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Volumn 9, Issue 12, 2014, Pages

Cellular responses during morphological transformation in Azospirillum brasilense and its flcA knockout mutant

Author keywords

[No Author keywords available]

Indexed keywords

ACETYL COENZYME A ACYLTRANSFERASE; CITRATE SYNTHASE; ENDOPEPTIDASE CLP; GLUTAMATE AMMONIA LIGASE; NITRIC OXIDE SYNTHASE; SUPEROXIDE DISMUTASE; BACTERIAL PROTEIN; CONGO RED; FLCA PROTEIN, AZOSPIRILLUM BRASILENSE; TRANSCRIPTION FACTOR;

EID: 84918561780     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0114435     Document Type: Article
Times cited : (17)

References (91)
  • 1
    • 27444437888 scopus 로고    scopus 로고
    • Inoculation with the plant-growth-promoting rhizobacterium Azospirillum brasilense causes little disturbance in the rhizosphere and rhizoplane of maize (Zea mays)
    • Herschkovitz Y, Lerner A, Davidov Y, Rothballer M, Hartmann A, et al. (2005) Inoculation with the plant-growth-promoting rhizobacterium Azospirillum brasilense causes little disturbance in the rhizosphere and rhizoplane of maize (Zea mays). Microb Ecol 50: 277-288.
    • (2005) Microb Ecol , vol.50 , pp. 277-288
    • Herschkovitz, Y.1    Lerner, A.2    Davidov, Y.3    Rothballer, M.4    Hartmann, A.5
  • 2
    • 0033818519 scopus 로고    scopus 로고
    • Azospirillum, a free-living nitrogen-fixing bacterium closely associated with grasses: Genetic, biochemical and ecological aspects
    • Steenhoudt O, Vanderleyden J (2000) Azospirillum, a free-living nitrogen-fixing bacterium closely associated with grasses: genetic, biochemical and ecological aspects. FEMS Microbiol Rev 24: 487-506.
    • (2000) FEMS Microbiol Rev , vol.24 , pp. 487-506
    • Steenhoudt, O.1    Vanderleyden, J.2
  • 3
    • 0021796438 scopus 로고
    • Flocculation in Azospirillum brasilense and Azospirillum lipoferum: Exopolysaccharides and cyst formation
    • Sadasivan L, Neyra CA (1985) Flocculation in Azospirillum brasilense and Azospirillum lipoferum: exopolysaccharides and cyst formation. J Bacteriol 163: 716-723.
    • (1985) J Bacteriol , vol.163 , pp. 716-723
    • Sadasivan, L.1    Neyra, C.A.2
  • 4
    • 0023179708 scopus 로고
    • Cyst production and brown pigment formation in aging cultures of Azospirillum brasilense ATCC 29145
    • Sadasivan L, Neyra CA (1987) Cyst production and brown pigment formation in aging cultures of Azospirillum brasilense ATCC 29145. J Bacteriol 169: 1670-1677.
    • (1987) J Bacteriol , vol.169 , pp. 1670-1677
    • Sadasivan, L.1    Neyra, C.A.2
  • 5
    • 0031825203 scopus 로고    scopus 로고
    • Aggregation in Azospirillum brasilense: Effects of chemical and physical factors and involvement of extracellular components
    • Burdman S, Jurkevitch E, Schwartsburd B, Hampel M, Okon Y (1998) Aggregation in Azospirillum brasilense: effects of chemical and physical factors and involvement of extracellular components. Microbiology 144: 1989-1999.
    • (1998) Microbiology , vol.144 , pp. 1989-1999
    • Burdman, S.1    Jurkevitch, E.2    Schwartsburd, B.3    Hampel, M.4    Okon, Y.5
  • 6
    • 0032031488 scopus 로고    scopus 로고
    • A transcriptional regulator of the LuxR-UhpA family, FlcA, controls flocculation and wheat root surface colonization by Azospirillum brasilense Sp7
    • Pereg Gerk L, Paquelin A, Gounon P, Kennedy IR, Elmerich C (1998) A transcriptional regulator of the LuxR-UhpA family, FlcA, controls flocculation and wheat root surface colonization by Azospirillum brasilense Sp7. Mol Plant Microbe Interact 11: 177-187.
    • (1998) Mol Plant Microbe Interact , vol.11 , pp. 177-187
    • Pereg Gerk, L.1    Paquelin, A.2    Gounon, P.3    Kennedy, I.R.4    Elmerich, C.5
  • 7
    • 0034664015 scopus 로고    scopus 로고
    • Extracellular polysaccharide composition of Azospirillum brasilense and its relation with cell aggregation
    • Burdman S, Jurkevitch E, Soria-Dias ME, Sarrano AMG, Okon Y (2000a) Extracellular polysaccharide composition of Azospirillum brasilense and its relation with cell aggregation. FEMS Microbiol Lett 189: 259-264.
    • (2000) FEMS Microbiol Lett , vol.189 , pp. 259-264
    • Burdman, S.1    Jurkevitch, E.2    Soria-Dias, M.E.3    Sarrano, A.M.G.4    Okon, Y.5
  • 8
    • 0033936201 scopus 로고    scopus 로고
    • Surface characteristics of Azospirillum brasilense in relation to cell aggregation and attachment to plant roots
    • Burdman S, Okon Y, Jurkevitch E (2000b) Surface characteristics of Azospirillum brasilense in relation to cell aggregation and attachment to plant roots. Crit Rev Microbiol 26: 91-110.
    • (2000) Crit Rev Microbiol , vol.26 , pp. 91-110
    • Burdman, S.1    Okon, Y.2    Jurkevitch, E.3
  • 9
    • 19944369426 scopus 로고    scopus 로고
    • Ecological and agricultural significance of bacterial polyhydroxyalkanoates
    • Kadouri D, Jurkevitch E, Okon Y, Castro-Sowinski S (2005) Ecological and agricultural significance of bacterial polyhydroxyalkanoates. Crit Rev Microbiol 31: 55-67.
    • (2005) Crit Rev Microbiol , vol.31 , pp. 55-67
    • Kadouri, D.1    Jurkevitch, E.2    Okon, Y.3    Castro-Sowinski, S.4
  • 10
    • 0028906668 scopus 로고
    • In situ localization of Azospirillum brasilense in the rhizosphere of wheat with fluorescently labeled, rRNA-targeted oligonucleotide probes and scanning confocal laser microscopy
    • Assmus B, Hutzler P, Kirchhof G, Amann R, Lawrence JR, et al. (1995) In situ localization of Azospirillum brasilense in the rhizosphere of wheat with fluorescently labeled, rRNA-targeted oligonucleotide probes and scanning confocal laser microscopy. Appl Environ Microbiol 61: 1013-1019.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 1013-1019
    • Assmus, B.1    Hutzler, P.2    Kirchhof, G.3    Amann, R.4    Lawrence, J.R.5
  • 11
    • 0034016243 scopus 로고    scopus 로고
    • Mutants with enhanced nitrogenase activity in hydroponic Azospirillum brasilense-wheat associations
    • Pereg Gerk L, Gilchrist K, Kennedy IR (2000) Mutants with enhanced nitrogenase activity in hydroponic Azospirillum brasilense-wheat associations. Appl Environ Microbiol 66: 2175-2184.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 2175-2184
    • Pereg Gerk, L.1    Gilchrist, K.2    Kennedy, I.R.3
  • 12
    • 33751249902 scopus 로고    scopus 로고
    • cDNA-AFLP reveals differentially expressed genes related to cell aggregation of Azospirillum brasilense
    • Valverde A, Okon Y, Burdman S (2006) cDNA-AFLP reveals differentially expressed genes related to cell aggregation of Azospirillum brasilense. FEMS Microbiol Lett 265: 186-194.
    • (2006) FEMS Microbiol Lett , vol.265 , pp. 186-194
    • Valverde, A.1    Okon, Y.2    Burdman, S.3
  • 13
    • 0029040821 scopus 로고
    • A mutant of Azospirillum brasilense Sp7 impaired in flocculation with a modified colonization pattern and superior nitrogen fixation in association with wheat
    • Katupitiya S, Millet J, Vesk M, Viccars L, Zeman A, et al. (1995) A mutant of Azospirillum brasilense Sp7 impaired in flocculation with a modified colonization pattern and superior nitrogen fixation in association with wheat. Appl Environ Microbiol 61: 1987-1995.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 1987-1995
    • Katupitiya, S.1    Millet, J.2    Vesk, M.3    Viccars, L.4    Zeman, A.5
  • 15
    • 33646358207 scopus 로고    scopus 로고
    • Identification and characterization of a hemolysin gene cluster in Vibrio anguillarum
    • Rock JL, Nelson DR (2006) Identification and characterization of a hemolysin gene cluster in Vibrio anguillarum. Infect Immun 74: 2777-2786
    • (2006) Infect Immun , vol.74 , pp. 2777-2786
    • Rock, J.L.1    Nelson, D.R.2
  • 16
    • 0001510436 scopus 로고
    • Solubilization of Plant Membrane Proteins for Analysis by Two- Dimensional Gel Electrophoresis
    • Hurkman WJ, Tanaka CK (1986) Solubilization of Plant Membrane Proteins for Analysis by Two- Dimensional Gel Electrophoresis. Plant Physiol 81: 802-806.
    • (1986) Plant Physiol , vol.81 , pp. 802-806
    • Hurkman, W.J.1    Tanaka, C.K.2
  • 17
    • 0034095972 scopus 로고    scopus 로고
    • The current state of two-dimensional electrophoresis with immobilized pH gradients
    • Görg A, Obermaier C, Boguth G, Harder A, Scheibe B, et al. (2000) The current state of two-dimensional electrophoresis with immobilized pH gradients. Electrophoresis 21: 1037-1053.
    • (2000) Electrophoresis , vol.21 , pp. 1037-1053
    • Görg, A.1    Obermaier, C.2    Boguth, G.3    Harder, A.4    Scheibe, B.5
  • 18
    • 3042665732 scopus 로고    scopus 로고
    • Blue silver: A very sensitive colloidal Coomassie G-250 staining for proteome analysis
    • Candiano G, Bruschi M, Musante L, Santucci L, Ghiggeri GM, et al. (2004) Blue silver: a very sensitive colloidal Coomassie G-250 staining for proteome analysis. Electrophoresis 25: 1327-1333.
    • (2004) Electrophoresis , vol.25 , pp. 1327-1333
    • Candiano, G.1    Bruschi, M.2    Musante, L.3    Santucci, L.4    Ghiggeri, G.M.5
  • 19
    • 84906921537 scopus 로고    scopus 로고
    • Proteomic changes during B cell maturation: 2D-DIGE approach
    • Salonen J, Rönnholm G, Kalkkinen N, Vihinen M (2013) Proteomic changes during B cell maturation: 2D-DIGE approach. PLoS ONE 8 (10): e77894.
    • (2013) PLoS ONE , vol.8 , Issue.10 , pp. e77894
    • Salonen, J.1    Rönnholm, G.2    Kalkkinen, N.3    Vihinen, M.4
  • 20
    • 84859237257 scopus 로고    scopus 로고
    • Assessment of the red cell proteome of young patients with unexplained hemolytic anemia by two-dimensional differential in-gel electrophoresis (DIGE)
    • von Löhneysen K, Scott TM, Soldau K, Xu X, Friedman JS (2012) Assessment of the red cell proteome of young patients with unexplained hemolytic anemia by two-dimensional differential in-gel electrophoresis (DIGE). PLoS ONE 7 (4): e34237.
    • (2012) PLoS ONE , vol.7 , Issue.4 , pp. e34237
    • Von Löhneysen, K.1    Scott, T.M.2    Soldau, K.3    Xu, X.4    Friedman, J.S.5
  • 21
    • 62549094876 scopus 로고    scopus 로고
    • Functional proteomics of Arabidopsis thaliana guard cells uncovers new stomatal signaling pathways
    • Zhao Z, Zhang W, Stanley BA, Assmann SM (2008) Functional proteomics of Arabidopsis thaliana guard cells uncovers new stomatal signaling pathways. Plant Cell 20 (12): 3210-3226.
    • (2008) Plant Cell , vol.20 , Issue.12 , pp. 3210-3226
    • Zhao, Z.1    Zhang, W.2    Stanley, B.A.3    Assmann, S.M.4
  • 22
    • 78650882578 scopus 로고    scopus 로고
    • Structural and Metabolic Transitions of C4 Leaf Development and Differentiation Defined by Microscopy and Quantitative Proteomics in Maize
    • Majeran W, Friso G, Ponnala L, Connolly B, Huang M, et al. (2010) Structural and Metabolic Transitions of C4 Leaf Development and Differentiation Defined by Microscopy and Quantitative Proteomics in Maize. Plant Cell 22 (11): 3509-42
    • (2010) Plant Cell , vol.22 , Issue.11 , pp. 3509-3542
    • Majeran, W.1    Friso, G.2    Ponnala, L.3    Connolly, B.4    Huang, M.5
  • 23
    • 60349101171 scopus 로고    scopus 로고
    • Analysis of cotton (Gossypium hirsutum) root proteomes during a compatible interaction with the black root rot fungus Thielaviopsis basicola
    • Coumans JV, Poljak A, Raftery MJ, Backhouse D, Pereg-Gerk L (2009) Analysis of cotton (Gossypium hirsutum) root proteomes during a compatible interaction with the black root rot fungus Thielaviopsis basicola. Proteomics 9: 335-349.
    • (2009) Proteomics , vol.9 , pp. 335-349
    • Coumans, J.V.1    Poljak, A.2    Raftery, M.J.3    Backhouse, D.4    Pereg-Gerk, L.5
  • 24
    • 77951674387 scopus 로고    scopus 로고
    • Plant extract induced changes in the proteome of the soilborne pathogenic fungus Thielaviopsis basicola
    • Coumans JVF, Moens PDJ, Poljak A, Al-Jaaidi S, Pereg L, et al. (2010) Plant extract induced changes in the proteome of the soilborne pathogenic fungus Thielaviopsis basicola. Proteomics 10: 1573-1591.
    • (2010) Proteomics , vol.10 , pp. 1573-1591
    • Coumans, J.V.F.1    Moens, P.D.J.2    Poljak, A.3    Al-Jaaidi, S.4    Pereg, L.5
  • 25
    • 79952085647 scopus 로고    scopus 로고
    • Proteomic assessment of host-associated microevolution in the fungus Thielaviopsis basicola
    • Coumans JVF, Harvey J, Backhouse D, Poljak A, Raftery MJ, et al. (2011) Proteomic assessment of host-associated microevolution in the fungus Thielaviopsis basicola. Environ Microbiol 13 (3): 576-588.
    • (2011) Environ Microbiol , vol.13 , Issue.3 , pp. 576-588
    • Coumans, J.V.F.1    Harvey, J.2    Backhouse, D.3    Poljak, A.4    Raftery, M.J.5
  • 26
    • 84901359861 scopus 로고    scopus 로고
    • Evaluation of reference genes for gene expression analysis using quantitative RT-PCR in Azospirillum brasilense
    • McMillan M, Pereg L (2014) Evaluation of reference genes for gene expression analysis using quantitative RT-PCR in Azospirillum brasilense. PLoS ONE 9 (5) e98162.
    • (2014) PLoS ONE , vol.9 , Issue.5 , pp. e98162
    • McMillan, M.1    Pereg, L.2
  • 27
    • 0023925816 scopus 로고
    • Congo red binding and salt aggregation as indicators of virulence in Shigella species
    • Qadri F, Hossain SA, Ciznar I, Haider K, Ljungh A, et al. (1988) Congo red binding and salt aggregation as indicators of virulence in Shigella species. J Clin Microbiol 26: 1343-1348.
    • (1988) J Clin Microbiol , vol.26 , pp. 1343-1348
    • Qadri, F.1    Hossain, S.A.2    Ciznar, I.3    Haider, K.4    Ljungh, A.5
  • 28
    • 0041884952 scopus 로고    scopus 로고
    • Identification of 2D-gel proteins: A comparison of MALDI/TOF peptide mass mapping to mu LC-ESI tandem mass spectrometry
    • Lim H, Eng J, Yates JR, Tollaksen SL, Giometti CS, et al. (2003) Identification of 2D-gel proteins: a comparison of MALDI/TOF peptide mass mapping to mu LC-ESI tandem mass spectrometry. J Am Soc Mass Spectrom 14: 957-970.
    • (2003) J Am Soc Mass Spectrom , vol.14 , pp. 957-970
    • Lim, H.1    Eng, J.2    Yates, J.R.3    Tollaksen, S.L.4    Giometti, C.S.5
  • 29
    • 0024064790 scopus 로고
    • Overproduction of peroxide-scavenging enzymes in Escherichia coli suppresses spontaneous mutagenesis and sensitivity to redox-cycling agents in oxyR-mutants
    • Greenberg JT, Demple B (1988) Overproduction of peroxide-scavenging enzymes in Escherichia coli suppresses spontaneous mutagenesis and sensitivity to redox-cycling agents in oxyR-mutants. EMBO J 7: 2611-2617.
    • (1988) EMBO J , vol.7 , pp. 2611-2617
    • Greenberg, J.T.1    Demple, B.2
  • 30
    • 0024604234 scopus 로고
    • An alkyl hydroperoxide reductase induced by oxidative stress in Salmonella typhimurium and Escherichia coli: Genetic characterization and cloning of ahp
    • Storz G, Jacobson FS, Tartaglia LA, Morgan RW, Silveira LA, et al. (1989) An alkyl hydroperoxide reductase induced by oxidative stress in Salmonella typhimurium and Escherichia coli: genetic characterization and cloning of ahp. J Bacteriol 171: 2049-2055.
    • (1989) J Bacteriol , vol.171 , pp. 2049-2055
    • Storz, G.1    Jacobson, F.S.2    Tartaglia, L.A.3    Morgan, R.W.4    Silveira, L.A.5
  • 31
    • 0023187678 scopus 로고
    • Oxidative mechanisms of toxicity of low-intensity near-UV light in Salmonella typhimurium
    • Kramer GF, Ames BN (1987) Oxidative mechanisms of toxicity of low-intensity near-UV light in Salmonella typhimurium. J Bacteriol 169: 2259-2266.
    • (1987) J Bacteriol , vol.169 , pp. 2259-2266
    • Kramer, G.F.1    Ames, B.N.2
  • 32
    • 0029144017 scopus 로고
    • A homologue to the Escherichia coli alkyl hydroperoxide reductase AhpC is induced by osmotic upshock in Staphylococcus aureus
    • Armstrong-Buisseret L, Cole MB, Stewart GS (1995) A homologue to the Escherichia coli alkyl hydroperoxide reductase AhpC is induced by osmotic upshock in Staphylococcus aureus. Microbiology 141: 1655-1661.
    • (1995) Microbiology , vol.141 , pp. 1655-1661
    • Armstrong-Buisseret, L.1    Cole, M.B.2    Stewart, G.S.3
  • 33
    • 0031884727 scopus 로고    scopus 로고
    • Heat shock response enhances acid tolerance of Escherichia coli O157:H7
    • Wang G, Doyle MP (1998) Heat shock response enhances acid tolerance of Escherichia coli O157:H7. Lett Appl Microbiol 26: 31-34.
    • (1998) Lett Appl Microbiol , vol.26 , pp. 31-34
    • Wang, G.1    Doyle, M.P.2
  • 34
    • 0035682033 scopus 로고    scopus 로고
    • Heat-shock-induced proteins from Myxococcus xanthus
    • Otani M, Tabata J, Ueki T, Sano K, Inouye S (2001) Heat-shock-induced proteins from Myxococcus xanthus. J Bacteriol 183: 6282-6287.
    • (2001) J Bacteriol , vol.183 , pp. 6282-6287
    • Otani, M.1    Tabata, J.2    Ueki, T.3    Sano, K.4    Inouye, S.5
  • 35
    • 65649110115 scopus 로고    scopus 로고
    • Alkyl hydroperoxide reductase has a role in oxidative stress resistance and in modulating changes in cell-surface properties in Azospirillum brasilense Sp245
    • Wasim M, Bible A, Xie Z, Alexandre G (2009) Alkyl hydroperoxide reductase has a role in oxidative stress resistance and in modulating changes in cell-surface properties in Azospirillum brasilense Sp245. Microbiology 115: 1192-1202.
    • (2009) Microbiology , vol.115 , pp. 1192-1202
    • Wasim, M.1    Bible, A.2    Xie, Z.3    Alexandre, G.4
  • 36
    • 0038236437 scopus 로고    scopus 로고
    • Alternative roles of ClpX and ClpP in Staphylococcus aureus stress tolerance and virulence
    • Frees D, Qazi SN, Hill PJ, Ingmer H (2003) Alternative roles of ClpX and ClpP in Staphylococcus aureus stress tolerance and virulence. Mol Microbiol 48: 1565-1578.
    • (2003) Mol Microbiol , vol.48 , pp. 1565-1578
    • Frees, D.1    Qazi, S.N.2    Hill, P.J.3    Ingmer, H.4
  • 37
    • 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
  • 38
    • 0037216549 scopus 로고    scopus 로고
    • Global role for ClpP-containing proteases in stationary-phase adaptation of Escherichia coli
    • Weichart D, Querfurth N, Dreger M, Hengge-Aronis R (2003) Global role for ClpP-containing proteases in stationary-phase adaptation of Escherichia coli. J Bacteriol 185: 115-125.
    • (2003) J Bacteriol , vol.185 , pp. 115-125
    • Weichart, D.1    Querfurth, N.2    Dreger, M.3    Hengge-Aronis, R.4
  • 39
    • 0034072580 scopus 로고    scopus 로고
    • The clp proteases of Bacillus subtillis are directly involved in degradation of misfolded proteins
    • Kruger E, Witt E, Ohlmeier S, Hanschke R, Hecker M (2000) The clp proteases of Bacillus subtillis are directly involved in degradation of misfolded proteins. J Bacteriol 182: 3259-3265.
    • (2000) J Bacteriol , vol.182 , pp. 3259-3265
    • Kruger, E.1    Witt, E.2    Ohlmeier, S.3    Hanschke, R.4    Hecker, M.5
  • 40
    • 0036736598 scopus 로고    scopus 로고
    • ClpP is involved in the stress response and degradation of misfolded proteins in Salmonella enterica serovar Typhimurium
    • Thomsen LE, Olsen JE, Foster JW, Ingmer H (2002) ClpP is involved in the stress response and degradation of misfolded proteins in Salmonella enterica serovar Typhimurium. Microbiology 148: 2727-2733.
    • (2002) Microbiology , vol.148 , pp. 2727-2733
    • Thomsen, L.E.1    Olsen, J.E.2    Foster, J.W.3    Ingmer, H.4
  • 41
    • 0032920907 scopus 로고    scopus 로고
    • ClpP participates in the degradation of misfolded protein in Lactococcus lactis
    • Frees D, Ingmer H (1999) ClpP participates in the degradation of misfolded protein in Lactococcus lactis. Mol Microbiol 31: 79-87.
    • (1999) Mol Microbiol , vol.31 , pp. 79-87
    • Frees, D.1    Ingmer, H.2
  • 42
    • 0031831529 scopus 로고    scopus 로고
    • Stress induction of the Bacillus subtilis clpP gene encoding a homologue of the proteolytic component of the Clp protease and the involvement of ClpP and ClpX in stress tolerance
    • Gerth U, Kruger E, Derre I, Msadek T, Hecker M (1998) Stress induction of the Bacillus subtilis clpP gene encoding a homologue of the proteolytic component of the Clp protease and the involvement of ClpP and ClpX in stress tolerance. Mol Microbiol 28: 787-802.
    • (1998) Mol Microbiol , vol.28 , pp. 787-802
    • Gerth, U.1    Kruger, E.2    Derre, I.3    Msadek, T.4    Hecker, M.5
  • 43
    • 4344696027 scopus 로고    scopus 로고
    • The ClpP peptidase is the major determinant of bulk protein turnover in Bacillus subtilis
    • Kock H, Gerth U, Hecker M (2004) The ClpP peptidase is the major determinant of bulk protein turnover in Bacillus subtilis. J Bacteriol 186: 5856-5864.
    • (2004) J Bacteriol , vol.186 , pp. 5856-5864
    • Kock, H.1    Gerth, U.2    Hecker, M.3
  • 44
    • 84855564138 scopus 로고    scopus 로고
    • New Insights into Staphylococcus aureus Stress Tolerance and Virulence Regulation from an Analysis of the Role of the ClpP Protease in the Strains Newman, COL, and SA564
    • Frees D, Andersen J, Hemmingsen L, Koskenniemi K, Bæk K, et al. (2012) New Insights into Staphylococcus aureus Stress Tolerance and Virulence Regulation from an Analysis of the Role of the ClpP Protease in the Strains Newman, COL, and SA564. J Proteome Res 11(1): 95-108.
    • (2012) J Proteome Res , vol.11 , Issue.1 , pp. 95-108
    • Frees, D.1    Andersen, J.2    Hemmingsen, L.3    Koskenniemi, K.4    Bæk, K.5
  • 45
    • 25444434412 scopus 로고    scopus 로고
    • NO-mediated cytoprotection: Instant adaptation to oxidative stress in bacteria
    • Gusarov I, Nudler E (2005) NO-mediated cytoprotection: Instant adaptation to oxidative stress in bacteria. PNAS 102(39): 13855-13860.
    • (2005) PNAS , vol.102 , Issue.39 , pp. 13855-13860
    • Gusarov, I.1    Nudler, E.2
  • 46
    • 70249096979 scopus 로고    scopus 로고
    • Endogenous nitric oxide protects bacteria against a wide spectrum of antibiotics
    • Gusarov I, Shatalin K, Starodubtseva M, Nudler E (2009) Endogenous nitric oxide protects bacteria against a wide spectrum of antibiotics. Science 325(5946): 1380-1384.
    • (2009) Science , vol.325 , Issue.5946 , pp. 1380-1384
    • Gusarov, I.1    Shatalin, K.2    Starodubtseva, M.3    Nudler, E.4
  • 47
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutases
    • Fridovich I (1995) Superoxide radical and superoxide dismutases. Ann Rev Biochem 64: 97-112.
    • (1995) Ann Rev Biochem , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 48
    • 58149178679 scopus 로고    scopus 로고
    • Host defense and pathogenesis in Staphylococcus aureus infections
    • DeLeo FR, Diep BA, Otto M (2009) Host defense and pathogenesis in Staphylococcus aureus infections. Infect Dis Clin North Am 23(1): 17-34.
    • (2009) Infect Dis Clin North Am , vol.23 , Issue.1 , pp. 17-34
    • DeLeo, F.R.1    Diep, B.A.2    Otto, M.3
  • 49
    • 0001298780 scopus 로고
    • Oxygen-dependent mutagenesis in E. coli lacking superoxide dismutase
    • Farr SB, Dari R, Touati D (1986) Oxygen-dependent mutagenesis in E. coli lacking superoxide dismutase. PNAS 83: 8268-8272.
    • (1986) PNAS , vol.83 , pp. 8268-8272
    • Farr, S.B.1    Dari, R.2    Touati, D.3
  • 50
    • 71449125819 scopus 로고    scopus 로고
    • The Azospirillum brasilense Sp7 noeJ and noeL genes are involved in extracellular polysaccharide biosynthesis
    • Lerner A, Castro-Sowinski S, Valverde A, Lerner H, Dror R, et al. (2009) The Azospirillum brasilense Sp7 noeJ and noeL genes are involved in extracellular polysaccharide biosynthesis. Microbiology 155: 4058-4068.
    • (2009) Microbiology , vol.155 , pp. 4058-4068
    • Lerner, A.1    Castro-Sowinski, S.2    Valverde, A.3    Lerner, H.4    Dror, R.5
  • 51
    • 33745960944 scopus 로고    scopus 로고
    • The role of PHB metabolism in the symbiosis of rhizobia with legumes
    • Trainer MA, Charles TC (2006) The role of PHB metabolism in the symbiosis of rhizobia with legumes. Appl Microbiol Biotechnol 71: 377-386.
    • (2006) Appl Microbiol Biotechnol , vol.71 , pp. 377-386
    • Trainer, M.A.1    Charles, T.C.2
  • 52
    • 0036271335 scopus 로고    scopus 로고
    • Identification and isolation of genes involved in poly(beta-hydroxybutyrate) biosynthesis in Azospirillum brasilense and characterization of a phbC mutant
    • Kadouri D, Burdman S, Jurkevitch E, Okon Y (2002) Identification and isolation of genes involved in poly(beta-hydroxybutyrate) biosynthesis in Azospirillum brasilense and characterization of a phbC mutant. Appl Environ Microbiol 68: 2943-2949.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 2943-2949
    • Kadouri, D.1    Burdman, S.2    Jurkevitch, E.3    Okon, Y.4
  • 53
    • 0037641233 scopus 로고    scopus 로고
    • Involvement of the reserve material poly-beta-hydroxybutyrate in Azospirillum brasilense stress endurance and root colonization
    • Kadouri D, Jurkevitch E, Okon Y (2003) Involvement of the reserve material poly-beta-hydroxybutyrate in Azospirillum brasilense stress endurance and root colonization. Appl Environ Microbiol 69: 3244-3250.
    • (2003) Appl Environ Microbiol , vol.69 , pp. 3244-3250
    • Kadouri, D.1    Jurkevitch, E.2    Okon, Y.3
  • 54
    • 0031959475 scopus 로고    scopus 로고
    • Regulation of poly(beta-hydroxybutyrate) synthesis in Methylobacterium rhodesianum MB 126 growing on methanol or fructose
    • Mothes G, Ackermann JU, Babel W (1998) Regulation of poly(beta-hydroxybutyrate) synthesis in Methylobacterium rhodesianum MB 126 growing on methanol or fructose. Arch Microbiol 169: 360-363.
    • (1998) Arch Microbiol , vol.169 , pp. 360-363
    • Mothes, G.1    Ackermann, J.U.2    Babel, W.3
  • 55
    • 8044240279 scopus 로고    scopus 로고
    • Competition between beta-ketothiolase and citrate synthase during poly(beta-hydroxybutyrate) synthesis in Methylobacterium rhodesianum
    • Mothes G, Rivera IS, Babel W (1996) Competition between beta-ketothiolase and citrate synthase during poly(beta-hydroxybutyrate) synthesis in Methylobacterium rhodesianum. Arch Microbiol 166: 405-410.
    • (1996) Arch Microbiol , vol.166 , pp. 405-410
    • Mothes, G.1    Rivera, I.S.2    Babel, W.3
  • 56
    • 0017662892 scopus 로고
    • Identification of UDP-glucose as intermediate in the biosynthesis of the membrane-derived oligosaccharides of Escherichia coli
    • Schulman H, Kennedy EP (1977) Identification of UDP-glucose as intermediate in the biosynthesis of the membrane-derived oligosaccharides of Escherichia coli. J Biol Chem 252: 6299-6303.
    • (1977) J Biol Chem , vol.252 , pp. 6299-6303
    • Schulman, H.1    Kennedy, E.P.2
  • 57
    • 0029882684 scopus 로고    scopus 로고
    • Virulence and outer membrane properties of a galU mutant of Klebsiella pneumoniae CG43
    • Chang HY, Lee JH, Deng WL, Fu TF, Peng HL (1996) Virulence and outer membrane properties of a galU mutant of Klebsiella pneumoniae CG43. Microb Pathog 20: 255-261.
    • (1996) Microb Pathog , vol.20 , pp. 255-261
    • Chang, H.Y.1    Lee, J.H.2    Deng, W.L.3    Fu, T.F.4    Peng, H.L.5
  • 58
    • 3042640931 scopus 로고    scopus 로고
    • The galU gene of Pseudomonas aeruginosa is required for corneal infection and efficient systemic spread following pneumonia but not for infection confined to the lung
    • Priebe GP, Dean CR, Zaidi T, Meluleni GJ, Coleman FT, et al. (2004) The galU gene of Pseudomonas aeruginosa is required for corneal infection and efficient systemic spread following pneumonia but not for infection confined to the lung. Infect Immun 72: 4224-4232.
    • (2004) Infect Immun , vol.72 , pp. 4224-4232
    • Priebe, G.P.1    Dean, C.R.2    Zaidi, T.3    Meluleni, G.J.4    Coleman, F.T.5
  • 59
    • 0028861531 scopus 로고
    • Avirulence of rough mutants of Shigella flexneri: Requirement of O antigen for correct unipolar localization of IcsA in the bacterial outer membrane
    • Sandlin RC, Lampel KA, Keasler SP, Goldberg MB, Stolzer AL, et al. (1995) Avirulence of rough mutants of Shigella flexneri: Requirement of O antigen for correct unipolar localization of IcsA in the bacterial outer membrane. Infect Immun 63: 229-237.
    • (1995) Infect Immun , vol.63 , pp. 229-237
    • Sandlin, R.C.1    Lampel, K.A.2    Keasler, S.P.3    Goldberg, M.B.4    Stolzer, A.L.5
  • 60
    • 0031744365 scopus 로고    scopus 로고
    • Characterization of the galU gene of Streptococcus pneumoniae encoding a uridine diphosphoglucose pyrophosphorylase: A gene essential for capsular polysaccharide biosynthesis
    • Mollerach M, Lopez R, Garcia E (1998) Characterization of the galU gene of Streptococcus pneumoniae encoding a uridine diphosphoglucose pyrophosphorylase: a gene essential for capsular polysaccharide biosynthesis. J Exp Med 188: 2047-2056.
    • (1998) J Exp Med , vol.188 , pp. 2047-2056
    • Mollerach, M.1    Lopez, R.2    Garcia, E.3
  • 61
    • 0032587729 scopus 로고    scopus 로고
    • Identification of Tn10 insertions in the rfaG, rfaP, and galU genes involved in lipopolysaccharide core biosynthesis that affect Escherichia coli adhesion
    • Genevaux P, Bauda P, DuBow M, Oudega B (1999) Identification of Tn10 insertions in the rfaG, rfaP, and galU genes involved in lipopolysaccharide core biosynthesis that affect Escherichia coli adhesion. Arch Microbiol 172: 1-8.
    • (1999) Arch Microbiol , vol.172 , pp. 1-8
    • Genevaux, P.1    Bauda, P.2    DuBow, M.3    Oudega, B.4
  • 62
    • 0025220127 scopus 로고
    • A mutant of Escherichia coli defective in the first step of endotoxin biosynthesis
    • Galloway SM, Raetz CR (1990) A mutant of Escherichia coli defective in the first step of endotoxin biosynthesis. J Biol Chem 265: 6394-6402.
    • (1990) J Biol Chem , vol.265 , pp. 6394-6402
    • Galloway, S.M.1    Raetz, C.R.2
  • 63
    • 35348926770 scopus 로고    scopus 로고
    • Structural basis for the acyl chain selectivity and mechanism of UDP-Nacetylglucosamine acyltransferase
    • Williams AH, Raetz CR (2007) Structural basis for the acyl chain selectivity and mechanism of UDP-Nacetylglucosamine acyltransferase. PNAS 104: 13543-13550.
    • (2007) PNAS , vol.104 , pp. 13543-13550
    • Williams, A.H.1    Raetz, C.R.2
  • 64
    • 0027304442 scopus 로고
    • UDP-N-acetylglucosamine acyltransferase of Escherichia coli. The first step of endotoxin biosynthesis is thermodynamically unfavorable
    • Anderson MS, Bull HG, Galloway SM, Kelly TM, Mohan S, et al. (1993) UDP-N-acetylglucosamine acyltransferase of Escherichia coli. The first step of endotoxin biosynthesis is thermodynamically unfavorable. J Biol Chem 268: 19858-19865.
    • (1993) J Biol Chem , vol.268 , pp. 19858-19865
    • Anderson, M.S.1    Bull, H.G.2    Galloway, S.M.3    Kelly, T.M.4    Mohan, S.5
  • 65
    • 52649087801 scopus 로고    scopus 로고
    • Function of a Chemotaxis-Like Signal Transduction Pathway in Modulating Motility, Cell Clumping, and Cell Length in the Alphaproteobacterium Azospirillum brasilense
    • Bible A, Stephens B, Ortega R, Xie Z, Alexandre G, (2008) Function of a Chemotaxis-Like Signal Transduction Pathway in Modulating Motility, Cell Clumping, and Cell Length in the Alphaproteobacterium Azospirillum brasilense. J Bacteriol 190 (19): 6365-6375
    • (2008) J Bacteriol , vol.190 , Issue.19 , pp. 6365-6375
    • Bible, A.1    Stephens, B.2    Ortega, R.3    Xie, Z.4    Alexandre, G.5
  • 66
    • 84864003543 scopus 로고    scopus 로고
    • The Azospirillum brasilense Che1 Chemotaxis Pathway Controls Swimming Velocity, Which Affects Transient Cell-to-Cell Clumping
    • Bible A, Russell M, Alexandre G (2012) The Azospirillum brasilense Che1 Chemotaxis Pathway Controls Swimming Velocity, Which Affects Transient Cell-to-Cell Clumping. J Bacteriol 194 (13): 3343-3355
    • (2012) J Bacteriol , vol.194 , Issue.13 , pp. 3343-3355
    • Bible, A.1    Russell, M.2    Alexandre, G.3
  • 67
    • 20344393380 scopus 로고    scopus 로고
    • Involvement of a Che-like signal transduction cascade in regulating cyst cell development in Rhodospirillum centenum
    • Berleman JE, Bauer CE (2005) Involvement of a Che-like signal transduction cascade in regulating cyst cell development in Rhodospirillum centenum. Mol Microbiol 56: 1457-1466.
    • (2005) Mol Microbiol , vol.56 , pp. 1457-1466
    • Berleman, J.E.1    Bauer, C.E.2
  • 68
    • 0036786228 scopus 로고    scopus 로고
    • A CheW homologue is required for Myxococcus xanthus fruiting body development, social gliding motility, and fibril biogenesis
    • Bellenger K, Ma X, Shi W, Yang Z (2002) A CheW homologue is required for Myxococcus xanthus fruiting body development, social gliding motility, and fibril biogenesis. J Bacteriol 184: 5654-5660.
    • (2002) J Bacteriol , vol.184 , pp. 5654-5660
    • Bellenger, K.1    Ma, X.2    Shi, W.3    Yang, Z.4
  • 69
    • 0022516759 scopus 로고
    • Cloning and characterization of the glnA gene of Azospirillum brasilense Sp7
    • Bozouklian H, Fogher C, Elmerich C (1986) Cloning and characterization of the glnA gene of Azospirillum brasilense Sp7. Ann Inst Pasteur Microbiol 137B (1): 3-18.
    • (1986) Ann Inst Pasteur Microbiol , vol.137 B , Issue.1 , pp. 3-18
    • Bozouklian, H.1    Fogher, C.2    Elmerich, C.3
  • 70
    • 0020400997 scopus 로고
    • Genetic control of nitrogen assimilation in bacteria
    • Magasanik B (1982) Genetic control of nitrogen assimilation in bacteria. Annu Rev Genet 16: 135-168.
    • (1982) Annu Rev Genet , vol.16 , pp. 135-168
    • Magasanik, B.1
  • 71
    • 0141592641 scopus 로고    scopus 로고
    • Phenotypic changes resulting from distinct point mutations in the Azospirillum brasilense glnA gene, encoding glutamine synthetase
    • Van Dommelen A, Keijers V, Wollebrants A, Vanderleyden J (2003) Phenotypic changes resulting from distinct point mutations in the Azospirillum brasilense glnA gene, encoding glutamine synthetase. Appl Environ Microbiol 69: 5699-5701.
    • (2003) Appl Environ Microbiol , vol.69 , pp. 5699-5701
    • Van Dommelen, A.1    Keijers, V.2    Wollebrants, A.3    Vanderleyden, J.4
  • 72
    • 0025612734 scopus 로고
    • Characterization of three different nitrogen-regulated promoter regions for the expression of glnB and glnA in Azospirillum brasilense
    • de Zamaroczy M, Delorme F, Elmerich C (1990) Characterization of three different nitrogen-regulated promoter regions for the expression of glnB and glnA in Azospirillum brasilense. Mol Gen Genet 224 (3): 421-30
    • (1990) Mol Gen Genet , vol.224 , Issue.3 , pp. 421-430
    • De Zamaroczy, M.1    Delorme, F.2    Elmerich, C.3
  • 73
    • 0027322266 scopus 로고
    • Functional organization of the glnB-glnA cluster of Azospirillum brasilense
    • de Zamaroczy M, Paquelin A, Elmerich C (1993) Functional organization of the glnB-glnA cluster of Azospirillum brasilense. J Bacteriol 175 (9): 2507-15
    • (1993) J Bacteriol , vol.175 , Issue.9 , pp. 2507-2515
    • De Zamaroczy, M.1    Paquelin, A.2    Elmerich, C.3
  • 74
    • 0026705854 scopus 로고
    • Either of two functionally redundant sensor proteins, NarX and NarQ, is sufficient for nitrate regulation in Escherichia coli K-12
    • Rabin RS, Stewart V (1992) Either of two functionally redundant sensor proteins, NarX and NarQ, is sufficient for nitrate regulation in Escherichia coli K-12. PNAS 89: 8419-8423.
    • (1992) PNAS , vol.89 , pp. 8419-8423
    • Rabin, R.S.1    Stewart, V.2
  • 75
    • 0027251261 scopus 로고
    • Dual response regulators (NarL and NarP) interact with dual sensors (NarX and NarQ) to control nitrate- and nitrite-regulated gene expression in Escherichia coli K-12
    • Rabin RS, Stewart V (1993) Dual response regulators (NarL and NarP) interact with dual sensors (NarX and NarQ) to control nitrate- and nitrite-regulated gene expression in Escherichia coli K-12. J Bacteriol 175: 3259-3268.
    • (1993) J Bacteriol , vol.175 , pp. 3259-3268
    • Rabin, R.S.1    Stewart, V.2
  • 76
    • 0032835113 scopus 로고    scopus 로고
    • Signal-dependent phosphorylation of the membrane-bound NarX two-component sensor-transmitter protein of Escherichia coli: Nitrate elicits a superior anion ligand response compared to nitrite
    • Lee AI, Delgado A, Gunsalus RP (1999) Signal-dependent phosphorylation of the membrane-bound NarX two-component sensor-transmitter protein of Escherichia coli: nitrate elicits a superior anion ligand response compared to nitrite. J Bacteriol 181: 5309-5316.
    • (1999) J Bacteriol , vol.181 , pp. 5309-5316
    • Lee, A.I.1    Delgado, A.2    Gunsalus, R.P.3
  • 77
    • 27144480291 scopus 로고    scopus 로고
    • Proteomics-based identification of outer-membrane proteins responsible for import of macromolecules in Sphingomonas sp. A1: Alginatebinding flagellin on the cell surface
    • Hashimoto W, He J, Wada Y, Nankai H, Mikami B, et al. (2005) Proteomics-based identification of outer-membrane proteins responsible for import of macromolecules in Sphingomonas sp. A1: alginatebinding flagellin on the cell surface. Biochemistry 44: 13783-13794.
    • (2005) Biochemistry , vol.44 , pp. 13783-13794
    • Hashimoto, W.1    He, J.2    Wada, Y.3    Nankai, H.4    Mikami, B.5
  • 78
    • 0029586501 scopus 로고
    • The envA permeability/cell division gene of Escherichia coli encodes the second enzyme of lipid A biosynthesis. UDP-3-O-(R-3- hydroxymyristoyl)-N-acetylglucosamine deacetylase
    • Young K, Silver LL, Bramhill D, Cameron P, Eveland SS, et al. (1995) The envA permeability/cell division gene of Escherichia coli encodes the second enzyme of lipid A biosynthesis. UDP-3-O-(R-3- hydroxymyristoyl)-N-acetylglucosamine deacetylase. J Biol Chem 270: 30384-30391.
    • (1995) J Biol Chem , vol.270 , pp. 30384-30391
    • Young, K.1    Silver, L.L.2    Bramhill, D.3    Cameron, P.4    Eveland, S.S.5
  • 79
    • 0035997382 scopus 로고    scopus 로고
    • Lipopolysaccharide endotoxins
    • Raetz CR, Whitfield C (2002) Lipopolysaccharide endotoxins. Ann Rev Biochem 71: 635-700.
    • (2002) Ann Rev Biochem , vol.71 , pp. 635-700
    • Raetz, C.R.1    Whitfield, C.2
  • 80
  • 81
    • 0036225848 scopus 로고    scopus 로고
    • The roles of the polytopic membrane proteins NarK, NarU and NirC in Escherichia coli K-12: Two nitrate and three nitrite transporters
    • Clegg S, Yu F, Griffiths L, Cole JA (2002) The roles of the polytopic membrane proteins NarK, NarU and NirC in Escherichia coli K-12: two nitrate and three nitrite transporters. Mol Microbiol 44: 143-155.
    • (2002) Mol Microbiol , vol.44 , pp. 143-155
    • Clegg, S.1    Yu, F.2    Griffiths, L.3    Cole, J.A.4
  • 82
    • 0027507306 scopus 로고
    • A major superfamily of transmembrane facilitators that catalyse uniport, symport and antiport
    • Marger MD, Saier MH (1993) A major superfamily of transmembrane facilitators that catalyse uniport, symport and antiport. Trends Biochem Sci 18: 13-20.
    • (1993) Trends Biochem Sci , vol.18 , pp. 13-20
    • Marger, M.D.1    Saier, M.H.2
  • 83
    • 14644444550 scopus 로고    scopus 로고
    • Nitrate and nitrite transport in Escherichia coli
    • Jia W, Cole JA (2005) Nitrate and nitrite transport in Escherichia coli. Biochem Soc Trans 33: 159-161.
    • (2005) Biochem Soc Trans , vol.33 , pp. 159-161
    • Jia, W.1    Cole, J.A.2
  • 84
    • 0026747312 scopus 로고
    • Identification of functional cis-acting sequences involved in regulation of nark gene expression in Escherichia coli
    • Bonnefoy V, DeMoss J (1992) Identification of functional cis-acting sequences involved in regulation of nark gene expression in Escherichia coli. Mol Microbiol 6 (23): 3595-3602.
    • (1992) Mol Microbiol , vol.6 , Issue.23 , pp. 3595-3602
    • Bonnefoy, V.1    DeMoss, J.2
  • 85
    • 0027157744 scopus 로고
    • E. coli host strains significantly affect the quality of small scale plasmid DNA preparations used for sequencing
    • Taylor R, Walker D, McInnes R (1993) E. coli host strains significantly affect the quality of small scale plasmid DNA preparations used for sequencing. Nucleic Acids Res 21 (7): 1677-1678.
    • (1993) Nucleic Acids Res , vol.21 , Issue.7 , pp. 1677-1678
    • Taylor, R.1    Walker, D.2    McInnes, R.3
  • 86
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron C, Vieira J, Messing J (1985) Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33 (1): 103-119.
    • (1985) Gene , vol.33 , Issue.1 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 87
    • 0025343547 scopus 로고
    • The three operators of the lac operon cooperate in repression
    • Oehler S, Eismann ER, Krämer H, Müller-Hill B (1990) The three operators of the lac operon cooperate in repression. EMBO J 9 (4): 973-979.
    • (1990) EMBO J , vol.9 , Issue.4 , pp. 973-979
    • Oehler, S.1    Eismann, E.R.2    Krämer, H.3    Müller-Hill, B.4
  • 88
    • 0018079153 scopus 로고
    • pBR322 restriction map derived from the DNA sequence: Accurate DNA size markers up to 4361 nucleotide pairs long
    • Sutcliffe JG (1978) pBR322 restriction map derived from the DNA sequence: accurate DNA size markers up to 4361 nucleotide pairs long. Nucleic Acids Res 5 (8): 2721-2728.
    • (1978) Nucleic Acids Res , vol.5 , Issue.8 , pp. 2721-2728
    • Sutcliffe, J.G.1
  • 89
  • 90
    • 57549088879 scopus 로고    scopus 로고
    • Structural organization of the glnBA region of the Azospirillum brasilense genome
    • Castellena P, Wassam R, Monteiroa R, Cruza L, Steffens M, et al. (2009) Structural organization of the glnBA region of the Azospirillum brasilense genome. Eur J Soil Biol 45: 100-105.
    • (2009) Eur J Soil Biol , vol.45 , pp. 100-105
    • Castellena, P.1    Wassam, R.2    Monteiroa, R.3    Cruza, L.4    Steffens, M.5


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