yamashita D, Koyama S, Oshima T, Kurokawa K et al,. Cell lysis directed by sigma E in early stationary phase and effect of induction of the rpoE gene on global gene expression in Escherichia coli, Microbiology, 151 (2005) 2721-2735.
    • (2005) Microbiology , vol.151 , pp. 2721-2735
    • Kabir, M.S.1    Yamashita, D.2    Koyama, S.3    Oshima, T.4    Kurokawa, K.5
  • 131
    • 10644252538 scopus 로고    scopus 로고
    • Differential gene expression shows natural brominated furanones interfere with the autoinducer-2 bacterial signaling system of Escherichia coli
    • Ren D, Bedzyk L A, Ye R W, Thomas S M&Wood T K,. Differential gene expression shows natural brominated furanones interfere with the autoinducer-2 bacterial signaling system of Escherichia coli, Biotechnol Bioeng, 88 (2004) 630-642.
    • (2004) Biotechnol Bioeng , vol.88 , pp. 630-642
    • Ren, D.1    Bedzyk, L.A.2    Ye, R.W.3    Thomas, S.M.4    Wood, T.K.5
  • 132
    • 0032932220 scopus 로고    scopus 로고
    • Acid and base induced proteins during aerobic and anaerobic growth of Escherichia coli revealed by two dimensional gel electrophoresis
    • Blackenhorn D, Philips J&Slonczewski J L,. Acid and base induced proteins during aerobic and anaerobic growth of Escherichia coli revealed by two dimensional gel electrophoresis, J Bacteriol, 181 (1999) 2209-2216.
    • (1999) J Bacteriol , vol.181 , pp. 2209-2216
    • Blackenhorn, D.1    Philips, J.2    Slonczewski, J.L.3
  • 133
    • 0034767798 scopus 로고    scopus 로고
    • Involvement of gacS and rpoS in enhancement of the plant growth-promoting capabilities of Enterobacter cloacae CAL2 and UW4
    • Saleh S S&Glick B R,. Involvement of gacS and rpoS in enhancement of the plant growth-promoting capabilities of Enterobacter cloacae CAL2 and UW4, Can J Microbiol, 47 (2001) 698-705.
    • (2001) Can J Microbiol , vol.47 , pp. 698-705
    • Saleh, S.S.1    Glick, B.R.2


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